HEADER    MEMBRANE PROTEIN                        16-DEC-19   6TQ7              
TITLE     CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH SB-334867  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OREXIN RECEPTOR TYPE 1;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: OX1R,HYPOCRETIN RECEPTOR TYPE 1;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: SB-334867 BOUND IN THE ORTHOSTERIC SITE               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCRTR1;                                                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    7TM, GPCR, MEMBRANE PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE,         
AUTHOR   2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI,          
AUTHOR   3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR,           
AUTHOR   4 J.A.CHRISTOPHER                                                      
REVDAT   4   29-JUL-20 6TQ7    1       COMPND REMARK HETNAM SITE                
REVDAT   3   11-MAR-20 6TQ7    1       JRNL                                     
REVDAT   2   29-JAN-20 6TQ7    1       JRNL                                     
REVDAT   1   01-JAN-20 6TQ7    0                                                
JRNL        AUTH   M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,       
JRNL        AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,  
JRNL        AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,         
JRNL        AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER                             
JRNL        TITL   COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES     
JRNL        TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.      
JRNL        REF    J.MED.CHEM.                   V.  63  1528 2020              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   31860301                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.9B01787                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 58.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 19273                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 963                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 33.9210 -  5.0904    1.00     4523   244  0.2330 0.2456        
REMARK   3     2  5.0904 -  4.0426    1.00     4440   265  0.1899 0.2267        
REMARK   3     3  4.0426 -  3.5322    0.90     4032   196  0.2099 0.2671        
REMARK   3     4  3.5322 -  3.2095    0.60     2705   122  0.2591 0.3416        
REMARK   3     5  3.2095 -  2.9796    0.37     1657    79  0.2880 0.3375        
REMARK   3     6  2.9796 -  2.8040    0.18      777    49  0.3047 0.4162        
REMARK   3     7  2.8040 -  2.6640    0.04      176     8  0.3195 0.3188        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.910           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 71.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 45:377)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  34.3464 -25.9828  -7.8831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2559 T22:   0.2041                                     
REMARK   3      T33:   0.1395 T12:  -0.0071                                     
REMARK   3      T13:  -0.0203 T23:  -0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3378 L22:   4.2872                                     
REMARK   3      L33:   2.3429 L12:   0.6301                                     
REMARK   3      L13:  -0.6375 L23:  -1.1781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0741 S12:  -0.3413 S13:   0.0278                       
REMARK   3      S21:   0.6145 S22:   0.0904 S23:   0.1023                       
REMARK   3      S31:   0.1666 S32:   0.0756 S33:  -0.0377                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 25:378)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1766  -4.0026 -33.1519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0128 T22:   0.4175                                     
REMARK   3      T33:   0.5394 T12:  -0.0569                                     
REMARK   3      T13:  -0.1852 T23:   0.1543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9789 L22:   4.0362                                     
REMARK   3      L33:   3.7006 L12:   0.2542                                     
REMARK   3      L13:  -0.9494 L23:  -2.0359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0889 S12:   0.3342 S13:   0.2190                       
REMARK   3      S21:  -0.2712 S22:   0.4367 S23:   0.7210                       
REMARK   3      S31:   0.0738 S32:  -0.7253 S33:  -0.1448                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND (RESID 45 THROUGH 187 OR       
REMARK   3                          RESID 199 THROUGH 377 OR RESID 401          
REMARK   3                          THROUGH 501))                               
REMARK   3     SELECTION          : (CHAIN B AND (RESID 45 THROUGH 377 OR       
REMARK   3                          RESID 401 THROUGH 501))                     
REMARK   3     ATOM PAIRS NUMBER  : 2730                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6TQ7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105894.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 3.0-6.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : STARANISO                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19273                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.664                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.923                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 58.4                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6TO7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM       
REMARK 280  CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 5.2, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 284K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       74.12150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     SER A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     LEU A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     LEU A    35                                                      
REMARK 465     TRP A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     TYR A    39                                                      
REMARK 465     LEU A    40                                                      
REMARK 465     TYR A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     GLN A    44                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     ARG A   256                                                      
REMARK 465     ASN A   257                                                      
REMARK 465     TRP A   258                                                      
REMARK 465     LYS A   259                                                      
REMARK 465     ARG A   260                                                      
REMARK 465     PRO A   261                                                      
REMARK 465     SER A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     GLN A   264                                                      
REMARK 465     LEU A   265                                                      
REMARK 465     GLY A   266                                                      
REMARK 465     ASP A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     GLU A   269                                                      
REMARK 465     GLN A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     LEU A   272                                                      
REMARK 465     SER A   273                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     GLU A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     GLN A   277                                                      
REMARK 465     PRO A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     ALA A   280                                                      
REMARK 465     ARG A   281                                                      
REMARK 465     ALA A   282                                                      
REMARK 465     PHE A   283                                                      
REMARK 465     LEU A   284                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     LEU A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     ALA A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS A   389                                                      
REMARK 465     HIS A   390                                                      
REMARK 465     HIS A   391                                                      
REMARK 465     HIS A   392                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     LEU B   189                                                      
REMARK 465     PRO B   190                                                      
REMARK 465     GLU B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     ALA B   193                                                      
REMARK 465     ALA B   194                                                      
REMARK 465     ARG B   195                                                      
REMARK 465     THR B   196                                                      
REMARK 465     ARG B   197                                                      
REMARK 465     ALA B   198                                                      
REMARK 465     ALA B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     VAL B   255                                                      
REMARK 465     ARG B   256                                                      
REMARK 465     ASN B   257                                                      
REMARK 465     TRP B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     ARG B   260                                                      
REMARK 465     PRO B   261                                                      
REMARK 465     SER B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     GLN B   264                                                      
REMARK 465     LEU B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ASP B   267                                                      
REMARK 465     LEU B   268                                                      
REMARK 465     GLU B   269                                                      
REMARK 465     GLN B   270                                                      
REMARK 465     GLY B   271                                                      
REMARK 465     LEU B   272                                                      
REMARK 465     SER B   273                                                      
REMARK 465     GLY B   274                                                      
REMARK 465     GLU B   275                                                      
REMARK 465     PRO B   276                                                      
REMARK 465     GLN B   277                                                      
REMARK 465     PRO B   278                                                      
REMARK 465     ARG B   279                                                      
REMARK 465     ALA B   280                                                      
REMARK 465     ARG B   281                                                      
REMARK 465     ALA B   282                                                      
REMARK 465     PHE B   283                                                      
REMARK 465     LEU B   284                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     LEU B   380                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     ALA B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     HIS B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     HIS B   386                                                      
REMARK 465     HIS B   387                                                      
REMARK 465     HIS B   388                                                      
REMARK 465     HIS B   389                                                      
REMARK 465     HIS B   390                                                      
REMARK 465     HIS B   391                                                      
REMARK 465     HIS B   392                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A 126   CG    GLN A 126   CD      0.197                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  76       40.43    -83.59                                   
REMARK 500    TYR A 224      -66.37   -133.75                                   
REMARK 500    GLN A 246       55.04   -116.17                                   
REMARK 500    ASP A 332       45.46   -103.97                                   
REMARK 500    SER B  27       74.24   -101.42                                   
REMARK 500    TYR B  39      -60.78   -139.78                                   
REMARK 500    TYR B 224      -66.39   -133.73                                   
REMARK 500    ASP B 332       60.80   -105.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 508        DISTANCE =  6.33 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     SOG A  408                                                       
REMARK 610     SOG A  409                                                       
REMARK 610     SOG A  410                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6TO7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TOT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TP6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TP3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TP4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TQ4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6TQ6   RELATED DB: PDB                                   
DBREF  6TQ7 A   28   380  UNP    O43613   OX1R_HUMAN      28    380             
DBREF  6TQ7 B   28   380  UNP    O43613   OX1R_HUMAN      28    380             
SEQADV 6TQ7 ALA A   25  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA A   26  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 SER A   27  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA A   46  UNP  O43613    GLU    46 ENGINEERED MUTATION            
SEQADV 6TQ7 LEU A   85  UNP  O43613    ILE    85 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A   95  UNP  O43613    VAL    95 ENGINEERED MUTATION            
SEQADV 6TQ7 LEU A  162  UNP  O43613    ARG   162 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A  194  UNP  O43613    ASN   194 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A  198  UNP  O43613    LEU   198 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A  211  UNP  O43613    TYR   211 ENGINEERED MUTATION            
SEQADV 6TQ7 VAL A  304  UNP  O43613    LEU   304 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A  339  UNP  O43613    CYS   339 ENGINEERED MUTATION            
SEQADV 6TQ7 TRP A  375  UNP  O43613    CYS   375 ENGINEERED MUTATION            
SEQADV 6TQ7 TRP A  376  UNP  O43613    CYS   376 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA A  381  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA A  382  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA A  383  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  384  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  385  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  386  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  387  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  388  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  389  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  390  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  391  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS A  392  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA B   25  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA B   26  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 SER B   27  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA B   46  UNP  O43613    GLU    46 ENGINEERED MUTATION            
SEQADV 6TQ7 LEU B   85  UNP  O43613    ILE    85 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B   95  UNP  O43613    VAL    95 ENGINEERED MUTATION            
SEQADV 6TQ7 LEU B  162  UNP  O43613    ARG   162 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B  194  UNP  O43613    ASN   194 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B  198  UNP  O43613    LEU   198 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B  211  UNP  O43613    TYR   211 ENGINEERED MUTATION            
SEQADV 6TQ7 VAL B  304  UNP  O43613    LEU   304 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B  339  UNP  O43613    CYS   339 ENGINEERED MUTATION            
SEQADV 6TQ7 TRP B  375  UNP  O43613    CYS   375 ENGINEERED MUTATION            
SEQADV 6TQ7 TRP B  376  UNP  O43613    CYS   376 ENGINEERED MUTATION            
SEQADV 6TQ7 ALA B  381  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA B  382  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 ALA B  383  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  384  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  385  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  386  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  387  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  388  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  389  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  390  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  391  UNP  O43613              EXPRESSION TAG                 
SEQADV 6TQ7 HIS B  392  UNP  O43613              EXPRESSION TAG                 
SEQRES   1 A  368  ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG          
SEQRES   2 A  368  ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE          
SEQRES   3 A  368  ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY          
SEQRES   4 A  368  ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS          
SEQRES   5 A  368  MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER          
SEQRES   6 A  368  LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA          
SEQRES   7 A  368  SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY          
SEQRES   8 A  368  HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL          
SEQRES   9 A  368  SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA          
SEQRES  10 A  368  LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE          
SEQRES  11 A  368  LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY          
SEQRES  12 A  368  ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA          
SEQRES  13 A  368  ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA          
SEQRES  14 A  368  ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP          
SEQRES  15 A  368  ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE          
SEQRES  16 A  368  PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA          
SEQRES  17 A  368  MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG          
SEQRES  18 A  368  GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP          
SEQRES  19 A  368  LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY          
SEQRES  20 A  368  LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU          
SEQRES  21 A  368  ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA          
SEQRES  22 A  368  LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS          
SEQRES  23 A  368  TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL          
SEQRES  24 A  368  PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL          
SEQRES  25 A  368  TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA          
SEQRES  26 A  368  ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER          
SEQRES  27 A  368  GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP          
SEQRES  28 A  368  TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  29 A  368  HIS HIS HIS HIS                                              
SEQRES   1 B  368  ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG          
SEQRES   2 B  368  ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE          
SEQRES   3 B  368  ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY          
SEQRES   4 B  368  ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS          
SEQRES   5 B  368  MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER          
SEQRES   6 B  368  LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA          
SEQRES   7 B  368  SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY          
SEQRES   8 B  368  HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL          
SEQRES   9 B  368  SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA          
SEQRES  10 B  368  LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE          
SEQRES  11 B  368  LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY          
SEQRES  12 B  368  ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA          
SEQRES  13 B  368  ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA          
SEQRES  14 B  368  ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP          
SEQRES  15 B  368  ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE          
SEQRES  16 B  368  PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA          
SEQRES  17 B  368  MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG          
SEQRES  18 B  368  GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP          
SEQRES  19 B  368  LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY          
SEQRES  20 B  368  LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU          
SEQRES  21 B  368  ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA          
SEQRES  22 B  368  LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS          
SEQRES  23 B  368  TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL          
SEQRES  24 B  368  PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL          
SEQRES  25 B  368  TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA          
SEQRES  26 B  368  ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER          
SEQRES  27 B  368  GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP          
SEQRES  28 B  368  TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS          
SEQRES  29 B  368  HIS HIS HIS HIS                                              
HET    NVK  A 401      37                                                       
HET    NVK  A 402      37                                                       
HET    SO4  A 403       5                                                       
HET    SOG  A 404      20                                                       
HET    SOG  A 405      20                                                       
HET    SOG  A 406      20                                                       
HET    SOG  A 407      20                                                       
HET    SOG  A 408       7                                                       
HET    SOG  A 409       4                                                       
HET    SOG  A 410       4                                                       
HET    PGW  A 411      51                                                       
HET    NVK  B 401      37                                                       
HET    NVK  B 402      37                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SOG  B 405      20                                                       
HET    SOG  B 406      20                                                       
HET    SOG  B 407      20                                                       
HET    SOG  B 408      20                                                       
HET    PGW  B 409      51                                                       
HETNAM     NVK 1-(2-METHYL-1,3-BENZOXAZOL-6-YL)-3-(1,5-NAPHTHYRIDIN-4-          
HETNAM   2 NVK  YL)UREA                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE                              
HETNAM     PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)            
HETNAM   2 PGW  PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)-          
HETNAM   3 PGW  OCTADEC-9-ENOATE                                                
HETSYN     SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE                                   
HETSYN     PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1-                   
HETSYN   2 PGW  GLYCEROL)]; PHOSPHATIDYLGLYCEROL                                
FORMUL   3  NVK    4(C17 H13 N5 O2)                                             
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   6  SOG    11(C14 H28 O5 S)                                             
FORMUL  13  PGW    2(C40 H77 O10 P)                                             
FORMUL  23  HOH   *19(H2 O)                                                     
HELIX    1 AA1 TYR A   45  ASN A   74  1                                  30    
HELIX    2 AA2 HIS A   75  ARG A   78  5                                   4    
HELIX    3 AA3 THR A   79  GLU A  110  1                                  32    
HELIX    4 AA4 PHE A  114  CYS A  149  1                                  36    
HELIX    5 AA5 THR A  157  MET A  176  1                                  20    
HELIX    6 AA6 MET A  176  VAL A  182  1                                   7    
HELIX    7 AA7 LEU A  189  ARG A  195  5                                   7    
HELIX    8 AA8 ASP A  209  TYR A  224  1                                  16    
HELIX    9 AA9 TYR A  224  TRP A  243  1                                  20    
HELIX   10 AB1 THR A  251  VAL A  323  1                                  41    
HELIX   11 AB2 GLN A  329  SER A  331  5                                   3    
HELIX   12 AB3 ASP A  332  SER A  362  1                                  31    
HELIX   13 AB4 SER A  362  LEU A  377  1                                  16    
HELIX   14 AB5 SER B   27  TYR B   39  1                                  13    
HELIX   15 AB6 TYR B   39  ASN B   74  1                                  36    
HELIX   16 AB7 THR B   79  GLU B  110  1                                  32    
HELIX   17 AB8 PHE B  114  CYS B  149  1                                  36    
HELIX   18 AB9 THR B  157  MET B  176  1                                  20    
HELIX   19 AC1 MET B  176  VAL B  182  1                                   7    
HELIX   20 AC2 ASP B  209  TYR B  224  1                                  16    
HELIX   21 AC3 TYR B  224  GLY B  244  1                                  21    
HELIX   22 AC4 THR B  251  VAL B  323  1                                  41    
HELIX   23 AC5 GLN B  329  SER B  331  5                                   3    
HELIX   24 AC6 ASP B  332  SER B  362  1                                  31    
HELIX   25 AC7 SER B  362  TRP B  376  1                                  15    
SHEET    1 AA1 2 MET A 183  SER A 187  0                                        
SHEET    2 AA1 2 SER A 200  GLU A 204 -1  O  VAL A 201   N  SER A 186           
SHEET    1 AA2 2 MET B 183  SER B 186  0                                        
SHEET    2 AA2 2 VAL B 201  GLU B 204 -1  O  VAL B 201   N  SER B 186           
SSBOND   1 CYS A  119    CYS A  202                          1555   1555  2.03  
SSBOND   2 CYS B  119    CYS B  202                          1555   1555  2.03  
CRYST1   59.766  148.243   71.668  90.00 112.17  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016732  0.000000  0.006819        0.00000                         
SCALE2      0.000000  0.006746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015067        0.00000                         
ATOM      1  N   TYR A  45      51.178 -46.123  -1.987  1.00 95.03           N  
ANISOU    1  N   TYR A  45    12349  10894  12862   2740  -1838   2388       N  
ATOM      2  CA  TYR A  45      50.614 -45.059  -2.802  1.00 98.51           C  
ANISOU    2  CA  TYR A  45    12720  11419  13289   2564  -1725   2194       C  
ATOM      3  C   TYR A  45      49.171 -45.405  -3.174  1.00 95.99           C  
ANISOU    3  C   TYR A  45    12620  10916  12936   2390  -1530   2152       C  
ATOM      4  O   TYR A  45      48.293 -44.542  -3.119  1.00 87.99           O  
ANISOU    4  O   TYR A  45    11707  10003  11724   2162  -1587   1999       O  
ATOM      5  CB  TYR A  45      51.480 -44.814  -4.053  1.00104.69           C  
ANISOU    5  CB  TYR A  45    13307  12127  14343   2695  -1625   2014       C  
ATOM      6  CG  TYR A  45      50.927 -43.789  -5.031  1.00106.03           C  
ANISOU    6  CG  TYR A  45    13426  12351  14511   2545  -1482   1808       C  
ATOM      7  CD1 TYR A  45      51.343 -42.461  -4.998  1.00107.41           C  
ANISOU    7  CD1 TYR A  45    13377  12780  14653   2419  -1616   1730       C  
ATOM      8  CD2 TYR A  45      49.976 -44.151  -5.975  1.00105.80           C  
ANISOU    8  CD2 TYR A  45    13566  12103  14532   2484  -1220   1687       C  
ATOM      9  CE1 TYR A  45      50.839 -41.527  -5.885  1.00106.75           C  
ANISOU    9  CE1 TYR A  45    13268  12723  14570   2285  -1512   1528       C  
ATOM     10  CE2 TYR A  45      49.471 -43.226  -6.869  1.00101.70           C  
ANISOU   10  CE2 TYR A  45    13017  11601  14024   2341  -1146   1478       C  
ATOM     11  CZ  TYR A  45      49.904 -41.915  -6.817  1.00105.91           C  
ANISOU   11  CZ  TYR A  45    13356  12392  14493   2264  -1286   1396       C  
ATOM     12  OH  TYR A  45      49.399 -40.989  -7.703  1.00109.13           O  
ANISOU   12  OH  TYR A  45    13779  12828  14857   2152  -1209   1160       O  
ATOM     13  N   ALA A  46      48.926 -46.661  -3.557  1.00100.62           N  
ANISOU   13  N   ALA A  46    13307  11210  13712   2447  -1343   2204       N  
ATOM     14  CA  ALA A  46      47.598 -47.034  -4.030  1.00 93.41           C  
ANISOU   14  CA  ALA A  46    12655  10067  12768   2279  -1238   2069       C  
ATOM     15  C   ALA A  46      46.551 -46.934  -2.923  1.00 88.83           C  
ANISOU   15  C   ALA A  46    12306   9604  11841   2106  -1331   2133       C  
ATOM     16  O   ALA A  46      45.452 -46.416  -3.149  1.00 88.55           O  
ANISOU   16  O   ALA A  46    12451   9596  11600   1935  -1269   1953       O  
ATOM     17  CB  ALA A  46      47.627 -48.450  -4.605  1.00 92.66           C  
ANISOU   17  CB  ALA A  46    12668   9598  12941   2364  -1115   2060       C  
ATOM     18  N   TRP A  47      46.857 -47.429  -1.717  1.00 89.01           N  
ANISOU   18  N   TRP A  47    12329   9697  11794   2151  -1462   2393       N  
ATOM     19  CA  TRP A  47      45.868 -47.349  -0.641  1.00 90.13           C  
ANISOU   19  CA  TRP A  47    12696   9940  11610   1974  -1531   2446       C  
ATOM     20  C   TRP A  47      45.679 -45.918  -0.164  1.00 80.07           C  
ANISOU   20  C   TRP A  47    11408   8967  10047   1820  -1676   2318       C  
ATOM     21  O   TRP A  47      44.566 -45.521   0.200  1.00 75.50           O  
ANISOU   21  O   TRP A  47    11027   8441   9219   1635  -1638   2227       O  
ATOM     22  CB  TRP A  47      46.233 -48.273   0.517  1.00107.97           C  
ANISOU   22  CB  TRP A  47    14984  12194  13847   2065  -1619   2754       C  
ATOM     23  CG  TRP A  47      45.243 -48.193   1.648  1.00123.83           C  
ANISOU   23  CG  TRP A  47    17225  14306  15517   1881  -1665   2810       C  
ATOM     24  CD1 TRP A  47      43.989 -48.734   1.683  1.00129.55           C  
ANISOU   24  CD1 TRP A  47    18187  14873  16162   1742  -1512   2780       C  
ATOM     25  CD2 TRP A  47      45.462 -47.612   2.939  1.00133.72           C  
ANISOU   25  CD2 TRP A  47    18500  15834  16473   1825  -1860   2912       C  
ATOM     26  NE1 TRP A  47      43.397 -48.481   2.897  1.00135.68           N  
ANISOU   26  NE1 TRP A  47    19117  15814  16622   1609  -1575   2863       N  
ATOM     27  CE2 TRP A  47      44.284 -47.801   3.689  1.00138.59           C  
ANISOU   27  CE2 TRP A  47    19372  16443  16844   1654  -1789   2938       C  
ATOM     28  CE3 TRP A  47      46.535 -46.936   3.529  1.00136.83           C  
ANISOU   28  CE3 TRP A  47    18734  16478  16776   1895  -2083   2963       C  
ATOM     29  CZ2 TRP A  47      44.149 -47.339   4.997  1.00141.56           C  
ANISOU   29  CZ2 TRP A  47    19857  17043  16888   1554  -1917   3015       C  
ATOM     30  CZ3 TRP A  47      46.398 -46.478   4.827  1.00140.08           C  
ANISOU   30  CZ3 TRP A  47    19264  17109  16852   1777  -2239   3025       C  
ATOM     31  CH2 TRP A  47      45.215 -46.681   5.546  1.00142.35           C  
ANISOU   31  CH2 TRP A  47    19816  17375  16895   1613  -2146   3051       C  
ATOM     32  N   VAL A  48      46.752 -45.130  -0.150  1.00 78.33           N  
ANISOU   32  N   VAL A  48    10951   8941   9868   1889  -1827   2306       N  
ATOM     33  CA  VAL A  48      46.605 -43.736   0.241  1.00 73.66           C  
ANISOU   33  CA  VAL A  48    10342   8609   9035   1718  -1962   2159       C  
ATOM     34  C   VAL A  48      45.633 -43.037  -0.692  1.00 70.65           C  
ANISOU   34  C   VAL A  48    10053   8179   8612   1589  -1816   1898       C  
ATOM     35  O   VAL A  48      44.901 -42.130  -0.278  1.00 66.90           O  
ANISOU   35  O   VAL A  48     9691   7844   7885   1412  -1838   1780       O  
ATOM     36  CB  VAL A  48      47.979 -43.042   0.251  1.00 69.18           C  
ANISOU   36  CB  VAL A  48     9483   8232   8571   1805  -2137   2169       C  
ATOM     37  CG1 VAL A  48      47.822 -41.584   0.617  1.00 59.45           C  
ANISOU   37  CG1 VAL A  48     8239   7239   7109   1603  -2262   1998       C  
ATOM     38  CG2 VAL A  48      48.913 -43.759   1.209  1.00 68.23           C  
ANISOU   38  CG2 VAL A  48     9298   8168   8458   1955  -2291   2421       C  
ATOM     39  N   LEU A  49      45.611 -43.439  -1.964  1.00 73.09           N  
ANISOU   39  N   LEU A  49    10325   8286   9160   1684  -1648   1802       N  
ATOM     40  CA  LEU A  49      44.656 -42.876  -2.910  1.00 64.75           C  
ANISOU   40  CA  LEU A  49     9376   7175   8053   1578  -1502   1567       C  
ATOM     41  C   LEU A  49      43.226 -43.239  -2.526  1.00 58.94           C  
ANISOU   41  C   LEU A  49     8920   6359   7117   1426  -1390   1564       C  
ATOM     42  O   LEU A  49      42.344 -42.373  -2.476  1.00 60.32           O  
ANISOU   42  O   LEU A  49     9184   6634   7099   1267  -1363   1438       O  
ATOM     43  CB  LEU A  49      44.973 -43.365  -4.323  1.00 62.24           C  
ANISOU   43  CB  LEU A  49     8990   6644   8012   1713  -1327   1467       C  
ATOM     44  CG  LEU A  49      44.372 -42.561  -5.475  1.00 64.80           C  
ANISOU   44  CG  LEU A  49     9325   6979   8318   1612  -1188   1207       C  
ATOM     45  CD1 LEU A  49      44.949 -41.151  -5.507  1.00 70.64           C  
ANISOU   45  CD1 LEU A  49     9840   7976   9024   1561  -1304   1104       C  
ATOM     46  CD2 LEU A  49      44.606 -43.273  -6.797  1.00 66.19           C  
ANISOU   46  CD2 LEU A  49     9495   6927   8728   1719   -969   1109       C  
ATOM     47  N   ILE A  50      42.976 -44.522  -2.253  1.00 52.97           N  
ANISOU   47  N   ILE A  50     8286   5414   6425   1468  -1309   1712       N  
ATOM     48  CA  ILE A  50      41.619 -44.949  -1.924  1.00 54.17           C  
ANISOU   48  CA  ILE A  50     8676   5478   6427   1314  -1181   1722       C  
ATOM     49  C   ILE A  50      41.167 -44.342  -0.604  1.00 60.69           C  
ANISOU   49  C   ILE A  50     9583   6516   6959   1182  -1271   1789       C  
ATOM     50  O   ILE A  50      40.007 -43.940  -0.457  1.00 60.39           O  
ANISOU   50  O   ILE A  50     9679   6509   6757   1019  -1163   1713       O  
ATOM     51  CB  ILE A  50      41.535 -46.484  -1.892  1.00 54.56           C  
ANISOU   51  CB  ILE A  50     8822   5273   6635   1382  -1079   1871       C  
ATOM     52  CG1 ILE A  50      42.144 -47.075  -3.164  1.00 43.88           C  
ANISOU   52  CG1 ILE A  50     7389   3706   5577   1523   -973   1786       C  
ATOM     53  CG2 ILE A  50      40.092 -46.924  -1.728  1.00 63.33           C  
ANISOU   53  CG2 ILE A  50    10146   6279   7636   1202   -927   1863       C  
ATOM     54  CD1 ILE A  50      42.533 -48.523  -3.022  1.00 46.80           C  
ANISOU   54  CD1 ILE A  50     7789   3842   6153   1642   -918   1956       C  
ATOM     55  N   ALA A  51      42.068 -44.267   0.377  1.00 65.20           N  
ANISOU   55  N   ALA A  51    10073   7238   7462   1246  -1453   1935       N  
ATOM     56  CA  ALA A  51      41.707 -43.658   1.651  1.00 67.70           C  
ANISOU   56  CA  ALA A  51    10491   7759   7474   1116  -1528   1974       C  
ATOM     57  C   ALA A  51      41.378 -42.180   1.480  1.00 69.65           C  
ANISOU   57  C   ALA A  51    10711   8181   7571    988  -1533   1755       C  
ATOM     58  O   ALA A  51      40.402 -41.682   2.054  1.00 67.67           O  
ANISOU   58  O   ALA A  51    10610   8003   7100    839  -1440   1700       O  
ATOM     59  CB  ALA A  51      42.838 -43.846   2.661  1.00 70.74           C  
ANISOU   59  CB  ALA A  51    10788   8276   7814   1206  -1743   2165       C  
ATOM     60  N   ALA A  52      42.187 -41.458   0.700  1.00 68.95           N  
ANISOU   60  N   ALA A  52    10424   8157   7617   1047  -1623   1633       N  
ATOM     61  CA  ALA A  52      41.914 -40.041   0.479  1.00 59.64           C  
ANISOU   61  CA  ALA A  52     9208   7131   6322    928  -1624   1427       C  
ATOM     62  C   ALA A  52      40.640 -39.839  -0.329  1.00 66.99           C  
ANISOU   62  C   ALA A  52    10247   7959   7247    838  -1414   1291       C  
ATOM     63  O   ALA A  52      39.872 -38.907  -0.066  1.00 76.14           O  
ANISOU   63  O   ALA A  52    11476   9221   8233    701  -1341   1179       O  
ATOM     64  CB  ALA A  52      43.103 -39.378  -0.217  1.00 55.53           C  
ANISOU   64  CB  ALA A  52     8429   6691   5979   1011  -1759   1344       C  
ATOM     65  N   TYR A  53      40.401 -40.696  -1.322  1.00 66.40           N  
ANISOU   65  N   TYR A  53    10187   7675   7369    910  -1303   1300       N  
ATOM     66  CA  TYR A  53      39.183 -40.569  -2.111  1.00 59.04           C  
ANISOU   66  CA  TYR A  53     9294   6668   6471    781  -1086   1163       C  
ATOM     67  C   TYR A  53      37.943 -40.901  -1.295  1.00 57.26           C  
ANISOU   67  C   TYR A  53     9280   6404   6071    655   -966   1256       C  
ATOM     68  O   TYR A  53      36.881 -40.303  -1.510  1.00 51.52           O  
ANISOU   68  O   TYR A  53     8553   5720   5304    510   -815   1147       O  
ATOM     69  CB  TYR A  53      39.261 -41.464  -3.346  1.00 56.48           C  
ANISOU   69  CB  TYR A  53     8926   6134   6401    849   -982   1123       C  
ATOM     70  CG  TYR A  53      39.683 -40.741  -4.607  1.00 56.86           C  
ANISOU   70  CG  TYR A  53     8779   6230   6597    861   -947    922       C  
ATOM     71  CD1 TYR A  53      41.001 -40.770  -5.044  1.00 59.80           C  
ANISOU   71  CD1 TYR A  53     8993   6601   7126   1026  -1032    920       C  
ATOM     72  CD2 TYR A  53      38.759 -40.030  -5.360  1.00 55.03           C  
ANISOU   72  CD2 TYR A  53     8512   6042   6355    709   -824    756       C  
ATOM     73  CE1 TYR A  53      41.386 -40.112  -6.200  1.00 62.69           C  
ANISOU   73  CE1 TYR A  53     9194   7007   7617   1033   -972    747       C  
ATOM     74  CE2 TYR A  53      39.133 -39.371  -6.515  1.00 56.14           C  
ANISOU   74  CE2 TYR A  53     8497   6226   6609    715   -792    591       C  
ATOM     75  CZ  TYR A  53      40.445 -39.414  -6.931  1.00 62.96           C  
ANISOU   75  CZ  TYR A  53     9228   7086   7607    873   -856    583       C  
ATOM     76  OH  TYR A  53      40.809 -38.754  -8.082  1.00 64.72           O  
ANISOU   76  OH  TYR A  53     9310   7348   7931    874   -797    427       O  
ATOM     77  N   VAL A  54      38.053 -41.841  -0.354  1.00 60.10           N  
ANISOU   77  N   VAL A  54     9754   6707   6372    694   -996   1446       N  
ATOM     78  CA  VAL A  54      36.900 -42.188   0.469  1.00 56.68           C  
ANISOU   78  CA  VAL A  54     9483   6254   5799    566   -847   1532       C  
ATOM     79  C   VAL A  54      36.598 -41.078   1.465  1.00 65.15           C  
ANISOU   79  C   VAL A  54    10601   7540   6613    470   -842   1482       C  
ATOM     80  O   VAL A  54      35.433 -40.736   1.699  1.00 70.29           O  
ANISOU   80  O   VAL A  54    11333   8203   7171    342   -658   1450       O  
ATOM     81  CB  VAL A  54      37.134 -43.532   1.176  1.00 49.48           C  
ANISOU   81  CB  VAL A  54     8654   5228   4919    632   -865   1743       C  
ATOM     82  CG1 VAL A  54      36.090 -43.736   2.261  1.00 51.75           C  
ANISOU   82  CG1 VAL A  54     9097   5543   5024    506   -729   1844       C  
ATOM     83  CG2 VAL A  54      37.101 -44.662   0.166  1.00 44.54           C  
ANISOU   83  CG2 VAL A  54     8022   4346   4556    689   -792   1764       C  
ATOM     84  N   ALA A  55      37.640 -40.497   2.067  1.00 62.08           N  
ANISOU   84  N   ALA A  55    10152   7315   6120    523  -1032   1472       N  
ATOM     85  CA  ALA A  55      37.428 -39.414   3.021  1.00 56.45           C  
ANISOU   85  CA  ALA A  55     9502   6787   5158    423  -1026   1395       C  
ATOM     86  C   ALA A  55      36.788 -38.209   2.348  1.00 57.25           C  
ANISOU   86  C   ALA A  55     9555   6939   5259    337   -906   1192       C  
ATOM     87  O   ALA A  55      35.876 -37.586   2.905  1.00 58.40           O  
ANISOU   87  O   ALA A  55     9799   7138   5251    231   -740   1137       O  
ATOM     88  CB  ALA A  55      38.752 -39.018   3.674  1.00 40.24           C  
ANISOU   88  CB  ALA A  55     7373   4890   3026    476  -1277   1411       C  
ATOM     89  N   VAL A  56      37.254 -37.860   1.149  1.00 61.79           N  
ANISOU   89  N   VAL A  56     9974   7492   6011    390   -974   1085       N  
ATOM     90  CA  VAL A  56      36.665 -36.731   0.435  1.00 59.53           C  
ANISOU   90  CA  VAL A  56     9611   7255   5752    311   -861    902       C  
ATOM     91  C   VAL A  56      35.218 -37.025   0.070  1.00 60.74           C  
ANISOU   91  C   VAL A  56     9786   7307   5984    216   -602    904       C  
ATOM     92  O   VAL A  56      34.364 -36.130   0.071  1.00 59.04           O  
ANISOU   92  O   VAL A  56     9546   7148   5738    122   -442    804       O  
ATOM     93  CB  VAL A  56      37.505 -36.394  -0.808  1.00 52.12           C  
ANISOU   93  CB  VAL A  56     8425   6325   5053    380   -954    776       C  
ATOM     94  CG1 VAL A  56      36.776 -35.378  -1.666  1.00 52.27           C  
ANISOU   94  CG1 VAL A  56     8313   6379   5168    289   -800    595       C  
ATOM     95  CG2 VAL A  56      38.864 -35.877  -0.391  1.00 48.70           C  
ANISOU   95  CG2 VAL A  56     7928   6016   4559    446  -1200    768       C  
ATOM     96  N   PHE A  57      34.919 -38.284  -0.249  1.00 62.14           N  
ANISOU   96  N   PHE A  57    10002   7322   6286    235   -559   1026       N  
ATOM     97  CA  PHE A  57      33.555 -38.660  -0.603  1.00 60.66           C  
ANISOU   97  CA  PHE A  57     9820   7031   6199    121   -342   1048       C  
ATOM     98  C   PHE A  57      32.603 -38.441   0.566  1.00 53.45           C  
ANISOU   98  C   PHE A  57     9066   6160   5083     32   -170   1132       C  
ATOM     99  O   PHE A  57      31.543 -37.821   0.415  1.00 44.53           O  
ANISOU   99  O   PHE A  57     7867   5056   3998    -67     21   1072       O  
ATOM    100  CB  PHE A  57      33.529 -40.118  -1.063  1.00 59.97           C  
ANISOU  100  CB  PHE A  57     9779   6739   6267    147   -348   1165       C  
ATOM    101  CG  PHE A  57      32.216 -40.557  -1.640  1.00 55.61           C  
ANISOU  101  CG  PHE A  57     9199   6067   5863      5   -170   1175       C  
ATOM    102  CD1 PHE A  57      31.829 -40.141  -2.903  1.00 54.46           C  
ANISOU  102  CD1 PHE A  57     8877   5918   5898    -63   -144   1026       C  
ATOM    103  CD2 PHE A  57      31.380 -41.406  -0.934  1.00 46.36           C  
ANISOU  103  CD2 PHE A  57     8175   4786   4653    -71    -42   1347       C  
ATOM    104  CE1 PHE A  57      30.628 -40.554  -3.448  1.00 50.87           C  
ANISOU  104  CE1 PHE A  57     8381   5360   5585   -214    -23   1048       C  
ATOM    105  CE2 PHE A  57      30.177 -41.823  -1.474  1.00 42.15           C  
ANISOU  105  CE2 PHE A  57     7588   4141   4285   -222    103   1367       C  
ATOM    106  CZ  PHE A  57      29.800 -41.395  -2.734  1.00 47.67           C  
ANISOU  106  CZ  PHE A  57     8099   4846   5167   -298     98   1217       C  
ATOM    107  N   VAL A  58      32.965 -38.947   1.743  1.00 57.24           N  
ANISOU  107  N   VAL A  58     9719   6655   5374     71   -223   1266       N  
ATOM    108  CA  VAL A  58      32.091 -38.820   2.905  1.00 57.47           C  
ANISOU  108  CA  VAL A  58     9864   6735   5238    -10    -34   1324       C  
ATOM    109  C   VAL A  58      31.979 -37.366   3.345  1.00 56.46           C  
ANISOU  109  C   VAL A  58     9743   6761   4949    -46     32   1170       C  
ATOM    110  O   VAL A  58      30.876 -36.845   3.553  1.00 44.20           O  
ANISOU  110  O   VAL A  58     8198   5214   3381   -127    282   1141       O  
ATOM    111  CB  VAL A  58      32.592 -39.714   4.049  1.00 46.31           C  
ANISOU  111  CB  VAL A  58     8582   5325   3691     38   -124   1482       C  
ATOM    112  CG1 VAL A  58      31.697 -39.549   5.260  1.00 41.48           C  
ANISOU  112  CG1 VAL A  58     8107   4766   2889    -43     82   1535       C  
ATOM    113  CG2 VAL A  58      32.630 -41.151   3.589  1.00 39.86           C  
ANISOU  113  CG2 VAL A  58     7757   4326   3061     76   -155   1629       C  
ATOM    114  N   VAL A  59      33.118 -36.692   3.503  1.00 52.87           N  
ANISOU  114  N   VAL A  59     9267   6421   4399     11   -180   1069       N  
ATOM    115  CA  VAL A  59      33.100 -35.332   4.030  1.00 39.61           C  
ANISOU  115  CA  VAL A  59     7614   4869   2566    -33   -129    910       C  
ATOM    116  C   VAL A  59      32.325 -34.398   3.109  1.00 39.39           C  
ANISOU  116  C   VAL A  59     7477   4828   2662    -79     47    779       C  
ATOM    117  O   VAL A  59      31.527 -33.571   3.569  1.00 45.43           O  
ANISOU  117  O   VAL A  59     8283   5622   3358   -135    268    705       O  
ATOM    118  CB  VAL A  59      34.535 -34.833   4.257  1.00 36.34           C  
ANISOU  118  CB  VAL A  59     7158   4570   2081     15   -416    831       C  
ATOM    119  CG1 VAL A  59      34.511 -33.390   4.704  1.00 44.60           C  
ANISOU  119  CG1 VAL A  59     8228   5717   2999    -48   -362    647       C  
ATOM    120  CG2 VAL A  59      35.227 -35.710   5.280  1.00 39.14           C  
ANISOU  120  CG2 VAL A  59     7616   4951   2303     53   -577    987       C  
ATOM    121  N   ALA A  60      32.548 -34.506   1.797  1.00 35.44           N  
ANISOU  121  N   ALA A  60     6794   4282   2389    -50    -37    740       N  
ATOM    122  CA  ALA A  60      31.855 -33.626   0.860  1.00 34.50           C  
ANISOU  122  CA  ALA A  60     6461   4167   2480    -92    103    607       C  
ATOM    123  C   ALA A  60      30.348 -33.860   0.877  1.00 47.91           C  
ANISOU  123  C   ALA A  60     8134   5791   4278   -171    386    689       C  
ATOM    124  O   ALA A  60      29.566 -32.903   0.833  1.00 49.02           O  
ANISOU  124  O   ALA A  60     8195   5957   4473   -209    580    614       O  
ATOM    125  CB  ALA A  60      32.409 -33.826  -0.551  1.00 31.87           C  
ANISOU  125  CB  ALA A  60     5902   3803   2402    -52    -51    548       C  
ATOM    126  N   LEU A  61      29.923 -35.124   0.934  1.00 59.24           N  
ANISOU  126  N   LEU A  61     9621   7121   5765   -195    420    853       N  
ATOM    127  CA  LEU A  61      28.494 -35.424   0.960  1.00 59.26           C  
ANISOU  127  CA  LEU A  61     9573   7050   5892   -288    680    954       C  
ATOM    128  C   LEU A  61      27.864 -34.979   2.273  1.00 65.82           C  
ANISOU  128  C   LEU A  61    10590   7918   6500   -312    931   1001       C  
ATOM    129  O   LEU A  61      26.858 -34.259   2.280  1.00 74.87           O  
ANISOU  129  O   LEU A  61    11633   9072   7743   -355   1180    974       O  
ATOM    130  CB  LEU A  61      28.262 -36.920   0.735  1.00 55.79           C  
ANISOU  130  CB  LEU A  61     9166   6471   5561   -325    645   1118       C  
ATOM    131  CG  LEU A  61      28.673 -37.482  -0.627  1.00 52.93           C  
ANISOU  131  CG  LEU A  61     8649   6033   5430   -320    456   1070       C  
ATOM    132  CD1 LEU A  61      28.594 -39.004  -0.636  1.00 59.22           C  
ANISOU  132  CD1 LEU A  61     9551   6662   6288   -348    425   1225       C  
ATOM    133  CD2 LEU A  61      27.814 -36.885  -1.727  1.00 39.26           C  
ANISOU  133  CD2 LEU A  61     6665   4309   3942   -406    525    989       C  
ATOM    134  N   VAL A  62      28.441 -35.400   3.399  1.00 59.51           N  
ANISOU  134  N   VAL A  62    10004   7150   5455   -275    855   1052       N  
ATOM    135  CA  VAL A  62      27.905 -34.999   4.698  1.00 51.67           C  
ANISOU  135  CA  VAL A  62     9136   6209   4289   -291   1054   1047       C  
ATOM    136  C   VAL A  62      27.914 -33.480   4.835  1.00 52.06           C  
ANISOU  136  C   VAL A  62     9175   6337   4267   -280   1144    854       C  
ATOM    137  O   VAL A  62      26.921 -32.870   5.248  1.00 49.66           O  
ANISOU  137  O   VAL A  62     8850   6024   3996   -304   1429    827       O  
ATOM    138  CB  VAL A  62      28.691 -35.668   5.837  1.00 47.34           C  
ANISOU  138  CB  VAL A  62     8794   5697   3495   -258    894   1122       C  
ATOM    139  CG1 VAL A  62      28.368 -34.983   7.152  1.00 43.88           C  
ANISOU  139  CG1 VAL A  62     8520   5327   2825   -277   1059   1067       C  
ATOM    140  CG2 VAL A  62      28.362 -37.144   5.900  1.00 41.70           C  
ANISOU  140  CG2 VAL A  62     8097   4879   2867   -276    901   1329       C  
ATOM    141  N   GLY A  63      29.041 -32.850   4.497  1.00 49.24           N  
ANISOU  141  N   GLY A  63     8820   6050   3841   -239    905    718       N  
ATOM    142  CA  GLY A  63      29.141 -31.404   4.633  1.00 43.51           C  
ANISOU  142  CA  GLY A  63     8090   5381   3061   -237    968    525       C  
ATOM    143  C   GLY A  63      28.172 -30.651   3.741  1.00 50.14           C  
ANISOU  143  C   GLY A  63     8739   6177   4136   -250   1208    475       C  
ATOM    144  O   GLY A  63      27.421 -29.790   4.206  1.00 52.57           O  
ANISOU  144  O   GLY A  63     9045   6471   4461   -253   1459    405       O  
ATOM    145  N   ASN A  64      28.178 -30.959   2.440  1.00 52.76           N  
ANISOU  145  N   ASN A  64     8853   6481   4713   -251   1106    505       N  
ATOM    146  CA  ASN A  64      27.348 -30.200   1.506  1.00 47.50           C  
ANISOU  146  CA  ASN A  64     7906   5790   4350   -259   1250    455       C  
ATOM    147  C   ASN A  64      25.862 -30.415   1.757  1.00 57.02           C  
ANISOU  147  C   ASN A  64     9039   6930   5697   -302   1584    591       C  
ATOM    148  O   ASN A  64      25.055 -29.517   1.491  1.00 65.15           O  
ANISOU  148  O   ASN A  64     9901   7943   6909   -294   1794    557       O  
ATOM    149  CB  ASN A  64      27.703 -30.565   0.065  1.00 38.10           C  
ANISOU  149  CB  ASN A  64     6466   4593   3418   -259   1012    451       C  
ATOM    150  CG  ASN A  64      28.999 -29.929  -0.387  1.00 53.82           C  
ANISOU  150  CG  ASN A  64     8439   6651   5360   -210    761    296       C  
ATOM    151  OD1 ASN A  64      29.117 -28.703  -0.419  1.00 63.56           O  
ANISOU  151  OD1 ASN A  64     9638   7917   6595   -195    812    162       O  
ATOM    152  ND2 ASN A  64      29.978 -30.752  -0.733  1.00 62.65           N  
ANISOU  152  ND2 ASN A  64     9575   7775   6454   -183    506    318       N  
ATOM    153  N   THR A  65      25.476 -31.582   2.272  1.00 54.30           N  
ANISOU  153  N   THR A  65     8800   6537   5292   -345   1646    761       N  
ATOM    154  CA  THR A  65      24.077 -31.763   2.641  1.00 58.13           C  
ANISOU  154  CA  THR A  65     9174   6970   5943   -385   1945    882       C  
ATOM    155  C   THR A  65      23.710 -30.901   3.840  1.00 66.96           C  
ANISOU  155  C   THR A  65    10414   8111   6917   -335   2170    792       C  
ATOM    156  O   THR A  65      22.606 -30.347   3.901  1.00 71.58           O  
ANISOU  156  O   THR A  65    10832   8663   7703   -325   2428    808       O  
ATOM    157  CB  THR A  65      23.785 -33.232   2.933  1.00 54.70           C  
ANISOU  157  CB  THR A  65     8786   6479   5517   -444   1911   1063       C  
ATOM    158  OG1 THR A  65      24.345 -34.052   1.896  1.00 59.14           O  
ANISOU  158  OG1 THR A  65     9305   6994   6172   -482   1667   1116       O  
ATOM    159  CG2 THR A  65      22.285 -33.460   2.998  1.00 50.65           C  
ANISOU  159  CG2 THR A  65     8058   5920   5269   -503   2163   1190       C  
ATOM    160  N   LEU A  66      24.625 -30.773   4.804  1.00 64.58           N  
ANISOU  160  N   LEU A  66    10397   7857   6284   -307   2057    700       N  
ATOM    161  CA  LEU A  66      24.381 -29.896   5.943  1.00 55.26           C  
ANISOU  161  CA  LEU A  66     9373   6680   4942   -277   2246    592       C  
ATOM    162  C   LEU A  66      24.342 -28.434   5.526  1.00 54.79           C  
ANISOU  162  C   LEU A  66     9216   6610   4991   -234   2330    418       C  
ATOM    163  O   LEU A  66      23.652 -27.627   6.161  1.00 57.81           O  
ANISOU  163  O   LEU A  66     9627   6944   5394   -205   2584    357       O  
ATOM    164  CB  LEU A  66      25.451 -30.111   7.015  1.00 48.91           C  
ANISOU  164  CB  LEU A  66     8881   5935   3769   -282   2048    541       C  
ATOM    165  CG  LEU A  66      25.497 -31.500   7.656  1.00 45.87           C  
ANISOU  165  CG  LEU A  66     8625   5552   3253   -311   1982    721       C  
ATOM    166  CD1 LEU A  66      26.521 -31.540   8.779  1.00 46.95           C  
ANISOU  166  CD1 LEU A  66     9045   5757   3036   -313   1787    675       C  
ATOM    167  CD2 LEU A  66      24.121 -31.900   8.169  1.00 47.35           C  
ANISOU  167  CD2 LEU A  66     8770   5676   3546   -334   2316    850       C  
ATOM    168  N   VAL A  67      25.070 -28.070   4.470  1.00 55.08           N  
ANISOU  168  N   VAL A  67     9143   6679   5106   -227   2129    342       N  
ATOM    169  CA  VAL A  67      25.045 -26.684   4.019  1.00 56.97           C  
ANISOU  169  CA  VAL A  67     9276   6899   5471   -187   2204    187       C  
ATOM    170  C   VAL A  67      23.664 -26.319   3.494  1.00 60.61           C  
ANISOU  170  C   VAL A  67     9451   7288   6289   -159   2486    272       C  
ATOM    171  O   VAL A  67      23.187 -25.194   3.686  1.00 61.54           O  
ANISOU  171  O   VAL A  67     9524   7347   6511   -107   2673    183       O  
ATOM    172  CB  VAL A  67      26.132 -26.448   2.957  1.00 52.34           C  
ANISOU  172  CB  VAL A  67     8623   6366   4896   -190   1924     99       C  
ATOM    173  CG1 VAL A  67      25.987 -25.057   2.365  1.00 49.68           C  
ANISOU  173  CG1 VAL A  67     8138   5995   4743   -150   2020    -35       C  
ATOM    174  CG2 VAL A  67      27.508 -26.630   3.572  1.00 56.46           C  
ANISOU  174  CG2 VAL A  67     9382   6961   5111   -207   1619     11       C  
ATOM    175  N   CYS A  68      23.002 -27.261   2.821  1.00 62.49           N  
ANISOU  175  N   CYS A  68     9478   7521   6746   -198   2495    455       N  
ATOM    176  CA  CYS A  68      21.644 -27.016   2.354  1.00 62.40           C  
ANISOU  176  CA  CYS A  68     9146   7455   7107   -183   2704    566       C  
ATOM    177  C   CYS A  68      20.656 -27.025   3.510  1.00 71.90           C  
ANISOU  177  C   CYS A  68    10416   8604   8298   -156   2985    615       C  
ATOM    178  O   CYS A  68      19.732 -26.204   3.555  1.00 76.69           O  
ANISOU  178  O   CYS A  68    10865   9148   9127    -94   3204    615       O  
ATOM    179  CB  CYS A  68      21.253 -28.059   1.310  1.00 56.47           C  
ANISOU  179  CB  CYS A  68     8145   6714   6596   -266   2574    745       C  
ATOM    180  SG  CYS A  68      22.307 -28.078  -0.152  1.00 61.73           S  
ANISOU  180  SG  CYS A  68     8716   7424   7313   -301   2241    695       S  
ATOM    181  N   LEU A  69      20.829 -27.956   4.450  1.00 74.89           N  
ANISOU  181  N   LEU A  69    11030   8999   8428   -198   2985    668       N  
ATOM    182  CA  LEU A  69      19.927 -28.025   5.594  1.00 72.96           C  
ANISOU  182  CA  LEU A  69    10874   8704   8144   -180   3267    719       C  
ATOM    183  C   LEU A  69      20.039 -26.784   6.468  1.00 70.66           C  
ANISOU  183  C   LEU A  69    10790   8364   7693   -109   3436    542       C  
ATOM    184  O   LEU A  69      19.040 -26.332   7.041  1.00 78.98           O  
ANISOU  184  O   LEU A  69    11811   9339   8860    -61   3734    562       O  
ATOM    185  CB  LEU A  69      20.223 -29.282   6.413  1.00 77.68           C  
ANISOU  185  CB  LEU A  69    11702   9331   8481   -243   3202    816       C  
ATOM    186  CG  LEU A  69      19.833 -30.615   5.776  1.00 73.98           C  
ANISOU  186  CG  LEU A  69    11049   8865   8195   -326   3102   1017       C  
ATOM    187  CD1 LEU A  69      20.844 -31.696   6.123  1.00 67.21           C  
ANISOU  187  CD1 LEU A  69    10443   8041   7051   -373   2866   1060       C  
ATOM    188  CD2 LEU A  69      18.438 -31.030   6.215  1.00 81.72           C  
ANISOU  188  CD2 LEU A  69    11881   9796   9373   -349   3373   1168       C  
ATOM    189  N   ALA A  70      21.244 -26.220   6.588  1.00 66.23           N  
ANISOU  189  N   ALA A  70    10444   7839   6879   -110   3244    370       N  
ATOM    190  CA  ALA A  70      21.424 -25.053   7.446  1.00 71.50           C  
ANISOU  190  CA  ALA A  70    11335   8451   7381    -73   3372    193       C  
ATOM    191  C   ALA A  70      20.696 -23.836   6.892  1.00 76.18           C  
ANISOU  191  C   ALA A  70    11707   8945   8293      6   3567    143       C  
ATOM    192  O   ALA A  70      20.069 -23.082   7.646  1.00 75.83           O  
ANISOU  192  O   ALA A  70    11757   8798   8258     54   3840     91       O  
ATOM    193  CB  ALA A  70      22.913 -24.747   7.618  1.00 72.04           C  
ANISOU  193  CB  ALA A  70    11641   8590   7141   -113   3067     31       C  
ATOM    194  N   VAL A  71      20.755 -23.632   5.577  1.00 82.84           N  
ANISOU  194  N   VAL A  71    12261   9809   9406     22   3435    170       N  
ATOM    195  CA  VAL A  71      20.046 -22.501   4.995  1.00 82.41           C  
ANISOU  195  CA  VAL A  71    11973   9659   9681    103   3594    154       C  
ATOM    196  C   VAL A  71      18.547 -22.747   4.996  1.00 87.32           C  
ANISOU  196  C   VAL A  71    12344  10214  10618    150   3851    334       C  
ATOM    197  O   VAL A  71      17.753 -21.805   5.110  1.00 94.76           O  
ANISOU  197  O   VAL A  71    13194  11040  11773    235   4082    330       O  
ATOM    198  CB  VAL A  71      20.569 -22.220   3.579  1.00 71.55           C  
ANISOU  198  CB  VAL A  71    10361   8331   8492    102   3359    143       C  
ATOM    199  CG1 VAL A  71      19.768 -21.100   2.954  1.00 71.58           C  
ANISOU  199  CG1 VAL A  71    10105   8233   8860    190   3503    164       C  
ATOM    200  CG2 VAL A  71      22.042 -21.864   3.640  1.00 68.10           C  
ANISOU  200  CG2 VAL A  71    10167   7950   7757     61   3120    -46       C  
ATOM    201  N   TRP A  72      18.137 -24.010   4.862  1.00 88.82           N  
ANISOU  201  N   TRP A  72    12417  10470  10861     92   3806    503       N  
ATOM    202  CA  TRP A  72      16.718 -24.344   4.869  1.00 97.11           C  
ANISOU  202  CA  TRP A  72    13209  11470  12216    116   4017    685       C  
ATOM    203  C   TRP A  72      16.115 -24.171   6.255  1.00 97.47           C  
ANISOU  203  C   TRP A  72    13476  11428  12130    159   4349    668       C  
ATOM    204  O   TRP A  72      14.999 -23.659   6.394  1.00100.46           O  
ANISOU  204  O   TRP A  72    13689  11705  12774    237   4612    738       O  
ATOM    205  CB  TRP A  72      16.519 -25.775   4.379  1.00102.74           C  
ANISOU  205  CB  TRP A  72    13763  12273  13003     13   3855    861       C  
ATOM    206  CG  TRP A  72      15.089 -26.217   4.403  1.00109.73           C  
ANISOU  206  CG  TRP A  72    14378  13119  14194     11   4036   1053       C  
ATOM    207  CD1 TRP A  72      14.106 -25.859   3.528  1.00111.95           C  
ANISOU  207  CD1 TRP A  72    14273  13373  14891     44   4045   1170       C  
ATOM    208  CD2 TRP A  72      14.480 -27.102   5.351  1.00117.72           C  
ANISOU  208  CD2 TRP A  72    15483  14119  15126    -31   4219   1160       C  
ATOM    209  NE1 TRP A  72      12.922 -26.469   3.870  1.00120.75           N  
ANISOU  209  NE1 TRP A  72    15225  14460  16196     23   4218   1340       N  
ATOM    210  CE2 TRP A  72      13.125 -27.238   4.986  1.00122.42           C  
ANISOU  210  CE2 TRP A  72    15724  14678  16113    -24   4342   1335       C  
ATOM    211  CE3 TRP A  72      14.949 -27.795   6.472  1.00119.24           C  
ANISOU  211  CE3 TRP A  72    16024  14329  14954    -75   4277   1135       C  
ATOM    212  CZ2 TRP A  72      12.234 -28.038   5.703  1.00123.26           C  
ANISOU  212  CZ2 TRP A  72    15807  14761  16264    -65   4544   1477       C  
ATOM    213  CZ3 TRP A  72      14.063 -28.589   7.183  1.00120.62           C  
ANISOU  213  CZ3 TRP A  72    16186  14480  15164   -112   4480   1282       C  
ATOM    214  CH2 TRP A  72      12.722 -28.704   6.795  1.00123.20           C  
ANISOU  214  CH2 TRP A  72    16151  14768  15893   -109   4621   1447       C  
ATOM    215  N   ARG A  73      16.839 -24.588   7.293  1.00 94.71           N  
ANISOU  215  N   ARG A  73    13504  11112  11371    109   4337    583       N  
ATOM    216  CA  ARG A  73      16.301 -24.506   8.646  1.00 95.44           C  
ANISOU  216  CA  ARG A  73    13837  11128  11300    134   4648    571       C  
ATOM    217  C   ARG A  73      16.273 -23.064   9.156  1.00 98.65           C  
ANISOU  217  C   ARG A  73    14404  11406  11671    215   4853    402       C  
ATOM    218  O   ARG A  73      15.307 -22.649   9.804  1.00106.64           O  
ANISOU  218  O   ARG A  73    15428  12299  12791    282   5197    432       O  
ATOM    219  CB  ARG A  73      17.117 -25.410   9.574  1.00 93.87           C  
ANISOU  219  CB  ARG A  73    13995  11011  10662     47   4531    548       C  
ATOM    220  CG  ARG A  73      16.615 -25.495  11.010  1.00 98.47           C  
ANISOU  220  CG  ARG A  73    14856  11532  11028     53   4834    552       C  
ATOM    221  CD  ARG A  73      17.094 -26.777  11.680  1.00 98.74           C  
ANISOU  221  CD  ARG A  73    15112  11660  10744    -39   4704    637       C  
ATOM    222  NE  ARG A  73      17.000 -26.711  13.136  1.00101.20           N  
ANISOU  222  NE  ARG A  73    15790  11931  10728    -46   4925    591       N  
ATOM    223  CZ  ARG A  73      18.018 -26.408  13.934  1.00100.37           C  
ANISOU  223  CZ  ARG A  73    16066  11861  10210    -85   4790    442       C  
ATOM    224  NH1 ARG A  73      19.211 -26.146  13.417  1.00 95.52           N  
ANISOU  224  NH1 ARG A  73    15495  11320   9479   -115   4437    326       N  
ATOM    225  NH2 ARG A  73      17.848 -26.370  15.248  1.00106.73           N  
ANISOU  225  NH2 ARG A  73    17203  12629  10719   -100   5001    413       N  
ATOM    226  N   ASN A  74      17.324 -22.291   8.895  1.00 95.25           N  
ANISOU  226  N   ASN A  74    14108  10989  11093    205   4656    225       N  
ATOM    227  CA  ASN A  74      17.419 -20.914   9.370  1.00 95.40           C  
ANISOU  227  CA  ASN A  74    14308  10880  11059    256   4820     53       C  
ATOM    228  C   ASN A  74      16.873 -19.969   8.305  1.00101.35           C  
ANISOU  228  C   ASN A  74    14725  11543  12238    347   4871     83       C  
ATOM    229  O   ASN A  74      17.431 -19.890   7.210  1.00101.53           O  
ANISOU  229  O   ASN A  74    14563  11637  12377    332   4602     78       O  
ATOM    230  CB  ASN A  74      18.867 -20.607   9.753  1.00 89.86           C  
ANISOU  230  CB  ASN A  74    13941  10242   9959    175   4560   -147       C  
ATOM    231  CG  ASN A  74      18.988 -19.388  10.611  1.00 90.01           C  
ANISOU  231  CG  ASN A  74    14246  10132   9821    189   4743   -328       C  
ATOM    232  OD1 ASN A  74      18.335 -18.379  10.352  1.00 94.36           O  
ANISOU  232  OD1 ASN A  74    14672  10539  10640    272   4963   -346       O  
ATOM    233  ND2 ASN A  74      19.821 -19.461  11.645  1.00 89.19           N  
ANISOU  233  ND2 ASN A  74    14530  10072   9285    102   4647   -455       N  
ATOM    234  N   HIS A  75      15.763 -19.282   8.609  1.00107.98           N  
ANISOU  234  N   HIS A  75    15482  12225  13320    444   5218    132       N  
ATOM    235  CA  HIS A  75      15.164 -18.416   7.596  1.00106.95           C  
ANISOU  235  CA  HIS A  75    15013  12003  13620    539   5258    200       C  
ATOM    236  C   HIS A  75      15.980 -17.155   7.335  1.00106.48           C  
ANISOU  236  C   HIS A  75    15078  11876  13503    546   5168     17       C  
ATOM    237  O   HIS A  75      16.299 -16.847   6.179  1.00109.79           O  
ANISOU  237  O   HIS A  75    15263  12334  14117    554   4946     38       O  
ATOM    238  CB  HIS A  75      13.752 -18.047   8.025  1.00113.37           C  
ANISOU  238  CB  HIS A  75    15700  12654  14721    648   5657    322       C  
ATOM    239  CG  HIS A  75      12.739 -19.113   7.776  1.00120.24           C  
ANISOU  239  CG  HIS A  75    16266  13583  15837    656   5704    556       C  
ATOM    240  ND1 HIS A  75      12.735 -20.317   8.448  1.00123.41           N  
ANISOU  240  ND1 HIS A  75    16795  14082  16012    578   5715    607       N  
ATOM    241  CD2 HIS A  75      11.615 -19.098   7.024  1.00122.28           C  
ANISOU  241  CD2 HIS A  75    16107  13801  16555    730   5768    763       C  
ATOM    242  CE1 HIS A  75      11.702 -21.037   8.050  1.00124.12           C  
ANISOU  242  CE1 HIS A  75    16546  14198  16416    590   5766    827       C  
ATOM    243  NE2 HIS A  75      11.011 -20.322   7.179  1.00123.80           N  
ANISOU  243  NE2 HIS A  75    16166  14081  16793    680   5785    924       N  
ATOM    244  N   HIS A  76      16.355 -16.416   8.375  1.00106.64           N  
ANISOU  244  N   HIS A  76    15469  11798  13250    531   5326   -163       N  
ATOM    245  CA  HIS A  76      17.216 -15.255   8.130  1.00108.81           C  
ANISOU  245  CA  HIS A  76    15868  12018  13457    512   5211   -343       C  
ATOM    246  C   HIS A  76      18.687 -15.682   8.050  1.00 97.23           C  
ANISOU  246  C   HIS A  76    14583  10722  11637    387   4824   -478       C  
ATOM    247  O   HIS A  76      19.583 -15.089   8.648  1.00 94.62           O  
ANISOU  247  O   HIS A  76    14561  10378  11012    318   4748   -670       O  
ATOM    248  CB  HIS A  76      16.941 -14.133   9.140  1.00120.86           C  
ANISOU  248  CB  HIS A  76    17681  13345  14896    546   5543   -475       C  
ATOM    249  CG  HIS A  76      17.060 -14.512  10.586  1.00125.71           C  
ANISOU  249  CG  HIS A  76    18700  13957  15109    484   5693   -570       C  
ATOM    250  ND1 HIS A  76      18.266 -14.555  11.254  1.00127.04           N  
ANISOU  250  ND1 HIS A  76    19230  14212  14826    359   5477   -755       N  
ATOM    251  CD2 HIS A  76      16.110 -14.788  11.514  1.00130.96           C  
ANISOU  251  CD2 HIS A  76    19471  14532  15757    531   6047   -503       C  
ATOM    252  CE1 HIS A  76      18.063 -14.903  12.515  1.00131.36           C  
ANISOU  252  CE1 HIS A  76    20095  14736  15081    325   5669   -791       C  
ATOM    253  NE2 HIS A  76      16.761 -15.049  12.701  1.00134.61           N  
ANISOU  253  NE2 HIS A  76    20366  15038  15742    430   6032   -644       N  
ATOM    254  N   MET A  77      18.868 -16.844   7.376  1.00 91.46           N  
ANISOU  254  N   MET A  77    13658  10156  10937    354   4586   -357       N  
ATOM    255  CA  MET A  77      20.117 -17.208   6.721  1.00 77.88           C  
ANISOU  255  CA  MET A  77    11940   8589   9062    272   4197   -424       C  
ATOM    256  C   MET A  77      19.976 -17.252   5.197  1.00 66.93           C  
ANISOU  256  C   MET A  77    10156   7247   8029    312   4039   -308       C  
ATOM    257  O   MET A  77      20.977 -17.484   4.507  1.00 65.57           O  
ANISOU  257  O   MET A  77     9955   7188   7770    256   3737   -358       O  
ATOM    258  CB  MET A  77      20.615 -18.566   7.260  1.00 73.70           C  
ANISOU  258  CB  MET A  77    11572   8210   8219    188   4034   -389       C  
ATOM    259  CG  MET A  77      22.112 -18.716   7.282  1.00 69.35           C  
ANISOU  259  CG  MET A  77    11217   7782   7350     91   3679   -525       C  
ATOM    260  SD  MET A  77      22.529 -20.333   7.932  1.00 72.25           S  
ANISOU  260  SD  MET A  77    11754   8300   7398     13   3513   -434       S  
ATOM    261  CE  MET A  77      22.352 -20.046   9.692  1.00 82.34           C  
ANISOU  261  CE  MET A  77    13446   9504   8335    -17   3739   -525       C  
ATOM    262  N   ARG A  78      18.770 -17.033   4.655  1.00 68.90           N  
ANISOU  262  N   ARG A  78    10097   7410   8671    406   4224   -146       N  
ATOM    263  CA  ARG A  78      18.506 -17.105   3.214  1.00 70.25           C  
ANISOU  263  CA  ARG A  78     9878   7626   9188    438   4061     -7       C  
ATOM    264  C   ARG A  78      18.848 -15.778   2.532  1.00 69.78           C  
ANISOU  264  C   ARG A  78     9751   7479   9284    479   4016    -86       C  
ATOM    265  O   ARG A  78      18.003 -15.043   2.016  1.00 58.66           O  
ANISOU  265  O   ARG A  78     8112   5957   8219    568   4142     22       O  
ATOM    266  CB  ARG A  78      17.056 -17.505   2.969  1.00 67.97           C  
ANISOU  266  CB  ARG A  78     9279   7297   9248    507   4231    223       C  
ATOM    267  CG  ARG A  78      16.615 -18.819   3.660  1.00 64.14           C  
ANISOU  267  CG  ARG A  78     8843   6887   8639    460   4301    319       C  
ATOM    268  CD  ARG A  78      15.100 -19.066   3.454  1.00 73.70           C  
ANISOU  268  CD  ARG A  78     9728   8041  10233    527   4484    546       C  
ATOM    269  NE  ARG A  78      14.724 -20.465   3.283  1.00 86.91           N  
ANISOU  269  NE  ARG A  78    11251   9836  11934    452   4384    701       N  
ATOM    270  CZ  ARG A  78      14.237 -21.261   4.230  1.00100.97           C  
ANISOU  270  CZ  ARG A  78    13142  11619  13601    426   4563    759       C  
ATOM    271  NH1 ARG A  78      14.088 -20.845   5.484  1.00103.38           N  
ANISOU  271  NH1 ARG A  78    13737  11821  13722    469   4859    666       N  
ATOM    272  NH2 ARG A  78      13.924 -22.502   3.920  1.00109.45           N  
ANISOU  272  NH2 ARG A  78    14054  12799  14734    343   4441    909       N  
ATOM    273  N   THR A  79      20.131 -15.470   2.579  1.00 68.74           N  
ANISOU  273  N   THR A  79     9833   7398   8887    408   3825   -272       N  
ATOM    274  CA  THR A  79      20.706 -14.320   1.913  1.00 66.23           C  
ANISOU  274  CA  THR A  79     9478   7021   8667    418   3732   -365       C  
ATOM    275  C   THR A  79      21.068 -14.677   0.481  1.00 68.18           C  
ANISOU  275  C   THR A  79     9440   7381   9086    408   3459   -277       C  
ATOM    276  O   THR A  79      21.153 -15.850   0.105  1.00 68.96           O  
ANISOU  276  O   THR A  79     9439   7618   9146    368   3308   -191       O  
ATOM    277  CB  THR A  79      21.941 -13.841   2.667  1.00 64.50           C  
ANISOU  277  CB  THR A  79     9614   6809   8082    331   3633   -604       C  
ATOM    278  OG1 THR A  79      23.001 -14.781   2.477  1.00 61.23           O  
ANISOU  278  OG1 THR A  79     9266   6573   7426    243   3328   -653       O  
ATOM    279  CG2 THR A  79      21.623 -13.745   4.148  1.00 65.67           C  
ANISOU  279  CG2 THR A  79    10075   6876   7999    319   3873   -684       C  
ATOM    280  N   VAL A  80      21.271 -13.641  -0.329  1.00 68.71           N  
ANISOU  280  N   VAL A  80     9384   7379   9343    439   3406   -293       N  
ATOM    281  CA  VAL A  80      21.693 -13.867  -1.706  1.00 62.84           C  
ANISOU  281  CA  VAL A  80     8395   6736   8746    426   3146   -220       C  
ATOM    282  C   VAL A  80      22.981 -14.682  -1.746  1.00 59.54           C  
ANISOU  282  C   VAL A  80     8125   6475   8022    329   2896   -347       C  
ATOM    283  O   VAL A  80      23.090 -15.669  -2.484  1.00 64.29           O  
ANISOU  283  O   VAL A  80     8568   7203   8655    301   2731   -251       O  
ATOM    284  CB  VAL A  80      21.860 -12.528  -2.440  1.00 60.15           C  
ANISOU  284  CB  VAL A  80     7958   6287   8611    465   3132   -237       C  
ATOM    285  CG1 VAL A  80      22.746 -12.720  -3.651  1.00 56.43           C  
ANISOU  285  CG1 VAL A  80     7350   5929   8163    422   2841   -239       C  
ATOM    286  CG2 VAL A  80      20.503 -11.990  -2.841  1.00 62.36           C  
ANISOU  286  CG2 VAL A  80     7983   6443   9266    568   3301    -29       C  
ATOM    287  N   THR A  81      23.981 -14.272  -0.962  1.00 52.78           N  
ANISOU  287  N   THR A  81     7575   5610   6871    268   2849   -556       N  
ATOM    288  CA  THR A  81      25.235 -15.015  -0.912  1.00 44.71           C  
ANISOU  288  CA  THR A  81     6704   4729   5554    177   2586   -669       C  
ATOM    289  C   THR A  81      25.007 -16.475  -0.551  1.00 48.25           C  
ANISOU  289  C   THR A  81     7186   5290   5856    151   2563   -577       C  
ATOM    290  O   THR A  81      25.495 -17.380  -1.235  1.00 54.19           O  
ANISOU  290  O   THR A  81     7856   6161   6573    117   2372   -535       O  
ATOM    291  CB  THR A  81      26.191 -14.369   0.089  1.00 45.35           C  
ANISOU  291  CB  THR A  81     7105   4783   5342    105   2523   -878       C  
ATOM    292  OG1 THR A  81      26.530 -13.055  -0.365  1.00 38.34           O  
ANISOU  292  OG1 THR A  81     6178   3795   4595    111   2518   -962       O  
ATOM    293  CG2 THR A  81      27.457 -15.200   0.220  1.00 46.94           C  
ANISOU  293  CG2 THR A  81     7445   5138   5253     12   2215   -962       C  
ATOM    294  N   ASN A  82      24.267 -16.723   0.532  1.00 57.93           N  
ANISOU  294  N   ASN A  82     8546   6471   6995    164   2770   -541       N  
ATOM    295  CA  ASN A  82      24.057 -18.092   0.987  1.00 58.50           C  
ANISOU  295  CA  ASN A  82     8676   6636   6913    131   2758   -446       C  
ATOM    296  C   ASN A  82      23.190 -18.906   0.036  1.00 54.65           C  
ANISOU  296  C   ASN A  82     7864   6193   6709    157   2775   -231       C  
ATOM    297  O   ASN A  82      23.302 -20.137   0.022  1.00 56.36           O  
ANISOU  297  O   ASN A  82     8092   6507   6817    105   2681   -148       O  
ATOM    298  CB  ASN A  82      23.454 -18.090   2.392  1.00 65.00           C  
ANISOU  298  CB  ASN A  82     9725   7390   7584    137   2991   -458       C  
ATOM    299  CG  ASN A  82      24.492 -17.825   3.466  1.00 73.61           C  
ANISOU  299  CG  ASN A  82    11177   8499   8292     64   2882   -642       C  
ATOM    300  OD1 ASN A  82      25.665 -18.163   3.308  1.00 73.58           O  
ANISOU  300  OD1 ASN A  82    11261   8603   8093     -3   2589   -717       O  
ATOM    301  ND2 ASN A  82      24.066 -17.211   4.563  1.00 82.13           N  
ANISOU  301  ND2 ASN A  82    12460   9472   9272     74   3106   -707       N  
ATOM    302  N   TYR A  83      22.326 -18.268  -0.757  1.00 53.98           N  
ANISOU  302  N   TYR A  83     7485   6035   6988    225   2866   -122       N  
ATOM    303  CA  TYR A  83      21.634 -19.031  -1.791  1.00 53.32           C  
ANISOU  303  CA  TYR A  83     7069   6016   7173    218   2785     87       C  
ATOM    304  C   TYR A  83      22.603 -19.477  -2.876  1.00 53.30           C  
ANISOU  304  C   TYR A  83     6987   6127   7136    155   2513     72       C  
ATOM    305  O   TYR A  83      22.498 -20.598  -3.387  1.00 50.74           O  
ANISOU  305  O   TYR A  83     6544   5891   6843     87   2393    201       O  
ATOM    306  CB  TYR A  83      20.495 -18.223  -2.412  1.00 59.92           C  
ANISOU  306  CB  TYR A  83     7608   6757   8402    301   2880    227       C  
ATOM    307  CG  TYR A  83      19.188 -18.268  -1.651  1.00 67.42           C  
ANISOU  307  CG  TYR A  83     8511   7618   9488    357   3135    340       C  
ATOM    308  CD1 TYR A  83      18.965 -19.214  -0.658  1.00 64.19           C  
ANISOU  308  CD1 TYR A  83     8260   7240   8891    318   3247    352       C  
ATOM    309  CD2 TYR A  83      18.159 -17.386  -1.960  1.00 76.66           C  
ANISOU  309  CD2 TYR A  83     9470   8669  10987    450   3264    452       C  
ATOM    310  CE1 TYR A  83      17.765 -19.258   0.027  1.00 70.14           C  
ANISOU  310  CE1 TYR A  83     8961   7909   9781    370   3499    458       C  
ATOM    311  CE2 TYR A  83      16.958 -17.425  -1.285  1.00 81.36           C  
ANISOU  311  CE2 TYR A  83    10008   9175  11728    509   3513    562       C  
ATOM    312  CZ  TYR A  83      16.766 -18.362  -0.293  1.00 79.99           C  
ANISOU  312  CZ  TYR A  83     9989   9037  11366    468   3637    559       C  
ATOM    313  OH  TYR A  83      15.569 -18.401   0.381  1.00 90.42           O  
ANISOU  313  OH  TYR A  83    11247  10266  12841    528   3905    671       O  
ATOM    314  N   PHE A  84      23.550 -18.610  -3.245  1.00 59.09           N  
ANISOU  314  N   PHE A  84     7788   6848   7815    167   2415    -82       N  
ATOM    315  CA  PHE A  84      24.576 -19.004  -4.205  1.00 54.71           C  
ANISOU  315  CA  PHE A  84     7188   6396   7204    103   2059   -112       C  
ATOM    316  C   PHE A  84      25.481 -20.084  -3.628  1.00 51.82           C  
ANISOU  316  C   PHE A  84     7059   6122   6508     31   1865   -181       C  
ATOM    317  O   PHE A  84      25.937 -20.973  -4.357  1.00 60.74           O  
ANISOU  317  O   PHE A  84     8113   7337   7628    -23   1591   -125       O  
ATOM    318  CB  PHE A  84      25.402 -17.789  -4.629  1.00 51.51           C  
ANISOU  318  CB  PHE A  84     6809   5945   6817    125   1980   -259       C  
ATOM    319  CG  PHE A  84      24.746 -16.938  -5.682  1.00 45.60           C  
ANISOU  319  CG  PHE A  84     5771   5135   6420    184   2027   -142       C  
ATOM    320  CD1 PHE A  84      24.307 -17.496  -6.874  1.00 45.10           C  
ANISOU  320  CD1 PHE A  84     5434   5146   6555    154   1840     47       C  
ATOM    321  CD2 PHE A  84      24.576 -15.579  -5.484  1.00 44.00           C  
ANISOU  321  CD2 PHE A  84     5590   4793   6336    258   2217   -210       C  
ATOM    322  CE1 PHE A  84      23.710 -16.710  -7.844  1.00 39.65           C  
ANISOU  322  CE1 PHE A  84     4484   4410   6172    202   1852    179       C  
ATOM    323  CE2 PHE A  84      23.978 -14.789  -6.449  1.00 40.41           C  
ANISOU  323  CE2 PHE A  84     4883   4276   6195    310   2201    -70       C  
ATOM    324  CZ  PHE A  84      23.545 -15.356  -7.630  1.00 40.01           C  
ANISOU  324  CZ  PHE A  84     4549   4316   6337    290   2028    128       C  
ATOM    325  N   LEU A  85      25.760 -20.018  -2.324  1.00 50.12           N  
ANISOU  325  N   LEU A  85     7145   5882   6017     29   2005   -300       N  
ATOM    326  CA  LEU A  85      26.587 -21.044  -1.700  1.00 53.44           C  
ANISOU  326  CA  LEU A  85     7790   6388   6126    -31   1815   -334       C  
ATOM    327  C   LEU A  85      25.880 -22.391  -1.687  1.00 62.27           C  
ANISOU  327  C   LEU A  85     8837   7541   7281    -59   1827   -147       C  
ATOM    328  O   LEU A  85      26.538 -23.437  -1.753  1.00 67.33           O  
ANISOU  328  O   LEU A  85     9545   8251   7787   -103   1589   -116       O  
ATOM    329  CB  LEU A  85      26.970 -20.621  -0.279  1.00 49.32           C  
ANISOU  329  CB  LEU A  85     7630   5833   5276    -41   1956   -490       C  
ATOM    330  CG  LEU A  85      27.925 -19.428  -0.174  1.00 45.49           C  
ANISOU  330  CG  LEU A  85     7244   5319   4720    -58   1832   -685       C  
ATOM    331  CD1 LEU A  85      28.196 -19.062   1.278  1.00 45.74           C  
ANISOU  331  CD1 LEU A  85     7558   5327   4493    -94   1851   -783       C  
ATOM    332  CD2 LEU A  85      29.227 -19.720  -0.908  1.00 46.30           C  
ANISOU  332  CD2 LEU A  85     7306   5517   4768   -104   1473   -739       C  
ATOM    333  N   VAL A  86      24.550 -22.390  -1.606  1.00 58.95           N  
ANISOU  333  N   VAL A  86     8271   7062   7065    -33   2107    -11       N  
ATOM    334  CA  VAL A  86      23.817 -23.647  -1.695  1.00 51.86           C  
ANISOU  334  CA  VAL A  86     7268   6186   6249    -83   2112    181       C  
ATOM    335  C   VAL A  86      23.883 -24.198  -3.112  1.00 57.07           C  
ANISOU  335  C   VAL A  86     7670   6892   7120   -133   1820    273       C  
ATOM    336  O   VAL A  86      24.012 -25.410  -3.318  1.00 68.01           O  
ANISOU  336  O   VAL A  86     9070   8311   8461   -200   1654    353       O  
ATOM    337  CB  VAL A  86      22.366 -23.454  -1.225  1.00 46.30           C  
ANISOU  337  CB  VAL A  86     6442   5407   5745    -48   2484    312       C  
ATOM    338  CG1 VAL A  86      21.514 -24.635  -1.661  1.00 43.11           C  
ANISOU  338  CG1 VAL A  86     5828   5020   5532   -123   2444    531       C  
ATOM    339  CG2 VAL A  86      22.327 -23.288   0.285  1.00 48.47           C  
ANISOU  339  CG2 VAL A  86     7018   5638   5762    -16   2657    221       C  
ATOM    340  N   ASN A  87      23.798 -23.318  -4.111  1.00 56.25           N  
ANISOU  340  N   ASN A  87     7351   6782   7238   -106   1760    262       N  
ATOM    341  CA  ASN A  87      23.966 -23.759  -5.490  1.00 54.23           C  
ANISOU  341  CA  ASN A  87     6901   6575   7128   -163   1473    327       C  
ATOM    342  C   ASN A  87      25.368 -24.309  -5.715  1.00 56.86           C  
ANISOU  342  C   ASN A  87     7405   6966   7233   -187   1189    208       C  
ATOM    343  O   ASN A  87      25.557 -25.253  -6.490  1.00 60.50           O  
ANISOU  343  O   ASN A  87     7815   7455   7716   -248    981    263       O  
ATOM    344  CB  ASN A  87      23.676 -22.605  -6.446  1.00 46.89           C  
ANISOU  344  CB  ASN A  87     5744   5628   6445   -123   1469    345       C  
ATOM    345  CG  ASN A  87      23.831 -22.999  -7.897  1.00 41.83           C  
ANISOU  345  CG  ASN A  87     4936   5041   5917   -193   1176    412       C  
ATOM    346  OD1 ASN A  87      23.184 -23.932  -8.373  1.00 40.55           O  
ANISOU  346  OD1 ASN A  87     4658   4896   5855   -279   1088    550       O  
ATOM    347  ND2 ASN A  87      24.698 -22.292  -8.611  1.00 41.80           N  
ANISOU  347  ND2 ASN A  87     4937   5058   5888   -169   1030    313       N  
ATOM    348  N   LEU A  88      26.366 -23.728  -5.045  1.00 49.57           N  
ANISOU  348  N   LEU A  88     6685   6052   6099   -143   1180     45       N  
ATOM    349  CA  LEU A  88      27.717 -24.271  -5.123  1.00 47.02           C  
ANISOU  349  CA  LEU A  88     6500   5786   5581   -156    923    -46       C  
ATOM    350  C   LEU A  88      27.794 -25.660  -4.502  1.00 55.15           C  
ANISOU  350  C   LEU A  88     7677   6825   6454   -186    873     27       C  
ATOM    351  O   LEU A  88      28.561 -26.509  -4.974  1.00 60.95           O  
ANISOU  351  O   LEU A  88     8433   7586   7141   -199    654     31       O  
ATOM    352  CB  LEU A  88      28.698 -23.316  -4.441  1.00 47.67           C  
ANISOU  352  CB  LEU A  88     6751   5875   5485   -124    915   -220       C  
ATOM    353  CG  LEU A  88      30.169 -23.718  -4.332  1.00 43.57           C  
ANISOU  353  CG  LEU A  88     6358   5420   4776   -131    656   -307       C  
ATOM    354  CD1 LEU A  88      30.757 -23.999  -5.705  1.00 32.31           C  
ANISOU  354  CD1 LEU A  88     4758   4026   3491   -134    447   -291       C  
ATOM    355  CD2 LEU A  88      30.956 -22.627  -3.623  1.00 37.85           C  
ANISOU  355  CD2 LEU A  88     5781   4697   3905   -131    655   -472       C  
ATOM    356  N   SER A  89      27.014 -25.910  -3.446  1.00 58.83           N  
ANISOU  356  N   SER A  89     8251   7258   6846   -190   1093     93       N  
ATOM    357  CA  SER A  89      26.965 -27.247  -2.863  1.00 57.15           C  
ANISOU  357  CA  SER A  89     8174   7038   6503   -224   1067    195       C  
ATOM    358  C   SER A  89      26.258 -28.231  -3.783  1.00 61.28           C  
ANISOU  358  C   SER A  89     8515   7529   7238   -290   1004    339       C  
ATOM    359  O   SER A  89      26.628 -29.410  -3.839  1.00 57.69           O  
ANISOU  359  O   SER A  89     8144   7059   6717   -320    863    393       O  
ATOM    360  CB  SER A  89      26.273 -27.199  -1.501  1.00 52.08           C  
ANISOU  360  CB  SER A  89     7707   6364   5717   -220   1352    236       C  
ATOM    361  OG  SER A  89      27.149 -26.711  -0.501  1.00 49.74           O  
ANISOU  361  OG  SER A  89     7679   6098   5122   -191   1336    104       O  
ATOM    362  N   LEU A  90      25.234 -27.770  -4.507  1.00 62.36           N  
ANISOU  362  N   LEU A  90     8407   7648   7638   -319   1098    410       N  
ATOM    363  CA  LEU A  90      24.536 -28.655  -5.434  1.00 54.60           C  
ANISOU  363  CA  LEU A  90     7251   6638   6855   -414   1002    542       C  
ATOM    364  C   LEU A  90      25.454 -29.110  -6.555  1.00 50.84           C  
ANISOU  364  C   LEU A  90     6774   6180   6362   -436    709    476       C  
ATOM    365  O   LEU A  90      25.318 -30.233  -7.051  1.00 50.85           O  
ANISOU  365  O   LEU A  90     6778   6140   6403   -516    592    543       O  
ATOM    366  CB  LEU A  90      23.304 -27.961  -6.013  1.00 55.44           C  
ANISOU  366  CB  LEU A  90     7073   6737   7257   -442   1124    646       C  
ATOM    367  CG  LEU A  90      21.990 -28.120  -5.248  1.00 67.71           C  
ANISOU  367  CG  LEU A  90     8536   8246   8945   -469   1409    802       C  
ATOM    368  CD1 LEU A  90      22.142 -27.659  -3.807  1.00 67.30           C  
ANISOU  368  CD1 LEU A  90     8706   8179   8688   -378   1677    735       C  
ATOM    369  CD2 LEU A  90      20.877 -27.355  -5.950  1.00 79.53           C  
ANISOU  369  CD2 LEU A  90     9701   9740  10778   -480   1491    919       C  
ATOM    370  N   ALA A  91      26.390 -28.256  -6.970  1.00 56.82           N  
ANISOU  370  N   ALA A  91     7536   6985   7067   -370    608    342       N  
ATOM    371  CA  ALA A  91      27.388 -28.681  -7.942  1.00 63.21           C  
ANISOU  371  CA  ALA A  91     8368   7809   7841   -374    371    271       C  
ATOM    372  C   ALA A  91      28.353 -29.687  -7.328  1.00 67.38           C  
ANISOU  372  C   ALA A  91     9105   8319   8179   -338    282    242       C  
ATOM    373  O   ALA A  91      28.661 -30.718  -7.937  1.00 73.20           O  
ANISOU  373  O   ALA A  91     9879   9010   8925   -368    152    261       O  
ATOM    374  CB  ALA A  91      28.142 -27.471  -8.492  1.00 68.33           C  
ANISOU  374  CB  ALA A  91     8955   8509   8498   -315    313    152       C  
ATOM    375  N   ASP A  92      28.854 -29.397  -6.124  1.00 66.78           N  
ANISOU  375  N   ASP A  92     9179   8269   7926   -274    345    199       N  
ATOM    376  CA  ASP A  92      29.835 -30.283  -5.503  1.00 69.48           C  
ANISOU  376  CA  ASP A  92     9705   8602   8090   -230    231    197       C  
ATOM    377  C   ASP A  92      29.264 -31.675  -5.255  1.00 69.67           C  
ANISOU  377  C   ASP A  92     9809   8542   8119   -279    257    333       C  
ATOM    378  O   ASP A  92      29.973 -32.675  -5.408  1.00 77.99           O  
ANISOU  378  O   ASP A  92    10951   9549   9133   -252    123    354       O  
ATOM    379  CB  ASP A  92      30.330 -29.671  -4.193  1.00 83.52           C  
ANISOU  379  CB  ASP A  92    11646  10432   9656   -181    281    142       C  
ATOM    380  CG  ASP A  92      31.018 -28.343  -4.396  1.00 94.45           C  
ANISOU  380  CG  ASP A  92    12974  11878  11034   -148    236     -4       C  
ATOM    381  OD1 ASP A  92      31.530 -28.106  -5.510  1.00 97.32           O  
ANISOU  381  OD1 ASP A  92    13197  12256  11523   -138    118    -56       O  
ATOM    382  OD2 ASP A  92      31.039 -27.536  -3.442  1.00 95.69           O  
ANISOU  382  OD2 ASP A  92    13244  12061  11055   -142    331    -68       O  
ATOM    383  N   VAL A  93      27.989 -31.767  -4.871  1.00 58.78           N  
ANISOU  383  N   VAL A  93     8394   7130   6810   -348    441    437       N  
ATOM    384  CA  VAL A  93      27.413 -33.092  -4.645  1.00 57.66           C  
ANISOU  384  CA  VAL A  93     8321   6895   6693   -416    472    578       C  
ATOM    385  C   VAL A  93      27.237 -33.847  -5.954  1.00 59.72           C  
ANISOU  385  C   VAL A  93     8479   7085   7126   -496    336    594       C  
ATOM    386  O   VAL A  93      27.343 -35.080  -5.987  1.00 56.58           O  
ANISOU  386  O   VAL A  93     8190   6587   6723   -530    275    658       O  
ATOM    387  CB  VAL A  93      26.078 -32.989  -3.884  1.00 60.28           C  
ANISOU  387  CB  VAL A  93     8619   7208   7078   -479    729    698       C  
ATOM    388  CG1 VAL A  93      26.337 -32.794  -2.398  1.00 62.65           C  
ANISOU  388  CG1 VAL A  93     9140   7537   7126   -415    867    705       C  
ATOM    389  CG2 VAL A  93      25.236 -31.858  -4.444  1.00 73.09           C  
ANISOU  389  CG2 VAL A  93    10003   8873   8896   -502    836    680       C  
ATOM    390  N   LEU A  94      26.957 -33.136  -7.048  1.00 55.77           N  
ANISOU  390  N   LEU A  94     7794   6624   6772   -534    285    539       N  
ATOM    391  CA  LEU A  94      26.853 -33.807  -8.337  1.00 51.93           C  
ANISOU  391  CA  LEU A  94     7253   6075   6401   -625    137    534       C  
ATOM    392  C   LEU A  94      28.192 -34.393  -8.756  1.00 45.17           C  
ANISOU  392  C   LEU A  94     6538   5181   5442   -546    -13    436       C  
ATOM    393  O   LEU A  94      28.247 -35.487  -9.329  1.00 61.44           O  
ANISOU  393  O   LEU A  94     8680   7129   7534   -603    -92    448       O  
ATOM    394  CB  LEU A  94      26.342 -32.835  -9.398  1.00 62.38           C  
ANISOU  394  CB  LEU A  94     8367   7464   7869   -677     99    508       C  
ATOM    395  CG  LEU A  94      26.585 -33.251 -10.851  1.00 62.48           C  
ANISOU  395  CG  LEU A  94     8371   7443   7926   -753    -86    454       C  
ATOM    396  CD1 LEU A  94      25.492 -34.187 -11.348  1.00 69.37           C  
ANISOU  396  CD1 LEU A  94     9204   8228   8925   -937   -133    560       C  
ATOM    397  CD2 LEU A  94      26.701 -32.026 -11.748  1.00 57.69           C  
ANISOU  397  CD2 LEU A  94     7620   6931   7370   -734   -140    393       C  
ATOM    398  N   ALA A  95      29.283 -33.673  -8.487  1.00 34.77           N  
ANISOU  398  N   ALA A  95     5248   3943   4018   -417    -47    339       N  
ATOM    399  CA  ALA A  95      30.609 -34.190  -8.806  1.00 41.76           C  
ANISOU  399  CA  ALA A  95     6231   4798   4839   -322   -170    267       C  
ATOM    400  C   ALA A  95      30.996 -35.324  -7.866  1.00 55.12           C  
ANISOU  400  C   ALA A  95     8098   6404   6442   -268   -175    350       C  
ATOM    401  O   ALA A  95      31.479 -36.374  -8.307  1.00 67.76           O  
ANISOU  401  O   ALA A  95     9788   7890   8068   -244   -241    355       O  
ATOM    402  CB  ALA A  95      31.641 -33.064  -8.743  1.00 44.20           C  
ANISOU  402  CB  ALA A  95     6485   5221   5089   -217   -213    160       C  
ATOM    403  N   THR A  96      30.796 -35.126  -6.562  1.00 54.37           N  
ANISOU  403  N   THR A  96     8072   6353   6233   -245    -96    419       N  
ATOM    404  CA  THR A  96      31.203 -36.131  -5.587  1.00 51.68           C  
ANISOU  404  CA  THR A  96     7912   5944   5781   -189   -113    522       C  
ATOM    405  C   THR A  96      30.437 -37.433  -5.777  1.00 56.11           C  
ANISOU  405  C   THR A  96     8544   6344   6431   -279    -68    633       C  
ATOM    406  O   THR A  96      31.032 -38.515  -5.825  1.00 67.62           O  
ANISOU  406  O   THR A  96    10120   7679   7893   -226   -137    677       O  
ATOM    407  CB  THR A  96      31.001 -35.594  -4.172  1.00 54.43           C  
ANISOU  407  CB  THR A  96     8350   6376   5954   -173    -21    575       C  
ATOM    408  OG1 THR A  96      31.833 -34.443  -3.983  1.00 50.39           O  
ANISOU  408  OG1 THR A  96     7800   5994   5352   -103    -89    458       O  
ATOM    409  CG2 THR A  96      31.365 -36.653  -3.147  1.00 59.37           C  
ANISOU  409  CG2 THR A  96     9179   6935   6443   -125    -49    712       C  
ATOM    410  N   ALA A  97      29.111 -37.347  -5.890  1.00 58.20           N  
ANISOU  410  N   ALA A  97     8729   6593   6791   -418     51    688       N  
ATOM    411  CA  ALA A  97      28.294 -38.555  -5.945  1.00 61.19           C  
ANISOU  411  CA  ALA A  97     9171   6816   7263   -536     97    807       C  
ATOM    412  C   ALA A  97      28.539 -39.345  -7.226  1.00 58.49           C  
ANISOU  412  C   ALA A  97     8844   6344   7036   -586    -24    740       C  
ATOM    413  O   ALA A  97      28.737 -40.564  -7.186  1.00 66.91           O  
ANISOU  413  O   ALA A  97    10062   7243   8119   -591    -46    797       O  
ATOM    414  CB  ALA A  97      26.815 -38.191  -5.819  1.00 62.63           C  
ANISOU  414  CB  ALA A  97     9214   7026   7558   -683    247    891       C  
ATOM    415  N   ILE A  98      28.527 -38.673  -8.372  1.00 46.86           N  
ANISOU  415  N   ILE A  98     7238   4932   5634   -624    -94    620       N  
ATOM    416  CA  ILE A  98      28.570 -39.366  -9.657  1.00 53.13           C  
ANISOU  416  CA  ILE A  98     8073   5603   6512   -708   -191    547       C  
ATOM    417  C   ILE A  98      29.992 -39.478 -10.190  1.00 57.16           C  
ANISOU  417  C   ILE A  98     8667   6088   6964   -552   -268    424       C  
ATOM    418  O   ILE A  98      30.453 -40.569 -10.535  1.00 68.54           O  
ANISOU  418  O   ILE A  98    10263   7357   8424   -530   -292    407       O  
ATOM    419  CB  ILE A  98      27.648 -38.653 -10.669  1.00 53.23           C  
ANISOU  419  CB  ILE A  98     7909   5690   6625   -863   -231    511       C  
ATOM    420  CG1 ILE A  98      26.187 -38.779 -10.240  1.00 53.19           C  
ANISOU  420  CG1 ILE A  98     7797   5675   6738  -1030   -153    659       C  
ATOM    421  CG2 ILE A  98      27.851 -39.222 -12.058  1.00 55.43           C  
ANISOU  421  CG2 ILE A  98     8270   5863   6928   -949   -349    404       C  
ATOM    422  CD1 ILE A  98      25.265 -37.793 -10.917  1.00 58.27           C  
ANISOU  422  CD1 ILE A  98     8204   6436   7499  -1140   -180    671       C  
ATOM    423  N   CYS A  99      30.711 -38.357 -10.272  1.00 48.88           N  
ANISOU  423  N   CYS A  99     7514   5197   5863   -441   -292    340       N  
ATOM    424  CA  CYS A  99      31.997 -38.361 -10.959  1.00 45.54           C  
ANISOU  424  CA  CYS A  99     7122   4760   5423   -310   -350    226       C  
ATOM    425  C   CYS A  99      33.128 -38.911 -10.098  1.00 55.82           C  
ANISOU  425  C   CYS A  99     8515   6017   6678   -129   -363    275       C  
ATOM    426  O   CYS A  99      34.055 -39.527 -10.634  1.00 68.18           O  
ANISOU  426  O   CYS A  99    10147   7477   8280    -26   -382    226       O  
ATOM    427  CB  CYS A  99      32.345 -36.951 -11.431  1.00 41.60           C  
ANISOU  427  CB  CYS A  99     6463   4435   4909   -276   -372    131       C  
ATOM    428  SG  CYS A  99      31.010 -36.122 -12.314  1.00 46.25           S  
ANISOU  428  SG  CYS A  99     6911   5101   5563   -466   -375    120       S  
ATOM    429  N   LEU A 100      33.085 -38.694  -8.783  1.00 50.71           N  
ANISOU  429  N   LEU A 100     7875   5445   5950    -85   -350    377       N  
ATOM    430  CA  LEU A 100      34.165 -39.175  -7.924  1.00 52.42           C  
ANISOU  430  CA  LEU A 100     8171   5638   6110     80   -404    449       C  
ATOM    431  C   LEU A 100      34.364 -40.684  -8.023  1.00 63.36           C  
ANISOU  431  C   LEU A 100     9713   6796   7563    121   -395    525       C  
ATOM    432  O   LEU A 100      35.516 -41.123  -8.194  1.00 72.18           O  
ANISOU  432  O   LEU A 100    10848   7848   8728    280   -442    520       O  
ATOM    433  CB  LEU A 100      33.908 -38.747  -6.476  1.00 47.19           C  
ANISOU  433  CB  LEU A 100     7540   5086   5304     82   -393    553       C  
ATOM    434  CG  LEU A 100      35.064 -38.969  -5.498  1.00 38.35           C  
ANISOU  434  CG  LEU A 100     6485   3998   4090    238   -499    637       C  
ATOM    435  CD1 LEU A 100      35.061 -37.892  -4.425  1.00 38.50           C  
ANISOU  435  CD1 LEU A 100     6496   4200   3933    226   -519    641       C  
ATOM    436  CD2 LEU A 100      35.010 -40.358  -4.875  1.00 41.13           C  
ANISOU  436  CD2 LEU A 100     7013   4181   4435    274   -493    808       C  
ATOM    437  N   PRO A 101      33.329 -41.526  -7.925  1.00 57.08           N  
ANISOU  437  N   PRO A 101     9028   5861   6799    -10   -329    603       N  
ATOM    438  CA  PRO A 101      33.582 -42.974  -8.019  1.00 47.76           C  
ANISOU  438  CA  PRO A 101     8020   4433   5695     33   -314    671       C  
ATOM    439  C   PRO A 101      34.270 -43.403  -9.310  1.00 47.41           C  
ANISOU  439  C   PRO A 101     8007   4254   5754     91   -315    532       C  
ATOM    440  O   PRO A 101      35.123 -44.298  -9.277  1.00 53.59           O  
ANISOU  440  O   PRO A 101     8889   4870   6602    241   -309    573       O  
ATOM    441  CB  PRO A 101      32.174 -43.572  -7.886  1.00 46.34           C  
ANISOU  441  CB  PRO A 101     7917   4144   5547   -175   -239    750       C  
ATOM    442  CG  PRO A 101      31.425 -42.541  -7.087  1.00 48.75           C  
ANISOU  442  CG  PRO A 101     8106   4657   5759   -248   -201    802       C  
ATOM    443  CD  PRO A 101      31.916 -41.235  -7.644  1.00 51.95           C  
ANISOU  443  CD  PRO A 101     8344   5257   6137   -195   -254    653       C  
ATOM    444  N   ALA A 102      33.915 -42.791 -10.444  1.00 43.69           N  
ANISOU  444  N   ALA A 102     7462   3840   5297    -21   -312    379       N  
ATOM    445  CA  ALA A 102      34.624 -43.040 -11.695  1.00 45.44           C  
ANISOU  445  CA  ALA A 102     7731   3958   5575     35   -291    230       C  
ATOM    446  C   ALA A 102      36.055 -42.559 -11.586  1.00 56.36           C  
ANISOU  446  C   ALA A 102     9007   5435   6973    266   -307    209       C  
ATOM    447  O   ALA A 102      36.953 -43.059 -12.279  1.00 65.37           O  
ANISOU  447  O   ALA A 102    10200   6446   8190    394   -253    140       O  
ATOM    448  CB  ALA A 102      33.929 -42.326 -12.856  1.00 46.43           C  
ANISOU  448  CB  ALA A 102     7801   4168   5674   -143   -305     92       C  
ATOM    449  N   SER A 103      36.249 -41.533 -10.718  1.00 59.95           N  
ANISOU  449  N   SER A 103     9307   6111   7362    314   -374    266       N  
ATOM    450  CA  SER A 103      37.556 -40.927 -10.524  1.00 60.78           C  
ANISOU  450  CA  SER A 103     9272   6335   7485    498   -424    258       C  
ATOM    451  C   SER A 103      38.544 -41.926  -9.953  1.00 54.34           C  
ANISOU  451  C   SER A 103     8513   5382   6751    695   -443    379       C  
ATOM    452  O   SER A 103      39.655 -42.084 -10.466  1.00 51.57           O  
ANISOU  452  O   SER A 103     8100   4981   6513    858   -419    345       O  
ATOM    453  CB  SER A 103      37.400 -39.755  -9.551  1.00 81.94           C  
ANISOU  453  CB  SER A 103    11827   9251  10055    466   -504    299       C  
ATOM    454  OG  SER A 103      36.465 -38.796 -10.029  1.00 95.87           O  
ANISOU  454  OG  SER A 103    13557  11105  11763    283   -468    240       O  
ATOM    455  N   LEU A 104      38.138 -42.680  -8.923  1.00 51.44           N  
ANISOU  455  N   LEU A 104     8264   4940   6342    687   -471    538       N  
ATOM    456  CA  LEU A 104      39.029 -43.599  -8.235  1.00 49.24           C  
ANISOU  456  CA  LEU A 104     8035   4539   6135    879   -513    698       C  
ATOM    457  C   LEU A 104      39.401 -44.776  -9.129  1.00 56.49           C  
ANISOU  457  C   LEU A 104     9070   5171   7222    973   -396    662       C  
ATOM    458  O   LEU A 104      40.573 -45.164  -9.208  1.00 68.71           O  
ANISOU  458  O   LEU A 104    10558   6641   8907   1189   -394    710       O  
ATOM    459  CB  LEU A 104      38.356 -44.063  -6.948  1.00 41.65           C  
ANISOU  459  CB  LEU A 104     7202   3561   5060    822   -556    884       C  
ATOM    460  CG  LEU A 104      38.983 -45.167  -6.119  1.00 44.45           C  
ANISOU  460  CG  LEU A 104     7659   3762   5467    987   -606   1098       C  
ATOM    461  CD1 LEU A 104      40.243 -44.641  -5.458  1.00 53.09           C  
ANISOU  461  CD1 LEU A 104     8594   5024   6552   1164   -772   1189       C  
ATOM    462  CD2 LEU A 104      37.970 -45.589  -5.087  1.00 41.65           C  
ANISOU  462  CD2 LEU A 104     7471   3377   4976    863   -595   1252       C  
ATOM    463  N   LEU A 105      38.415 -45.352  -9.813  1.00 48.23           N  
ANISOU  463  N   LEU A 105     8191   3957   6177    808   -295    577       N  
ATOM    464  CA  LEU A 105      38.679 -46.523 -10.638  1.00 57.51           C  
ANISOU  464  CA  LEU A 105     9536   4826   7489    872   -170    522       C  
ATOM    465  C   LEU A 105      39.593 -46.195 -11.815  1.00 59.59           C  
ANISOU  465  C   LEU A 105     9725   5084   7833    984    -82    352       C  
ATOM    466  O   LEU A 105      40.424 -47.021 -12.209  1.00 67.68           O  
ANISOU  466  O   LEU A 105    10742   5966   9008   1128     25    340       O  
ATOM    467  CB  LEU A 105      37.354 -47.103 -11.129  1.00 63.12           C  
ANISOU  467  CB  LEU A 105    10400   5419   8162    610   -108    446       C  
ATOM    468  CG  LEU A 105      36.534 -47.826 -10.056  1.00 72.27           C  
ANISOU  468  CG  LEU A 105    11635   6521   9302    515   -131    623       C  
ATOM    469  CD1 LEU A 105      35.234 -48.366 -10.635  1.00 74.70           C  
ANISOU  469  CD1 LEU A 105    12047   6728   9608    246    -81    543       C  
ATOM    470  CD2 LEU A 105      37.339 -48.938  -9.393  1.00 77.06           C  
ANISOU  470  CD2 LEU A 105    12264   6984  10030    706   -107    777       C  
ATOM    471  N   VAL A 106      39.461 -44.999 -12.388  1.00 51.72           N  
ANISOU  471  N   VAL A 106     8591   4312   6749    887   -108    219       N  
ATOM    472  CA  VAL A 106      40.295 -44.644 -13.533  1.00 58.81           C  
ANISOU  472  CA  VAL A 106     9429   5211   7706    979     -3     65       C  
ATOM    473  C   VAL A 106      41.747 -44.436 -13.117  1.00 64.70           C  
ANISOU  473  C   VAL A 106     9968   6024   8592   1246    -16    159       C  
ATOM    474  O   VAL A 106      42.671 -44.878 -13.809  1.00 60.72           O  
ANISOU  474  O   VAL A 106     9463   5375   8232   1418    128    110       O  
ATOM    475  CB  VAL A 106      39.728 -43.401 -14.236  1.00 66.05           C  
ANISOU  475  CB  VAL A 106    10257   6348   8493    797    -35    -75       C  
ATOM    476  CG1 VAL A 106      40.669 -42.945 -15.339  1.00 70.25           C  
ANISOU  476  CG1 VAL A 106    10718   6902   9072    898     81   -211       C  
ATOM    477  CG2 VAL A 106      38.354 -43.703 -14.794  1.00 70.52           C  
ANISOU  477  CG2 VAL A 106    11010   6829   8957    536    -33   -155       C  
ATOM    478  N   ASP A 107      41.974 -43.763 -11.986  1.00 76.51           N  
ANISOU  478  N   ASP A 107    11283   7737  10051   1280   -186    296       N  
ATOM    479  CA  ASP A 107      43.339 -43.497 -11.545  1.00 77.18           C  
ANISOU  479  CA  ASP A 107    11141   7911  10273   1503   -249    401       C  
ATOM    480  C   ASP A 107      44.050 -44.735 -11.016  1.00 71.15           C  
ANISOU  480  C   ASP A 107    10421   6930   9682   1725   -235    579       C  
ATOM    481  O   ASP A 107      45.285 -44.774 -11.029  1.00 74.84           O  
ANISOU  481  O   ASP A 107    10696   7401  10339   1937   -229    651       O  
ATOM    482  CB  ASP A 107      43.338 -42.396 -10.483  1.00 77.73           C  
ANISOU  482  CB  ASP A 107    11041   8270  10223   1441   -458    482       C  
ATOM    483  CG  ASP A 107      43.057 -41.023 -11.072  1.00 79.51           C  
ANISOU  483  CG  ASP A 107    11152   8707  10353   1294   -457    319       C  
ATOM    484  OD1 ASP A 107      43.443 -40.789 -12.240  1.00 80.41           O  
ANISOU  484  OD1 ASP A 107    11219   8791  10543   1318   -323    185       O  
ATOM    485  OD2 ASP A 107      42.455 -40.180 -10.372  1.00 81.61           O  
ANISOU  485  OD2 ASP A 107    11387   9156  10466   1159   -573    330       O  
ATOM    486  N   ILE A 108      43.314 -45.742 -10.557  1.00 68.10           N  
ANISOU  486  N   ILE A 108    10248   6368   9260   1667   -226    662       N  
ATOM    487  CA  ILE A 108      43.935 -46.968 -10.069  1.00 76.82           C  
ANISOU  487  CA  ILE A 108    11334   7312  10543   1809   -206    825       C  
ATOM    488  C   ILE A 108      44.111 -47.946 -11.223  1.00 87.80           C  
ANISOU  488  C   ILE A 108    12820   8455  12085   1832     21    682       C  
ATOM    489  O   ILE A 108      45.234 -48.362 -11.531  1.00 95.12           O  
ANISOU  489  O   ILE A 108    13610   9307  13224   2018     93    701       O  
ATOM    490  CB  ILE A 108      43.122 -47.589  -8.920  1.00 71.53           C  
ANISOU  490  CB  ILE A 108    10809   6604   9765   1715   -306    997       C  
ATOM    491  CG1 ILE A 108      43.295 -46.755  -7.653  1.00 70.37           C  
ANISOU  491  CG1 ILE A 108    10547   6714   9477   1729   -538   1162       C  
ATOM    492  CG2 ILE A 108      43.559 -49.015  -8.662  1.00 79.85           C  
ANISOU  492  CG2 ILE A 108    11898   7429  11013   1829   -251   1131       C  
ATOM    493  CD1 ILE A 108      42.520 -47.286  -6.483  1.00 74.75           C  
ANISOU  493  CD1 ILE A 108    11245   7261   9894   1626   -615   1334       C  
ATOM    494  N   THR A 109      43.005 -48.325 -11.865  1.00 77.55           N  
ANISOU  494  N   THR A 109    11754   7039  10675   1629    120    535       N  
ATOM    495  CA  THR A 109      43.077 -49.282 -12.960  1.00 58.70           C  
ANISOU  495  CA  THR A 109     9495   4429   8379   1614    315    382       C  
ATOM    496  C   THR A 109      43.699 -48.686 -14.217  1.00 64.05           C  
ANISOU  496  C   THR A 109    10101   5162   9072   1652    452    185       C  
ATOM    497  O   THR A 109      44.208 -49.436 -15.054  1.00 74.64           O  
ANISOU  497  O   THR A 109    11501   6345  10515   1719    620     85       O  
ATOM    498  CB  THR A 109      41.686 -49.814 -13.296  1.00 45.17           C  
ANISOU  498  CB  THR A 109     8032   2603   6527   1353    344    284       C  
ATOM    499  OG1 THR A 109      40.958 -48.813 -14.017  1.00 47.43           O  
ANISOU  499  OG1 THR A 109     8351   3038   6633   1160    329    119       O  
ATOM    500  CG2 THR A 109      40.926 -50.168 -12.027  1.00 43.45           C  
ANISOU  500  CG2 THR A 109     7871   2377   6261   1279    215    481       C  
ATOM    501  N   GLU A 110      43.667 -47.362 -14.371  1.00 60.41           N  
ANISOU  501  N   GLU A 110     9529   4923   8503   1608    391    130       N  
ATOM    502  CA  GLU A 110      44.173 -46.696 -15.570  1.00 66.88           C  
ANISOU  502  CA  GLU A 110    10283   5816   9312   1616    523    -48       C  
ATOM    503  C   GLU A 110      43.399 -47.091 -16.824  1.00 71.29           C  
ANISOU  503  C   GLU A 110    11081   6274   9732   1412    652   -259       C  
ATOM    504  O   GLU A 110      43.934 -47.033 -17.934  1.00 71.37           O  
ANISOU  504  O   GLU A 110    11098   6273   9745   1436    810   -399       O  
ATOM    505  CB  GLU A 110      45.667 -46.974 -15.778  1.00 76.43           C  
ANISOU  505  CB  GLU A 110    11297   6989  10756   1868    635     -7       C  
ATOM    506  CG  GLU A 110      46.597 -46.053 -15.010  1.00 82.81           C  
ANISOU  506  CG  GLU A 110    11791   7996  11677   2031    503    142       C  
ATOM    507  CD  GLU A 110      48.055 -46.217 -15.412  1.00 97.38           C  
ANISOU  507  CD  GLU A 110    13415   9830  13754   2246    619    161       C  
ATOM    508  OE1 GLU A 110      48.915 -46.333 -14.512  1.00104.75           O  
ANISOU  508  OE1 GLU A 110    14129  10809  14863   2417    488    353       O  
ATOM    509  OE2 GLU A 110      48.341 -46.227 -16.628  1.00102.36           O  
ANISOU  509  OE2 GLU A 110    14096  10418  14377   2233    833     -7       O  
ATOM    510  N   SER A 111      42.142 -47.496 -16.671  1.00 71.73           N  
ANISOU  510  N   SER A 111    11328   6268   9659   1199    577   -273       N  
ATOM    511  CA  SER A 111      41.316 -47.818 -17.825  1.00 68.29           C  
ANISOU  511  CA  SER A 111    11100   5770   9077    973    643   -455       C  
ATOM    512  C   SER A 111      39.865 -47.481 -17.514  1.00 66.27           C  
ANISOU  512  C   SER A 111    10923   5593   8663    711    481   -443       C  
ATOM    513  O   SER A 111      39.475 -47.344 -16.351  1.00 61.06           O  
ANISOU  513  O   SER A 111    10211   4970   8019    712    358   -291       O  
ATOM    514  CB  SER A 111      41.463 -49.290 -18.223  1.00 72.73           C  
ANISOU  514  CB  SER A 111    11837   6073   9724   1002    775   -496       C  
ATOM    515  OG  SER A 111      41.005 -50.134 -17.183  1.00 75.13           O  
ANISOU  515  OG  SER A 111    12194   6246  10107    998    697   -349       O  
ATOM    516  N   TRP A 112      39.069 -47.349 -18.575  1.00 71.89           N  
ANISOU  516  N   TRP A 112    11754   6341   9222    484    478   -589       N  
ATOM    517  CA  TRP A 112      37.650 -47.024 -18.479  1.00 62.33           C  
ANISOU  517  CA  TRP A 112    10583   5217   7881    216    323   -580       C  
ATOM    518  C   TRP A 112      36.837 -48.309 -18.589  1.00 59.21           C  
ANISOU  518  C   TRP A 112    10370   4632   7495     63    324   -589       C  
ATOM    519  O   TRP A 112      36.900 -48.999 -19.611  1.00 56.68           O  
ANISOU  519  O   TRP A 112    10203   4196   7137     11    413   -718       O  
ATOM    520  CB  TRP A 112      37.238 -46.041 -19.575  1.00 54.79           C  
ANISOU  520  CB  TRP A 112     9609   4443   6766     54    282   -702       C  
ATOM    521  CG  TRP A 112      35.822 -45.572 -19.468  1.00 50.42           C  
ANISOU  521  CG  TRP A 112     9032   4008   6116   -205    109   -666       C  
ATOM    522  CD1 TRP A 112      34.764 -45.984 -20.224  1.00 49.93           C  
ANISOU  522  CD1 TRP A 112     9076   3930   5965   -446     41   -718       C  
ATOM    523  CD2 TRP A 112      35.309 -44.591 -18.559  1.00 55.74           C  
ANISOU  523  CD2 TRP A 112     9553   4837   6789   -244    -18   -558       C  
ATOM    524  NE1 TRP A 112      33.622 -45.324 -19.839  1.00 58.13           N  
ANISOU  524  NE1 TRP A 112    10001   5111   6974   -626   -118   -636       N  
ATOM    525  CE2 TRP A 112      33.930 -44.463 -18.818  1.00 58.11           C  
ANISOU  525  CE2 TRP A 112     9846   5210   7023   -508   -144   -542       C  
ATOM    526  CE3 TRP A 112      35.881 -43.812 -17.549  1.00 55.79           C  
ANISOU  526  CE3 TRP A 112     9427   4924   6848    -81    -41   -468       C  
ATOM    527  CZ2 TRP A 112      33.114 -43.587 -18.104  1.00 57.77           C  
ANISOU  527  CZ2 TRP A 112     9655   5312   6983   -608   -263   -438       C  
ATOM    528  CZ3 TRP A 112      35.070 -42.942 -16.842  1.00 54.47           C  
ANISOU  528  CZ3 TRP A 112     9154   4892   6651   -189   -168   -383       C  
ATOM    529  CH2 TRP A 112      33.702 -42.837 -17.122  1.00 57.47           C  
ANISOU  529  CH2 TRP A 112     9517   5337   6983   -450   -263   -368       C  
ATOM    530  N   LEU A 113      36.081 -48.626 -17.538  1.00 58.77           N  
ANISOU  530  N   LEU A 113    10305   4541   7484    -10    231   -450       N  
ATOM    531  CA  LEU A 113      35.290 -49.848 -17.477  1.00 60.82           C  
ANISOU  531  CA  LEU A 113    10713   4614   7782   -154    229   -434       C  
ATOM    532  C   LEU A 113      33.781 -49.593 -17.429  1.00 64.41           C  
ANISOU  532  C   LEU A 113    11148   5163   8161   -446     84   -404       C  
ATOM    533  O   LEU A 113      33.028 -50.498 -17.059  1.00 80.76           O  
ANISOU  533  O   LEU A 113    13293   7101  10292   -569     64   -342       O  
ATOM    534  CB  LEU A 113      35.719 -50.681 -16.264  1.00 62.57           C  
ANISOU  534  CB  LEU A 113    10937   4677   8158     15    270   -265       C  
ATOM    535  CG  LEU A 113      37.215 -50.781 -15.958  1.00 58.29           C  
ANISOU  535  CG  LEU A 113    10328   4082   7738    335    371   -218       C  
ATOM    536  CD1 LEU A 113      37.424 -51.232 -14.518  1.00 52.78           C  
ANISOU  536  CD1 LEU A 113     9577   3321   7154    472    332     12       C  
ATOM    537  CD2 LEU A 113      37.900 -51.735 -16.922  1.00 54.59           C  
ANISOU  537  CD2 LEU A 113     9990   3414   7337    419    530   -350       C  
ATOM    538  N   PHE A 114      33.310 -48.397 -17.799  1.00 57.68           N  
ANISOU  538  N   PHE A 114    10179   4536   7202   -560    -15   -435       N  
ATOM    539  CA  PHE A 114      31.892 -48.060 -17.665  1.00 58.43           C  
ANISOU  539  CA  PHE A 114    10195   4740   7266   -814   -155   -373       C  
ATOM    540  C   PHE A 114      31.136 -47.961 -18.991  1.00 55.24           C  
ANISOU  540  C   PHE A 114     9832   4403   6755  -1036   -237   -491       C  
ATOM    541  O   PHE A 114      29.960 -47.576 -18.991  1.00 46.91           O  
ANISOU  541  O   PHE A 114     8668   3462   5692  -1240   -367   -430       O  
ATOM    542  CB  PHE A 114      31.721 -46.746 -16.900  1.00 66.69           C  
ANISOU  542  CB  PHE A 114    11047   5995   8298   -791   -228   -270       C  
ATOM    543  CG  PHE A 114      32.413 -46.719 -15.572  1.00 73.56           C  
ANISOU  543  CG  PHE A 114    11885   6829   9236   -584   -178   -136       C  
ATOM    544  CD1 PHE A 114      31.782 -47.210 -14.445  1.00 80.11           C  
ANISOU  544  CD1 PHE A 114    12707   7600  10131   -631   -186     30       C  
ATOM    545  CD2 PHE A 114      33.704 -46.231 -15.458  1.00 76.23           C  
ANISOU  545  CD2 PHE A 114    12195   7197   9573   -339   -124   -160       C  
ATOM    546  CE1 PHE A 114      32.406 -47.196 -13.226  1.00 85.34           C  
ANISOU  546  CE1 PHE A 114    13355   8249  10822   -441   -156    175       C  
ATOM    547  CE2 PHE A 114      34.340 -46.210 -14.232  1.00 80.13           C  
ANISOU  547  CE2 PHE A 114    12653   7675  10119   -145   -114    -15       C  
ATOM    548  CZ  PHE A 114      33.687 -46.698 -13.113  1.00 84.80           C  
ANISOU  548  CZ  PHE A 114    13259   8221  10741   -197   -136    157       C  
ATOM    549  N   GLY A 115      31.753 -48.311 -20.112  1.00 60.91           N  
ANISOU  549  N   GLY A 115    10697   5052   7394   -999   -164   -642       N  
ATOM    550  CA  GLY A 115      31.056 -48.308 -21.381  1.00 61.81           C  
ANISOU  550  CA  GLY A 115    10889   5215   7379  -1210   -250   -739       C  
ATOM    551  C   GLY A 115      31.074 -46.960 -22.082  1.00 57.70           C  
ANISOU  551  C   GLY A 115    10249   4936   6738  -1231   -320   -764       C  
ATOM    552  O   GLY A 115      31.493 -45.933 -21.543  1.00 46.60           O  
ANISOU  552  O   GLY A 115     8677   3673   5356  -1108   -315   -708       O  
ATOM    553  N   HIS A 116      30.607 -46.987 -23.332  1.00 68.80           N  
ANISOU  553  N   HIS A 116    11757   6377   8007  -1396   -389   -845       N  
ATOM    554  CA  HIS A 116      30.762 -45.842 -24.223  1.00 64.97           C  
ANISOU  554  CA  HIS A 116    11208   6088   7391  -1405   -431   -874       C  
ATOM    555  C   HIS A 116      29.851 -44.683 -23.832  1.00 60.64           C  
ANISOU  555  C   HIS A 116    10405   5762   6875  -1501   -597   -740       C  
ATOM    556  O   HIS A 116      30.245 -43.516 -23.944  1.00 57.62           O  
ANISOU  556  O   HIS A 116     9891   5543   6461  -1416   -595   -722       O  
ATOM    557  CB  HIS A 116      30.463 -46.283 -25.651  1.00 73.17           C  
ANISOU  557  CB  HIS A 116    12458   7081   8260  -1566   -468   -979       C  
ATOM    558  CG  HIS A 116      31.337 -47.398 -26.122  1.00 91.04           C  
ANISOU  558  CG  HIS A 116    14986   9118  10487  -1476   -285  -1120       C  
ATOM    559  ND1 HIS A 116      31.042 -48.720 -25.868  1.00 96.93           N  
ANISOU  559  ND1 HIS A 116    15887   9642  11299  -1540   -260  -1153       N  
ATOM    560  CD2 HIS A 116      32.510 -47.399 -26.793  1.00 94.21           C  
ANISOU  560  CD2 HIS A 116    15514   9467  10814  -1318    -99  -1231       C  
ATOM    561  CE1 HIS A 116      31.981 -49.490 -26.384  1.00 99.45           C  
ANISOU  561  CE1 HIS A 116    16426   9778  11583  -1423    -70  -1281       C  
ATOM    562  NE2 HIS A 116      32.885 -48.713 -26.950  1.00 96.67           N  
ANISOU  562  NE2 HIS A 116    16056   9528  11148  -1285     36  -1329       N  
ATOM    563  N   ALA A 117      28.634 -44.981 -23.367  1.00 63.92           N  
ANISOU  563  N   ALA A 117    10736   6178   7372  -1675   -729   -641       N  
ATOM    564  CA  ALA A 117      27.680 -43.923 -23.037  1.00 64.84           C  
ANISOU  564  CA  ALA A 117    10595   6496   7546  -1767   -872   -502       C  
ATOM    565  C   ALA A 117      28.152 -43.091 -21.848  1.00 70.03           C  
ANISOU  565  C   ALA A 117    11071   7234   8302  -1600   -805   -427       C  
ATOM    566  O   ALA A 117      28.090 -41.855 -21.877  1.00 67.97           O  
ANISOU  566  O   ALA A 117    10637   7154   8036  -1572   -851   -375       O  
ATOM    567  CB  ALA A 117      26.303 -44.528 -22.761  1.00 70.19           C  
ANISOU  567  CB  ALA A 117    11206   7140   8321  -1980  -1001   -406       C  
ATOM    568  N   LEU A 118      28.621 -43.751 -20.787  1.00 78.18           N  
ANISOU  568  N   LEU A 118    12153   8125   9425  -1489   -700   -411       N  
ATOM    569  CA  LEU A 118      29.104 -43.032 -19.614  1.00 66.51           C  
ANISOU  569  CA  LEU A 118    10546   6704   8021  -1337   -644   -337       C  
ATOM    570  C   LEU A 118      30.427 -42.325 -19.876  1.00 60.87           C  
ANISOU  570  C   LEU A 118     9848   6041   7238  -1134   -556   -426       C  
ATOM    571  O   LEU A 118      30.805 -41.436 -19.104  1.00 66.74           O  
ANISOU  571  O   LEU A 118    10467   6874   8019  -1026   -543   -378       O  
ATOM    572  CB  LEU A 118      29.242 -43.992 -18.431  1.00 55.92           C  
ANISOU  572  CB  LEU A 118     9278   5187   6784  -1271   -563   -270       C  
ATOM    573  CG  LEU A 118      27.916 -44.508 -17.869  1.00 47.16           C  
ANISOU  573  CG  LEU A 118     8094   4047   5779  -1458   -624   -144       C  
ATOM    574  CD1 LEU A 118      28.157 -45.547 -16.787  1.00 53.10           C  
ANISOU  574  CD1 LEU A 118     8949   4608   6618  -1381   -523    -71       C  
ATOM    575  CD2 LEU A 118      27.078 -43.357 -17.335  1.00 40.59           C  
ANISOU  575  CD2 LEU A 118     7007   3407   5008  -1530   -689    -15       C  
ATOM    576  N   CYS A 119      31.137 -42.697 -20.944  1.00 60.58           N  
ANISOU  576  N   CYS A 119     9962   5947   7109  -1085   -487   -554       N  
ATOM    577  CA  CYS A 119      32.363 -41.986 -21.296  1.00 66.62           C  
ANISOU  577  CA  CYS A 119    10713   6774   7827   -902   -389   -631       C  
ATOM    578  C   CYS A 119      32.079 -40.541 -21.676  1.00 70.68           C  
ANISOU  578  C   CYS A 119    11050   7512   8292   -950   -473   -600       C  
ATOM    579  O   CYS A 119      32.949 -39.678 -21.521  1.00 65.93           O  
ANISOU  579  O   CYS A 119    10364   6993   7694   -802   -414   -622       O  
ATOM    580  CB  CYS A 119      33.077 -42.717 -22.438  1.00 67.86           C  
ANISOU  580  CB  CYS A 119    11069   6816   7898   -861   -273   -764       C  
ATOM    581  SG  CYS A 119      34.569 -41.912 -23.098  1.00 76.92           S  
ANISOU  581  SG  CYS A 119    12195   8035   8998   -655   -120   -857       S  
ATOM    582  N   LYS A 120      30.881 -40.261 -22.183  1.00 72.22           N  
ANISOU  582  N   LYS A 120    11181   7803   8457  -1148   -613   -540       N  
ATOM    583  CA  LYS A 120      30.484 -38.894 -22.490  1.00 59.19           C  
ANISOU  583  CA  LYS A 120     9343   6354   6790  -1190   -699   -478       C  
ATOM    584  C   LYS A 120      29.728 -38.239 -21.342  1.00 41.79           C  
ANISOU  584  C   LYS A 120     6926   4239   4714  -1221   -770   -347       C  
ATOM    585  O   LYS A 120      29.915 -37.045 -21.077  1.00 37.94           O  
ANISOU  585  O   LYS A 120     6278   3885   4252  -1157   -773   -314       O  
ATOM    586  CB  LYS A 120      29.624 -38.859 -23.756  1.00 54.42           C  
ANISOU  586  CB  LYS A 120     8777   5807   6092  -1370   -817   -461       C  
ATOM    587  CG  LYS A 120      30.351 -39.290 -25.026  1.00 44.21           C  
ANISOU  587  CG  LYS A 120     7709   4446   4643  -1357   -741   -588       C  
ATOM    588  CD  LYS A 120      29.435 -39.228 -26.249  1.00 43.82           C  
ANISOU  588  CD  LYS A 120     7722   4449   4479  -1555   -885   -557       C  
ATOM    589  CE  LYS A 120      30.111 -38.535 -27.432  1.00 42.72           C  
ANISOU  589  CE  LYS A 120     7666   4375   4190  -1521   -835   -613       C  
ATOM    590  NZ  LYS A 120      31.141 -39.386 -28.089  1.00 41.72           N  
ANISOU  590  NZ  LYS A 120     7802   4102   3950  -1451   -667   -768       N  
ATOM    591  N   VAL A 121      28.863 -38.994 -20.662  1.00 37.60           N  
ANISOU  591  N   VAL A 121     6387   3629   4270  -1325   -812   -271       N  
ATOM    592  CA  VAL A 121      28.038 -38.416 -19.602  1.00 37.40           C  
ANISOU  592  CA  VAL A 121     6155   3680   4376  -1372   -851   -132       C  
ATOM    593  C   VAL A 121      28.904 -37.951 -18.439  1.00 45.86           C  
ANISOU  593  C   VAL A 121     7206   4738   5481  -1211   -758   -134       C  
ATOM    594  O   VAL A 121      28.916 -36.768 -18.082  1.00 59.81           O  
ANISOU  594  O   VAL A 121     8786   6657   7281  -1146   -749    -88       O  
ATOM    595  CB  VAL A 121      26.975 -39.424 -19.135  1.00 47.54           C  
ANISOU  595  CB  VAL A 121     7440   4869   5755  -1516   -886    -43       C  
ATOM    596  CG1 VAL A 121      26.169 -38.835 -17.989  1.00 50.63           C  
ANISOU  596  CG1 VAL A 121     7609   5333   6296  -1549   -873    114       C  
ATOM    597  CG2 VAL A 121      26.080 -39.798 -20.296  1.00 50.16           C  
ANISOU  597  CG2 VAL A 121     7786   5222   6051  -1688  -1009    -40       C  
ATOM    598  N   ILE A 122      29.638 -38.880 -17.826  1.00 40.48           N  
ANISOU  598  N   ILE A 122     6692   3893   4796  -1106   -673   -172       N  
ATOM    599  CA  ILE A 122      30.381 -38.548 -16.607  1.00 35.40           C  
ANISOU  599  CA  ILE A 122     5955   3314   4181   -884   -571   -124       C  
ATOM    600  C   ILE A 122      31.371 -37.408 -16.825  1.00 39.84           C  
ANISOU  600  C   ILE A 122     6409   4027   4699   -722   -540   -191       C  
ATOM    601  O   ILE A 122      31.373 -36.458 -16.027  1.00 37.08           O  
ANISOU  601  O   ILE A 122     5885   3824   4379   -645   -517   -130       O  
ATOM    602  CB  ILE A 122      31.048 -39.807 -16.033  1.00 36.78           C  
ANISOU  602  CB  ILE A 122     6314   3296   4365   -776   -498   -127       C  
ATOM    603  CG1 ILE A 122      29.991 -40.781 -15.516  1.00 32.06           C  
ANISOU  603  CG1 ILE A 122     5784   2562   3833   -934   -512    -22       C  
ATOM    604  CG2 ILE A 122      32.018 -39.416 -14.935  1.00 46.78           C  
ANISOU  604  CG2 ILE A 122     7495   4645   5633   -543   -433    -83       C  
ATOM    605  CD1 ILE A 122      30.434 -42.215 -15.508  1.00 36.05           C  
ANISOU  605  CD1 ILE A 122     6537   2809   4350   -904   -464    -51       C  
ATOM    606  N   PRO A 123      32.231 -37.437 -17.840  1.00 41.05           N  
ANISOU  606  N   PRO A 123     6666   4145   4786   -670   -520   -314       N  
ATOM    607  CA  PRO A 123      33.112 -36.279 -18.073  1.00 32.30           C  
ANISOU  607  CA  PRO A 123     5430   3185   3657   -539   -484   -361       C  
ATOM    608  C   PRO A 123      32.341 -34.994 -18.307  1.00 31.05           C  
ANISOU  608  C   PRO A 123     5089   3199   3509   -635   -550   -309       C  
ATOM    609  O   PRO A 123      32.813 -33.917 -17.926  1.00 40.62           O  
ANISOU  609  O   PRO A 123     6146   4540   4746   -530   -518   -300       O  
ATOM    610  CB  PRO A 123      33.923 -36.704 -19.307  1.00 35.51           C  
ANISOU  610  CB  PRO A 123     6012   3494   3985   -512   -430   -495       C  
ATOM    611  CG  PRO A 123      33.901 -38.194 -19.247  1.00 35.12           C  
ANISOU  611  CG  PRO A 123     6183   3220   3940   -530   -397   -522       C  
ATOM    612  CD  PRO A 123      32.523 -38.535 -18.780  1.00 38.15           C  
ANISOU  612  CD  PRO A 123     6552   3584   4358   -718   -498   -423       C  
ATOM    613  N   TYR A 124      31.167 -35.086 -18.928  1.00 34.46           N  
ANISOU  613  N   TYR A 124     5531   3624   3937   -837   -647   -268       N  
ATOM    614  CA  TYR A 124      30.335 -33.909 -19.125  1.00 42.39           C  
ANISOU  614  CA  TYR A 124     6340   4778   4989   -919   -714   -183       C  
ATOM    615  C   TYR A 124      29.806 -33.374 -17.799  1.00 54.92           C  
ANISOU  615  C   TYR A 124     7738   6437   6690   -866   -663    -73       C  
ATOM    616  O   TYR A 124      29.853 -32.165 -17.539  1.00 58.94           O  
ANISOU  616  O   TYR A 124     8085   7067   7243   -796   -629    -45       O  
ATOM    617  CB  TYR A 124      29.181 -34.248 -20.071  1.00 40.20           C  
ANISOU  617  CB  TYR A 124     6087   4484   4701  -1135   -844   -132       C  
ATOM    618  CG  TYR A 124      28.098 -33.203 -20.162  1.00 47.54           C  
ANISOU  618  CG  TYR A 124     6780   5550   5732  -1217   -921      6       C  
ATOM    619  CD1 TYR A 124      28.265 -32.062 -20.938  1.00 46.74           C  
ANISOU  619  CD1 TYR A 124     6590   5564   5603  -1184   -942     18       C  
ATOM    620  CD2 TYR A 124      26.895 -33.369 -19.489  1.00 43.85           C  
ANISOU  620  CD2 TYR A 124     6170   5083   5408  -1318   -953    142       C  
ATOM    621  CE1 TYR A 124      27.264 -31.111 -21.030  1.00 45.73           C  
ANISOU  621  CE1 TYR A 124     6242   5540   5593  -1235  -1004    162       C  
ATOM    622  CE2 TYR A 124      25.890 -32.425 -19.576  1.00 32.01           C  
ANISOU  622  CE2 TYR A 124     4429   3697   4035  -1360   -997    283       C  
ATOM    623  CZ  TYR A 124      26.080 -31.299 -20.348  1.00 36.29           C  
ANISOU  623  CZ  TYR A 124     4893   4343   4552  -1312  -1028    293       C  
ATOM    624  OH  TYR A 124      25.082 -30.357 -20.436  1.00 30.89           O  
ANISOU  624  OH  TYR A 124     3971   3750   4013  -1328  -1062    447       O  
ATOM    625  N   LEU A 125      29.308 -34.265 -16.937  1.00 55.14           N  
ANISOU  625  N   LEU A 125     7807   6381   6764   -898   -638    -11       N  
ATOM    626  CA  LEU A 125      28.830 -33.832 -15.628  1.00 49.80           C  
ANISOU  626  CA  LEU A 125     6994   5763   6166   -845   -554     88       C  
ATOM    627  C   LEU A 125      29.959 -33.239 -14.795  1.00 43.32           C  
ANISOU  627  C   LEU A 125     6165   5003   5292   -648   -470     33       C  
ATOM    628  O   LEU A 125      29.743 -32.294 -14.028  1.00 43.81           O  
ANISOU  628  O   LEU A 125     6104   5157   5387   -596   -404     72       O  
ATOM    629  CB  LEU A 125      28.177 -35.001 -14.892  1.00 48.41           C  
ANISOU  629  CB  LEU A 125     6894   5470   6028   -921   -527    171       C  
ATOM    630  CG  LEU A 125      26.888 -35.538 -15.514  1.00 49.36           C  
ANISOU  630  CG  LEU A 125     6981   5535   6239  -1150   -619    253       C  
ATOM    631  CD1 LEU A 125      26.403 -36.759 -14.755  1.00 50.69           C  
ANISOU  631  CD1 LEU A 125     7244   5566   6451  -1221   -575    330       C  
ATOM    632  CD2 LEU A 125      25.817 -34.457 -15.545  1.00 44.24           C  
ANISOU  632  CD2 LEU A 125     6074   5014   5721  -1218   -627    369       C  
ATOM    633  N   GLN A 126      31.173 -33.777 -14.933  1.00 39.72           N  
ANISOU  633  N   GLN A 126     5839   4491   4763   -539   -471    -57       N  
ATOM    634  CA  GLN A 126      32.318 -33.185 -14.246  1.00 50.60           C  
ANISOU  634  CA  GLN A 126     7183   5938   6106   -370   -432   -101       C  
ATOM    635  C   GLN A 126      32.602 -31.782 -14.770  1.00 48.04           C  
ANISOU  635  C   GLN A 126     6721   5736   5797   -349   -432   -150       C  
ATOM    636  O   GLN A 126      32.820 -30.848 -13.989  1.00 54.56           O  
ANISOU  636  O   GLN A 126     7456   6646   6627   -284   -397   -149       O  
ATOM    637  CB  GLN A 126      33.545 -34.085 -14.404  1.00 55.05           C  
ANISOU  637  CB  GLN A 126     7874   6409   6635   -255   -434   -163       C  
ATOM    638  CG  GLN A 126      34.872 -33.360 -14.249  1.00 51.09           C  
ANISOU  638  CG  GLN A 126     7295   5991   6128   -106   -427   -222       C  
ATOM    639  CD  GLN A 126      35.055 -33.235 -12.560  1.00 63.80           C  
ANISOU  639  CD  GLN A 126     8860   7669   7711    -24   -436   -172       C  
ATOM    640  OE1 GLN A 126      34.525 -32.302 -11.959  1.00 71.44           O  
ANISOU  640  OE1 GLN A 126     9727   8748   8671    -37   -429   -180       O  
ATOM    641  NE2 GLN A 126      35.825 -34.134 -11.954  1.00 67.32           N  
ANISOU  641  NE2 GLN A 126     9403   8040   8136     57   -454   -119       N  
ATOM    642  N   ALA A 127      32.599 -31.616 -16.096  1.00 32.10           N  
ANISOU  642  N   ALA A 127     4707   3716   3773   -412   -469   -193       N  
ATOM    643  CA  ALA A 127      32.822 -30.295 -16.674  1.00 27.90           C  
ANISOU  643  CA  ALA A 127     4054   3287   3260   -400   -466   -218       C  
ATOM    644  C   ALA A 127      31.723 -29.324 -16.271  1.00 46.42           C  
ANISOU  644  C   ALA A 127     6249   5703   5687   -458   -454   -130       C  
ATOM    645  O   ALA A 127      31.996 -28.159 -15.963  1.00 58.62           O  
ANISOU  645  O   ALA A 127     7688   7317   7267   -398   -409   -142       O  
ATOM    646  CB  ALA A 127      32.904 -30.393 -18.198  1.00 29.24           C  
ANISOU  646  CB  ALA A 127     4292   3438   3379   -475   -508   -260       C  
ATOM    647  N   VAL A 128      30.471 -29.783 -16.271  1.00 51.84           N  
ANISOU  647  N   VAL A 128     6917   6358   6424   -576   -484    -36       N  
ATOM    648  CA  VAL A 128      29.373 -28.909 -15.867  1.00 42.35           C  
ANISOU  648  CA  VAL A 128     5545   5209   5338   -614   -444     68       C  
ATOM    649  C   VAL A 128      29.520 -28.502 -14.407  1.00 37.74           C  
ANISOU  649  C   VAL A 128     4939   4642   4759   -510   -318     63       C  
ATOM    650  O   VAL A 128      29.215 -27.364 -14.030  1.00 22.42           O  
ANISOU  650  O   VAL A 128     2883   2747   2889   -472   -238     85       O  
ATOM    651  CB  VAL A 128      28.022 -29.594 -16.124  1.00 27.84           C  
ANISOU  651  CB  VAL A 128     3663   3332   3581   -769   -503    187       C  
ATOM    652  CG1 VAL A 128      26.912 -28.794 -15.471  1.00 19.15           C  
ANISOU  652  CG1 VAL A 128     2365   2272   2639   -775   -414    313       C  
ATOM    653  CG2 VAL A 128      27.784 -29.734 -17.614  1.00 30.20           C  
ANISOU  653  CG2 VAL A 128     3985   3634   3857   -898   -654    196       C  
ATOM    654  N   SER A 129      29.990 -29.424 -13.563  1.00 46.82           N  
ANISOU  654  N   SER A 129     6220   5744   5825   -464   -297     37       N  
ATOM    655  CA  SER A 129      30.176 -29.111 -12.152  1.00 49.01           C  
ANISOU  655  CA  SER A 129     6525   6041   6056   -381   -197     32       C  
ATOM    656  C   SER A 129      31.210 -28.013 -11.958  1.00 50.90           C  
ANISOU  656  C   SER A 129     6743   6344   6254   -286   -190    -68       C  
ATOM    657  O   SER A 129      31.115 -27.226 -11.009  1.00 58.38           O  
ANISOU  657  O   SER A 129     7680   7318   7182   -249   -100    -82       O  
ATOM    658  CB  SER A 129      30.588 -30.367 -11.386  1.00 53.99           C  
ANISOU  658  CB  SER A 129     7315   6608   6589   -351   -210     44       C  
ATOM    659  OG  SER A 129      30.525 -30.146  -9.990  1.00 66.94           O  
ANISOU  659  OG  SER A 129     9008   8270   8158   -301   -116     66       O  
ATOM    660  N   VAL A 130      32.201 -27.938 -12.846  1.00 39.83           N  
ANISOU  660  N   VAL A 130     5340   4956   4837   -256   -271   -141       N  
ATOM    661  CA  VAL A 130      33.213 -26.894 -12.737  1.00 37.76           C  
ANISOU  661  CA  VAL A 130     5035   4749   4563   -187   -272   -226       C  
ATOM    662  C   VAL A 130      32.645 -25.549 -13.165  1.00 40.53           C  
ANISOU  662  C   VAL A 130     5260   5130   5011   -217   -216   -216       C  
ATOM    663  O   VAL A 130      32.852 -24.527 -12.499  1.00 34.37           O  
ANISOU  663  O   VAL A 130     4453   4369   4238   -184   -156   -261       O  
ATOM    664  CB  VAL A 130      34.452 -27.262 -13.567  1.00 24.60           C  
ANISOU  664  CB  VAL A 130     3388   3082   2878   -140   -344   -290       C  
ATOM    665  CG1 VAL A 130      35.448 -26.131 -13.514  1.00 17.30           C  
ANISOU  665  CG1 VAL A 130     2385   2214   1975    -92   -345   -362       C  
ATOM    666  CG2 VAL A 130      35.062 -28.543 -13.036  1.00 13.88           C  
ANISOU  666  CG2 VAL A 130     2142   1675   1456    -81   -386   -286       C  
ATOM    667  N   SER A 131      31.931 -25.527 -14.291  1.00 43.99           N  
ANISOU  667  N   SER A 131     5630   5563   5522   -286   -243   -151       N  
ATOM    668  CA  SER A 131      31.353 -24.279 -14.771  1.00 35.39           C  
ANISOU  668  CA  SER A 131     4409   4493   4545   -306   -202   -106       C  
ATOM    669  C   SER A 131      30.361 -23.704 -13.770  1.00 39.51           C  
ANISOU  669  C   SER A 131     4868   4996   5149   -294    -75    -51       C  
ATOM    670  O   SER A 131      30.320 -22.486 -13.553  1.00 37.02           O  
ANISOU  670  O   SER A 131     4485   4673   4906   -255     11    -67       O  
ATOM    671  CB  SER A 131      30.676 -24.509 -16.120  1.00 32.31           C  
ANISOU  671  CB  SER A 131     3968   4107   4200   -397   -290    -18       C  
ATOM    672  OG  SER A 131      30.140 -23.298 -16.618  1.00 34.59           O  
ANISOU  672  OG  SER A 131     4121   4413   4608   -406   -267     56       O  
ATOM    673  N   VAL A 132      29.547 -24.561 -13.154  1.00 41.62           N  
ANISOU  673  N   VAL A 132     5162   5239   5414   -325    -40     16       N  
ATOM    674  CA  VAL A 132      28.594 -24.078 -12.158  1.00 41.36           C  
ANISOU  674  CA  VAL A 132     5077   5180   5458   -305    126     72       C  
ATOM    675  C   VAL A 132      29.322 -23.465 -10.971  1.00 45.37           C  
ANISOU  675  C   VAL A 132     5699   5683   5856   -228    226    -48       C  
ATOM    676  O   VAL A 132      28.898 -22.440 -10.424  1.00 45.99           O  
ANISOU  676  O   VAL A 132     5742   5731   6000   -190    379    -58       O  
ATOM    677  CB  VAL A 132      27.664 -25.218 -11.716  1.00 45.66           C  
ANISOU  677  CB  VAL A 132     5635   5698   6016   -364    156    174       C  
ATOM    678  CG1 VAL A 132      26.778 -24.742 -10.583  1.00 38.22           C  
ANISOU  678  CG1 VAL A 132     4657   4727   5139   -329    375    226       C  
ATOM    679  CG2 VAL A 132      26.838 -25.684 -12.888  1.00 51.22           C  
ANISOU  679  CG2 VAL A 132     6215   6403   6841   -472     40    294       C  
ATOM    680  N   ALA A 133      30.424 -24.087 -10.551  1.00 35.14           N  
ANISOU  680  N   ALA A 133     4547   4408   4396   -206    136   -136       N  
ATOM    681  CA  ALA A 133      31.186 -23.578  -9.418  1.00 21.57           C  
ANISOU  681  CA  ALA A 133     2952   2697   2548   -160    177   -245       C  
ATOM    682  C   ALA A 133      31.746 -22.190  -9.706  1.00 40.17           C  
ANISOU  682  C   ALA A 133     5251   5052   4960   -141    189   -336       C  
ATOM    683  O   ALA A 133      31.478 -21.231  -8.977  1.00 60.97           O  
ANISOU  683  O   ALA A 133     7921   7647   7597   -126    325   -388       O  
ATOM    684  CB  ALA A 133      32.314 -24.550  -9.073  1.00 16.53           C  
ANISOU  684  CB  ALA A 133     2436   2088   1755   -140     33   -288       C  
ATOM    685  N   VAL A 134      32.537 -22.067 -10.772  1.00 34.55           N  
ANISOU  685  N   VAL A 134     4465   4368   4293   -146     68   -359       N  
ATOM    686  CA  VAL A 134      33.199 -20.794 -11.035  1.00 32.58           C  
ANISOU  686  CA  VAL A 134     4167   4111   4099   -140     75   -439       C  
ATOM    687  C   VAL A 134      32.187 -19.700 -11.347  1.00 39.30           C  
ANISOU  687  C   VAL A 134     4918   4903   5111   -137    214   -385       C  
ATOM    688  O   VAL A 134      32.391 -18.535 -10.983  1.00 45.02           O  
ANISOU  688  O   VAL A 134     5654   5576   5874   -126    298   -460       O  
ATOM    689  CB  VAL A 134      34.227 -20.954 -12.168  1.00 29.36           C  
ANISOU  689  CB  VAL A 134     3698   3744   3715   -144    -54   -454       C  
ATOM    690  CG1 VAL A 134      33.521 -21.065 -13.511  1.00 25.74           C  
ANISOU  690  CG1 VAL A 134     3141   3284   3355   -171    -63   -349       C  
ATOM    691  CG2 VAL A 134      35.193 -19.790 -12.159  1.00 34.14           C  
ANISOU  691  CG2 VAL A 134     4273   4344   4356   -148    -60   -548       C  
ATOM    692  N   LEU A 135      31.086 -20.042 -12.026  1.00 38.11           N  
ANISOU  692  N   LEU A 135     4661   4748   5070   -151    234   -248       N  
ATOM    693  CA  LEU A 135      30.062 -19.034 -12.288  1.00 33.74           C  
ANISOU  693  CA  LEU A 135     3980   4137   4705   -133    362   -160       C  
ATOM    694  C   LEU A 135      29.338 -18.621 -11.015  1.00 34.98           C  
ANISOU  694  C   LEU A 135     4187   4224   4879    -90    573   -181       C  
ATOM    695  O   LEU A 135      28.928 -17.462 -10.888  1.00 41.66           O  
ANISOU  695  O   LEU A 135     4982   4987   5859    -46    724   -180       O  
ATOM    696  CB  LEU A 135      29.057 -19.551 -13.320  1.00 35.63           C  
ANISOU  696  CB  LEU A 135     4075   4401   5062   -174    295     13       C  
ATOM    697  CG  LEU A 135      29.448 -19.405 -14.792  1.00 25.17           C  
ANISOU  697  CG  LEU A 135     2685   3115   3763   -215    143     61       C  
ATOM    698  CD1 LEU A 135      28.470 -20.160 -15.681  1.00 31.44           C  
ANISOU  698  CD1 LEU A 135     3388   3944   4615   -290     33    218       C  
ATOM    699  CD2 LEU A 135      29.502 -17.936 -15.180  1.00 22.71           C  
ANISOU  699  CD2 LEU A 135     2288   2753   3588   -176    213     81       C  
ATOM    700  N   THR A 136      29.176 -19.545 -10.064  1.00 27.01           N  
ANISOU  700  N   THR A 136     3295   3234   3735    -97    606   -197       N  
ATOM    701  CA  THR A 136      28.554 -19.183  -8.796  1.00 32.08           C  
ANISOU  701  CA  THR A 136     4029   3810   4351    -59    835   -228       C  
ATOM    702  C   THR A 136      29.458 -18.263  -7.990  1.00 34.63           C  
ANISOU  702  C   THR A 136     4525   4089   4543    -46    883   -412       C  
ATOM    703  O   THR A 136      28.995 -17.269  -7.418  1.00 45.34           O  
ANISOU  703  O   THR A 136     5921   5346   5959     -7   1097   -460       O  
ATOM    704  CB  THR A 136      28.215 -20.435  -7.994  1.00 35.44           C  
ANISOU  704  CB  THR A 136     4559   4268   4639    -81    855   -187       C  
ATOM    705  OG1 THR A 136      27.218 -21.192  -8.695  1.00 37.36           O  
ANISOU  705  OG1 THR A 136     4632   4527   5035   -115    830    -13       O  
ATOM    706  CG2 THR A 136      27.681 -20.054  -6.625  1.00 42.84           C  
ANISOU  706  CG2 THR A 136     5637   5138   5501    -45   1115   -232       C  
ATOM    707  N   LEU A 137      30.752 -18.579  -7.937  1.00 25.32           N  
ANISOU  707  N   LEU A 137     3448   2974   3198    -83    688   -516       N  
ATOM    708  CA  LEU A 137      31.692 -17.706  -7.245  1.00 22.74           C  
ANISOU  708  CA  LEU A 137     3269   2616   2756   -104    682   -687       C  
ATOM    709  C   LEU A 137      31.777 -16.339  -7.910  1.00 38.68           C  
ANISOU  709  C   LEU A 137     5188   4551   4957    -96    742   -723       C  
ATOM    710  O   LEU A 137      31.992 -15.329  -7.229  1.00 45.01           O  
ANISOU  710  O   LEU A 137     6113   5261   5726   -108    849   -853       O  
ATOM    711  CB  LEU A 137      33.071 -18.366  -7.195  1.00 17.92           C  
ANISOU  711  CB  LEU A 137     2722   2101   1986   -145    432   -751       C  
ATOM    712  CG  LEU A 137      33.150 -19.693  -6.434  1.00 18.18           C  
ANISOU  712  CG  LEU A 137     2880   2200   1828   -146    357   -713       C  
ATOM    713  CD1 LEU A 137      34.504 -20.363  -6.631  1.00 19.07           C  
ANISOU  713  CD1 LEU A 137     2990   2398   1858   -161    105   -736       C  
ATOM    714  CD2 LEU A 137      32.868 -19.482  -4.953  1.00 34.75           C  
ANISOU  714  CD2 LEU A 137     5213   4263   3729   -161    488   -790       C  
ATOM    715  N   SER A 138      31.621 -16.285  -9.234  1.00 43.07           N  
ANISOU  715  N   SER A 138     5546   5127   5693    -85    673   -608       N  
ATOM    716  CA  SER A 138      31.664 -15.002  -9.927  1.00 39.21           C  
ANISOU  716  CA  SER A 138     4960   4553   5387    -74    731   -608       C  
ATOM    717  C   SER A 138      30.446 -14.152  -9.595  1.00 42.23           C  
ANISOU  717  C   SER A 138     5309   4802   5934     -6    989   -558       C  
ATOM    718  O   SER A 138      30.573 -12.947  -9.346  1.00 48.15           O  
ANISOU  718  O   SER A 138     6110   5424   6760      7   1116   -645       O  
ATOM    719  CB  SER A 138      31.767 -15.227 -11.434  1.00 32.53           C  
ANISOU  719  CB  SER A 138     3935   3769   4655    -83    589   -478       C  
ATOM    720  OG  SER A 138      32.970 -15.901 -11.753  1.00 30.33           O  
ANISOU  720  OG  SER A 138     3688   3589   4248   -128    398   -535       O  
ATOM    721  N   PHE A 139      29.258 -14.758  -9.589  1.00 42.30           N  
ANISOU  721  N   PHE A 139     5224   4826   6023     36   1079   -413       N  
ATOM    722  CA  PHE A 139      28.059 -13.996  -9.267  1.00 44.34           C  
ANISOU  722  CA  PHE A 139     5412   4955   6480    119   1350   -341       C  
ATOM    723  C   PHE A 139      28.062 -13.539  -7.816  1.00 48.33           C  
ANISOU  723  C   PHE A 139     6155   5357   6852    140   1579   -512       C  
ATOM    724  O   PHE A 139      27.533 -12.465  -7.506  1.00 58.33           O  
ANISOU  724  O   PHE A 139     7432   6464   8266    210   1826   -536       O  
ATOM    725  CB  PHE A 139      26.811 -14.824  -9.563  1.00 55.36           C  
ANISOU  725  CB  PHE A 139     6625   6401   8008    143   1382   -133       C  
ATOM    726  CG  PHE A 139      26.500 -14.958 -11.029  1.00 61.72           C  
ANISOU  726  CG  PHE A 139     7195   7268   8987    123   1199     55       C  
ATOM    727  CD1 PHE A 139      27.475 -14.752 -11.996  1.00 59.99           C  
ANISOU  727  CD1 PHE A 139     6975   7098   8722     76    992     23       C  
ATOM    728  CD2 PHE A 139      25.221 -15.280 -11.439  1.00 71.33           C  
ANISOU  728  CD2 PHE A 139     8193   8496  10412    142   1234    271       C  
ATOM    729  CE1 PHE A 139      27.173 -14.880 -13.345  1.00 65.99           C  
ANISOU  729  CE1 PHE A 139     7560   7916   9598     47    828    194       C  
ATOM    730  CE2 PHE A 139      24.913 -15.407 -12.779  1.00 71.96           C  
ANISOU  730  CE2 PHE A 139     8080   8640  10622    102   1034    448       C  
ATOM    731  CZ  PHE A 139      25.888 -15.207 -13.734  1.00 69.47           C  
ANISOU  731  CZ  PHE A 139     7805   8371  10217     54    834    404       C  
ATOM    732  N   ILE A 140      28.649 -14.334  -6.916  1.00 50.12           N  
ANISOU  732  N   ILE A 140     6589   5661   6795     82   1506   -627       N  
ATOM    733  CA  ILE A 140      28.764 -13.912  -5.524  1.00 53.37           C  
ANISOU  733  CA  ILE A 140     7279   5984   7013     76   1692   -804       C  
ATOM    734  C   ILE A 140      29.611 -12.651  -5.422  1.00 59.53           C  
ANISOU  734  C   ILE A 140     8176   6661   7780     37   1675   -974       C  
ATOM    735  O   ILE A 140      29.223 -11.673  -4.774  1.00 65.41           O  
ANISOU  735  O   ILE A 140     9015   7287   8551     54   1840  -1008       O  
ATOM    736  CB  ILE A 140      29.343 -15.048  -4.665  1.00 46.23           C  
ANISOU  736  CB  ILE A 140     6575   5202   5788      8   1553   -866       C  
ATOM    737  CG1 ILE A 140      28.302 -16.151  -4.485  1.00 43.19           C  
ANISOU  737  CG1 ILE A 140     6118   4870   5421     44   1649   -700       C  
ATOM    738  CG2 ILE A 140      29.800 -14.512  -3.317  1.00 53.63           C  
ANISOU  738  CG2 ILE A 140     7819   6085   6475    -40   1614  -1044       C  
ATOM    739  CD1 ILE A 140      28.894 -17.485  -4.106  1.00 50.37           C  
ANISOU  739  CD1 ILE A 140     7140   5913   6085    -16   1440   -690       C  
ATOM    740  N   ALA A 141      30.787 -12.658  -6.057  1.00 55.70           N  
ANISOU  740  N   ALA A 141     7656   6248   7258    -37   1413  -1029       N  
ATOM    741  CA  ALA A 141      31.646 -11.480  -6.021  1.00 50.55           C  
ANISOU  741  CA  ALA A 141     7086   5504   6615    -98   1371  -1170       C  
ATOM    742  C   ALA A 141      30.974 -10.287  -6.691  1.00 48.68           C  
ANISOU  742  C   ALA A 141     6707   5115   6674    -27   1547  -1086       C  
ATOM    743  O   ALA A 141      31.055  -9.159  -6.193  1.00 55.75           O  
ANISOU  743  O   ALA A 141     7714   5891   7579    -46   1639  -1161       O  
ATOM    744  CB  ALA A 141      32.993 -11.788  -6.680  1.00 53.40           C  
ANISOU  744  CB  ALA A 141     7384   5978   6926   -187   1069  -1208       C  
ATOM    745  N   LEU A 142      30.298 -10.517  -7.820  1.00 42.54           N  
ANISOU  745  N   LEU A 142     5678   4347   6137     53   1571   -905       N  
ATOM    746  CA  LEU A 142      29.589  -9.428  -8.480  1.00 45.12           C  
ANISOU  746  CA  LEU A 142     5852   4535   6758    131   1720   -781       C  
ATOM    747  C   LEU A 142      28.488  -8.873  -7.589  1.00 53.22           C  
ANISOU  747  C   LEU A 142     6943   5450   7829    194   1973   -740       C  
ATOM    748  O   LEU A 142      28.196  -7.672  -7.630  1.00 51.16           O  
ANISOU  748  O   LEU A 142     6675   5041   7722    223   2105   -718       O  
ATOM    749  CB  LEU A 142      29.008  -9.910  -9.810  1.00 42.94           C  
ANISOU  749  CB  LEU A 142     5285   4344   6686    185   1620   -538       C  
ATOM    750  CG  LEU A 142      28.341  -8.885 -10.728  1.00 43.21           C  
ANISOU  750  CG  LEU A 142     5123   4251   7043    269   1718   -364       C  
ATOM    751  CD1 LEU A 142      29.362  -7.892 -11.265  1.00 35.54           C  
ANISOU  751  CD1 LEU A 142     4193   3195   6114    216   1646   -444       C  
ATOM    752  CD2 LEU A 142      27.629  -9.593 -11.872  1.00 48.82           C  
ANISOU  752  CD2 LEU A 142     5572   5093   7884    292   1570   -102       C  
ATOM    753  N   ASP A 143      27.864  -9.735  -6.787  1.00 66.77           N  
ANISOU  753  N   ASP A 143     8722   7225   9422    214   2056   -723       N  
ATOM    754  CA  ASP A 143      26.843  -9.282  -5.853  1.00 66.90           C  
ANISOU  754  CA  ASP A 143     8818   7130   9471    268   2313   -694       C  
ATOM    755  C   ASP A 143      27.457  -8.456  -4.731  1.00 63.26           C  
ANISOU  755  C   ASP A 143     8653   6579   8804    203   2381   -906       C  
ATOM    756  O   ASP A 143      26.955  -7.377  -4.394  1.00 60.58           O  
ANISOU  756  O   ASP A 143     8361   6079   8578    240   2583   -910       O  
ATOM    757  CB  ASP A 143      26.091 -10.489  -5.295  1.00 68.97           C  
ANISOU  757  CB  ASP A 143     9075   7481   9647    293   2378   -616       C  
ATOM    758  CG  ASP A 143      24.979 -10.094  -4.358  1.00 71.86           C  
ANISOU  758  CG  ASP A 143     9509   7726  10069    353   2661   -571       C  
ATOM    759  OD1 ASP A 143      24.021  -9.441  -4.821  1.00 73.48           O  
ANISOU  759  OD1 ASP A 143     9528   7821  10569    435   2796   -411       O  
ATOM    760  OD2 ASP A 143      25.064 -10.434  -3.159  1.00 70.70           O  
ANISOU  760  OD2 ASP A 143     9603   7589   9671    316   2743   -685       O  
ATOM    761  N   ARG A 144      28.551  -8.947  -4.143  1.00 64.38           N  
ANISOU  761  N   ARG A 144     8995   6822   8644    100   2198  -1075       N  
ATOM    762  CA  ARG A 144      29.199  -8.221  -3.058  1.00 62.66           C  
ANISOU  762  CA  ARG A 144     9057   6540   8211     18   2206  -1268       C  
ATOM    763  C   ARG A 144      29.812  -6.913  -3.543  1.00 62.77           C  
ANISOU  763  C   ARG A 144     9061   6436   8354    -19   2176  -1338       C  
ATOM    764  O   ARG A 144      29.840  -5.926  -2.799  1.00 71.27           O  
ANISOU  764  O   ARG A 144    10318   7379   9382    -46   2301  -1450       O  
ATOM    765  CB  ARG A 144      30.280  -9.095  -2.421  1.00 58.21           C  
ANISOU  765  CB  ARG A 144     8666   6132   7318    -90   1953  -1390       C  
ATOM    766  CG  ARG A 144      29.808 -10.466  -1.967  1.00 59.43           C  
ANISOU  766  CG  ARG A 144     8845   6410   7325    -65   1958  -1316       C  
ATOM    767  CD  ARG A 144      29.044 -10.411  -0.657  1.00 59.33           C  
ANISOU  767  CD  ARG A 144     9039   6332   7171    -47   2188  -1340       C  
ATOM    768  NE  ARG A 144      27.688  -9.902  -0.825  1.00 53.70           N  
ANISOU  768  NE  ARG A 144     8203   5480   6722     64   2501  -1218       N  
ATOM    769  CZ  ARG A 144      27.189  -8.878  -0.142  1.00 47.19           C  
ANISOU  769  CZ  ARG A 144     7509   4492   5930     86   2739  -1272       C  
ATOM    770  NH1 ARG A 144      27.936  -8.259   0.761  1.00 53.11           N  
ANISOU  770  NH1 ARG A 144     8533   5199   6448     -4   2699  -1460       N  
ATOM    771  NH2 ARG A 144      25.941  -8.482  -0.353  1.00 41.95           N  
ANISOU  771  NH2 ARG A 144     6699   3703   5538    196   3011  -1132       N  
ATOM    772  N   TRP A 145      30.301  -6.888  -4.785  1.00 55.24           N  
ANISOU  772  N   TRP A 145     7906   5517   7564    -24   2023  -1273       N  
ATOM    773  CA  TRP A 145      30.969  -5.696  -5.295  1.00 52.20           C  
ANISOU  773  CA  TRP A 145     7508   5023   7303    -71   1984  -1328       C  
ATOM    774  C   TRP A 145      29.984  -4.555  -5.519  1.00 58.69           C  
ANISOU  774  C   TRP A 145     8258   5654   8386     24   2251  -1232       C  
ATOM    775  O   TRP A 145      30.269  -3.405  -5.164  1.00 72.08           O  
ANISOU  775  O   TRP A 145    10086   7206  10097    -14   2331  -1336       O  
ATOM    776  CB  TRP A 145      31.721  -6.040  -6.578  1.00 47.19           C  
ANISOU  776  CB  TRP A 145     6678   4476   6776   -102   1766  -1267       C  
ATOM    777  CG  TRP A 145      32.511  -4.910  -7.165  1.00 44.69           C  
ANISOU  777  CG  TRP A 145     6337   4058   6585   -165   1710  -1309       C  
ATOM    778  CD1 TRP A 145      33.746  -4.477  -6.772  1.00 44.84           C  
ANISOU  778  CD1 TRP A 145     6494   4077   6466   -301   1547  -1470       C  
ATOM    779  CD2 TRP A 145      32.139  -4.098  -8.283  1.00 51.57           C  
ANISOU  779  CD2 TRP A 145     7021   4818   7754   -101   1800  -1164       C  
ATOM    780  NE1 TRP A 145      34.156  -3.431  -7.565  1.00 47.38           N  
ANISOU  780  NE1 TRP A 145     6731   4284   6987   -330   1553  -1446       N  
ATOM    781  CE2 TRP A 145      33.187  -3.181  -8.502  1.00 56.50           C  
ANISOU  781  CE2 TRP A 145     7695   5370   8403   -204   1711  -1257       C  
ATOM    782  CE3 TRP A 145      31.017  -4.052  -9.115  1.00 48.31           C  
ANISOU  782  CE3 TRP A 145     6395   4365   7595     30   1930   -943       C  
ATOM    783  CZ2 TRP A 145      33.145  -2.228  -9.521  1.00 62.71           C  
ANISOU  783  CZ2 TRP A 145     8342   6037   9446   -175   1771  -1142       C  
ATOM    784  CZ3 TRP A 145      30.976  -3.108 -10.124  1.00 55.76           C  
ANISOU  784  CZ3 TRP A 145     7198   5201   8787     61   1964   -819       C  
ATOM    785  CH2 TRP A 145      32.033  -2.208 -10.318  1.00 61.91           C  
ANISOU  785  CH2 TRP A 145     8046   5902   9574    -38   1897   -922       C  
ATOM    786  N   TYR A 146      28.820  -4.849  -6.103  1.00 59.03           N  
ANISOU  786  N   TYR A 146     8089   5691   8649    145   2380  -1024       N  
ATOM    787  CA  TYR A 146      27.782  -3.831  -6.232  1.00 61.57           C  
ANISOU  787  CA  TYR A 146     8328   5837   9230    244   2633   -902       C  
ATOM    788  C   TYR A 146      27.147  -3.485  -4.894  1.00 67.57           C  
ANISOU  788  C   TYR A 146     9301   6487   9887    266   2885   -991       C  
ATOM    789  O   TYR A 146      26.567  -2.405  -4.756  1.00 77.11           O  
ANISOU  789  O   TYR A 146    10523   7512  11264    323   3111   -961       O  
ATOM    790  CB  TYR A 146      26.702  -4.299  -7.213  1.00 55.37           C  
ANISOU  790  CB  TYR A 146     7236   5090   8712    355   2656   -626       C  
ATOM    791  CG  TYR A 146      27.005  -4.016  -8.667  1.00 51.33           C  
ANISOU  791  CG  TYR A 146     6501   4595   8406    365   2501   -484       C  
ATOM    792  CD1 TYR A 146      26.931  -2.725  -9.169  1.00 59.97           C  
ANISOU  792  CD1 TYR A 146     7541   5533   9711    394   2593   -420       C  
ATOM    793  CD2 TYR A 146      27.353  -5.040  -9.542  1.00 43.75           C  
ANISOU  793  CD2 TYR A 146     5395   3800   7426    346   2271   -406       C  
ATOM    794  CE1 TYR A 146      27.195  -2.455 -10.498  1.00 56.04           C  
ANISOU  794  CE1 TYR A 146     6853   5051   9390    401   2455   -271       C  
ATOM    795  CE2 TYR A 146      27.621  -4.779 -10.877  1.00 51.36           C  
ANISOU  795  CE2 TYR A 146     6174   4776   8563    352   2134   -265       C  
ATOM    796  CZ  TYR A 146      27.540  -3.483 -11.348  1.00 56.87           C  
ANISOU  796  CZ  TYR A 146     6826   5324   9459    378   2223   -192       C  
ATOM    797  OH  TYR A 146      27.804  -3.208 -12.671  1.00 57.67           O  
ANISOU  797  OH  TYR A 146     6757   5437   9716    382   2088    -34       O  
ATOM    798  N   ALA A 147      27.246  -4.375  -3.907  1.00 62.46           N  
ANISOU  798  N   ALA A 147     8826   5939   8967    223   2861  -1092       N  
ATOM    799  CA  ALA A 147      26.693  -4.088  -2.590  1.00 55.59           C  
ANISOU  799  CA  ALA A 147     8188   4965   7968    234   3104  -1182       C  
ATOM    800  C   ALA A 147      27.629  -3.206  -1.776  1.00 52.64           C  
ANISOU  800  C   ALA A 147     8112   4504   7385    125   3082  -1424       C  
ATOM    801  O   ALA A 147      27.193  -2.234  -1.150  1.00 51.83           O  
ANISOU  801  O   ALA A 147     8155   4217   7320    148   3328  -1485       O  
ATOM    802  CB  ALA A 147      26.404  -5.387  -1.841  1.00 52.66           C  
ANISOU  802  CB  ALA A 147     7895   4732   7381    227   3091  -1178       C  
ATOM    803  N   ILE A 148      28.917  -3.543  -1.755  1.00 56.36           N  
ANISOU  803  N   ILE A 148     8676   5100   7640      0   2785  -1559       N  
ATOM    804  CA  ILE A 148      29.850  -2.806  -0.915  1.00 56.38           C  
ANISOU  804  CA  ILE A 148     8958   5036   7429   -124   2715  -1784       C  
ATOM    805  C   ILE A 148      30.367  -1.560  -1.619  1.00 61.11           C  
ANISOU  805  C   ILE A 148     9504   5495   8220   -154   2695  -1819       C  
ATOM    806  O   ILE A 148      30.472  -0.490  -1.009  1.00 67.46           O  
ANISOU  806  O   ILE A 148    10506   6128   8996   -196   2822  -1953       O  
ATOM    807  CB  ILE A 148      31.005  -3.728  -0.498  1.00 51.35           C  
ANISOU  807  CB  ILE A 148     8429   4594   6486   -250   2384  -1893       C  
ATOM    808  CG1 ILE A 148      30.450  -5.054   0.021  1.00 47.52           C  
ANISOU  808  CG1 ILE A 148     7960   4252   5842   -208   2401  -1819       C  
ATOM    809  CG2 ILE A 148      31.865  -3.028   0.536  1.00 49.75           C  
ANISOU  809  CG2 ILE A 148     8525   4329   6049   -386   2301  -2114       C  
ATOM    810  CD1 ILE A 148      29.703  -4.937   1.322  1.00 58.56           C  
ANISOU  810  CD1 ILE A 148     9605   5564   7080   -191   2655  -1878       C  
ATOM    811  N   CYS A 149      30.702  -1.677  -2.905  1.00 50.30           N  
ANISOU  811  N   CYS A 149     7881   4186   7045   -139   2544  -1701       N  
ATOM    812  CA  CYS A 149      31.392  -0.600  -3.605  1.00 55.07           C  
ANISOU  812  CA  CYS A 149     8439   4677   7806   -191   2481  -1733       C  
ATOM    813  C   CYS A 149      30.458   0.368  -4.324  1.00 60.99           C  
ANISOU  813  C   CYS A 149     9032   5247   8893    -67   2736  -1580       C  
ATOM    814  O   CYS A 149      30.737   1.571  -4.362  1.00 77.43           O  
ANISOU  814  O   CYS A 149    11191   7155  11073    -98   2812  -1649       O  
ATOM    815  CB  CYS A 149      32.394  -1.184  -4.603  1.00 52.87           C  
ANISOU  815  CB  CYS A 149     7988   4552   7546   -258   2178  -1690       C  
ATOM    816  SG  CYS A 149      33.693  -2.188  -3.848  1.00 65.00           S  
ANISOU  816  SG  CYS A 149     9678   6290   8728   -413   1838  -1852       S  
ATOM    817  N   HIS A 150      29.365  -0.115  -4.909  1.00 54.71           N  
ANISOU  817  N   HIS A 150     8011   4487   8290     69   2854  -1363       N  
ATOM    818  CA  HIS A 150      28.440   0.726  -5.671  1.00 56.53           C  
ANISOU  818  CA  HIS A 150     8048   4566   8862    193   3059  -1172       C  
ATOM    819  C   HIS A 150      27.018   0.435  -5.202  1.00 65.70           C  
ANISOU  819  C   HIS A 150     9158   5690  10116    319   3314  -1042       C  
ATOM    820  O   HIS A 150      26.211  -0.170  -5.916  1.00 64.27           O  
ANISOU  820  O   HIS A 150     8721   5584  10115    411   3310   -816       O  
ATOM    821  CB  HIS A 150      28.632   0.493  -7.170  1.00 48.69           C  
ANISOU  821  CB  HIS A 150     6767   3662   8071    219   2883   -982       C  
ATOM    822  CG  HIS A 150      30.052   0.665  -7.618  1.00 49.52           C  
ANISOU  822  CG  HIS A 150     6917   3811   8089     89   2640  -1100       C  
ATOM    823  ND1 HIS A 150      30.609   1.898  -7.884  1.00 47.99           N  
ANISOU  823  ND1 HIS A 150     6774   3459   8001     42   2666  -1154       N  
ATOM    824  CD2 HIS A 150      31.039  -0.240  -7.814  1.00 50.26           C  
ANISOU  824  CD2 HIS A 150     7010   4079   8007    -10   2372  -1171       C  
ATOM    825  CE1 HIS A 150      31.870   1.745  -8.246  1.00 47.62           C  
ANISOU  825  CE1 HIS A 150     6745   3492   7858    -87   2422  -1243       C  
ATOM    826  NE2 HIS A 150      32.156   0.457  -8.210  1.00 50.41           N  
ANISOU  826  NE2 HIS A 150     7063   4048   8043   -118   2242  -1254       N  
ATOM    827  N   PRO A 151      26.680   0.902  -3.997  1.00 66.32           N  
ANISOU  827  N   PRO A 151     9480   5637  10083    320   3542  -1177       N  
ATOM    828  CA  PRO A 151      25.531   0.348  -3.257  1.00 76.12           C  
ANISOU  828  CA  PRO A 151    10735   6872  11315    405   3762  -1102       C  
ATOM    829  C   PRO A 151      24.160   0.524  -3.899  1.00 87.21           C  
ANISOU  829  C   PRO A 151    11856   8195  13086    561   3961   -822       C  
ATOM    830  O   PRO A 151      23.291  -0.320  -3.651  1.00102.18           O  
ANISOU  830  O   PRO A 151    13663  10156  15005    622   4035   -702       O  
ATOM    831  CB  PRO A 151      25.605   1.102  -1.919  1.00 75.09           C  
ANISOU  831  CB  PRO A 151    10954   6576  11001    361   3979  -1322       C  
ATOM    832  CG  PRO A 151      27.066   1.432  -1.773  1.00 73.44           C  
ANISOU  832  CG  PRO A 151    10942   6399  10565    204   3733  -1550       C  
ATOM    833  CD  PRO A 151      27.481   1.817  -3.163  1.00 65.27           C  
ANISOU  833  CD  PRO A 151     9655   5373   9772    214   3574  -1429       C  
ATOM    834  N   LEU A 152      23.919   1.550  -4.719  1.00 78.94           N  
ANISOU  834  N   LEU A 152    10651   7010  12331    624   4036   -696       N  
ATOM    835  CA  LEU A 152      22.547   1.860  -5.115  1.00 82.17           C  
ANISOU  835  CA  LEU A 152    10821   7311  13088    772   4253   -431       C  
ATOM    836  C   LEU A 152      22.289   1.713  -6.613  1.00 81.51           C  
ANISOU  836  C   LEU A 152    10382   7314  13273    822   4064   -156       C  
ATOM    837  O   LEU A 152      21.277   2.218  -7.110  1.00 84.12           O  
ANISOU  837  O   LEU A 152    10499   7540  13925    934   4206     82       O  
ATOM    838  CB  LEU A 152      22.160   3.268  -4.654  1.00 89.97           C  
ANISOU  838  CB  LEU A 152    11930   8026  14229    834   4577   -474       C  
ATOM    839  CG  LEU A 152      22.018   3.457  -3.138  1.00 81.78           C  
ANISOU  839  CG  LEU A 152    11230   6865  12976    814   4840   -692       C  
ATOM    840  CD1 LEU A 152      21.939   4.936  -2.763  1.00 68.30           C  
ANISOU  840  CD1 LEU A 152     9688   4878  11385    848   5123   -786       C  
ATOM    841  CD2 LEU A 152      20.805   2.699  -2.615  1.00 75.31           C  
ANISOU  841  CD2 LEU A 152    10332   6062  12222    906   5030   -552       C  
ATOM    842  N   LEU A 153      23.170   1.035  -7.347  1.00 83.59           N  
ANISOU  842  N   LEU A 153    10582   7764  13416    740   3746   -173       N  
ATOM    843  CA  LEU A 153      22.922   0.814  -8.768  1.00 83.34           C  
ANISOU  843  CA  LEU A 153    10237   7824  13605    777   3553     90       C  
ATOM    844  C   LEU A 153      21.935  -0.334  -8.988  1.00 77.23           C  
ANISOU  844  C   LEU A 153     9258   7180  12904    827   3487    297       C  
ATOM    845  O   LEU A 153      20.832  -0.131  -9.508  1.00 70.62           O  
ANISOU  845  O   LEU A 153     8189   6292  12352    919   3555    562       O  
ATOM    846  CB  LEU A 153      24.244   0.546  -9.492  1.00 81.46           C  
ANISOU  846  CB  LEU A 153    10018   7718  13217    672   3259     -5       C  
ATOM    847  CG  LEU A 153      24.907   1.777 -10.112  1.00 81.84           C  
ANISOU  847  CG  LEU A 153    10075   7642  13380    654   3256    -22       C  
ATOM    848  CD1 LEU A 153      25.214   2.818  -9.048  1.00 79.47           C  
ANISOU  848  CD1 LEU A 153    10049   7145  13003    630   3479   -252       C  
ATOM    849  CD2 LEU A 153      26.169   1.374 -10.851  1.00 83.14           C  
ANISOU  849  CD2 LEU A 153    10238   7941  13409    551   2968    -93       C  
ATOM    850  N   PHE A 154      22.316  -1.545  -8.593  1.00 76.37           N  
ANISOU  850  N   PHE A 154     9233   7239  12546    763   3346    187       N  
ATOM    851  CA  PHE A 154      21.486  -2.734  -8.733  1.00 72.68           C  
ANISOU  851  CA  PHE A 154     8599   6901  12115    793   3265    353       C  
ATOM    852  C   PHE A 154      21.114  -3.268  -7.357  1.00 75.40           C  
ANISOU  852  C   PHE A 154     9128   7230  12289    799   3456    221       C  
ATOM    853  O   PHE A 154      21.914  -3.200  -6.418  1.00 77.28           O  
ANISOU  853  O   PHE A 154     9649   7458  12255    732   3509    -39       O  
ATOM    854  CB  PHE A 154      22.204  -3.828  -9.532  1.00 69.13           C  
ANISOU  854  CB  PHE A 154     8072   6669  11526    719   2932    361       C  
ATOM    855  CG  PHE A 154      22.552  -3.427 -10.937  1.00 68.25           C  
ANISOU  855  CG  PHE A 154     7784   6587  11560    709   2733    509       C  
ATOM    856  CD1 PHE A 154      23.780  -2.854 -11.225  1.00 69.43           C  
ANISOU  856  CD1 PHE A 154     8047   6721  11614    645   2654    355       C  
ATOM    857  CD2 PHE A 154      21.656  -3.633 -11.972  1.00 67.14           C  
ANISOU  857  CD2 PHE A 154     7373   6493  11642    753   2611    809       C  
ATOM    858  CE1 PHE A 154      24.104  -2.489 -12.516  1.00 66.75           C  
ANISOU  858  CE1 PHE A 154     7554   6405  11402    637   2487    502       C  
ATOM    859  CE2 PHE A 154      21.974  -3.270 -13.266  1.00 69.46           C  
ANISOU  859  CE2 PHE A 154     7528   6823  12039    735   2421    957       C  
ATOM    860  CZ  PHE A 154      23.201  -2.697 -13.538  1.00 69.48           C  
ANISOU  860  CZ  PHE A 154     7645   6804  11948    682   2373    805       C  
ATOM    861  N   LYS A 155      19.899  -3.798  -7.239  1.00 78.30           N  
ANISOU  861  N   LYS A 155     9340   7598  12814    872   3548    410       N  
ATOM    862  CA  LYS A 155      19.407  -4.365  -5.991  1.00 92.28           C  
ANISOU  862  CA  LYS A 155    11260   9352  14452    886   3746    326       C  
ATOM    863  C   LYS A 155      19.321  -5.879  -6.123  1.00 96.40           C  
ANISOU  863  C   LYS A 155    11693  10077  14857    849   3546    379       C  
ATOM    864  O   LYS A 155      18.724  -6.390  -7.076  1.00 95.32           O  
ANISOU  864  O   LYS A 155    11283  10024  14911    873   3377    609       O  
ATOM    865  CB  LYS A 155      18.033  -3.793  -5.633  1.00104.22           C  
ANISOU  865  CB  LYS A 155    12665  10682  16253   1006   4053    499       C  
ATOM    866  CG  LYS A 155      17.356  -4.479  -4.451  1.00109.44           C  
ANISOU  866  CG  LYS A 155    13438  11327  16818   1032   4267    462       C  
ATOM    867  CD  LYS A 155      17.784  -3.872  -3.122  1.00114.69           C  
ANISOU  867  CD  LYS A 155    14469  11862  17247   1009   4531    198       C  
ATOM    868  CE  LYS A 155      16.998  -4.461  -1.953  1.00119.63           C  
ANISOU  868  CE  LYS A 155    15208  12449  17798   1046   4784    188       C  
ATOM    869  NZ  LYS A 155      17.385  -5.865  -1.626  1.00120.64           N  
ANISOU  869  NZ  LYS A 155    15406  12784  17647    967   4602    119       N  
ATOM    870  N   SER A 156      19.916  -6.588  -5.170  1.00 95.14           N  
ANISOU  870  N   SER A 156    11774   9999  14378    783   3554    174       N  
ATOM    871  CA  SER A 156      19.921  -8.044  -5.170  1.00 86.54           C  
ANISOU  871  CA  SER A 156    10635   9097  13150    741   3389    201       C  
ATOM    872  C   SER A 156      18.818  -8.567  -4.260  1.00 83.63           C  
ANISOU  872  C   SER A 156    10271   8686  12819    795   3618    277       C  
ATOM    873  O   SER A 156      18.684  -8.117  -3.117  1.00 83.07           O  
ANISOU  873  O   SER A 156    10428   8492  12641    812   3884    153       O  
ATOM    874  CB  SER A 156      21.280  -8.583  -4.729  1.00 85.60           C  
ANISOU  874  CB  SER A 156    10766   9103  12657    633   3240    -46       C  
ATOM    875  OG  SER A 156      21.425  -8.515  -3.322  1.00 89.49           O  
ANISOU  875  OG  SER A 156    11563   9538  12903    608   3435   -228       O  
ATOM    876  N   THR A 157      18.022  -9.499  -4.772  1.00 82.77           N  
ANISOU  876  N   THR A 157     9914   8674  12861    816   3515    482       N  
ATOM    877  CA  THR A 157      16.969 -10.131  -3.991  1.00 82.76           C  
ANISOU  877  CA  THR A 157     9882   8649  12913    860   3710    572       C  
ATOM    878  C   THR A 157      17.126 -11.646  -4.019  1.00 92.49           C  
ANISOU  878  C   THR A 157    11079  10082  13980    786   3523    585       C  
ATOM    879  O   THR A 157      17.914 -12.203  -4.788  1.00 97.51           O  
ANISOU  879  O   THR A 157    11669  10869  14510    712   3238    560       O  
ATOM    880  CB  THR A 157      15.584  -9.749  -4.524  1.00 76.93           C  
ANISOU  880  CB  THR A 157     8838   7808  12583    962   3801    851       C  
ATOM    881  OG1 THR A 157      15.546  -9.963  -5.940  1.00 72.48           O  
ANISOU  881  OG1 THR A 157     8003   7354  12182    939   3482   1027       O  
ATOM    882  CG2 THR A 157      15.293  -8.292  -4.234  1.00 75.79           C  
ANISOU  882  CG2 THR A 157     8756   7437  12604   1045   4072    842       C  
ATOM    883  N   ALA A 158      16.357 -12.314  -3.157  1.00 98.13           N  
ANISOU  883  N   ALA A 158    11818  10787  14679    805   3706    630       N  
ATOM    884  CA  ALA A 158      16.309 -13.768  -3.208  1.00100.34           C  
ANISOU  884  CA  ALA A 158    12029  11242  14852    735   3552    684       C  
ATOM    885  C   ALA A 158      15.573 -14.243  -4.453  1.00101.99           C  
ANISOU  885  C   ALA A 158    11869  11537  15345    730   3320    932       C  
ATOM    886  O   ALA A 158      15.876 -15.317  -4.984  1.00 97.50           O  
ANISOU  886  O   ALA A 158    11223  11137  14686    638   3073    964       O  
ATOM    887  CB  ALA A 158      15.660 -14.323  -1.938  1.00107.31           C  
ANISOU  887  CB  ALA A 158    13042  12086  15646    751   3822    677       C  
ATOM    888  N   ARG A 159      14.612 -13.447  -4.935  1.00110.98           N  
ANISOU  888  N   ARG A 159    12790  12558  16820    819   3388   1115       N  
ATOM    889  CA  ARG A 159      13.900 -13.777  -6.166  1.00114.45           C  
ANISOU  889  CA  ARG A 159    12893  13075  17518    804   3136   1362       C  
ATOM    890  C   ARG A 159      14.811 -13.686  -7.383  1.00110.36           C  
ANISOU  890  C   ARG A 159    12338  12665  16929    735   2799   1340       C  
ATOM    891  O   ARG A 159      14.744 -14.532  -8.284  1.00111.51           O  
ANISOU  891  O   ARG A 159    12325  12960  17083    649   2507   1448       O  
ATOM    892  CB  ARG A 159      12.706 -12.832  -6.321  1.00120.68           C  
ANISOU  892  CB  ARG A 159    13481  13694  18677    920   3306   1569       C  
ATOM    893  CG  ARG A 159      12.016 -12.855  -7.674  1.00123.84           C  
ANISOU  893  CG  ARG A 159    13554  14150  19349    906   3032   1837       C  
ATOM    894  CD  ARG A 159      11.133 -14.057  -7.888  1.00129.85           C  
ANISOU  894  CD  ARG A 159    14099  15030  20209    843   2896   2010       C  
ATOM    895  NE  ARG A 159      10.679 -14.092  -9.272  1.00137.78           N  
ANISOU  895  NE  ARG A 159    14842  16108  21401    794   2572   2238       N  
ATOM    896  CZ  ARG A 159      11.391 -14.605 -10.268  1.00139.10           C  
ANISOU  896  CZ  ARG A 159    15016  16433  21401    676   2218   2211       C  
ATOM    897  NH1 ARG A 159      12.582 -15.134 -10.023  1.00132.21           N  
ANISOU  897  NH1 ARG A 159    14371  15659  20203    604   2153   1974       N  
ATOM    898  NH2 ARG A 159      10.911 -14.596 -11.504  1.00143.20           N  
ANISOU  898  NH2 ARG A 159    15325  17010  22074    622   1933   2427       N  
ATOM    899  N   ARG A 160      15.674 -12.672  -7.424  1.00 99.20           N  
ANISOU  899  N   ARG A 160    11080  11173  15436    760   2840   1199       N  
ATOM    900  CA  ARG A 160      16.631 -12.544  -8.516  1.00 90.98           C  
ANISOU  900  CA  ARG A 160    10025  10227  14315    697   2551   1165       C  
ATOM    901  C   ARG A 160      17.787 -13.529  -8.398  1.00 96.59           C  
ANISOU  901  C   ARG A 160    10895  11098  14705    592   2397    983       C  
ATOM    902  O   ARG A 160      18.380 -13.902  -9.415  1.00105.18           O  
ANISOU  902  O   ARG A 160    11916  12311  15737    519   2115   1003       O  
ATOM    903  CB  ARG A 160      17.147 -11.107  -8.583  1.00 86.17           C  
ANISOU  903  CB  ARG A 160     9518   9471  13751    752   2661   1084       C  
ATOM    904  CG  ARG A 160      16.140 -10.140  -9.185  1.00 85.81           C  
ANISOU  904  CG  ARG A 160     9261   9292  14051    836   2718   1318       C  
ATOM    905  CD  ARG A 160      16.560  -8.690  -9.005  1.00 84.92           C  
ANISOU  905  CD  ARG A 160     9273   9004  13991    890   2904   1229       C  
ATOM    906  NE  ARG A 160      15.757  -7.792  -9.830  1.00 87.01           N  
ANISOU  906  NE  ARG A 160     9316   9163  14582    954   2904   1477       N  
ATOM    907  CZ  ARG A 160      14.531  -7.382  -9.520  1.00 95.58           C  
ANISOU  907  CZ  ARG A 160    10262  10112  15943   1047   3120   1655       C  
ATOM    908  NH1 ARG A 160      13.956  -7.790  -8.397  1.00102.98           N  
ANISOU  908  NH1 ARG A 160    11266  10998  16865   1089   3363   1605       N  
ATOM    909  NH2 ARG A 160      13.877  -6.566 -10.335  1.00 96.55           N  
ANISOU  909  NH2 ARG A 160    10175  10149  16362   1099   3100   1894       N  
ATOM    910  N   ALA A 161      18.119 -13.958  -7.179  1.00 90.90           N  
ANISOU  910  N   ALA A 161    10395  10374  13767    580   2581    815       N  
ATOM    911  CA  ALA A 161      19.210 -14.911  -7.010  1.00 79.87           C  
ANISOU  911  CA  ALA A 161     9155   9121  12071    482   2451    661       C  
ATOM    912  C   ALA A 161      18.858 -16.259  -7.624  1.00 77.17           C  
ANISOU  912  C   ALA A 161     8641   8935  11747    394   2232    802       C  
ATOM    913  O   ALA A 161      19.664 -16.849  -8.352  1.00 78.83           O  
ANISOU  913  O   ALA A 161     8844   9268  11841    304   1993    772       O  
ATOM    914  CB  ALA A 161      19.566 -15.062  -5.531  1.00 80.13           C  
ANISOU  914  CB  ALA A 161     9487   9111  11847    483   2688    474       C  
ATOM    915  N   LEU A 162      17.657 -16.768  -7.336  1.00 77.23           N  
ANISOU  915  N   LEU A 162     8514   8929  11902    407   2315    955       N  
ATOM    916  CA  LEU A 162      17.248 -18.048  -7.908  1.00 74.48           C  
ANISOU  916  CA  LEU A 162     8010   8713  11576    299   2099   1088       C  
ATOM    917  C   LEU A 162      17.168 -17.976  -9.426  1.00 71.91           C  
ANISOU  917  C   LEU A 162     7485   8457  11381    248   1779   1220       C  
ATOM    918  O   LEU A 162      17.370 -18.990 -10.107  1.00 81.93           O  
ANISOU  918  O   LEU A 162     8709   9848  12570    121   1528   1257       O  
ATOM    919  CB  LEU A 162      15.905 -18.483  -7.317  1.00 79.99           C  
ANISOU  919  CB  LEU A 162     8584   9368  12441    324   2260   1235       C  
ATOM    920  CG  LEU A 162      15.916 -18.785  -5.818  1.00 87.28           C  
ANISOU  920  CG  LEU A 162     9725  10240  13198    351   2563   1124       C  
ATOM    921  CD1 LEU A 162      14.545 -18.528  -5.210  1.00 94.79           C  
ANISOU  921  CD1 LEU A 162    10553  11078  14385    439   2816   1261       C  
ATOM    922  CD2 LEU A 162      16.357 -20.219  -5.572  1.00 86.24           C  
ANISOU  922  CD2 LEU A 162     9689  10231  12847    220   2462   1092       C  
ATOM    923  N   GLY A 163      16.877 -16.796  -9.976  1.00 62.28           N  
ANISOU  923  N   GLY A 163     6168   7148  10345    334   1782   1296       N  
ATOM    924  CA  GLY A 163      16.911 -16.650 -11.421  1.00 63.69           C  
ANISOU  924  CA  GLY A 163     6207   7392  10599    282   1478   1417       C  
ATOM    925  C   GLY A 163      18.322 -16.720 -11.968  1.00 62.89           C  
ANISOU  925  C   GLY A 163     6245   7375  10274    214   1306   1264       C  
ATOM    926  O   GLY A 163      18.556 -17.284 -13.040  1.00 67.07           O  
ANISOU  926  O   GLY A 163     6726   8015  10744    109   1019   1319       O  
ATOM    927  N   SER A 164      19.281 -16.145 -11.243  1.00 55.97           N  
ANISOU  927  N   SER A 164     5557   6441   9266    266   1480   1067       N  
ATOM    928  CA  SER A 164      20.676 -16.278 -11.645  1.00 52.90           C  
ANISOU  928  CA  SER A 164     5293   6131   8675    201   1340    916       C  
ATOM    929  C   SER A 164      21.147 -17.719 -11.513  1.00 57.25           C  
ANISOU  929  C   SER A 164     5911   6808   9035     78   1226    863       C  
ATOM    930  O   SER A 164      21.890 -18.219 -12.367  1.00 68.69           O  
ANISOU  930  O   SER A 164     7370   8349  10380    -18    994    844       O  
ATOM    931  CB  SER A 164      21.557 -15.351 -10.812  1.00 53.22           C  
ANISOU  931  CB  SER A 164     5527   6073   8622    274   1558    711       C  
ATOM    932  OG  SER A 164      21.052 -14.030 -10.818  1.00 58.97           O  
ANISOU  932  OG  SER A 164     6215   6651   9540    376   1697    763       O  
ATOM    933  N   ILE A 165      20.737 -18.398 -10.441  1.00 44.91           N  
ANISOU  933  N   ILE A 165     4411   5233   7419     77   1398    843       N  
ATOM    934  CA  ILE A 165      21.161 -19.778 -10.238  1.00 42.00           C  
ANISOU  934  CA  ILE A 165     4126   4954   6879    -43   1314    813       C  
ATOM    935  C   ILE A 165      20.658 -20.663 -11.369  1.00 51.87           C  
ANISOU  935  C   ILE A 165     5229   6287   8194   -165   1019    961       C  
ATOM    936  O   ILE A 165      21.343 -21.603 -11.791  1.00 65.37           O  
ANISOU  936  O   ILE A 165     7011   8062   9766   -285    839    928       O  
ATOM    937  CB  ILE A 165      20.682 -20.286  -8.867  1.00 44.32           C  
ANISOU  937  CB  ILE A 165     4528   5207   7104    -19   1568    793       C  
ATOM    938  CG1 ILE A 165      21.538 -19.684  -7.752  1.00 44.22           C  
ANISOU  938  CG1 ILE A 165     4775   5136   6890     55   1806    588       C  
ATOM    939  CG2 ILE A 165      20.719 -21.805  -8.826  1.00 42.41           C  
ANISOU  939  CG2 ILE A 165     4322   5035   6756   -154   1457    844       C  
ATOM    940  CD1 ILE A 165      20.810 -19.517  -6.447  1.00 45.49           C  
ANISOU  940  CD1 ILE A 165     5049   5211   7026    130   2094    570       C  
ATOM    941  N   LEU A 166      19.449 -20.392 -11.870  1.00 56.06           N  
ANISOU  941  N   LEU A 166     5572   6800   8929   -140    965   1126       N  
ATOM    942  CA  LEU A 166      18.961 -21.142 -13.021  1.00 57.97           C  
ANISOU  942  CA  LEU A 166     5706   7115   9205   -264    669   1252       C  
ATOM    943  C   LEU A 166      19.691 -20.751 -14.298  1.00 61.83           C  
ANISOU  943  C   LEU A 166     6218   7653   9623   -303    428   1235       C  
ATOM    944  O   LEU A 166      19.804 -21.563 -15.219  1.00 71.08           O  
ANISOU  944  O   LEU A 166     7414   8892  10699   -434    176   1259       O  
ATOM    945  CB  LEU A 166      17.453 -20.946 -13.184  1.00 59.54           C  
ANISOU  945  CB  LEU A 166     5695   7279   9650   -231    680   1451       C  
ATOM    946  CG  LEU A 166      16.581 -21.761 -12.230  1.00 58.87           C  
ANISOU  946  CG  LEU A 166     5563   7173   9632   -252    836   1505       C  
ATOM    947  CD1 LEU A 166      15.178 -21.175 -12.152  1.00 69.11           C  
ANISOU  947  CD1 LEU A 166     6642   8401  11216   -165    938   1693       C  
ATOM    948  CD2 LEU A 166      16.535 -23.216 -12.674  1.00 53.02           C  
ANISOU  948  CD2 LEU A 166     4846   6507   8792   -435    616   1525       C  
ATOM    949  N   GLY A 167      20.188 -19.516 -14.372  1.00 54.91           N  
ANISOU  949  N   GLY A 167     5354   6729   8779   -196    512   1188       N  
ATOM    950  CA  GLY A 167      20.993 -19.124 -15.515  1.00 53.95           C  
ANISOU  950  CA  GLY A 167     5274   6651   8572   -232    314   1165       C  
ATOM    951  C   GLY A 167      22.369 -19.759 -15.492  1.00 58.58           C  
ANISOU  951  C   GLY A 167     6028   7292   8936   -310    248    994       C  
ATOM    952  O   GLY A 167      22.930 -20.090 -16.542  1.00 59.85           O  
ANISOU  952  O   GLY A 167     6248   7516   8978   -400     27    982       O  
ATOM    953  N   ILE A 168      22.940 -19.922 -14.297  1.00 53.43           N  
ANISOU  953  N   ILE A 168     5478   6608   8214   -274    447    860       N  
ATOM    954  CA  ILE A 168      24.256 -20.543 -14.190  1.00 46.00           C  
ANISOU  954  CA  ILE A 168     4797   5702   6981   -301    351    658       C  
ATOM    955  C   ILE A 168      24.221 -21.970 -14.714  1.00 52.69           C  
ANISOU  955  C   ILE A 168     5699   6603   7716   -432    149    683       C  
ATOM    956  O   ILE A 168      25.180 -22.444 -15.336  1.00 59.74           O  
ANISOU  956  O   ILE A 168     6740   7531   8427   -475     -8    580       O  
ATOM    957  CB  ILE A 168      24.752 -20.492 -12.735  1.00 34.90           C  
ANISOU  957  CB  ILE A 168     3565   4250   5445   -221    556    499       C  
ATOM    958  CG1 ILE A 168      25.033 -19.048 -12.332  1.00 38.15           C  
ANISOU  958  CG1 ILE A 168     3985   4589   5921   -112    730    422       C  
ATOM    959  CG2 ILE A 168      25.984 -21.355 -12.574  1.00 35.71           C  
ANISOU  959  CG2 ILE A 168     3895   4396   5279   -253    429    339       C  
ATOM    960  CD1 ILE A 168      25.234 -18.865 -10.858  1.00 41.83           C  
ANISOU  960  CD1 ILE A 168     4623   4998   6274    -49    954    286       C  
ATOM    961  N   TRP A 169      23.119 -22.677 -14.471  1.00 44.41           N  
ANISOU  961  N   TRP A 169     4537   5550   6789   -501    168    820       N  
ATOM    962  CA  TRP A 169      22.996 -24.041 -14.966  1.00 36.85           C  
ANISOU  962  CA  TRP A 169     3642   4617   5744   -648    -21    845       C  
ATOM    963  C   TRP A 169      22.689 -24.081 -16.458  1.00 43.14           C  
ANISOU  963  C   TRP A 169     4363   5461   6568   -757   -275    938       C  
ATOM    964  O   TRP A 169      23.202 -24.947 -17.174  1.00 52.87           O  
ANISOU  964  O   TRP A 169     5743   6708   7637   -866   -456    875       O  
ATOM    965  CB  TRP A 169      21.929 -24.792 -14.175  1.00 26.00           C  
ANISOU  965  CB  TRP A 169     2175   3211   4492   -702     87    961       C  
ATOM    966  CG  TRP A 169      22.434 -25.280 -12.857  1.00 34.85           C  
ANISOU  966  CG  TRP A 169     3493   4293   5456   -634    265    840       C  
ATOM    967  CD1 TRP A 169      22.325 -24.652 -11.651  1.00 40.72           C  
ANISOU  967  CD1 TRP A 169     4255   5002   6217   -515    534    810       C  
ATOM    968  CD2 TRP A 169      23.144 -26.500 -12.613  1.00 34.64           C  
ANISOU  968  CD2 TRP A 169     3694   4250   5216   -683    185    739       C  
ATOM    969  NE1 TRP A 169      22.919 -25.410 -10.669  1.00 47.85           N  
ANISOU  969  NE1 TRP A 169     5388   5885   6908   -498    602    705       N  
ATOM    970  CE2 TRP A 169      23.429 -26.549 -11.234  1.00 36.93           C  
ANISOU  970  CE2 TRP A 169     4121   4511   5399   -591    389    672       C  
ATOM    971  CE3 TRP A 169      23.562 -27.557 -13.427  1.00 41.25           C  
ANISOU  971  CE3 TRP A 169     4649   5082   5942   -791    -31    701       C  
ATOM    972  CZ2 TRP A 169      24.114 -27.614 -10.652  1.00 37.31           C  
ANISOU  972  CZ2 TRP A 169     4393   4534   5248   -599    361    595       C  
ATOM    973  CZ3 TRP A 169      24.242 -28.613 -12.848  1.00 39.42           C  
ANISOU  973  CZ3 TRP A 169     4637   4806   5535   -787    -30    612       C  
ATOM    974  CH2 TRP A 169      24.511 -28.634 -11.474  1.00 36.81           C  
ANISOU  974  CH2 TRP A 169     4413   4456   5117   -688    154    573       C  
ATOM    975  N   ALA A 170      21.846 -23.168 -16.944  1.00 46.68           N  
ANISOU  975  N   ALA A 170     4657   5917   7161   -694   -282   1061       N  
ATOM    976  CA  ALA A 170      21.554 -23.139 -18.371  1.00 49.64           C  
ANISOU  976  CA  ALA A 170     5032   6333   7496   -767   -519   1142       C  
ATOM    977  C   ALA A 170      22.818 -22.886 -19.181  1.00 54.34           C  
ANISOU  977  C   ALA A 170     5780   6960   7908   -784   -617   1029       C  
ATOM    978  O   ALA A 170      22.986 -23.438 -20.275  1.00 59.58           O  
ANISOU  978  O   ALA A 170     6564   7653   8419   -891   -809   1022       O  
ATOM    979  CB  ALA A 170      20.499 -22.075 -18.674  1.00 53.80           C  
ANISOU  979  CB  ALA A 170     5363   6845   8231   -687   -500   1324       C  
ATOM    980  N   VAL A 171      23.717 -22.045 -18.665  1.00 53.48           N  
ANISOU  980  N   VAL A 171     5679   6836   7806   -684   -475    937       N  
ATOM    981  CA  VAL A 171      24.972 -21.779 -19.361  1.00 47.16           C  
ANISOU  981  CA  VAL A 171     5007   6063   6849   -696   -550    828       C  
ATOM    982  C   VAL A 171      25.929 -22.957 -19.217  1.00 42.57           C  
ANISOU  982  C   VAL A 171     4667   5478   6031   -729   -579    644       C  
ATOM    983  O   VAL A 171      26.502 -23.436 -20.202  1.00 32.88           O  
ANISOU  983  O   VAL A 171     3583   4272   4637   -802   -714    589       O  
ATOM    984  CB  VAL A 171      25.601 -20.474 -18.845  1.00 38.41           C  
ANISOU  984  CB  VAL A 171     3879   4917   5799   -543   -368    760       C  
ATOM    985  CG1 VAL A 171      26.963 -20.256 -19.488  1.00 37.17           C  
ANISOU  985  CG1 VAL A 171     3888   4779   5457   -530   -411    623       C  
ATOM    986  CG2 VAL A 171      24.674 -19.309 -19.120  1.00 24.62           C  
ANISOU  986  CG2 VAL A 171     1931   3143   4280   -485   -329    941       C  
ATOM    987  N   SER A 172      26.117 -23.441 -17.987  1.00 43.75           N  
ANISOU  987  N   SER A 172     4875   5589   6160   -668   -443    554       N  
ATOM    988  CA  SER A 172      27.060 -24.530 -17.759  1.00 37.11           C  
ANISOU  988  CA  SER A 172     4248   4730   5124   -672   -463    401       C  
ATOM    989  C   SER A 172      26.692 -25.770 -18.564  1.00 41.93           C  
ANISOU  989  C   SER A 172     4946   5330   5658   -823   -630    430       C  
ATOM    990  O   SER A 172      27.571 -26.442 -19.118  1.00 47.03           O  
ANISOU  990  O   SER A 172     5776   5959   6134   -842   -691    315       O  
ATOM    991  CB  SER A 172      27.121 -24.864 -16.269  1.00 31.36           C  
ANISOU  991  CB  SER A 172     3560   3964   4390   -596   -309    345       C  
ATOM    992  OG  SER A 172      27.576 -23.756 -15.515  1.00 40.09           O  
ANISOU  992  OG  SER A 172     4640   5069   5523   -476   -164    283       O  
ATOM    993  N   LEU A 173      25.400 -26.096 -18.633  1.00 42.74           N  
ANISOU  993  N   LEU A 173     4916   5429   5892   -937   -698    582       N  
ATOM    994  CA  LEU A 173      24.975 -27.251 -19.418  1.00 34.96           C  
ANISOU  994  CA  LEU A 173     4028   4423   4834  -1103   -872    604       C  
ATOM    995  C   LEU A 173      25.245 -27.042 -20.903  1.00 36.83           C  
ANISOU  995  C   LEU A 173     4369   4695   4931  -1136  -1003    586       C  
ATOM    996  O   LEU A 173      25.582 -27.993 -21.618  1.00 45.54           O  
ANISOU  996  O   LEU A 173     5679   5760   5864  -1209  -1080    502       O  
ATOM    997  CB  LEU A 173      23.491 -27.535 -19.179  1.00 32.53           C  
ANISOU  997  CB  LEU A 173     3558   4111   4692  -1158   -881    763       C  
ATOM    998  CG  LEU A 173      23.107 -28.001 -17.772  1.00 36.99           C  
ANISOU  998  CG  LEU A 173     4055   4625   5373  -1149   -727    794       C  
ATOM    999  CD1 LEU A 173      21.620 -27.790 -17.517  1.00 36.39           C  
ANISOU  999  CD1 LEU A 173     3754   4566   5509  -1148   -683    966       C  
ATOM   1000  CD2 LEU A 173      23.490 -29.458 -17.565  1.00 41.48           C  
ANISOU 1000  CD2 LEU A 173     4834   5111   5813  -1245   -769    706       C  
ATOM   1001  N   ALA A 174      25.111 -25.804 -21.382  1.00 37.92           N  
ANISOU 1001  N   ALA A 174     4382   4890   5137  -1083  -1008    672       N  
ATOM   1002  CA  ALA A 174      25.279 -25.526 -22.806  1.00 46.87           C  
ANISOU 1002  CA  ALA A 174     5613   6056   6139  -1134  -1128    693       C  
ATOM   1003  C   ALA A 174      26.746 -25.565 -23.219  1.00 46.63           C  
ANISOU 1003  C   ALA A 174     5781   6021   5914  -1101  -1091    522       C  
ATOM   1004  O   ALA A 174      27.129 -26.302 -24.134  1.00 46.48           O  
ANISOU 1004  O   ALA A 174     5973   5979   5708  -1168  -1146    445       O  
ATOM   1005  CB  ALA A 174      24.670 -24.166 -23.147  1.00 48.23           C  
ANISOU 1005  CB  ALA A 174     5589   6274   6461  -1087  -1143    863       C  
ATOM   1006  N   ILE A 175      27.588 -24.770 -22.554  1.00 47.94           N  
ANISOU 1006  N   ILE A 175     5883   6202   6130   -995   -980    459       N  
ATOM   1007  CA  ILE A 175      28.967 -24.592 -22.994  1.00 41.39           C  
ANISOU 1007  CA  ILE A 175     5207   5372   5146   -925   -910    317       C  
ATOM   1008  C   ILE A 175      29.815 -25.844 -22.844  1.00 37.60           C  
ANISOU 1008  C   ILE A 175     4939   4831   4517   -912   -866    149       C  
ATOM   1009  O   ILE A 175      30.907 -25.909 -23.420  1.00 41.40           O  
ANISOU 1009  O   ILE A 175     5559   5303   4867   -867   -808     41       O  
ATOM   1010  CB  ILE A 175      29.623 -23.411 -22.246  1.00 27.75           C  
ANISOU 1010  CB  ILE A 175     3361   3653   3529   -764   -746    287       C  
ATOM   1011  CG1 ILE A 175      29.834 -23.738 -20.764  1.00 42.08           C  
ANISOU 1011  CG1 ILE A 175     5151   5430   5408   -667   -624    203       C  
ATOM   1012  CG2 ILE A 175      28.790 -22.154 -22.410  1.00 20.15           C  
ANISOU 1012  CG2 ILE A 175     2200   2718   2737   -759   -763    456       C  
ATOM   1013  CD1 ILE A 175      30.669 -22.716 -20.051  1.00 45.47           C  
ANISOU 1013  CD1 ILE A 175     5523   5858   5896   -537   -487    132       C  
ATOM   1014  N   MET A 176      29.358 -26.836 -22.087  1.00 34.93           N  
ANISOU 1014  N   MET A 176     4622   4439   4211   -941   -873    136       N  
ATOM   1015  CA  MET A 176      30.090 -28.086 -21.946  1.00 47.84           C  
ANISOU 1015  CA  MET A 176     6459   5990   5727   -923   -834     -2       C  
ATOM   1016  C   MET A 176      29.620 -29.166 -22.910  1.00 56.19           C  
ANISOU 1016  C   MET A 176     7683   6990   6676  -1047   -920     -6       C  
ATOM   1017  O   MET A 176      30.153 -30.282 -22.879  1.00 57.37           O  
ANISOU 1017  O   MET A 176     8008   7045   6743  -1030   -872   -112       O  
ATOM   1018  CB  MET A 176      29.983 -28.599 -20.507  1.00 49.15           C  
ANISOU 1018  CB  MET A 176     6577   6113   5985   -848   -753     -9       C  
ATOM   1019  CG  MET A 176      30.678 -27.710 -19.489  1.00 49.17           C  
ANISOU 1019  CG  MET A 176     6469   6156   6056   -683   -623    -39       C  
ATOM   1020  SD  MET A 176      32.321 -27.212 -20.044  1.00 46.68           S  
ANISOU 1020  SD  MET A 176     6218   5863   5656   -567   -553   -163       S  
ATOM   1021  CE  MET A 176      32.871 -26.258 -18.631  1.00 39.11           C  
ANISOU 1021  CE  MET A 176     5123   4944   4795   -428   -451   -186       C  
ATOM   1022  N   VAL A 177      28.633 -28.866 -23.755  1.00 57.66           N  
ANISOU 1022  N   VAL A 177     7814   7222   6872  -1153  -1030    116       N  
ATOM   1023  CA  VAL A 177      28.205 -29.831 -24.766  1.00 45.83           C  
ANISOU 1023  CA  VAL A 177     6486   5672   5255  -1273  -1111    110       C  
ATOM   1024  C   VAL A 177      29.341 -30.219 -25.702  1.00 42.89           C  
ANISOU 1024  C   VAL A 177     6352   5253   4692  -1244  -1036    -34       C  
ATOM   1025  O   VAL A 177      29.497 -31.416 -25.986  1.00 47.81           O  
ANISOU 1025  O   VAL A 177     7164   5776   5227  -1282  -1016   -121       O  
ATOM   1026  CB  VAL A 177      26.981 -29.292 -25.531  1.00 30.86           C  
ANISOU 1026  CB  VAL A 177     4481   3843   3401  -1392  -1262    282       C  
ATOM   1027  CG1 VAL A 177      26.719 -30.164 -26.751  1.00 29.95           C  
ANISOU 1027  CG1 VAL A 177     4579   3679   3121  -1531  -1357    258       C  
ATOM   1028  CG2 VAL A 177      25.768 -29.287 -24.618  1.00 23.14           C  
ANISOU 1028  CG2 VAL A 177     3284   2881   2627  -1423  -1312    420       C  
ATOM   1029  N   PRO A 178      30.140 -29.288 -26.227  1.00 39.55           N  
ANISOU 1029  N   PRO A 178     5936   4886   4205  -1181   -981    -60       N  
ATOM   1030  CA  PRO A 178      31.267 -29.692 -27.084  1.00 42.21           C  
ANISOU 1030  CA  PRO A 178     6498   5172   4370  -1144   -872   -197       C  
ATOM   1031  C   PRO A 178      32.241 -30.615 -26.384  1.00 43.77           C  
ANISOU 1031  C   PRO A 178     6788   5269   4575  -1024   -729   -340       C  
ATOM   1032  O   PRO A 178      32.861 -31.463 -27.036  1.00 39.84           O  
ANISOU 1032  O   PRO A 178     6494   4681   3961  -1012   -641   -445       O  
ATOM   1033  CB  PRO A 178      31.908 -28.351 -27.462  1.00 43.27           C  
ANISOU 1033  CB  PRO A 178     6570   5398   4475  -1092   -830   -174       C  
ATOM   1034  CG  PRO A 178      31.505 -27.420 -26.354  1.00 45.51           C  
ANISOU 1034  CG  PRO A 178     6595   5751   4945  -1046   -869    -82       C  
ATOM   1035  CD  PRO A 178      30.110 -27.829 -26.011  1.00 44.75           C  
ANISOU 1035  CD  PRO A 178     6399   5648   4956  -1138   -995     33       C  
ATOM   1036  N   GLN A 179      32.399 -30.470 -25.066  1.00 44.29           N  
ANISOU 1036  N   GLN A 179     6713   5340   4776   -933   -700   -341       N  
ATOM   1037  CA  GLN A 179      33.278 -31.377 -24.337  1.00 41.88           C  
ANISOU 1037  CA  GLN A 179     6494   4931   4488   -817   -586   -452       C  
ATOM   1038  C   GLN A 179      32.755 -32.807 -24.376  1.00 45.02           C  
ANISOU 1038  C   GLN A 179     7036   5206   4864   -889   -613   -470       C  
ATOM   1039  O   GLN A 179      33.532 -33.752 -24.559  1.00 55.75           O  
ANISOU 1039  O   GLN A 179     8561   6447   6173   -822   -506   -574       O  
ATOM   1040  CB  GLN A 179      33.429 -30.909 -22.891  1.00 40.95           C  
ANISOU 1040  CB  GLN A 179     6215   4843   4500   -728   -581   -432       C  
ATOM   1041  CG  GLN A 179      34.413 -31.728 -22.078  1.00 43.84           C  
ANISOU 1041  CG  GLN A 179     6634   5116   4906   -573   -469   -510       C  
ATOM   1042  CD  GLN A 179      35.843 -31.501 -22.516  1.00 52.51           C  
ANISOU 1042  CD  GLN A 179     7754   6212   5985   -427   -325   -596       C  
ATOM   1043  OE1 GLN A 179      36.340 -30.374 -22.486  1.00 50.02           O  
ANISOU 1043  OE1 GLN A 179     7281   6004   5720   -364   -289   -574       O  
ATOM   1044  NE2 GLN A 179      36.519 -32.570 -22.915  1.00 55.70           N  
ANISOU 1044  NE2 GLN A 179     8347   6481   6336   -370   -227   -691       N  
ATOM   1045  N   ALA A 180      31.443 -32.989 -24.198  1.00 41.89           N  
ANISOU 1045  N   ALA A 180     6574   4826   4518  -1025   -747   -365       N  
ATOM   1046  CA  ALA A 180      30.878 -34.330 -24.294  1.00 38.11           C  
ANISOU 1046  CA  ALA A 180     6237   4228   4016  -1122   -784   -378       C  
ATOM   1047  C   ALA A 180      31.004 -34.894 -25.702  1.00 54.36           C  
ANISOU 1047  C   ALA A 180     8508   6231   5915  -1199   -780   -444       C  
ATOM   1048  O   ALA A 180      31.154 -36.109 -25.869  1.00 60.26           O  
ANISOU 1048  O   ALA A 180     9441   6841   6615  -1221   -736   -522       O  
ATOM   1049  CB  ALA A 180      29.416 -34.325 -23.855  1.00 27.93           C  
ANISOU 1049  CB  ALA A 180     4807   2977   2828  -1262   -927   -239       C  
ATOM   1050  N   ALA A 181      30.924 -34.034 -26.721  1.00 56.34           N  
ANISOU 1050  N   ALA A 181     8752   6577   6079  -1249   -824   -411       N  
ATOM   1051  CA  ALA A 181      31.059 -34.503 -28.094  1.00 53.18           C  
ANISOU 1051  CA  ALA A 181     8581   6125   5500  -1335   -818   -473       C  
ATOM   1052  C   ALA A 181      32.440 -35.081 -28.355  1.00 52.81           C  
ANISOU 1052  C   ALA A 181     8716   5972   5377  -1200   -612   -629       C  
ATOM   1053  O   ALA A 181      32.582 -36.030 -29.134  1.00 60.44           O  
ANISOU 1053  O   ALA A 181     9914   6825   6223  -1255   -566   -713       O  
ATOM   1054  CB  ALA A 181      30.774 -33.364 -29.072  1.00 47.53           C  
ANISOU 1054  CB  ALA A 181     7827   5532   4702  -1407   -902   -392       C  
ATOM   1055  N   VAL A 182      33.471 -34.519 -27.724  1.00 52.84           N  
ANISOU 1055  N   VAL A 182     8616   6005   5457  -1023   -481   -667       N  
ATOM   1056  CA  VAL A 182      34.829 -34.976 -27.989  1.00 52.84           C  
ANISOU 1056  CA  VAL A 182     8750   5910   5416   -876   -269   -795       C  
ATOM   1057  C   VAL A 182      35.187 -36.245 -27.227  1.00 59.39           C  
ANISOU 1057  C   VAL A 182     9655   6582   6330   -788   -186   -861       C  
ATOM   1058  O   VAL A 182      36.120 -36.953 -27.626  1.00 64.12           O  
ANISOU 1058  O   VAL A 182    10403   7061   6897   -689    -12   -961       O  
ATOM   1059  CB  VAL A 182      35.828 -33.861 -27.645  1.00 48.08           C  
ANISOU 1059  CB  VAL A 182     7997   5399   4873   -724   -163   -802       C  
ATOM   1060  CG1 VAL A 182      37.247 -34.332 -27.898  1.00 59.98           C  
ANISOU 1060  CG1 VAL A 182     9607   6807   6376   -557     75   -917       C  
ATOM   1061  CG2 VAL A 182      35.515 -32.614 -28.453  1.00 49.25           C  
ANISOU 1061  CG2 VAL A 182     8096   5685   4934   -812   -233   -732       C  
ATOM   1062  N   MET A 183      34.475 -36.559 -26.146  1.00 52.12           N  
ANISOU 1062  N   MET A 183     8636   5646   5520   -819   -292   -797       N  
ATOM   1063  CA  MET A 183      34.788 -37.752 -25.370  1.00 55.42           C  
ANISOU 1063  CA  MET A 183     9136   5901   6020   -737   -220   -840       C  
ATOM   1064  C   MET A 183      34.488 -39.011 -26.177  1.00 64.62           C  
ANISOU 1064  C   MET A 183    10543   6918   7092   -839   -200   -904       C  
ATOM   1065  O   MET A 183      33.385 -39.171 -26.708  1.00 75.40           O  
ANISOU 1065  O   MET A 183    11960   8306   8383  -1035   -345   -864       O  
ATOM   1066  CB  MET A 183      34.002 -37.755 -24.061  1.00 59.10           C  
ANISOU 1066  CB  MET A 183     9463   6384   6607   -771   -339   -743       C  
ATOM   1067  CG  MET A 183      34.428 -36.654 -23.092  1.00 52.27           C  
ANISOU 1067  CG  MET A 183     8395   5631   5833   -652   -339   -699       C  
ATOM   1068  SD  MET A 183      36.220 -36.456 -22.951  1.00 51.10           S  
ANISOU 1068  SD  MET A 183     8246   5444   5724   -396   -144   -791       S  
ATOM   1069  CE  MET A 183      36.646 -37.930 -22.027  1.00 56.74           C  
ANISOU 1069  CE  MET A 183     9078   5940   6539   -271    -71   -803       C  
ATOM   1070  N   GLU A 184      35.473 -39.906 -26.267  1.00 62.86           N  
ANISOU 1070  N   GLU A 184    10463   6536   6885   -705    -20  -1000       N  
ATOM   1071  CA  GLU A 184      35.328 -41.171 -26.980  1.00 58.26           C  
ANISOU 1071  CA  GLU A 184    10132   5782   6221   -782     31  -1081       C  
ATOM   1072  C   GLU A 184      36.046 -42.264 -26.200  1.00 54.33           C  
ANISOU 1072  C   GLU A 184     9693   5093   5859   -617    172  -1118       C  
ATOM   1073  O   GLU A 184      37.172 -42.056 -25.738  1.00 54.09           O  
ANISOU 1073  O   GLU A 184     9571   5047   5935   -400    314  -1127       O  
ATOM   1074  CB  GLU A 184      35.896 -41.077 -28.405  1.00 71.83           C  
ANISOU 1074  CB  GLU A 184    12024   7491   7776   -792    151  -1173       C  
ATOM   1075  CG  GLU A 184      35.243 -40.011 -29.278  1.00 81.91           C  
ANISOU 1075  CG  GLU A 184    13270   8942   8910   -949     14  -1123       C  
ATOM   1076  CD  GLU A 184      33.884 -40.424 -29.806  1.00 88.24           C  
ANISOU 1076  CD  GLU A 184    14182   9739   9607  -1200   -188  -1088       C  
ATOM   1077  OE1 GLU A 184      33.624 -41.641 -29.885  1.00 95.10           O  
ANISOU 1077  OE1 GLU A 184    15233  10446  10455  -1267   -177  -1148       O  
ATOM   1078  OE2 GLU A 184      33.084 -39.529 -30.156  1.00 88.67           O  
ANISOU 1078  OE2 GLU A 184    14138   9946   9608  -1330   -358   -994       O  
ATOM   1079  N   CYS A 185      35.394 -43.419 -26.044  1.00 64.10           N  
ANISOU 1079  N   CYS A 185    11070   6179   7106   -719    127  -1127       N  
ATOM   1080  CA  CYS A 185      35.989 -44.587 -25.400  1.00 67.93           C  
ANISOU 1080  CA  CYS A 185    11639   6451   7720   -576    259  -1153       C  
ATOM   1081  C   CYS A 185      36.559 -45.519 -26.466  1.00 72.58           C  
ANISOU 1081  C   CYS A 185    12480   6868   8229   -554    431  -1283       C  
ATOM   1082  O   CYS A 185      35.828 -45.969 -27.357  1.00 74.57           O  
ANISOU 1082  O   CYS A 185    12923   7076   8333   -752    369  -1342       O  
ATOM   1083  CB  CYS A 185      34.954 -45.316 -24.541  1.00 66.78           C  
ANISOU 1083  CB  CYS A 185    11501   6223   7649   -699    126  -1078       C  
ATOM   1084  SG  CYS A 185      35.564 -46.778 -23.658  1.00 72.59           S  
ANISOU 1084  SG  CYS A 185    12340   6682   8561   -532    268  -1074       S  
ATOM   1085  N   SER A 186      37.857 -45.808 -26.377  1.00 73.41           N  
ANISOU 1085  N   SER A 186    12584   6872   8436   -313    649  -1323       N  
ATOM   1086  CA  SER A 186      38.522 -46.661 -27.354  1.00 79.66           C  
ANISOU 1086  CA  SER A 186    13607   7490   9171   -262    855  -1445       C  
ATOM   1087  C   SER A 186      39.624 -47.451 -26.660  1.00 80.80           C  
ANISOU 1087  C   SER A 186    13713   7455   9533      4   1047  -1432       C  
ATOM   1088  O   SER A 186      40.305 -46.927 -25.774  1.00 79.18           O  
ANISOU 1088  O   SER A 186    13273   7319   9491    194   1064  -1342       O  
ATOM   1089  CB  SER A 186      39.101 -45.834 -28.503  1.00 91.48           C  
ANISOU 1089  CB  SER A 186    15134   9101  10524   -250    962  -1508       C  
ATOM   1090  OG  SER A 186      39.775 -44.694 -27.995  1.00 97.08           O  
ANISOU 1090  OG  SER A 186    15576   9978  11333    -99    979  -1435       O  
ATOM   1091  N   SER A 187      39.794 -48.708 -27.072  1.00 91.22           N  
ANISOU 1091  N   SER A 187    15261   8538  10859     18   1183  -1514       N  
ATOM   1092  CA  SER A 187      40.820 -49.606 -26.554  1.00 95.96           C  
ANISOU 1092  CA  SER A 187    15849   8936  11676    271   1377  -1497       C  
ATOM   1093  C   SER A 187      42.105 -49.503 -27.370  1.00 98.78           C  
ANISOU 1093  C   SER A 187    16221   9261  12050    457   1646  -1566       C  
ATOM   1094  O   SER A 187      42.109 -49.039 -28.512  1.00103.58           O  
ANISOU 1094  O   SER A 187    16951   9943  12463    356   1709  -1657       O  
ATOM   1095  CB  SER A 187      40.315 -51.053 -26.546  1.00103.47           C  
ANISOU 1095  CB  SER A 187    17042   9626  12646    191   1397  -1547       C  
ATOM   1096  OG  SER A 187      41.285 -51.943 -26.015  1.00114.53           O  
ANISOU 1096  OG  SER A 187    18422  10820  14275    445   1578  -1510       O  
ATOM   1097  N   VAL A 188      43.200 -49.964 -26.769  1.00 98.76           N  
ANISOU 1097  N   VAL A 188    16091   9143  12292    731   1806  -1504       N  
ATOM   1098  CA  VAL A 188      44.516 -49.959 -27.403  1.00102.02           C  
ANISOU 1098  CA  VAL A 188    16473   9507  12782    940   2085  -1541       C  
ATOM   1099  C   VAL A 188      44.430 -50.478 -28.833  1.00100.78           C  
ANISOU 1099  C   VAL A 188    16654   9225  12412    819   2262  -1708       C  
ATOM   1100  O   VAL A 188      44.641 -49.726 -29.792  1.00 89.79           O  
ANISOU 1100  O   VAL A 188    15305   7953  10858    762   2341  -1768       O  
ATOM   1101  CB  VAL A 188      45.512 -50.790 -26.579  1.00106.18           C  
ANISOU 1101  CB  VAL A 188    16867   9860  13617   1226   2218  -1445       C  
ATOM   1102  CG1 VAL A 188      46.853 -50.828 -27.276  1.00107.51           C  
ANISOU 1102  CG1 VAL A 188    16990   9974  13884   1438   2522  -1473       C  
ATOM   1103  CG2 VAL A 188      45.630 -50.211 -25.181  1.00105.73           C  
ANISOU 1103  CG2 VAL A 188    16486   9939  13748   1340   2027  -1268       C  
ATOM   1104  N   LEU A 189      44.138 -51.769 -28.986  1.00105.90           N  
ANISOU 1104  N   LEU A 189    17557   9620  13059    780   2330  -1779       N  
ATOM   1105  CA  LEU A 189      43.756 -52.322 -30.278  1.00106.78           C  
ANISOU 1105  CA  LEU A 189    18043   9603  12926    603   2437  -1947       C  
ATOM   1106  C   LEU A 189      42.242 -52.475 -30.263  1.00119.44           C  
ANISOU 1106  C   LEU A 189    19800  11235  14349    292   2153  -1977       C  
ATOM   1107  O   LEU A 189      41.719 -53.335 -29.533  1.00127.53           O  
ANISOU 1107  O   LEU A 189    20861  12113  15481    260   2059  -1946       O  
ATOM   1108  CB  LEU A 189      44.446 -53.667 -30.529  1.00100.76           C  
ANISOU 1108  CB  LEU A 189    17482   8523  12281    756   2718  -2020       C  
ATOM   1109  CG  LEU A 189      45.980 -53.653 -30.512  1.00 89.33           C  
ANISOU 1109  CG  LEU A 189    15860   7022  11060   1082   3017  -1970       C  
ATOM   1110  CD1 LEU A 189      46.537 -54.846 -29.744  1.00 77.26           C  
ANISOU 1110  CD1 LEU A 189    14298   5235   9822   1305   3140  -1909       C  
ATOM   1111  CD2 LEU A 189      46.534 -53.624 -31.928  1.00 83.42           C  
ANISOU 1111  CD2 LEU A 189    15348   6214  10136   1072   3304  -2107       C  
ATOM   1112  N   PRO A 190      41.507 -51.704 -31.066  1.00122.41           N  
ANISOU 1112  N   PRO A 190    20264  11784  14462     56   2012  -2024       N  
ATOM   1113  CA  PRO A 190      40.044 -51.642 -30.910  1.00123.07           C  
ANISOU 1113  CA  PRO A 190    20397  11948  14416   -231   1701  -2006       C  
ATOM   1114  C   PRO A 190      39.348 -52.985 -31.056  1.00119.37           C  
ANISOU 1114  C   PRO A 190    20214  11231  13910   -381   1678  -2093       C  
ATOM   1115  O   PRO A 190      38.250 -53.161 -30.511  1.00107.84           O  
ANISOU 1115  O   PRO A 190    18723   9794  12457   -561   1436  -2040       O  
ATOM   1116  CB  PRO A 190      39.625 -50.664 -32.011  1.00129.72           C  
ANISOU 1116  CB  PRO A 190    21318  12986  14984   -423   1613  -2047       C  
ATOM   1117  CG  PRO A 190      40.806 -49.756 -32.135  1.00129.73           C  
ANISOU 1117  CG  PRO A 190    21134  13108  15048   -203   1796  -2013       C  
ATOM   1118  CD  PRO A 190      42.001 -50.661 -31.980  1.00129.65           C  
ANISOU 1118  CD  PRO A 190    21161  12870  15229     61   2104  -2051       C  
ATOM   1119  N   GLU A 191      39.921 -53.921 -31.814  1.00105.08           N  
ANISOU 1119  N   GLU A 191    18688   9179  12057   -326   1928  -2226       N  
ATOM   1120  CA  GLU A 191      39.370 -55.271 -31.861  1.00 86.42           C  
ANISOU 1120  CA  GLU A 191    16597   6544   9693   -444   1930  -2313       C  
ATOM   1121  C   GLU A 191      39.341 -55.915 -30.480  1.00 77.40           C  
ANISOU 1121  C   GLU A 191    15280   5286   8843   -314   1882  -2198       C  
ATOM   1122  O   GLU A 191      38.572 -56.858 -30.263  1.00 80.18           O  
ANISOU 1122  O   GLU A 191    15787   5461   9215   -462   1791  -2226       O  
ATOM   1123  CB  GLU A 191      40.181 -56.140 -32.823  1.00 86.87           C  
ANISOU 1123  CB  GLU A 191    16977   6343   9687   -354   2256  -2472       C  
ATOM   1124  CG  GLU A 191      40.631 -55.414 -34.082  1.00 97.29           C  
ANISOU 1124  CG  GLU A 191    18430   7772  10765   -385   2392  -2558       C  
ATOM   1125  CD  GLU A 191      41.891 -54.591 -33.867  1.00111.01           C  
ANISOU 1125  CD  GLU A 191    19888   9637  12654    -93   2587  -2473       C  
ATOM   1126  OE1 GLU A 191      42.974 -55.192 -33.704  1.00120.07           O  
ANISOU 1126  OE1 GLU A 191    21022  10602  13997    169   2876  -2482       O  
ATOM   1127  OE2 GLU A 191      41.798 -53.344 -33.850  1.00110.14           O  
ANISOU 1127  OE2 GLU A 191    19560   9803  12482   -125   2450  -2391       O  
ATOM   1128  N   LEU A 192      40.180 -55.444 -29.550  1.00 76.47           N  
ANISOU 1128  N   LEU A 192    14850   5252   8955    -46   1940  -2063       N  
ATOM   1129  CA  LEU A 192      40.141 -55.956 -28.182  1.00 80.05           C  
ANISOU 1129  CA  LEU A 192    15129   5614   9673     74   1870  -1925       C  
ATOM   1130  C   LEU A 192      38.807 -55.669 -27.506  1.00 84.27           C  
ANISOU 1130  C   LEU A 192    15569   6277  10172   -162   1555  -1838       C  
ATOM   1131  O   LEU A 192      38.410 -56.401 -26.592  1.00 85.12           O  
ANISOU 1131  O   LEU A 192    15654   6247  10440   -165   1484  -1756       O  
ATOM   1132  CB  LEU A 192      41.274 -55.343 -27.355  1.00 85.22           C  
ANISOU 1132  CB  LEU A 192    15454   6372  10552    387   1955  -1785       C  
ATOM   1133  CG  LEU A 192      42.570 -56.138 -27.197  1.00 93.15           C  
ANISOU 1133  CG  LEU A 192    16449   7155  11789    699   2235  -1768       C  
ATOM   1134  CD1 LEU A 192      43.162 -56.489 -28.554  1.00101.97           C  
ANISOU 1134  CD1 LEU A 192    17826   8143  12775    718   2512  -1941       C  
ATOM   1135  CD2 LEU A 192      43.558 -55.341 -26.359  1.00 91.71           C  
ANISOU 1135  CD2 LEU A 192    15896   7133  11816    967   2248  -1606       C  
ATOM   1136  N   ALA A 193      38.109 -54.608 -27.923  1.00 88.35           N  
ANISOU 1136  N   ALA A 193    16020   7054  10496   -355   1372  -1839       N  
ATOM   1137  CA  ALA A 193      36.906 -54.199 -27.206  1.00 84.36           C  
ANISOU 1137  CA  ALA A 193    15369   6695   9988   -551   1088  -1730       C  
ATOM   1138  C   ALA A 193      35.848 -55.289 -27.226  1.00 80.72           C  
ANISOU 1138  C   ALA A 193    15112   6047   9513   -781    983  -1769       C  
ATOM   1139  O   ALA A 193      34.982 -55.331 -26.344  1.00 78.27           O  
ANISOU 1139  O   ALA A 193    14675   5771   9293   -891    803  -1654       O  
ATOM   1140  CB  ALA A 193      36.342 -52.909 -27.803  1.00 86.30           C  
ANISOU 1140  CB  ALA A 193    15524   7235  10033   -718    921  -1725       C  
ATOM   1141  N   ALA A 194      35.901 -56.175 -28.218  1.00 69.78           N  
ANISOU 1141  N   ALA A 194    14046   4454   8015   -863   1101  -1930       N  
ATOM   1142  CA  ALA A 194      34.963 -57.283 -28.274  1.00 72.84           C  
ANISOU 1142  CA  ALA A 194    14644   4634   8398  -1085   1012  -1982       C  
ATOM   1143  C   ALA A 194      35.206 -58.297 -27.163  1.00 87.99           C  
ANISOU 1143  C   ALA A 194    16530   6311  10591   -935   1094  -1898       C  
ATOM   1144  O   ALA A 194      34.333 -59.133 -26.905  1.00100.28           O  
ANISOU 1144  O   ALA A 194    18191   7711  12199  -1118    991  -1894       O  
ATOM   1145  CB  ALA A 194      35.041 -57.965 -29.641  1.00 77.50           C  
ANISOU 1145  CB  ALA A 194    15615   5048   8785  -1204   1133  -2187       C  
ATOM   1146  N   ARG A 195      36.365 -58.250 -26.504  1.00 77.15           N  
ANISOU 1146  N   ARG A 195    15008   4900   9404   -612   1268  -1819       N  
ATOM   1147  CA  ARG A 195      36.712 -59.220 -25.470  1.00 75.38           C  
ANISOU 1147  CA  ARG A 195    14754   4438   9447   -441   1350  -1716       C  
ATOM   1148  C   ARG A 195      36.678 -58.659 -24.055  1.00 70.84           C  
ANISOU 1148  C   ARG A 195    13859   4009   9046   -327   1226  -1492       C  
ATOM   1149  O   ARG A 195      36.208 -59.341 -23.141  1.00 75.97           O  
ANISOU 1149  O   ARG A 195    14491   4524   9852   -357   1159  -1376       O  
ATOM   1150  CB  ARG A 195      38.103 -59.809 -25.742  1.00 76.96           C  
ANISOU 1150  CB  ARG A 195    15043   4434   9763   -140   1650  -1771       C  
ATOM   1151  CG  ARG A 195      38.277 -60.378 -27.145  1.00 81.19           C  
ANISOU 1151  CG  ARG A 195    15923   4804  10120   -223   1825  -1996       C  
ATOM   1152  CD  ARG A 195      39.637 -61.049 -27.314  1.00 84.44           C  
ANISOU 1152  CD  ARG A 195    16410   4987  10687     90   2149  -2033       C  
ATOM   1153  NE  ARG A 195      39.639 -62.441 -26.867  1.00 88.14           N  
ANISOU 1153  NE  ARG A 195    17033   5105  11349    146   2238  -2022       N  
ATOM   1154  CZ  ARG A 195      40.737 -63.172 -26.695  1.00 91.10           C  
ANISOU 1154  CZ  ARG A 195    17428   5248  11938    441   2492  -1997       C  
ATOM   1155  NH1 ARG A 195      41.932 -62.643 -26.921  1.00 90.81           N  
ANISOU 1155  NH1 ARG A 195    17248   5300  11956    705   2685  -1980       N  
ATOM   1156  NH2 ARG A 195      40.641 -64.431 -26.289  1.00 94.57           N  
ANISOU 1156  NH2 ARG A 195    18018   5362  12552    474   2555  -1979       N  
ATOM   1157  N   THR A 196      37.160 -57.439 -23.835  1.00 66.70           N  
ANISOU 1157  N   THR A 196    13094   3750   8497   -204   1197  -1424       N  
ATOM   1158  CA  THR A 196      37.264 -56.923 -22.478  1.00 72.33           C  
ANISOU 1158  CA  THR A 196    13530   4585   9368    -73   1100  -1216       C  
ATOM   1159  C   THR A 196      37.334 -55.404 -22.517  1.00 76.67           C  
ANISOU 1159  C   THR A 196    13862   5465   9805    -70   1005  -1187       C  
ATOM   1160  O   THR A 196      37.564 -54.795 -23.564  1.00 84.98           O  
ANISOU 1160  O   THR A 196    14959   6636  10695   -107   1051  -1313       O  
ATOM   1161  CB  THR A 196      38.485 -57.497 -21.754  1.00 69.68           C  
ANISOU 1161  CB  THR A 196    13118   4083   9275    259   1261  -1109       C  
ATOM   1162  OG1 THR A 196      38.507 -57.027 -20.400  1.00 74.21           O  
ANISOU 1162  OG1 THR A 196    13447   4775   9976    362   1139   -892       O  
ATOM   1163  CG2 THR A 196      39.762 -57.058 -22.452  1.00 65.33           C  
ANISOU 1163  CG2 THR A 196    12520   3583   8720    483   1449  -1189       C  
ATOM   1164  N   ARG A 197      37.107 -54.801 -21.351  1.00 67.64           N  
ANISOU 1164  N   ARG A 197    12495   4462   8744    -33    874  -1014       N  
ATOM   1165  CA  ARG A 197      37.270 -53.368 -21.154  1.00 56.73           C  
ANISOU 1165  CA  ARG A 197    10890   3370   7296      6    791   -964       C  
ATOM   1166  C   ARG A 197      38.510 -53.016 -20.347  1.00 54.84           C  
ANISOU 1166  C   ARG A 197    10453   3162   7221    320    869   -845       C  
ATOM   1167  O   ARG A 197      38.723 -51.836 -20.052  1.00 52.90           O  
ANISOU 1167  O   ARG A 197    10015   3142   6943    371    801   -793       O  
ATOM   1168  CB  ARG A 197      36.029 -52.783 -20.472  1.00 54.71           C  
ANISOU 1168  CB  ARG A 197    10527   3273   6986   -204    577   -859       C  
ATOM   1169  CG  ARG A 197      34.807 -52.759 -21.365  1.00 61.55           C  
ANISOU 1169  CG  ARG A 197    11509   4194   7685   -520    457   -961       C  
ATOM   1170  CD  ARG A 197      33.569 -52.266 -20.634  1.00 62.92           C  
ANISOU 1170  CD  ARG A 197    11545   4510   7852   -716    261   -836       C  
ATOM   1171  NE  ARG A 197      32.390 -52.339 -21.493  1.00 66.73           N  
ANISOU 1171  NE  ARG A 197    12112   5033   8208  -1015    131   -912       N  
ATOM   1172  CZ  ARG A 197      31.172 -51.943 -21.136  1.00 67.66           C  
ANISOU 1172  CZ  ARG A 197    12107   5279   8322  -1225    -42   -819       C  
ATOM   1173  NH1 ARG A 197      30.962 -51.439 -19.928  1.00 67.45           N  
ANISOU 1173  NH1 ARG A 197    11890   5346   8392  -1172    -86   -656       N  
ATOM   1174  NH2 ARG A 197      30.162 -52.050 -21.990  1.00 69.37           N  
ANISOU 1174  NH2 ARG A 197    12387   5529   8440  -1486   -170   -880       N  
ATOM   1175  N   ALA A 198      39.328 -54.004 -19.977  1.00 58.85           N  
ANISOU 1175  N   ALA A 198    10995   3451   7915    531   1000   -790       N  
ATOM   1176  CA  ALA A 198      40.504 -53.721 -19.166  1.00 58.60           C  
ANISOU 1176  CA  ALA A 198    10748   3456   8063    830   1041   -647       C  
ATOM   1177  C   ALA A 198      41.517 -52.869 -19.907  1.00 66.83           C  
ANISOU 1177  C   ALA A 198    11671   4638   9082    971   1152   -732       C  
ATOM   1178  O   ALA A 198      42.363 -52.233 -19.269  1.00 71.17           O  
ANISOU 1178  O   ALA A 198    11986   5305   9749   1174   1134   -614       O  
ATOM   1179  CB  ALA A 198      41.166 -55.023 -18.712  1.00 58.90           C  
ANISOU 1179  CB  ALA A 198    10842   3220   8319   1025   1151   -560       C  
ATOM   1180  N   PHE A 199      41.465 -52.852 -21.237  1.00 72.03           N  
ANISOU 1180  N   PHE A 199    12487   5288   9592    865   1264   -924       N  
ATOM   1181  CA  PHE A 199      42.455 -52.143 -22.033  1.00 76.62           C  
ANISOU 1181  CA  PHE A 199    12980   5981  10153    995   1406  -1002       C  
ATOM   1182  C   PHE A 199      41.860 -50.971 -22.806  1.00 83.69           C  
ANISOU 1182  C   PHE A 199    13876   7113  10811    791   1322  -1101       C  
ATOM   1183  O   PHE A 199      42.492 -50.466 -23.740  1.00 88.89           O  
ANISOU 1183  O   PHE A 199    14530   7845  11399    837   1455  -1193       O  
ATOM   1184  CB  PHE A 199      43.150 -53.115 -22.987  1.00 75.38           C  
ANISOU 1184  CB  PHE A 199    13011   5602  10029   1090   1658  -1123       C  
ATOM   1185  CG  PHE A 199      43.644 -54.370 -22.322  1.00 72.55           C  
ANISOU 1185  CG  PHE A 199    12679   4981   9905   1276   1743  -1031       C  
ATOM   1186  CD1 PHE A 199      44.632 -54.319 -21.351  1.00 66.89           C  
ANISOU 1186  CD1 PHE A 199    11704   4274   9436   1551   1745   -850       C  
ATOM   1187  CD2 PHE A 199      43.129 -55.605 -22.678  1.00 71.43           C  
ANISOU 1187  CD2 PHE A 199    12820   4581   9740   1173   1810  -1115       C  
ATOM   1188  CE1 PHE A 199      45.090 -55.479 -20.743  1.00 64.51           C  
ANISOU 1188  CE1 PHE A 199    11423   3732   9356   1727   1808   -742       C  
ATOM   1189  CE2 PHE A 199      43.585 -56.767 -22.076  1.00 70.93           C  
ANISOU 1189  CE2 PHE A 199    12787   4261   9902   1348   1893  -1023       C  
ATOM   1190  CZ  PHE A 199      44.566 -56.703 -21.108  1.00 67.55           C  
ANISOU 1190  CZ  PHE A 199    12097   3849   9722   1629   1891   -829       C  
ATOM   1191  N   SER A 200      40.661 -50.526 -22.449  1.00 79.83           N  
ANISOU 1191  N   SER A 200    13388   6742  10204    569   1111  -1069       N  
ATOM   1192  CA  SER A 200      40.057 -49.383 -23.115  1.00 73.50           C  
ANISOU 1192  CA  SER A 200    12561   6170   9197    382   1007  -1134       C  
ATOM   1193  C   SER A 200      40.150 -48.148 -22.228  1.00 70.39           C  
ANISOU 1193  C   SER A 200    11902   5995   8848    446    881  -1016       C  
ATOM   1194  O   SER A 200      40.097 -48.236 -20.998  1.00 70.18           O  
ANISOU 1194  O   SER A 200    11766   5953   8948    525    796   -877       O  
ATOM   1195  CB  SER A 200      38.597 -49.670 -23.468  1.00 70.10           C  
ANISOU 1195  CB  SER A 200    12297   5734   8603     72    849  -1179       C  
ATOM   1196  OG  SER A 200      37.856 -49.986 -22.305  1.00 73.52           O  
ANISOU 1196  OG  SER A 200    12674   6131   9128     15    709  -1053       O  
ATOM   1197  N   VAL A 201      40.289 -46.989 -22.869  1.00 65.93           N  
ANISOU 1197  N   VAL A 201    11252   5629   8169    407    873  -1068       N  
ATOM   1198  CA  VAL A 201      40.430 -45.715 -22.176  1.00 67.53           C  
ANISOU 1198  CA  VAL A 201    11218   6039   8400    463    770   -982       C  
ATOM   1199  C   VAL A 201      39.444 -44.704 -22.747  1.00 65.42           C  
ANISOU 1199  C   VAL A 201    10950   5968   7939    226    627  -1021       C  
ATOM   1200  O   VAL A 201      39.174 -44.695 -23.953  1.00 64.86           O  
ANISOU 1200  O   VAL A 201    11013   5915   7714     91    659  -1121       O  
ATOM   1201  CB  VAL A 201      41.872 -45.179 -22.275  1.00 71.10           C  
ANISOU 1201  CB  VAL A 201    11495   6544   8974    711    922   -976       C  
ATOM   1202  CG1 VAL A 201      42.114 -44.552 -23.643  1.00 70.63           C  
ANISOU 1202  CG1 VAL A 201    11485   6584   8769    643   1026  -1096       C  
ATOM   1203  CG2 VAL A 201      42.139 -44.190 -21.160  1.00 73.47           C  
ANISOU 1203  CG2 VAL A 201    11550   6994   9370    819    807   -854       C  
ATOM   1204  N   CYS A 202      38.908 -43.852 -21.867  1.00 58.45           N  
ANISOU 1204  N   CYS A 202     9917   5228   7063    179    465   -928       N  
ATOM   1205  CA  CYS A 202      37.991 -42.772 -22.229  1.00 64.27           C  
ANISOU 1205  CA  CYS A 202    10596   6165   7660    -20    316   -930       C  
ATOM   1206  C   CYS A 202      38.776 -41.463 -22.275  1.00 63.95           C  
ANISOU 1206  C   CYS A 202    10375   6294   7631     97    349   -932       C  
ATOM   1207  O   CYS A 202      39.147 -40.921 -21.227  1.00 73.99           O  
ANISOU 1207  O   CYS A 202    11493   7617   9002    225    309   -856       O  
ATOM   1208  CB  CYS A 202      36.846 -42.686 -21.220  1.00 68.33           C  
ANISOU 1208  CB  CYS A 202    11058   6715   8189   -154    134   -824       C  
ATOM   1209  SG  CYS A 202      35.644 -41.351 -21.469  1.00 63.20           S  
ANISOU 1209  SG  CYS A 202    10277   6310   7428   -380    -56   -786       S  
ATOM   1210  N   ASP A 203      39.028 -40.956 -23.485  1.00 51.10           N  
ANISOU 1210  N   ASP A 203     8776   4746   5894     52    420  -1012       N  
ATOM   1211  CA  ASP A 203      39.784 -39.724 -23.666  1.00 55.51           C  
ANISOU 1211  CA  ASP A 203     9172   5457   6463    148    472  -1017       C  
ATOM   1212  C   ASP A 203      39.184 -38.902 -24.801  1.00 62.44           C  
ANISOU 1212  C   ASP A 203    10084   6477   7163    -37    414  -1048       C  
ATOM   1213  O   ASP A 203      38.284 -39.347 -25.520  1.00 77.04           O  
ANISOU 1213  O   ASP A 203    12087   8301   8885   -222    339  -1068       O  
ATOM   1214  CB  ASP A 203      41.262 -40.024 -23.931  1.00 69.01           C  
ANISOU 1214  CB  ASP A 203    10849   7084   8288    381    702  -1056       C  
ATOM   1215  CG  ASP A 203      42.171 -38.945 -23.403  1.00 83.57           C  
ANISOU 1215  CG  ASP A 203    12450   9051  10253    546    737  -1010       C  
ATOM   1216  OD1 ASP A 203      41.701 -37.796 -23.253  1.00 85.79           O  
ANISOU 1216  OD1 ASP A 203    12634   9494  10468    453    617   -989       O  
ATOM   1217  OD2 ASP A 203      43.357 -39.246 -23.149  1.00 94.98           O  
ANISOU 1217  OD2 ASP A 203    13784  10430  11873    767    881   -986       O  
ATOM   1218  N   GLU A 204      39.696 -37.682 -24.948  1.00 56.40           N  
ANISOU 1218  N   GLU A 204     9173   5859   6399     16    442  -1041       N  
ATOM   1219  CA  GLU A 204      39.261 -36.777 -26.005  1.00 46.85           C  
ANISOU 1219  CA  GLU A 204     7983   4785   5035   -132    397  -1046       C  
ATOM   1220  C   GLU A 204      39.798 -37.244 -27.354  1.00 46.84           C  
ANISOU 1220  C   GLU A 204     8171   4707   4920   -133    567  -1129       C  
ATOM   1221  O   GLU A 204      40.944 -37.691 -27.457  1.00 52.84           O  
ANISOU 1221  O   GLU A 204     8943   5371   5761     43    776  -1178       O  
ATOM   1222  CB  GLU A 204      39.753 -35.361 -25.708  1.00 46.61           C  
ANISOU 1222  CB  GLU A 204     7748   4910   5053    -61    403  -1013       C  
ATOM   1223  CG  GLU A 204      38.958 -34.643 -24.629  1.00 54.78           C  
ANISOU 1223  CG  GLU A 204     8626   6048   6139   -122    209   -932       C  
ATOM   1224  CD  GLU A 204      39.619 -33.356 -24.187  1.00 58.72           C  
ANISOU 1224  CD  GLU A 204     8903   6685   6724    -24    231   -899       C  
ATOM   1225  OE1 GLU A 204      40.153 -32.630 -25.051  1.00 57.63           O  
ANISOU 1225  OE1 GLU A 204     8754   6608   6533    -17    336   -924       O  
ATOM   1226  OE2 GLU A 204      39.618 -33.078 -22.970  1.00 60.27           O  
ANISOU 1226  OE2 GLU A 204     8892   6949   7058     41    143   -818       O  
ATOM   1227  N   ARG A 205      38.961 -37.152 -28.389  1.00 45.34           N  
ANISOU 1227  N   ARG A 205     8127   4555   4546   -329    476  -1132       N  
ATOM   1228  CA  ARG A 205      39.337 -37.538 -29.751  1.00 59.17           C  
ANISOU 1228  CA  ARG A 205    10105   6236   6143   -364    621  -1210       C  
ATOM   1229  C   ARG A 205      39.280 -36.309 -30.660  1.00 58.81           C  
ANISOU 1229  C   ARG A 205    10046   6339   5960   -447    601  -1178       C  
ATOM   1230  O   ARG A 205      38.200 -35.900 -31.100  1.00 60.66           O  
ANISOU 1230  O   ARG A 205    10316   6657   6074   -636    405  -1120       O  
ATOM   1231  CB  ARG A 205      38.444 -38.663 -30.274  1.00 71.86           C  
ANISOU 1231  CB  ARG A 205    11953   7722   7630   -530    537  -1249       C  
ATOM   1232  CG  ARG A 205      38.950 -39.295 -31.559  1.00 83.22           C  
ANISOU 1232  CG  ARG A 205    13668   9040   8911   -547    718  -1352       C  
ATOM   1233  CD  ARG A 205      38.034 -40.411 -32.024  1.00 91.25           C  
ANISOU 1233  CD  ARG A 205    14935   9930   9807   -727    621  -1399       C  
ATOM   1234  NE  ARG A 205      37.974 -41.502 -31.055  1.00 99.42           N  
ANISOU 1234  NE  ARG A 205    15960  10820  10994   -660    627  -1414       N  
ATOM   1235  CZ  ARG A 205      37.460 -42.701 -31.308  1.00107.52           C  
ANISOU 1235  CZ  ARG A 205    17209  11684  11960   -768    607  -1474       C  
ATOM   1236  NH1 ARG A 205      36.964 -42.972 -32.507  1.00113.36           N  
ANISOU 1236  NH1 ARG A 205    18205  12387  12481   -953    572  -1533       N  
ATOM   1237  NH2 ARG A 205      37.451 -43.635 -30.366  1.00107.81           N  
ANISOU 1237  NH2 ARG A 205    17226  11585  12152   -696    622  -1475       N  
ATOM   1238  N   TRP A 206      40.438 -35.717 -30.944  1.00 57.25           N  
ANISOU 1238  N   TRP A 206     9786   6172   5795   -304    805  -1200       N  
ATOM   1239  CA  TRP A 206      40.533 -34.568 -31.837  1.00 66.64           C  
ANISOU 1239  CA  TRP A 206    10980   7484   6855   -368    827  -1167       C  
ATOM   1240  C   TRP A 206      40.973 -35.008 -33.228  1.00 79.70           C  
ANISOU 1240  C   TRP A 206    12901   9051   8330   -401   1006  -1239       C  
ATOM   1241  O   TRP A 206      41.771 -35.938 -33.372  1.00 89.38           O  
ANISOU 1241  O   TRP A 206    14226  10131   9601   -283   1215  -1320       O  
ATOM   1242  CB  TRP A 206      41.506 -33.529 -31.283  1.00 68.71           C  
ANISOU 1242  CB  TRP A 206    10997   7841   7267   -208    949  -1135       C  
ATOM   1243  CG  TRP A 206      41.120 -33.035 -29.932  1.00 66.11           C  
ANISOU 1243  CG  TRP A 206    10434   7591   7093   -180    785  -1076       C  
ATOM   1244  CD1 TRP A 206      41.583 -33.488 -28.733  1.00 65.22           C  
ANISOU 1244  CD1 TRP A 206    10179   7423   7180    -27    811  -1086       C  
ATOM   1245  CD2 TRP A 206      40.176 -32.001 -29.635  1.00 62.19           C  
ANISOU 1245  CD2 TRP A 206     9830   7236   6565   -307    569   -990       C  
ATOM   1246  NE1 TRP A 206      40.992 -32.794 -27.706  1.00 60.07           N  
ANISOU 1246  NE1 TRP A 206     9358   6866   6600    -60    631  -1025       N  
ATOM   1247  CE2 TRP A 206      40.123 -31.876 -28.234  1.00 60.35           C  
ANISOU 1247  CE2 TRP A 206     9404   7022   6505   -230    488   -967       C  
ATOM   1248  CE3 TRP A 206      39.373 -31.166 -30.419  1.00 58.08           C  
ANISOU 1248  CE3 TRP A 206     9355   6820   5893   -476    436   -920       C  
ATOM   1249  CZ2 TRP A 206      39.300 -30.950 -27.598  1.00 59.00           C  
ANISOU 1249  CZ2 TRP A 206     9089   6968   6360   -318    297   -887       C  
ATOM   1250  CZ3 TRP A 206      38.555 -30.247 -29.785  1.00 52.97           C  
ANISOU 1250  CZ3 TRP A 206     8542   6290   5296   -552    240   -824       C  
ATOM   1251  CH2 TRP A 206      38.525 -30.147 -28.389  1.00 56.78           C  
ANISOU 1251  CH2 TRP A 206     8835   6786   5953   -474    181   -814       C  
ATOM   1252  N   ALA A 207      40.439 -34.342 -34.253  1.00 79.14           N  
ANISOU 1252  N   ALA A 207    12953   9061   8056   -562    923  -1204       N  
ATOM   1253  CA  ALA A 207      40.792 -34.650 -35.632  1.00 76.06           C  
ANISOU 1253  CA  ALA A 207    12846   8595   7460   -616   1082  -1269       C  
ATOM   1254  C   ALA A 207      42.026 -33.910 -36.132  1.00 83.96           C  
ANISOU 1254  C   ALA A 207    13801   9629   8470   -484   1354  -1271       C  
ATOM   1255  O   ALA A 207      42.473 -34.175 -37.253  1.00 90.63           O  
ANISOU 1255  O   ALA A 207    14881  10400   9155   -504   1535  -1328       O  
ATOM   1256  CB  ALA A 207      39.609 -34.340 -36.561  1.00 71.88           C  
ANISOU 1256  CB  ALA A 207    12490   8128   6693   -862    850  -1220       C  
ATOM   1257  N   ASP A 208      42.584 -32.994 -35.348  1.00 84.32           N  
ANISOU 1257  N   ASP A 208    13558   9780   8700   -357   1396  -1209       N  
ATOM   1258  CA  ASP A 208      43.753 -32.249 -35.794  1.00 90.50           C  
ANISOU 1258  CA  ASP A 208    14264  10600   9522   -241   1658  -1192       C  
ATOM   1259  C   ASP A 208      44.443 -31.635 -34.584  1.00 89.70           C  
ANISOU 1259  C   ASP A 208    13809  10571   9701    -73   1705  -1143       C  
ATOM   1260  O   ASP A 208      43.815 -31.400 -33.549  1.00 85.60           O  
ANISOU 1260  O   ASP A 208    13132  10114   9278    -92   1495  -1106       O  
ATOM   1261  CB  ASP A 208      43.370 -31.167 -36.813  1.00 96.94           C  
ANISOU 1261  CB  ASP A 208    15184  11529  10121   -389   1604  -1123       C  
ATOM   1262  CG  ASP A 208      42.480 -30.099 -36.216  1.00100.02           C  
ANISOU 1262  CG  ASP A 208    15397  12074  10531   -484   1337  -1014       C  
ATOM   1263  OD1 ASP A 208      41.332 -30.427 -35.851  1.00104.25           O  
ANISOU 1263  OD1 ASP A 208    15954  12619  11035   -604   1066   -995       O  
ATOM   1264  OD2 ASP A 208      42.933 -28.939 -36.104  1.00101.59           O  
ANISOU 1264  OD2 ASP A 208    15427  12379  10794   -440   1408   -938       O  
ATOM   1265  N   ASP A 209      45.752 -31.398 -34.727  1.00 94.36           N  
ANISOU 1265  N   ASP A 209    14272  11147  10433     88   1985  -1138       N  
ATOM   1266  CA  ASP A 209      46.540 -30.861 -33.622  1.00 92.88           C  
ANISOU 1266  CA  ASP A 209    13728  11021  10541    250   2040  -1085       C  
ATOM   1267  C   ASP A 209      46.072 -29.473 -33.208  1.00 89.04           C  
ANISOU 1267  C   ASP A 209    13074  10696  10060    168   1890  -1001       C  
ATOM   1268  O   ASP A 209      46.159 -29.116 -32.027  1.00 89.25           O  
ANISOU 1268  O   ASP A 209    12845  10776  10291    241   1808   -971       O  
ATOM   1269  CB  ASP A 209      48.019 -30.813 -34.012  1.00 99.57           C  
ANISOU 1269  CB  ASP A 209    14449  11830  11552    412   2361  -1069       C  
ATOM   1270  CG  ASP A 209      48.639 -32.186 -34.116  1.00105.97           C  
ANISOU 1270  CG  ASP A 209    15352  12471  12440    540   2528  -1138       C  
ATOM   1271  OD1 ASP A 209      48.049 -33.161 -33.607  1.00110.67           O  
ANISOU 1271  OD1 ASP A 209    16044  12980  13024    534   2394  -1191       O  
ATOM   1272  OD2 ASP A 209      49.725 -32.285 -34.723  1.00107.68           O  
ANISOU 1272  OD2 ASP A 209    15543  12632  12737    646   2807  -1132       O  
ATOM   1273  N   LEU A 210      45.582 -28.674 -34.154  1.00 83.02           N  
ANISOU 1273  N   LEU A 210    12457  10008   9079     18   1856   -956       N  
ATOM   1274  CA  LEU A 210      45.253 -27.288 -33.832  1.00 71.01           C  
ANISOU 1274  CA  LEU A 210    10775   8630   7578    -51   1757   -860       C  
ATOM   1275  C   LEU A 210      44.024 -27.187 -32.938  1.00 69.28           C  
ANISOU 1275  C   LEU A 210    10524   8460   7337   -149   1450   -846       C  
ATOM   1276  O   LEU A 210      43.989 -26.362 -32.017  1.00 70.09           O  
ANISOU 1276  O   LEU A 210    10394   8644   7593   -129   1386   -797       O  
ATOM   1277  CB  LEU A 210      45.032 -26.489 -35.116  1.00 65.86           C  
ANISOU 1277  CB  LEU A 210    10296   8036   6691   -185   1790   -791       C  
ATOM   1278  CG  LEU A 210      44.812 -24.981 -34.971  1.00 59.64           C  
ANISOU 1278  CG  LEU A 210     9357   7383   5922   -257   1735   -664       C  
ATOM   1279  CD1 LEU A 210      46.064 -24.292 -34.451  1.00 53.88           C  
ANISOU 1279  CD1 LEU A 210     8310   6679   5483   -116   1966   -626       C  
ATOM   1280  CD2 LEU A 210      44.372 -24.362 -36.292  1.00 64.83           C  
ANISOU 1280  CD2 LEU A 210    10236   8088   6311   -405   1707   -577       C  
ATOM   1281  N   ALA A 211      42.997 -27.996 -33.199  1.00 65.80           N  
ANISOU 1281  N   ALA A 211    10293   7972   6735   -266   1252   -877       N  
ATOM   1282  CA  ALA A 211      41.737 -27.860 -32.464  1.00 58.22           C  
ANISOU 1282  CA  ALA A 211     9289   7067   5766   -380    948   -834       C  
ATOM   1283  C   ALA A 211      41.900 -27.940 -30.952  1.00 53.18           C  
ANISOU 1283  C   ALA A 211     8423   6425   5358   -267    908   -859       C  
ATOM   1284  O   ALA A 211      41.412 -27.039 -30.256  1.00 44.93           O  
ANISOU 1284  O   ALA A 211     7152   5484   4436   -301    734   -757       O  
ATOM   1285  CB  ALA A 211      40.736 -28.910 -32.969  1.00 57.64           C  
ANISOU 1285  CB  ALA A 211     9434   6922   5546   -510    771   -858       C  
ATOM   1286  N   PRO A 212      42.541 -28.964 -30.379  1.00 49.91           N  
ANISOU 1286  N   PRO A 212     7972   5905   5088   -120   1009   -934       N  
ATOM   1287  CA  PRO A 212      42.728 -28.966 -28.915  1.00 40.93           C  
ANISOU 1287  CA  PRO A 212     6570   4781   4201     -8    928   -914       C  
ATOM   1288  C   PRO A 212      43.509 -27.770 -28.392  1.00 45.70           C  
ANISOU 1288  C   PRO A 212     6839   5499   5027     73    963   -827       C  
ATOM   1289  O   PRO A 212      43.218 -27.286 -27.291  1.00 43.83           O  
ANISOU 1289  O   PRO A 212     6379   5332   4943     77    786   -765       O  
ATOM   1290  CB  PRO A 212      43.475 -30.287 -28.660  1.00 37.22           C  
ANISOU 1290  CB  PRO A 212     6165   4158   3819    150   1083  -1003       C  
ATOM   1291  CG  PRO A 212      44.138 -30.606 -29.956  1.00 46.30           C  
ANISOU 1291  CG  PRO A 212     7463   5256   4874    167   1294  -1031       C  
ATOM   1292  CD  PRO A 212      43.151 -30.155 -31.003  1.00 49.32           C  
ANISOU 1292  CD  PRO A 212     8051   5698   4992    -44   1174  -1006       C  
ATOM   1293  N   LYS A 213      44.487 -27.269 -29.155  1.00 50.32           N  
ANISOU 1293  N   LYS A 213     7394   6098   5630    126   1195   -822       N  
ATOM   1294  CA  LYS A 213      45.286 -26.142 -28.685  1.00 45.62           C  
ANISOU 1294  CA  LYS A 213     6473   5595   5264    182   1230   -740       C  
ATOM   1295  C   LYS A 213      44.433 -24.893 -28.510  1.00 53.90           C  
ANISOU 1295  C   LYS A 213     7431   6753   6295     44   1029   -646       C  
ATOM   1296  O   LYS A 213      44.624 -24.130 -27.555  1.00 51.91           O  
ANISOU 1296  O   LYS A 213     6918   6562   6245     65    929   -595       O  
ATOM   1297  CB  LYS A 213      46.437 -25.874 -29.654  1.00 38.79           C  
ANISOU 1297  CB  LYS A 213     5607   4713   4418    247   1544   -742       C  
ATOM   1298  CG  LYS A 213      47.491 -26.965 -29.671  1.00 46.65           C  
ANISOU 1298  CG  LYS A 213     6604   5594   5529    429   1786   -814       C  
ATOM   1299  CD  LYS A 213      48.757 -26.495 -30.369  1.00 51.61           C  
ANISOU 1299  CD  LYS A 213     7096   6234   6281    501   2054   -763       C  
ATOM   1300  CE  LYS A 213      49.599 -27.659 -30.863  1.00 67.48           C  
ANISOU 1300  CE  LYS A 213     9184   8127   8328    628   2232   -799       C  
ATOM   1301  NZ  LYS A 213      50.386 -28.292 -29.777  1.00 74.09           N  
ANISOU 1301  NZ  LYS A 213     9757   8929   9465    801   2209   -779       N  
ATOM   1302  N   ILE A 214      43.485 -24.667 -29.422  1.00 52.83           N  
ANISOU 1302  N   ILE A 214     7515   6636   5923    -99    963   -617       N  
ATOM   1303  CA  ILE A 214      42.604 -23.509 -29.312  1.00 39.39           C  
ANISOU 1303  CA  ILE A 214     5724   5020   4224   -214    779   -504       C  
ATOM   1304  C   ILE A 214      41.538 -23.741 -28.250  1.00 35.93           C  
ANISOU 1304  C   ILE A 214     5218   4591   3841   -246    532   -493       C  
ATOM   1305  O   ILE A 214      41.280 -22.875 -27.405  1.00 30.60           O  
ANISOU 1305  O   ILE A 214     4336   3964   3325   -248    427   -433       O  
ATOM   1306  CB  ILE A 214      41.974 -23.180 -30.680  1.00 42.05           C  
ANISOU 1306  CB  ILE A 214     6303   5379   4295   -353    775   -444       C  
ATOM   1307  CG1 ILE A 214      43.060 -22.806 -31.695  1.00 46.30           C  
ANISOU 1307  CG1 ILE A 214     6904   5911   4775   -322   1054   -439       C  
ATOM   1308  CG2 ILE A 214      40.962 -22.057 -30.535  1.00 50.53           C  
ANISOU 1308  CG2 ILE A 214     7270   6526   5403   -455    569   -303       C  
ATOM   1309  CD1 ILE A 214      42.589 -22.856 -33.137  1.00 53.66           C  
ANISOU 1309  CD1 ILE A 214     8172   6847   5368   -452   1085   -410       C  
ATOM   1310  N   TYR A 215      40.903 -24.913 -28.283  1.00 47.12           N  
ANISOU 1310  N   TYR A 215     6824   5951   5130   -279    456   -554       N  
ATOM   1311  CA  TYR A 215      39.832 -25.226 -27.344  1.00 42.36           C  
ANISOU 1311  CA  TYR A 215     6172   5351   4574   -322    244   -531       C  
ATOM   1312  C   TYR A 215      40.290 -25.084 -25.897  1.00 41.06           C  
ANISOU 1312  C   TYR A 215     5768   5196   4635   -207    225   -541       C  
ATOM   1313  O   TYR A 215      39.690 -24.349 -25.107  1.00 33.97           O  
ANISOU 1313  O   TYR A 215     4721   4348   3837   -233    106   -479       O  
ATOM   1314  CB  TYR A 215      39.324 -26.642 -27.604  1.00 41.01           C  
ANISOU 1314  CB  TYR A 215     6243   5088   4250   -370    203   -609       C  
ATOM   1315  CG  TYR A 215      38.215 -27.078 -26.682  1.00 42.53           C  
ANISOU 1315  CG  TYR A 215     6391   5274   4495   -425      7   -576       C  
ATOM   1316  CD1 TYR A 215      36.916 -26.623 -26.863  1.00 51.57           C  
ANISOU 1316  CD1 TYR A 215     7524   6474   5596   -570   -178   -474       C  
ATOM   1317  CD2 TYR A 215      38.465 -27.949 -25.633  1.00 42.48           C  
ANISOU 1317  CD2 TYR A 215     6345   5201   4594   -328     14   -629       C  
ATOM   1318  CE1 TYR A 215      35.893 -27.024 -26.025  1.00 51.82           C  
ANISOU 1318  CE1 TYR A 215     7495   6497   5699   -620   -326   -432       C  
ATOM   1319  CE2 TYR A 215      37.453 -28.355 -24.791  1.00 46.63           C  
ANISOU 1319  CE2 TYR A 215     6840   5717   5162   -383   -137   -589       C  
ATOM   1320  CZ  TYR A 215      36.169 -27.891 -24.989  1.00 49.90           C  
ANISOU 1320  CZ  TYR A 215     7231   6186   5542   -530   -294   -495       C  
ATOM   1321  OH  TYR A 215      35.162 -28.300 -24.145  1.00 52.13           O  
ANISOU 1321  OH  TYR A 215     7462   6455   5891   -583   -415   -444       O  
ATOM   1322  N   HIS A 216      41.362 -25.790 -25.531  1.00 45.15           N  
ANISOU 1322  N   HIS A 216     6256   5662   5234    -76    343   -614       N  
ATOM   1323  CA  HIS A 216      41.802 -25.783 -24.141  1.00 40.62           C  
ANISOU 1323  CA  HIS A 216     5485   5104   4846     20    287   -614       C  
ATOM   1324  C   HIS A 216      42.442 -24.463 -23.734  1.00 46.01           C  
ANISOU 1324  C   HIS A 216     5934   5863   5684     36    299   -574       C  
ATOM   1325  O   HIS A 216      42.523 -24.172 -22.535  1.00 50.92           O  
ANISOU 1325  O   HIS A 216     6410   6514   6422     65    200   -567       O  
ATOM   1326  CB  HIS A 216      42.759 -26.948 -23.894  1.00 40.92           C  
ANISOU 1326  CB  HIS A 216     5544   5061   4945    160    388   -675       C  
ATOM   1327  CG  HIS A 216      42.072 -28.275 -23.818  1.00 37.49           C  
ANISOU 1327  CG  HIS A 216     5313   4525   4404    148    340   -714       C  
ATOM   1328  ND1 HIS A 216      41.394 -28.695 -22.694  1.00 35.90           N  
ANISOU 1328  ND1 HIS A 216     5089   4316   4234    140    187   -688       N  
ATOM   1329  CD2 HIS A 216      41.945 -29.271 -24.726  1.00 37.79           C  
ANISOU 1329  CD2 HIS A 216     5601   4454   4302    131    432   -781       C  
ATOM   1330  CE1 HIS A 216      40.884 -29.894 -22.908  1.00 40.76           C  
ANISOU 1330  CE1 HIS A 216     5910   4821   4755    116    181   -725       C  
ATOM   1331  NE2 HIS A 216      41.204 -30.266 -24.134  1.00 42.92           N  
ANISOU 1331  NE2 HIS A 216     6359   5026   4922    106    323   -791       N  
ATOM   1332  N   SER A 217      42.904 -23.660 -24.693  1.00 46.07           N  
ANISOU 1332  N   SER A 217     5923   5896   5686      7    418   -548       N  
ATOM   1333  CA  SER A 217      43.367 -22.322 -24.345  1.00 36.85           C  
ANISOU 1333  CA  SER A 217     4548   4782   4670    -10    419   -504       C  
ATOM   1334  C   SER A 217      42.199 -21.424 -23.961  1.00 39.09           C  
ANISOU 1334  C   SER A 217     4814   5094   4945   -105    277   -448       C  
ATOM   1335  O   SER A 217      42.289 -20.658 -22.995  1.00 55.98           O  
ANISOU 1335  O   SER A 217     6805   7250   7216   -107    213   -447       O  
ATOM   1336  CB  SER A 217      44.156 -21.713 -25.504  1.00 30.26           C  
ANISOU 1336  CB  SER A 217     3704   3955   3839    -21    606   -474       C  
ATOM   1337  OG  SER A 217      45.349 -22.440 -25.743  1.00 27.14           O  
ANISOU 1337  OG  SER A 217     3275   3528   3509     89    775   -518       O  
ATOM   1338  N   CYS A 218      41.093 -21.506 -24.706  1.00 39.30           N  
ANISOU 1338  N   CYS A 218     4992   5117   4821   -187    227   -399       N  
ATOM   1339  CA  CYS A 218      39.938 -20.665 -24.408  1.00 34.62           C  
ANISOU 1339  CA  CYS A 218     4357   4543   4256   -260    110   -319       C  
ATOM   1340  C   CYS A 218      39.290 -21.046 -23.083  1.00 42.49           C  
ANISOU 1340  C   CYS A 218     5306   5530   5307   -238     -2   -346       C  
ATOM   1341  O   CYS A 218      38.872 -20.170 -22.317  1.00 52.33           O  
ANISOU 1341  O   CYS A 218     6447   6779   6659   -247    -41   -320       O  
ATOM   1342  CB  CYS A 218      38.920 -20.756 -25.543  1.00 33.30           C  
ANISOU 1342  CB  CYS A 218     4342   4383   3927   -357     53   -235       C  
ATOM   1343  SG  CYS A 218      39.580 -20.295 -27.154  1.00 49.05           S  
ANISOU 1343  SG  CYS A 218     6449   6391   5796   -399    191   -187       S  
ATOM   1344  N   PHE A 219      39.199 -22.344 -22.786  1.00 43.32           N  
ANISOU 1344  N   PHE A 219     5507   5613   5341   -208    -36   -399       N  
ATOM   1345  CA  PHE A 219      38.550 -22.757 -21.547  1.00 42.37           C  
ANISOU 1345  CA  PHE A 219     5363   5483   5255   -194   -127   -409       C  
ATOM   1346  C   PHE A 219      39.436 -22.585 -20.320  1.00 44.12           C  
ANISOU 1346  C   PHE A 219     5473   5713   5579   -114   -124   -466       C  
ATOM   1347  O   PHE A 219      38.920 -22.590 -19.197  1.00 49.73           O  
ANISOU 1347  O   PHE A 219     6163   6423   6309   -111   -186   -468       O  
ATOM   1348  CB  PHE A 219      38.069 -24.205 -21.658  1.00 43.95           C  
ANISOU 1348  CB  PHE A 219     5715   5638   5346   -205   -169   -428       C  
ATOM   1349  CG  PHE A 219      36.625 -24.323 -22.052  1.00 60.41           C  
ANISOU 1349  CG  PHE A 219     7863   7721   7369   -318   -263   -351       C  
ATOM   1350  CD1 PHE A 219      35.637 -23.741 -21.275  1.00 63.24           C  
ANISOU 1350  CD1 PHE A 219     8117   8099   7814   -346   -320   -281       C  
ATOM   1351  CD2 PHE A 219      36.254 -25.007 -23.196  1.00 70.19           C  
ANISOU 1351  CD2 PHE A 219     9265   8934   8468   -401   -293   -345       C  
ATOM   1352  CE1 PHE A 219      34.304 -23.839 -21.629  1.00 61.01           C  
ANISOU 1352  CE1 PHE A 219     7844   7819   7519   -447   -410   -184       C  
ATOM   1353  CE2 PHE A 219      34.924 -25.110 -23.553  1.00 76.27           C  
ANISOU 1353  CE2 PHE A 219    10069   9712   9197   -526   -417   -258       C  
ATOM   1354  CZ  PHE A 219      33.947 -24.526 -22.770  1.00 70.12           C  
ANISOU 1354  CZ  PHE A 219     9137   8961   8544   -545   -479   -166       C  
ATOM   1355  N   PHE A 220      40.748 -22.438 -20.498  1.00 36.64           N  
ANISOU 1355  N   PHE A 220     4452   4776   4695    -58    -56   -505       N  
ATOM   1356  CA  PHE A 220      41.581 -22.053 -19.365  1.00 20.88           C  
ANISOU 1356  CA  PHE A 220     2325   2803   2808    -15    -94   -542       C  
ATOM   1357  C   PHE A 220      41.394 -20.578 -19.043  1.00 29.64           C  
ANISOU 1357  C   PHE A 220     3343   3923   3996    -81   -102   -535       C  
ATOM   1358  O   PHE A 220      41.257 -20.197 -17.874  1.00 47.88           O  
ANISOU 1358  O   PHE A 220     5627   6236   6332    -92   -170   -567       O  
ATOM   1359  CB  PHE A 220      43.051 -22.352 -19.652  1.00 25.41           C  
ANISOU 1359  CB  PHE A 220     2805   3383   3466     60    -28   -565       C  
ATOM   1360  CG  PHE A 220      43.988 -21.841 -18.595  1.00 40.69           C  
ANISOU 1360  CG  PHE A 220     4578   5353   5528     76   -102   -586       C  
ATOM   1361  CD1 PHE A 220      44.098 -22.487 -17.373  1.00 47.77           C  
ANISOU 1361  CD1 PHE A 220     5479   6261   6412    120   -227   -599       C  
ATOM   1362  CD2 PHE A 220      44.746 -20.705 -18.817  1.00 44.17           C  
ANISOU 1362  CD2 PHE A 220     4873   5814   6094     30    -63   -586       C  
ATOM   1363  CE1 PHE A 220      44.957 -22.010 -16.398  1.00 48.11           C  
ANISOU 1363  CE1 PHE A 220     5389   6346   6546    111   -333   -614       C  
ATOM   1364  CE2 PHE A 220      45.604 -20.226 -17.849  1.00 47.22           C  
ANISOU 1364  CE2 PHE A 220     5114   6232   6596     13   -162   -610       C  
ATOM   1365  CZ  PHE A 220      45.711 -20.877 -16.638  1.00 48.49           C  
ANISOU 1365  CZ  PHE A 220     5286   6414   6723     50   -310   -626       C  
ATOM   1366  N   ILE A 221      41.394 -19.737 -20.077  1.00 20.29           N  
ANISOU 1366  N   ILE A 221     2134   2733   2841   -126    -23   -493       N  
ATOM   1367  CA  ILE A 221      41.140 -18.312 -19.886  1.00 20.72           C  
ANISOU 1367  CA  ILE A 221     2118   2767   2987   -186    -11   -474       C  
ATOM   1368  C   ILE A 221      39.739 -18.097 -19.332  1.00 31.79           C  
ANISOU 1368  C   ILE A 221     3575   4143   4361   -209    -56   -444       C  
ATOM   1369  O   ILE A 221      39.547 -17.439 -18.304  1.00 33.44           O  
ANISOU 1369  O   ILE A 221     3758   4323   4625   -220    -72   -485       O  
ATOM   1370  CB  ILE A 221      41.334 -17.549 -21.207  1.00 23.38           C  
ANISOU 1370  CB  ILE A 221     2436   3095   3351   -226     88   -403       C  
ATOM   1371  CG1 ILE A 221      42.763 -17.721 -21.729  1.00 21.53           C  
ANISOU 1371  CG1 ILE A 221     2129   2882   3168   -199    176   -426       C  
ATOM   1372  CG2 ILE A 221      40.998 -16.079 -21.023  1.00 40.76           C  
ANISOU 1372  CG2 ILE A 221     4576   5247   5666   -281    107   -369       C  
ATOM   1373  CD1 ILE A 221      43.832 -17.238 -20.774  1.00 31.63           C  
ANISOU 1373  CD1 ILE A 221     3251   4165   4601   -200    145   -487       C  
ATOM   1374  N   VAL A 222      38.737 -18.650 -20.019  1.00 42.75           N  
ANISOU 1374  N   VAL A 222     5043   5535   5665   -223    -71   -372       N  
ATOM   1375  CA  VAL A 222      37.347 -18.319 -19.717  1.00 39.40           C  
ANISOU 1375  CA  VAL A 222     4624   5086   5261   -248    -96   -304       C  
ATOM   1376  C   VAL A 222      36.938 -18.809 -18.332  1.00 39.34           C  
ANISOU 1376  C   VAL A 222     4640   5069   5239   -220   -126   -359       C  
ATOM   1377  O   VAL A 222      36.229 -18.108 -17.601  1.00 35.58           O  
ANISOU 1377  O   VAL A 222     4138   4554   4829   -221    -91   -348       O  
ATOM   1378  CB  VAL A 222      36.421 -18.891 -20.803  1.00 36.60           C  
ANISOU 1378  CB  VAL A 222     4334   4749   4824   -292   -142   -201       C  
ATOM   1379  CG1 VAL A 222      34.982 -18.901 -20.310  1.00 41.52           C  
ANISOU 1379  CG1 VAL A 222     4930   5354   5491   -311   -183   -122       C  
ATOM   1380  CG2 VAL A 222      36.556 -18.089 -22.079  1.00 32.75           C  
ANISOU 1380  CG2 VAL A 222     3836   4264   4341   -332   -112   -115       C  
ATOM   1381  N   THR A 223      37.361 -20.013 -17.948  1.00 47.88           N  
ANISOU 1381  N   THR A 223     5784   6175   6233   -188   -172   -410       N  
ATOM   1382  CA  THR A 223      36.860 -20.634 -16.725  1.00 42.70           C  
ANISOU 1382  CA  THR A 223     5180   5512   5534   -168   -201   -433       C  
ATOM   1383  C   THR A 223      37.859 -20.668 -15.574  1.00 36.76           C  
ANISOU 1383  C   THR A 223     4432   4772   4762   -131   -234   -525       C  
ATOM   1384  O   THR A 223      37.523 -21.195 -14.507  1.00 39.80           O  
ANISOU 1384  O   THR A 223     4885   5155   5081   -116   -259   -539       O  
ATOM   1385  CB  THR A 223      36.375 -22.057 -17.015  1.00 39.16           C  
ANISOU 1385  CB  THR A 223     4819   5063   4998   -171   -246   -397       C  
ATOM   1386  OG1 THR A 223      37.504 -22.913 -17.220  1.00 28.47           O  
ANISOU 1386  OG1 THR A 223     3504   3716   3598   -121   -267   -450       O  
ATOM   1387  CG2 THR A 223      35.481 -22.071 -18.250  1.00 49.39           C  
ANISOU 1387  CG2 THR A 223     6121   6355   6292   -236   -258   -307       C  
ATOM   1388  N   TYR A 224      39.066 -20.131 -15.743  1.00 35.44           N  
ANISOU 1388  N   TYR A 224     4193   4623   4651   -127   -242   -574       N  
ATOM   1389  CA  TYR A 224      39.982 -20.074 -14.610  1.00 30.74           C  
ANISOU 1389  CA  TYR A 224     3587   4049   4045   -116   -315   -647       C  
ATOM   1390  C   TYR A 224      40.632 -18.703 -14.489  1.00 26.87           C  
ANISOU 1390  C   TYR A 224     3014   3544   3651   -171   -303   -702       C  
ATOM   1391  O   TYR A 224      40.386 -17.974 -13.522  1.00 27.75           O  
ANISOU 1391  O   TYR A 224     3175   3625   3746   -213   -309   -762       O  
ATOM   1392  CB  TYR A 224      41.062 -21.152 -14.718  1.00 33.89           C  
ANISOU 1392  CB  TYR A 224     3956   4484   4436    -51   -379   -644       C  
ATOM   1393  CG  TYR A 224      41.946 -21.242 -13.489  1.00 45.66           C  
ANISOU 1393  CG  TYR A 224     5428   6011   5912    -41   -501   -685       C  
ATOM   1394  CD1 TYR A 224      41.587 -22.041 -12.411  1.00 43.42           C  
ANISOU 1394  CD1 TYR A 224     5257   5733   5507    -16   -575   -675       C  
ATOM   1395  CD2 TYR A 224      43.130 -20.519 -13.402  1.00 49.80           C  
ANISOU 1395  CD2 TYR A 224     5821   6563   6539    -72   -555   -721       C  
ATOM   1396  CE1 TYR A 224      42.386 -22.124 -11.283  1.00 41.69           C  
ANISOU 1396  CE1 TYR A 224     5039   5555   5246    -18   -716   -695       C  
ATOM   1397  CE2 TYR A 224      43.937 -20.595 -12.278  1.00 36.85           C  
ANISOU 1397  CE2 TYR A 224     4157   4965   4878    -84   -710   -745       C  
ATOM   1398  CZ  TYR A 224      43.559 -21.398 -11.223  1.00 38.92           C  
ANISOU 1398  CZ  TYR A 224     4551   5241   4995    -56   -798   -731       C  
ATOM   1399  OH  TYR A 224      44.359 -21.475 -10.105  1.00 41.58           O  
ANISOU 1399  OH  TYR A 224     4883   5630   5286    -78   -980   -739       O  
ATOM   1400  N   LEU A 225      41.464 -18.340 -15.467  1.00 19.47           N  
ANISOU 1400  N   LEU A 225     1970   2617   2813   -179   -272   -686       N  
ATOM   1401  CA  LEU A 225      42.235 -17.108 -15.348  1.00 29.78           C  
ANISOU 1401  CA  LEU A 225     3184   3899   4231   -247   -269   -734       C  
ATOM   1402  C   LEU A 225      41.324 -15.887 -15.306  1.00 30.98           C  
ANISOU 1402  C   LEU A 225     3378   3968   4424   -300   -186   -740       C  
ATOM   1403  O   LEU A 225      41.442 -15.042 -14.410  1.00 39.56           O  
ANISOU 1403  O   LEU A 225     4494   5006   5532   -359   -203   -823       O  
ATOM   1404  CB  LEU A 225      43.230 -17.002 -16.505  1.00 37.11           C  
ANISOU 1404  CB  LEU A 225     3983   4848   5268   -243   -214   -692       C  
ATOM   1405  CG  LEU A 225      44.498 -16.184 -16.247  1.00 36.56           C  
ANISOU 1405  CG  LEU A 225     3770   4780   5339   -309   -252   -734       C  
ATOM   1406  CD1 LEU A 225      45.493 -16.995 -15.439  1.00 40.35           C  
ANISOU 1406  CD1 LEU A 225     4178   5329   5825   -277   -392   -758       C  
ATOM   1407  CD2 LEU A 225      45.114 -15.705 -17.553  1.00 36.16           C  
ANISOU 1407  CD2 LEU A 225     3608   4721   5410   -324   -126   -672       C  
ATOM   1408  N   ALA A 226      40.408 -15.771 -16.268  1.00 28.27           N  
ANISOU 1408  N   ALA A 226     3047   3600   4095   -281    -98   -650       N  
ATOM   1409  CA  ALA A 226      39.566 -14.577 -16.331  1.00 24.99           C  
ANISOU 1409  CA  ALA A 226     2641   3092   3761   -310     -9   -623       C  
ATOM   1410  C   ALA A 226      38.692 -14.401 -15.098  1.00 29.35           C  
ANISOU 1410  C   ALA A 226     3288   3592   4273   -302     13   -680       C  
ATOM   1411  O   ALA A 226      38.710 -13.310 -14.503  1.00 33.87           O  
ANISOU 1411  O   ALA A 226     3887   4071   4910   -342     68   -750       O  
ATOM   1412  CB  ALA A 226      38.722 -14.610 -17.610  1.00 17.78           C  
ANISOU 1412  CB  ALA A 226     1712   2178   2864   -291     44   -483       C  
ATOM   1413  N   PRO A 227      37.900 -15.390 -14.672  1.00 22.35           N  
ANISOU 1413  N   PRO A 227     2466   2743   3283   -258     -4   -655       N  
ATOM   1414  CA  PRO A 227      37.073 -15.179 -13.473  1.00 22.95           C  
ANISOU 1414  CA  PRO A 227     2639   2763   3317   -248     59   -704       C  
ATOM   1415  C   PRO A 227      37.885 -14.907 -12.219  1.00 42.68           C  
ANISOU 1415  C   PRO A 227     5233   5252   5733   -294      7   -851       C  
ATOM   1416  O   PRO A 227      37.571 -13.974 -11.468  1.00 51.61           O  
ANISOU 1416  O   PRO A 227     6447   6286   6877   -322     97   -931       O  
ATOM   1417  CB  PRO A 227      36.270 -16.487 -13.379  1.00 23.14           C  
ANISOU 1417  CB  PRO A 227     2700   2846   3247   -205     35   -632       C  
ATOM   1418  CG  PRO A 227      36.261 -17.018 -14.782  1.00 22.09           C  
ANISOU 1418  CG  PRO A 227     2487   2761   3145   -200    -10   -527       C  
ATOM   1419  CD  PRO A 227      37.617 -16.681 -15.318  1.00 24.53           C  
ANISOU 1419  CD  PRO A 227     2744   3094   3484   -221    -56   -575       C  
ATOM   1420  N   LEU A 228      38.938 -15.690 -11.980  1.00 46.52           N  
ANISOU 1420  N   LEU A 228     5711   5827   6135   -305   -139   -886       N  
ATOM   1421  CA  LEU A 228      39.751 -15.479 -10.788  1.00 32.33           C  
ANISOU 1421  CA  LEU A 228     3998   4039   4247   -366   -240  -1007       C  
ATOM   1422  C   LEU A 228      40.461 -14.132 -10.837  1.00 36.61           C  
ANISOU 1422  C   LEU A 228     4501   4508   4901   -459   -237  -1092       C  
ATOM   1423  O   LEU A 228      40.636 -13.474  -9.805  1.00 44.51           O  
ANISOU 1423  O   LEU A 228     5625   5452   5833   -537   -258  -1215       O  
ATOM   1424  CB  LEU A 228      40.758 -16.616 -10.631  1.00 21.63           C  
ANISOU 1424  CB  LEU A 228     2599   2796   2822   -346   -414   -986       C  
ATOM   1425  CG  LEU A 228      40.302 -17.778  -9.742  1.00 28.27           C  
ANISOU 1425  CG  LEU A 228     3570   3682   3487   -297   -463   -961       C  
ATOM   1426  CD1 LEU A 228      38.923 -18.279 -10.151  1.00 34.68           C  
ANISOU 1426  CD1 LEU A 228     4418   4465   4294   -236   -323   -877       C  
ATOM   1427  CD2 LEU A 228      41.321 -18.903  -9.781  1.00 37.51           C  
ANISOU 1427  CD2 LEU A 228     4671   4942   4639   -253   -623   -910       C  
ATOM   1428  N   GLY A 229      40.868 -13.699 -12.030  1.00 31.52           N  
ANISOU 1428  N   GLY A 229     3706   3854   4418   -464   -204  -1030       N  
ATOM   1429  CA  GLY A 229      41.471 -12.382 -12.152  1.00 32.16           C  
ANISOU 1429  CA  GLY A 229     3744   3844   4630   -560   -180  -1094       C  
ATOM   1430  C   GLY A 229      40.498 -11.271 -11.813  1.00 39.33           C  
ANISOU 1430  C   GLY A 229     4767   4596   5581   -574    -20  -1142       C  
ATOM   1431  O   GLY A 229      40.811 -10.369 -11.033  1.00 49.60           O  
ANISOU 1431  O   GLY A 229     6165   5799   6883   -669    -20  -1274       O  
ATOM   1432  N   LEU A 230      39.297 -11.324 -12.396  1.00 39.23           N  
ANISOU 1432  N   LEU A 230     4745   4548   5613   -482    118  -1033       N  
ATOM   1433  CA  LEU A 230      38.287 -10.314 -12.095  1.00 40.53           C  
ANISOU 1433  CA  LEU A 230     4992   4553   5857   -462    297  -1051       C  
ATOM   1434  C   LEU A 230      37.850 -10.386 -10.639  1.00 51.31           C  
ANISOU 1434  C   LEU A 230     6552   5873   7068   -469    341  -1183       C  
ATOM   1435  O   LEU A 230      37.569  -9.355 -10.015  1.00 66.51           O  
ANISOU 1435  O   LEU A 230     8602   7640   9028   -500    472  -1288       O  
ATOM   1436  CB  LEU A 230      37.084 -10.487 -13.022  1.00 33.32           C  
ANISOU 1436  CB  LEU A 230     3989   3633   5038   -359    402   -872       C  
ATOM   1437  CG  LEU A 230      37.307 -10.121 -14.490  1.00 34.09           C  
ANISOU 1437  CG  LEU A 230     3940   3736   5275   -358    396   -732       C  
ATOM   1438  CD1 LEU A 230      36.205 -10.696 -15.370  1.00 39.46           C  
ANISOU 1438  CD1 LEU A 230     4545   4470   5979   -278    414   -548       C  
ATOM   1439  CD2 LEU A 230      37.391  -8.610 -14.646  1.00 24.89           C  
ANISOU 1439  CD2 LEU A 230     2774   2395   4289   -394    513   -746       C  
ATOM   1440  N   MET A 231      37.783 -11.595 -10.079  1.00 45.16           N  
ANISOU 1440  N   MET A 231     5826   5220   6111   -441    251  -1179       N  
ATOM   1441  CA  MET A 231      37.358 -11.732  -8.689  1.00 45.32           C  
ANISOU 1441  CA  MET A 231     6059   5210   5951   -450    303  -1289       C  
ATOM   1442  C   MET A 231      38.420 -11.208  -7.730  1.00 51.55           C  
ANISOU 1442  C   MET A 231     6989   5983   6617   -571    176  -1442       C  
ATOM   1443  O   MET A 231      38.091 -10.578  -6.719  1.00 59.81           O  
ANISOU 1443  O   MET A 231     8225   6937   7561   -585    261  -1518       O  
ATOM   1444  CB  MET A 231      37.025 -13.191  -8.375  1.00 48.62           C  
ANISOU 1444  CB  MET A 231     6498   5763   6213   -391    234  -1214       C  
ATOM   1445  CG  MET A 231      35.659 -13.640  -8.867  1.00 53.63           C  
ANISOU 1445  CG  MET A 231     7059   6388   6928   -288    384  -1067       C  
ATOM   1446  SD  MET A 231      35.512 -15.435  -8.934  1.00 50.51           S  
ANISOU 1446  SD  MET A 231     6638   6147   6406   -243    259   -954       S  
ATOM   1447  CE  MET A 231      35.371 -15.819  -7.192  1.00 57.74           C  
ANISOU 1447  CE  MET A 231     7810   7063   7065   -265    290  -1056       C  
ATOM   1448  N   ALA A 232      39.699 -11.455  -8.029  1.00 45.03           N  
ANISOU 1448  N   ALA A 232     6053   5257   5800   -636    -42  -1431       N  
ATOM   1449  CA  ALA A 232      40.762 -10.954  -7.164  1.00 33.82           C  
ANISOU 1449  CA  ALA A 232     4733   3832   4285   -743   -209  -1504       C  
ATOM   1450  C   ALA A 232      40.740  -9.434  -7.091  1.00 42.72           C  
ANISOU 1450  C   ALA A 232     5930   4789   5514   -807    -99  -1582       C  
ATOM   1451  O   ALA A 232      41.019  -8.849  -6.038  1.00 51.14           O  
ANISOU 1451  O   ALA A 232     7179   5791   6460   -876   -156  -1683       O  
ATOM   1452  CB  ALA A 232      42.121 -11.451  -7.657  1.00 35.15           C  
ANISOU 1452  CB  ALA A 232     4717   4127   4511   -793   -430  -1440       C  
ATOM   1453  N   MET A 233      40.411  -8.774  -8.204  1.00 45.36           N  
ANISOU 1453  N   MET A 233     6124   5038   6073   -782     51  -1533       N  
ATOM   1454  CA  MET A 233      40.308  -7.319  -8.194  1.00 41.72           C  
ANISOU 1454  CA  MET A 233     5728   4395   5730   -827    179  -1587       C  
ATOM   1455  C   MET A 233      39.049  -6.859  -7.471  1.00 45.41           C  
ANISOU 1455  C   MET A 233     6379   4730   6144   -750    404  -1634       C  
ATOM   1456  O   MET A 233      39.053  -5.814  -6.809  1.00 59.49           O  
ANISOU 1456  O   MET A 233     8317   6377   7910   -797    469  -1728       O  
ATOM   1457  CB  MET A 233      40.339  -6.790  -9.627  1.00 35.02           C  
ANISOU 1457  CB  MET A 233     4671   3490   5143   -811    269  -1489       C  
ATOM   1458  CG  MET A 233      41.604  -7.169 -10.374  1.00 38.81           C  
ANISOU 1458  CG  MET A 233     4959   4098   5691   -878     87  -1430       C  
ATOM   1459  SD  MET A 233      41.725  -6.442 -12.017  1.00 55.06           S  
ANISOU 1459  SD  MET A 233     6808   6083   8030   -870    202  -1300       S  
ATOM   1460  CE  MET A 233      40.626  -7.509 -12.941  1.00 55.22           C  
ANISOU 1460  CE  MET A 233     6728   6174   8079   -728    284  -1171       C  
ATOM   1461  N   ALA A 234      37.959  -7.619  -7.595  1.00 38.42           N  
ANISOU 1461  N   ALA A 234     5472   3879   5247   -632    534  -1564       N  
ATOM   1462  CA  ALA A 234      36.718  -7.244  -6.927  1.00 38.11           C  
ANISOU 1462  CA  ALA A 234     5570   3724   5184   -545    776  -1576       C  
ATOM   1463  C   ALA A 234      36.861  -7.333  -5.414  1.00 39.77           C  
ANISOU 1463  C   ALA A 234     6031   3953   5128   -590    729  -1698       C  
ATOM   1464  O   ALA A 234      36.483  -6.407  -4.689  1.00 47.58           O  
ANISOU 1464  O   ALA A 234     7181   4806   6092   -593    876  -1778       O  
ATOM   1465  CB  ALA A 234      35.570  -8.131  -7.411  1.00 32.00           C  
ANISOU 1465  CB  ALA A 234     4689   2994   4476   -418    907  -1451       C  
ATOM   1466  N   TYR A 235      37.402  -8.446  -4.917  1.00 34.35           N  
ANISOU 1466  N   TYR A 235     5381   3429   4240   -621    526  -1708       N  
ATOM   1467  CA  TYR A 235      37.568  -8.587  -3.477  1.00 34.08           C  
ANISOU 1467  CA  TYR A 235     5579   3423   3946   -663    461  -1809       C  
ATOM   1468  C   TYR A 235      38.632  -7.646  -2.931  1.00 37.22           C  
ANISOU 1468  C   TYR A 235     6078   3764   4300   -793    303  -1939       C  
ATOM   1469  O   TYR A 235      38.585  -7.281  -1.750  1.00 47.02           O  
ANISOU 1469  O   TYR A 235     7537   4963   5364   -835    322  -2052       O  
ATOM   1470  CB  TYR A 235      37.881 -10.038  -3.126  1.00 43.23           C  
ANISOU 1470  CB  TYR A 235     6733   4769   4923   -652    275  -1759       C  
ATOM   1471  CG  TYR A 235      36.660 -10.926  -3.185  1.00 46.22           C  
ANISOU 1471  CG  TYR A 235     7104   5180   5278   -539    461  -1662       C  
ATOM   1472  CD1 TYR A 235      35.676 -10.846  -2.207  1.00 53.98           C  
ANISOU 1472  CD1 TYR A 235     8265   6104   6141   -495    674  -1683       C  
ATOM   1473  CD2 TYR A 235      36.480 -11.830  -4.222  1.00 38.05           C  
ANISOU 1473  CD2 TYR A 235     5881   4226   4350   -486    436  -1548       C  
ATOM   1474  CE1 TYR A 235      34.556 -11.648  -2.253  1.00 53.77           C  
ANISOU 1474  CE1 TYR A 235     8214   6097   6118   -400    852  -1579       C  
ATOM   1475  CE2 TYR A 235      35.362 -12.636  -4.276  1.00 51.69           C  
ANISOU 1475  CE2 TYR A 235     7597   5972   6070   -398    599  -1460       C  
ATOM   1476  CZ  TYR A 235      34.403 -12.541  -3.289  1.00 57.45           C  
ANISOU 1476  CZ  TYR A 235     8489   6641   6697   -354    807  -1468       C  
ATOM   1477  OH  TYR A 235      33.286 -13.342  -3.337  1.00 67.19           O  
ANISOU 1477  OH  TYR A 235     9692   7887   7948   -271    979  -1362       O  
ATOM   1478  N   PHE A 236      39.596  -7.240  -3.759  1.00 40.09           N  
ANISOU 1478  N   PHE A 236     6288   4121   4821   -869    153  -1925       N  
ATOM   1479  CA  PHE A 236      40.559  -6.249  -3.293  1.00 54.84           C  
ANISOU 1479  CA  PHE A 236     8241   5911   6686  -1004     14  -2044       C  
ATOM   1480  C   PHE A 236      39.892  -4.897  -3.086  1.00 61.63           C  
ANISOU 1480  C   PHE A 236     9239   6557   7621  -1003    261  -2128       C  
ATOM   1481  O   PHE A 236      40.192  -4.192  -2.115  1.00 74.71           O  
ANISOU 1481  O   PHE A 236    11090   8132   9163  -1091    226  -2272       O  
ATOM   1482  CB  PHE A 236      41.723  -6.127  -4.274  1.00 56.34           C  
ANISOU 1482  CB  PHE A 236     8215   6137   7054  -1092   -178  -1981       C  
ATOM   1483  CG  PHE A 236      42.778  -5.150  -3.838  1.00 58.02           C  
ANISOU 1483  CG  PHE A 236     8486   6268   7292  -1248   -347  -2089       C  
ATOM   1484  CD1 PHE A 236      43.650  -5.464  -2.808  1.00 63.06           C  
ANISOU 1484  CD1 PHE A 236     9194   6993   7773  -1335   -614  -2178       C  
ATOM   1485  CD2 PHE A 236      42.894  -3.916  -4.454  1.00 67.81           C  
ANISOU 1485  CD2 PHE A 236     9693   7342   8728  -1309   -240  -2103       C  
ATOM   1486  CE1 PHE A 236      44.620  -4.564  -2.403  1.00 72.95           C  
ANISOU 1486  CE1 PHE A 236    10476   8170   9072  -1490   -782  -2289       C  
ATOM   1487  CE2 PHE A 236      43.860  -3.014  -4.054  1.00 80.81           C  
ANISOU 1487  CE2 PHE A 236    11395   8900  10410  -1467   -401  -2204       C  
ATOM   1488  CZ  PHE A 236      44.724  -3.337  -3.028  1.00 80.07           C  
ANISOU 1488  CZ  PHE A 236    11365   8892  10168  -1563   -681  -2301       C  
ATOM   1489  N   GLN A 237      38.989  -4.514  -3.992  1.00 55.30           N  
ANISOU 1489  N   GLN A 237     8331   5657   7021   -903    513  -2038       N  
ATOM   1490  CA  GLN A 237      38.225  -3.289  -3.785  1.00 55.56           C  
ANISOU 1490  CA  GLN A 237     8483   5481   7148   -871    778  -2091       C  
ATOM   1491  C   GLN A 237      37.272  -3.434  -2.608  1.00 63.84           C  
ANISOU 1491  C   GLN A 237     9749   6500   8009   -807    959  -2155       C  
ATOM   1492  O   GLN A 237      37.064  -2.480  -1.847  1.00 73.76           O  
ANISOU 1492  O   GLN A 237    11204   7602   9218   -839   1090  -2274       O  
ATOM   1493  CB  GLN A 237      37.457  -2.923  -5.055  1.00 48.43           C  
ANISOU 1493  CB  GLN A 237     7379   4492   6529   -761    989  -1945       C  
ATOM   1494  CG  GLN A 237      38.317  -2.318  -6.154  1.00 51.95           C  
ANISOU 1494  CG  GLN A 237     7656   4899   7182   -836    890  -1897       C  
ATOM   1495  CD  GLN A 237      37.516  -1.453  -7.112  1.00 70.28           C  
ANISOU 1495  CD  GLN A 237     9858   7063   9781   -737   1135  -1783       C  
ATOM   1496  OE1 GLN A 237      36.320  -1.671  -7.311  1.00 77.35           O  
ANISOU 1496  OE1 GLN A 237    10699   7935  10754   -593   1336  -1680       O  
ATOM   1497  NE2 GLN A 237      38.173  -0.467  -7.713  1.00 82.31           N  
ANISOU 1497  NE2 GLN A 237    11328   8478  11467   -815   1112  -1779       N  
ATOM   1498  N   ILE A 238      36.682  -4.621  -2.444  1.00 63.90           N  
ANISOU 1498  N   ILE A 238     9727   6644   7909   -721    981  -2074       N  
ATOM   1499  CA  ILE A 238      35.829  -4.863  -1.285  1.00 59.66           C  
ANISOU 1499  CA  ILE A 238     9395   6093   7181   -673   1153  -2118       C  
ATOM   1500  C   ILE A 238      36.648  -4.789  -0.007  1.00 68.35           C  
ANISOU 1500  C   ILE A 238    10738   7229   8004   -803    974  -2281       C  
ATOM   1501  O   ILE A 238      36.179  -4.291   1.023  1.00 77.40           O  
ANISOU 1501  O   ILE A 238    12122   8276   9010   -816   1140  -2382       O  
ATOM   1502  CB  ILE A 238      35.118  -6.220  -1.417  1.00 52.27           C  
ANISOU 1502  CB  ILE A 238     8364   5300   6195   -571   1191  -1984       C  
ATOM   1503  CG1 ILE A 238      33.977  -6.126  -2.432  1.00 56.27           C  
ANISOU 1503  CG1 ILE A 238     8671   5733   6978   -434   1437  -1831       C  
ATOM   1504  CG2 ILE A 238      34.606  -6.676  -0.060  1.00 49.02           C  
ANISOU 1504  CG2 ILE A 238     8186   4917   5522   -565   1285  -2035       C  
ATOM   1505  CD1 ILE A 238      33.622  -7.453  -3.059  1.00 56.27           C  
ANISOU 1505  CD1 ILE A 238     8496   5882   7001   -364   1383  -1689       C  
ATOM   1506  N   PHE A 239      37.887  -5.284  -0.055  1.00 68.08           N  
ANISOU 1506  N   PHE A 239    10640   7335   7893   -903    635  -2301       N  
ATOM   1507  CA  PHE A 239      38.761  -5.230   1.111  1.00 68.10           C  
ANISOU 1507  CA  PHE A 239    10834   7387   7653  -1037    422  -2441       C  
ATOM   1508  C   PHE A 239      39.101  -3.792   1.482  1.00 72.77           C  
ANISOU 1508  C   PHE A 239    11581   7791   8276  -1146    460  -2601       C  
ATOM   1509  O   PHE A 239      39.116  -3.436   2.666  1.00 78.43           O  
ANISOU 1509  O   PHE A 239    12562   8464   8776  -1223    480  -2740       O  
ATOM   1510  CB  PHE A 239      40.024  -6.051   0.836  1.00 63.37           C  
ANISOU 1510  CB  PHE A 239    10066   6976   7037  -1107     51  -2398       C  
ATOM   1511  CG  PHE A 239      41.165  -5.756   1.768  1.00 67.70           C  
ANISOU 1511  CG  PHE A 239    10729   7565   7429  -1270   -215  -2533       C  
ATOM   1512  CD1 PHE A 239      41.200  -6.303   3.040  1.00 72.03           C  
ANISOU 1512  CD1 PHE A 239    11479   8213   7675  -1312   -287  -2585       C  
ATOM   1513  CD2 PHE A 239      42.223  -4.964   1.356  1.00 70.34           C  
ANISOU 1513  CD2 PHE A 239    10959   7842   7923  -1391   -400  -2593       C  
ATOM   1514  CE1 PHE A 239      42.258  -6.045   3.893  1.00 74.38           C  
ANISOU 1514  CE1 PHE A 239    11877   8562   7824  -1475   -545  -2701       C  
ATOM   1515  CE2 PHE A 239      43.284  -4.704   2.203  1.00 74.44           C  
ANISOU 1515  CE2 PHE A 239    11558   8408   8319  -1554   -656  -2716       C  
ATOM   1516  CZ  PHE A 239      43.302  -5.246   3.473  1.00 76.66           C  
ANISOU 1516  CZ  PHE A 239    12041   8798   8288  -1598   -734  -2771       C  
ATOM   1517  N   ARG A 240      39.390  -2.954   0.484  1.00 71.08           N  
ANISOU 1517  N   ARG A 240    11221   7462   8325  -1164    473  -2583       N  
ATOM   1518  CA  ARG A 240      39.702  -1.557   0.763  1.00 67.26           C  
ANISOU 1518  CA  ARG A 240    10882   6778   7896  -1270    518  -2729       C  
ATOM   1519  C   ARG A 240      38.500  -0.792   1.308  1.00 69.47           C  
ANISOU 1519  C   ARG A 240    11372   6869   8154  -1191    892  -2789       C  
ATOM   1520  O   ARG A 240      38.647   0.060   2.191  1.00 70.26           O  
ANISOU 1520  O   ARG A 240    11722   6834   8138  -1287    939  -2958       O  
ATOM   1521  CB  ARG A 240      40.231  -0.879  -0.501  1.00 58.40           C  
ANISOU 1521  CB  ARG A 240     9543   5570   7074  -1300    469  -2663       C  
ATOM   1522  CG  ARG A 240      41.615  -1.347  -0.925  1.00 64.02           C  
ANISOU 1522  CG  ARG A 240    10069   6426   7830  -1415    102  -2629       C  
ATOM   1523  CD  ARG A 240      42.125  -0.556  -2.124  1.00 81.76           C  
ANISOU 1523  CD  ARG A 240    12131   8566  10369  -1465     91  -2559       C  
ATOM   1524  NE  ARG A 240      42.047   0.886  -1.899  1.00 99.86           N  
ANISOU 1524  NE  ARG A 240    14581  10617  12745  -1536    227  -2679       N  
ATOM   1525  CZ  ARG A 240      43.008   1.613  -1.335  1.00109.02           C  
ANISOU 1525  CZ  ARG A 240    15844  11698  13882  -1716     36  -2824       C  
ATOM   1526  NH1 ARG A 240      44.134   1.039  -0.934  1.00113.71           N  
ANISOU 1526  NH1 ARG A 240    16370  12445  14387  -1839   -308  -2858       N  
ATOM   1527  NH2 ARG A 240      42.841   2.919  -1.170  1.00109.86           N  
ANISOU 1527  NH2 ARG A 240    16106  11565  14069  -1773    188  -2932       N  
ATOM   1528  N   LYS A 241      37.304  -1.077   0.790  1.00 70.45           N  
ANISOU 1528  N   LYS A 241    11392   6975   8400  -1020   1167  -2649       N  
ATOM   1529  CA  LYS A 241      36.124  -0.337   1.228  1.00 72.91           C  
ANISOU 1529  CA  LYS A 241    11858   7098   8747   -929   1545  -2676       C  
ATOM   1530  C   LYS A 241      35.670  -0.752   2.621  1.00 76.48           C  
ANISOU 1530  C   LYS A 241    12587   7578   8893   -941   1640  -2769       C  
ATOM   1531  O   LYS A 241      35.041   0.043   3.329  1.00 83.16           O  
ANISOU 1531  O   LYS A 241    13656   8245   9696   -932   1904  -2866       O  
ATOM   1532  CB  LYS A 241      34.985  -0.542   0.235  1.00 74.99           C  
ANISOU 1532  CB  LYS A 241    11887   7342   9265   -746   1791  -2476       C  
ATOM   1533  CG  LYS A 241      33.681   0.161   0.597  1.00 81.15           C  
ANISOU 1533  CG  LYS A 241    12618   7888  10329   -676   2060  -2442       C  
ATOM   1534  CD  LYS A 241      33.861   1.667   0.646  1.00 85.77           C  
ANISOU 1534  CD  LYS A 241    13387   8311  10890   -589   2425  -2476       C  
ATOM   1535  CE  LYS A 241      32.533   2.376   0.836  1.00 94.83           C  
ANISOU 1535  CE  LYS A 241    14528   9201  12300   -540   2672  -2473       C  
ATOM   1536  NZ  LYS A 241      32.693   3.832   1.102  1.00103.39           N  
ANISOU 1536  NZ  LYS A 241    15775  10165  13344   -701   2526  -2656       N  
ATOM   1537  N   LEU A 242      35.984  -1.980   3.041  1.00 74.16           N  
ANISOU 1537  N   LEU A 242    12295   7500   8384   -962   1440  -2735       N  
ATOM   1538  CA  LEU A 242      35.563  -2.438   4.359  1.00 69.43           C  
ANISOU 1538  CA  LEU A 242    11966   6935   7480   -978   1530  -2802       C  
ATOM   1539  C   LEU A 242      36.620  -2.128   5.408  1.00 77.31           C  
ANISOU 1539  C   LEU A 242    13216   7952   8206  -1167   1288  -2991       C  
ATOM   1540  O   LEU A 242      36.284  -1.817   6.556  1.00 80.78           O  
ANISOU 1540  O   LEU A 242    13965   8310   8417  -1214   1435  -3111       O  
ATOM   1541  CB  LEU A 242      35.256  -3.938   4.358  1.00 58.52           C  
ANISOU 1541  CB  LEU A 242    10476   5763   5997   -902   1463  -2654       C  
ATOM   1542  CG  LEU A 242      33.948  -4.392   3.704  1.00 53.30           C  
ANISOU 1542  CG  LEU A 242     9638   5082   5532   -723   1749  -2475       C  
ATOM   1543  CD1 LEU A 242      33.866  -5.909   3.676  1.00 50.03           C  
ANISOU 1543  CD1 LEU A 242     9122   4879   5009   -679   1621  -2344       C  
ATOM   1544  CD2 LEU A 242      32.760  -3.809   4.448  1.00 58.89           C  
ANISOU 1544  CD2 LEU A 242    10540   5611   6223   -655   2147  -2505       C  
ATOM   1545  N   TRP A 243      37.895  -2.216   5.039  1.00 75.49           N  
ANISOU 1545  N   TRP A 243    12854   7826   8002  -1281    922  -3015       N  
ATOM   1546  CA  TRP A 243      39.007  -1.918   5.936  1.00 77.24           C  
ANISOU 1546  CA  TRP A 243    13262   8078   8007  -1477    644  -3180       C  
ATOM   1547  C   TRP A 243      39.646  -0.618   5.455  1.00 93.46           C  
ANISOU 1547  C   TRP A 243    15288   9958  10264  -1579    589  -3291       C  
ATOM   1548  O   TRP A 243      40.465  -0.621   4.531  1.00 95.86           O  
ANISOU 1548  O   TRP A 243    15333  10314  10776  -1614    366  -3231       O  
ATOM   1549  CB  TRP A 243      40.017  -3.063   5.959  1.00 69.42           C  
ANISOU 1549  CB  TRP A 243    12119   7346   6912  -1536    257  -3106       C  
ATOM   1550  CG  TRP A 243      39.553  -4.294   6.695  1.00 74.87           C  
ANISOU 1550  CG  TRP A 243    12904   8199   7345  -1476    273  -3021       C  
ATOM   1551  CD1 TRP A 243      39.695  -4.555   8.028  1.00 81.03           C  
ANISOU 1551  CD1 TRP A 243    13972   9036   7779  -1572    206  -3103       C  
ATOM   1552  CD2 TRP A 243      38.880  -5.431   6.134  1.00 72.78           C  
ANISOU 1552  CD2 TRP A 243    12456   8051   7147  -1317    359  -2832       C  
ATOM   1553  NE1 TRP A 243      39.154  -5.782   8.331  1.00 81.45           N  
ANISOU 1553  NE1 TRP A 243    14030   9230   7687  -1478    251  -2966       N  
ATOM   1554  CE2 TRP A 243      38.646  -6.340   7.186  1.00 75.13           C  
ANISOU 1554  CE2 TRP A 243    12940   8466   7140  -1323    344  -2804       C  
ATOM   1555  CE3 TRP A 243      38.452  -5.767   4.846  1.00 72.30           C  
ANISOU 1555  CE3 TRP A 243    12104   8001   7365  -1182    444  -2684       C  
ATOM   1556  CZ2 TRP A 243      38.004  -7.563   6.990  1.00 74.28           C  
ANISOU 1556  CZ2 TRP A 243    12729   8477   7016  -1196    415  -2634       C  
ATOM   1557  CZ3 TRP A 243      37.814  -6.982   4.653  1.00 72.34           C  
ANISOU 1557  CZ3 TRP A 243    12012   8129   7344  -1062    507  -2527       C  
ATOM   1558  CH2 TRP A 243      37.597  -7.864   5.719  1.00 70.36           C  
ANISOU 1558  CH2 TRP A 243    11944   7986   6803  -1070    493  -2504       C  
ATOM   1559  N   GLY A 244      39.258   0.497   6.064  1.00107.16           N  
ANISOU 1559  N   GLY A 244    17294  11473  11948  -1627    808  -3447       N  
ATOM   1560  CA  GLY A 244      39.883   1.756   5.712  1.00117.97           C  
ANISOU 1560  CA  GLY A 244    18670  12658  13494  -1741    754  -3564       C  
ATOM   1561  C   GLY A 244      38.958   2.945   5.558  1.00123.75           C  
ANISOU 1561  C   GLY A 244    19528  13107  14385  -1665   1146  -3616       C  
ATOM   1562  O   GLY A 244      39.316   4.053   5.968  1.00117.34           O  
ANISOU 1562  O   GLY A 244    18919  12105  13561  -1794   1161  -3792       O  
ATOM   1563  N   ARG A 245      37.774   2.751   4.981  1.00131.76           N  
ANISOU 1563  N   ARG A 245    20420  14081  15560  -1461   1466  -3463       N  
ATOM   1564  CA  ARG A 245      36.855   3.872   4.780  1.00136.88           C  
ANISOU 1564  CA  ARG A 245    21146  14460  16400  -1368   1854  -3482       C  
ATOM   1565  C   ARG A 245      36.315   4.322   6.133  1.00130.19           C  
ANISOU 1565  C   ARG A 245    20695  13473  15298  -1405   2093  -3654       C  
ATOM   1566  O   ARG A 245      35.452   3.666   6.722  1.00127.11           O  
ANISOU 1566  O   ARG A 245    20399  13140  14757  -1308   2291  -3604       O  
ATOM   1567  CB  ARG A 245      35.715   3.464   3.856  1.00133.12           C  
ANISOU 1567  CB  ARG A 245    20411  14000  16169  -1144   2115  -3253       C  
ATOM   1568  CG  ARG A 245      36.140   3.040   2.458  1.00128.37           C  
ANISOU 1568  CG  ARG A 245    19438  13520  15816  -1101   1921  -3076       C  
ATOM   1569  CD  ARG A 245      36.690   4.197   1.648  1.00127.82           C  
ANISOU 1569  CD  ARG A 245    19285  13278  16004  -1161   1889  -3098       C  
ATOM   1570  NE  ARG A 245      37.172   3.750   0.345  1.00123.95           N  
ANISOU 1570  NE  ARG A 245    18462  12912  15720  -1139   1699  -2929       N  
ATOM   1571  CZ  ARG A 245      38.408   3.322   0.112  1.00125.16           C  
ANISOU 1571  CZ  ARG A 245    18517  13211  15829  -1274   1332  -2944       C  
ATOM   1572  NH1 ARG A 245      39.294   3.272   1.098  1.00128.62           N  
ANISOU 1572  NH1 ARG A 245    19140  13699  16032  -1441   1089  -3114       N  
ATOM   1573  NH2 ARG A 245      38.757   2.935  -1.106  1.00125.89           N  
ANISOU 1573  NH2 ARG A 245    18317  13400  16116  -1244   1212  -2781       N  
ATOM   1574  N   GLN A 246      36.818   5.453   6.632  1.00124.17           N  
ANISOU 1574  N   GLN A 246    20177  12514  14486  -1553   2085  -3860       N  
ATOM   1575  CA  GLN A 246      36.400   5.955   7.937  1.00124.65           C  
ANISOU 1575  CA  GLN A 246    20655  12423  14282  -1612   2307  -4050       C  
ATOM   1576  C   GLN A 246      35.683   7.301   7.842  1.00119.51           C  
ANISOU 1576  C   GLN A 246    20137  11440  13830  -1547   2701  -4121       C  
ATOM   1577  O   GLN A 246      36.091   8.262   8.501  1.00120.03           O  
ANISOU 1577  O   GLN A 246    20504  11316  13787  -1697   2713  -4341       O  
ATOM   1578  CB  GLN A 246      37.613   6.049   8.866  1.00133.28           C  
ANISOU 1578  CB  GLN A 246    21996  13574  15070  -1869   1952  -4262       C  
ATOM   1579  CG  GLN A 246      38.202   4.681   9.187  1.00133.23           C  
ANISOU 1579  CG  GLN A 246    21901  13890  14829  -1921   1607  -4187       C  
ATOM   1580  CD  GLN A 246      39.420   4.735  10.086  1.00134.60           C  
ANISOU 1580  CD  GLN A 246    22284  14142  14718  -2177   1230  -4369       C  
ATOM   1581  OE1 GLN A 246      39.383   5.311  11.173  1.00136.80           O  
ANISOU 1581  OE1 GLN A 246    22951  14289  14736  -2300   1318  -4567       O  
ATOM   1582  NE2 GLN A 246      40.525   4.166   9.613  1.00131.08           N  
ANISOU 1582  NE2 GLN A 246    21573  13900  14331  -2265    808  -4301       N  
ATOM   1583  N   ILE A 247      34.625   7.388   7.039  1.00112.00           N  
ANISOU 1583  N   ILE A 247    18965  10411  13178  -1329   3018  -3934       N  
ATOM   1584  CA  ILE A 247      33.993   8.698   6.833  1.00110.38           C  
ANISOU 1584  CA  ILE A 247    18841   9885  13213  -1255   3381  -3974       C  
ATOM   1585  C   ILE A 247      33.495   9.231   8.167  1.00115.09           C  
ANISOU 1585  C   ILE A 247    19878  10290  13560  -1297   3676  -4174       C  
ATOM   1586  O   ILE A 247      32.921   8.463   8.962  1.00116.00           O  
ANISOU 1586  O   ILE A 247    20128  10505  13441  -1253   3798  -4160       O  
ATOM   1587  CB  ILE A 247      32.856   8.618   5.801  1.00108.79           C  
ANISOU 1587  CB  ILE A 247    18310   9650  13374  -1005   3673  -3711       C  
ATOM   1588  CG1 ILE A 247      32.042   7.333   5.966  1.00108.71           C  
ANISOU 1588  CG1 ILE A 247    18180   9848  13276   -872   3756  -3545       C  
ATOM   1589  CG2 ILE A 247      33.420   8.723   4.392  1.00109.37           C  
ANISOU 1589  CG2 ILE A 247    18025   9781  13750   -992   3449  -3564       C  
ATOM   1590  CD1 ILE A 247      30.821   7.307   5.114  1.00108.72           C  
ANISOU 1590  CD1 ILE A 247    17887   9795  13626   -639   4065  -3297       C  
ATOM   1591  N   PRO A 248      33.664  10.522   8.463  1.00117.14           N  
ANISOU 1591  N   PRO A 248    20386  10263  13858  -1382   3815  -4362       N  
ATOM   1592  CA  PRO A 248      33.401  11.002   9.832  1.00125.85           C  
ANISOU 1592  CA  PRO A 248    21968  11191  14659  -1468   4044  -4594       C  
ATOM   1593  C   PRO A 248      32.000  10.738  10.375  1.00126.41           C  
ANISOU 1593  C   PRO A 248    22141  11188  14700  -1279   4518  -4513       C  
ATOM   1594  O   PRO A 248      31.877  10.407  11.558  1.00129.44           O  
ANISOU 1594  O   PRO A 248    22864  11594  14724  -1355   4588  -4644       O  
ATOM   1595  CB  PRO A 248      33.670  12.511   9.716  1.00131.53           C  
ANISOU 1595  CB  PRO A 248    22853  11578  15545  -1545   4165  -4761       C  
ATOM   1596  CG  PRO A 248      34.548  12.666   8.500  1.00122.40           C  
ANISOU 1596  CG  PRO A 248    21352  10491  14664  -1592   3826  -4664       C  
ATOM   1597  CD  PRO A 248      34.096  11.598   7.562  1.00112.21           C  
ANISOU 1597  CD  PRO A 248    19633   9450  13551  -1407   3780  -4368       C  
ATOM   1598  N   GLY A 249      30.946  10.849   9.584  1.00122.73           N  
ANISOU 1598  N   GLY A 249    21397  10640  14596  -1044   4838  -4295       N  
ATOM   1599  CA  GLY A 249      29.634  10.690  10.176  1.00124.01           C  
ANISOU 1599  CA  GLY A 249    21667  10701  14751   -879   5302  -4227       C  
ATOM   1600  C   GLY A 249      28.990   9.352   9.898  1.00118.98           C  
ANISOU 1600  C   GLY A 249    20743  10323  14143   -739   5289  -3979       C  
ATOM   1601  O   GLY A 249      27.954   9.314   9.229  1.00116.88           O  
ANISOU 1601  O   GLY A 249    20193  10005  14213   -528   5564  -3754       O  
ATOM   1602  N   THR A 250      29.573   8.255  10.387  1.00117.15           N  
ANISOU 1602  N   THR A 250    20570  10362  13581   -852   4970  -4007       N  
ATOM   1603  CA  THR A 250      28.984   6.939  10.171  1.00112.08           C  
ANISOU 1603  CA  THR A 250    19677   9956  12950   -730   4952  -3782       C  
ATOM   1604  C   THR A 250      28.200   6.530  11.412  1.00116.22           C  
ANISOU 1604  C   THR A 250    20511  10442  13207   -705   5255  -3827       C  
ATOM   1605  O   THR A 250      28.729   6.532  12.528  1.00118.71           O  
ANISOU 1605  O   THR A 250    21222  10759  13125   -871   5172  -4037       O  
ATOM   1606  CB  THR A 250      30.050   5.903   9.831  1.00104.16           C  
ANISOU 1606  CB  THR A 250    18507   9276  11793   -844   4430  -3746       C  
ATOM   1607  OG1 THR A 250      31.119   6.000  10.778  1.00105.84           O  
ANISOU 1607  OG1 THR A 250    19065   9531  11620  -1073   4158  -3987       O  
ATOM   1608  CG2 THR A 250      30.588   6.164   8.432  1.00 98.44           C  
ANISOU 1608  CG2 THR A 250    17411   8595  11399   -821   4197  -3637       C  
ATOM   1609  N   THR A 251      26.941   6.176  11.211  1.00117.13           N  
ANISOU 1609  N   THR A 251    20441  10518  13545   -503   5600  -3622       N  
ATOM   1610  CA  THR A 251      26.070   5.843  12.324  1.00106.10           C  
ANISOU 1610  CA  THR A 251    19314   9051  11950   -457   5948  -3640       C  
ATOM   1611  C   THR A 251      26.472   4.512  12.945  1.00115.17           C  
ANISOU 1611  C   THR A 251    20550  10480  12728   -552   5673  -3634       C  
ATOM   1612  O   THR A 251      27.183   3.700  12.346  1.00114.16           O  
ANISOU 1612  O   THR A 251    20182  10612  12581   -601   5259  -3550       O  
ATOM   1613  CB  THR A 251      24.622   5.779  11.862  1.00105.90           C  
ANISOU 1613  CB  THR A 251    19012   8914  12312   -214   6369  -3394       C  
ATOM   1614  OG1 THR A 251      24.437   4.589  11.087  1.00100.28           O  
ANISOU 1614  OG1 THR A 251    17903   8463  11736   -135   6155  -3152       O  
ATOM   1615  CG2 THR A 251      24.318   6.983  10.992  1.00106.60           C  
ANISOU 1615  CG2 THR A 251    18914   8770  12820   -108   6559  -3344       C  
ATOM   1616  N   SER A 252      26.016   4.312  14.180  1.00115.96           N  
ANISOU 1616  N   SER A 252    21016  10514  12530   -579   5922  -3723       N  
ATOM   1617  CA  SER A 252      26.243   3.047  14.860  1.00109.04           C  
ANISOU 1617  CA  SER A 252    20246   9881  11304   -653   5721  -3695       C  
ATOM   1618  C   SER A 252      25.648   1.884  14.081  1.00103.20           C  
ANISOU 1618  C   SER A 252    19076   9336  10797   -502   5675  -3409       C  
ATOM   1619  O   SER A 252      26.175   0.766  14.139  1.00100.63           O  
ANISOU 1619  O   SER A 252    18689   9273  10272   -568   5342  -3352       O  
ATOM   1620  CB  SER A 252      25.645   3.107  16.260  1.00113.90           C  
ANISOU 1620  CB  SER A 252    21319  10352  11605   -677   6083  -3813       C  
ATOM   1621  OG  SER A 252      25.930   1.926  16.981  1.00113.43           O  
ANISOU 1621  OG  SER A 252    21399  10522  11178   -763   5876  -3793       O  
ATOM   1622  N   ALA A 285      24.556   2.124  13.350  1.00101.69           N  
ANISOU 1622  N   ALA A 285    18586   9018  11036   -303   5997  -3222       N  
ATOM   1623  CA  ALA A 285      24.007   1.081  12.493  1.00 96.78           C  
ANISOU 1623  CA  ALA A 285    17533   8573  10668   -170   5926  -2950       C  
ATOM   1624  C   ALA A 285      24.876   0.841  11.265  1.00 91.06           C  
ANISOU 1624  C   ALA A 285    16463   8038  10097   -204   5483  -2880       C  
ATOM   1625  O   ALA A 285      24.932  -0.287  10.760  1.00 97.01           O  
ANISOU 1625  O   ALA A 285    16962   9019  10877   -178   5256  -2723       O  
ATOM   1626  CB  ALA A 285      22.585   1.444  12.061  1.00 97.98           C  
ANISOU 1626  CB  ALA A 285    17449   8529  11252     44   6380  -2758       C  
ATOM   1627  N   GLU A 286      25.565   1.875  10.769  1.00 91.13           N  
ANISOU 1627  N   GLU A 286    16468   7950  10208   -263   5364  -2995       N  
ATOM   1628  CA  GLU A 286      26.462   1.666   9.634  1.00 87.38           C  
ANISOU 1628  CA  GLU A 286    15690   7649   9862   -305   4947  -2938       C  
ATOM   1629  C   GLU A 286      27.648   0.790  10.006  1.00 88.71           C  
ANISOU 1629  C   GLU A 286    15967   8072   9667   -472   4498  -3029       C  
ATOM   1630  O   GLU A 286      28.172   0.062   9.154  1.00 87.73           O  
ANISOU 1630  O   GLU A 286    15556   8154   9622   -475   4174  -2918       O  
ATOM   1631  CB  GLU A 286      26.955   3.002   9.070  1.00 87.01           C  
ANISOU 1631  CB  GLU A 286    15632   7425  10004   -338   4931  -3043       C  
ATOM   1632  CG  GLU A 286      25.857   3.952   8.633  1.00 89.09           C  
ANISOU 1632  CG  GLU A 286    15770   7426  10654   -169   5357  -2941       C  
ATOM   1633  CD  GLU A 286      26.395   5.140   7.855  1.00121.41           C  
ANISOU 1633  CD  GLU A 286    19784  11373  14972   -192   5292  -3000       C  
ATOM   1634  OE1 GLU A 286      26.146   6.285   8.283  1.00127.49           O  
ANISOU 1634  OE1 GLU A 286    20778  11872  15789   -187   5579  -3126       O  
ATOM   1635  OE2 GLU A 286      27.080   4.932   6.828  1.00115.92           O  
ANISOU 1635  OE2 GLU A 286    18819  10823  14402   -219   4962  -2925       O  
ATOM   1636  N   VAL A 287      28.076   0.846  11.266  1.00 94.97           N  
ANISOU 1636  N   VAL A 287    17171   8850  10064   -612   4476  -3222       N  
ATOM   1637  CA  VAL A 287      29.199   0.036  11.718  1.00 97.79           C  
ANISOU 1637  CA  VAL A 287    17640   9444  10070   -775   4044  -3296       C  
ATOM   1638  C   VAL A 287      28.770  -1.398  11.982  1.00103.36           C  
ANISOU 1638  C   VAL A 287    18274  10348  10649   -718   4017  -3135       C  
ATOM   1639  O   VAL A 287      29.487  -2.345  11.640  1.00103.54           O  
ANISOU 1639  O   VAL A 287    18136  10610  10595   -766   3646  -3062       O  
ATOM   1640  CB  VAL A 287      29.827   0.683  12.959  1.00100.74           C  
ANISOU 1640  CB  VAL A 287    18487   9722  10067   -959   4012  -3557       C  
ATOM   1641  CG1 VAL A 287      30.995  -0.154  13.464  1.00105.09           C  
ANISOU 1641  CG1 VAL A 287    19141  10524  10264  -1130   3546  -3612       C  
ATOM   1642  CG2 VAL A 287      30.263   2.096  12.625  1.00 97.36           C  
ANISOU 1642  CG2 VAL A 287    18114   9086   9791  -1019   4032  -3715       C  
ATOM   1643  N   LYS A 288      27.598  -1.590  12.592  1.00111.42           N  
ANISOU 1643  N   LYS A 288    19410  11264  11658   -615   4415  -3071       N  
ATOM   1644  CA  LYS A 288      27.109  -2.951  12.781  1.00114.90           C  
ANISOU 1644  CA  LYS A 288    19762  11876  12018   -554   4413  -2901       C  
ATOM   1645  C   LYS A 288      26.911  -3.645  11.443  1.00109.12           C  
ANISOU 1645  C   LYS A 288    18554  11282  11624   -439   4275  -2681       C  
ATOM   1646  O   LYS A 288      26.972  -4.876  11.364  1.00108.76           O  
ANISOU 1646  O   LYS A 288    18390  11436  11496   -431   4099  -2556       O  
ATOM   1647  CB  LYS A 288      25.806  -2.951  13.581  1.00123.67           C  
ANISOU 1647  CB  LYS A 288    21047  12823  13120   -452   4902  -2858       C  
ATOM   1648  CG  LYS A 288      25.983  -3.043  15.086  1.00129.72           C  
ANISOU 1648  CG  LYS A 288    22300  13566  13421   -575   4973  -3017       C  
ATOM   1649  CD  LYS A 288      24.824  -3.830  15.686  1.00132.98           C  
ANISOU 1649  CD  LYS A 288    22764  13958  13803   -467   5315  -2879       C  
ATOM   1650  CE  LYS A 288      24.691  -3.589  17.183  1.00138.68           C  
ANISOU 1650  CE  LYS A 288    24005  14565  14123   -556   5545  -3044       C  
ATOM   1651  NZ  LYS A 288      23.456  -4.195  17.764  1.00138.20           N  
ANISOU 1651  NZ  LYS A 288    23998  14438  14074   -438   5953  -2912       N  
ATOM   1652  N   GLN A 289      26.679  -2.869  10.384  1.00106.34           N  
ANISOU 1652  N   GLN A 289    17939  10820  11648   -353   4352  -2628       N  
ATOM   1653  CA  GLN A 289      26.587  -3.437   9.046  1.00 98.89           C  
ANISOU 1653  CA  GLN A 289    16560  10003  11013   -262   4193  -2432       C  
ATOM   1654  C   GLN A 289      27.964  -3.852   8.543  1.00 93.12           C  
ANISOU 1654  C   GLN A 289    15741   9478  10163   -380   3705  -2480       C  
ATOM   1655  O   GLN A 289      28.117  -4.917   7.934  1.00 93.98           O  
ANISOU 1655  O   GLN A 289    15618   9778  10313   -354   3494  -2342       O  
ATOM   1656  CB  GLN A 289      25.956  -2.410   8.105  1.00100.23           C  
ANISOU 1656  CB  GLN A 289    16496   9984  11604   -142   4416  -2357       C  
ATOM   1657  CG  GLN A 289      26.049  -2.726   6.623  1.00 93.89           C  
ANISOU 1657  CG  GLN A 289    15268   9291  11115    -74   4216  -2184       C  
ATOM   1658  CD  GLN A 289      25.419  -1.633   5.775  1.00 96.40           C  
ANISOU 1658  CD  GLN A 289    15382   9411  11835     38   4440  -2101       C  
ATOM   1659  OE1 GLN A 289      24.198  -1.547   5.650  1.00 95.51           O  
ANISOU 1659  OE1 GLN A 289    15131   9184  11977    179   4757  -1945       O  
ATOM   1660  NE2 GLN A 289      26.259  -0.774   5.208  1.00 98.82           N  
ANISOU 1660  NE2 GLN A 289    15667   9671  12210    -25   4273  -2195       N  
ATOM   1661  N   MET A 290      28.971  -3.010   8.787  1.00 93.16           N  
ANISOU 1661  N   MET A 290    15927   9435  10035   -513   3529  -2672       N  
ATOM   1662  CA  MET A 290      30.331  -3.284   8.337  1.00 86.82           C  
ANISOU 1662  CA  MET A 290    15034   8806   9149   -631   3071  -2721       C  
ATOM   1663  C   MET A 290      30.947  -4.461   9.082  1.00 88.70           C  
ANISOU 1663  C   MET A 290    15399   9262   9040   -724   2799  -2724       C  
ATOM   1664  O   MET A 290      31.538  -5.359   8.470  1.00 88.59           O  
ANISOU 1664  O   MET A 290    15168   9445   9046   -730   2497  -2627       O  
ATOM   1665  CB  MET A 290      31.195  -2.044   8.547  1.00 86.45           C  
ANISOU 1665  CB  MET A 290    15168   8630   9049   -762   2971  -2930       C  
ATOM   1666  CG  MET A 290      32.596  -2.169   7.992  1.00 89.68           C  
ANISOU 1666  CG  MET A 290    15444   9188   9441   -882   2515  -2972       C  
ATOM   1667  SD  MET A 290      33.689  -0.938   8.719  1.00104.43           S  
ANISOU 1667  SD  MET A 290    17623  10930  11126  -1089   2358  -3244       S  
ATOM   1668  CE  MET A 290      33.599  -1.418  10.444  1.00108.78           C  
ANISOU 1668  CE  MET A 290    18607  11525  11201  -1188   2399  -3357       C  
ATOM   1669  N   ARG A 291      30.795  -4.487  10.410  1.00 91.41           N  
ANISOU 1669  N   ARG A 291    16101   9568   9062   -792   2914  -2827       N  
ATOM   1670  CA  ARG A 291      31.431  -5.532  11.203  1.00 94.04           C  
ANISOU 1670  CA  ARG A 291    16585  10101   9046   -890   2644  -2827       C  
ATOM   1671  C   ARG A 291      30.897  -6.908  10.840  1.00 89.65           C  
ANISOU 1671  C   ARG A 291    15813   9701   8547   -782   2640  -2612       C  
ATOM   1672  O   ARG A 291      31.608  -7.909  10.987  1.00 83.86           O  
ANISOU 1672  O   ARG A 291    15057   9170   7636   -840   2328  -2559       O  
ATOM   1673  CB  ARG A 291      31.249  -5.239  12.692  1.00104.52           C  
ANISOU 1673  CB  ARG A 291    18360  11336  10016   -980   2810  -2970       C  
ATOM   1674  CG  ARG A 291      31.866  -3.913  13.098  1.00114.99           C  
ANISOU 1674  CG  ARG A 291    19929  12506  11254  -1112   2783  -3200       C  
ATOM   1675  CD  ARG A 291      33.359  -4.030  13.347  1.00124.05           C  
ANISOU 1675  CD  ARG A 291    21140  13813  12182  -1299   2295  -3300       C  
ATOM   1676  NE  ARG A 291      33.969  -2.717  13.542  1.00132.63           N  
ANISOU 1676  NE  ARG A 291    22406  14741  13247  -1430   2251  -3515       N  
ATOM   1677  CZ  ARG A 291      34.180  -2.146  14.724  1.00142.44           C  
ANISOU 1677  CZ  ARG A 291    24067  15886  14168  -1574   2290  -3706       C  
ATOM   1678  NH1 ARG A 291      33.823  -2.766  15.840  1.00146.98           N  
ANISOU 1678  NH1 ARG A 291    24935  16507  14403  -1603   2383  -3704       N  
ATOM   1679  NH2 ARG A 291      34.744  -0.948  14.787  1.00147.76           N  
ANISOU 1679  NH2 ARG A 291    24878  16406  14857  -1697   2240  -3900       N  
ATOM   1680  N   ALA A 292      29.655  -6.986  10.365  1.00 88.75           N  
ANISOU 1680  N   ALA A 292    15534   9493   8692   -627   2979  -2479       N  
ATOM   1681  CA  ALA A 292      29.149  -8.268   9.888  1.00 82.70           C  
ANISOU 1681  CA  ALA A 292    14536   8867   8019   -532   2963  -2274       C  
ATOM   1682  C   ALA A 292      29.571  -8.521   8.443  1.00 79.27           C  
ANISOU 1682  C   ALA A 292    13723   8533   7864   -488   2730  -2175       C  
ATOM   1683  O   ALA A 292      29.871  -9.658   8.069  1.00 76.24           O  
ANISOU 1683  O   ALA A 292    13190   8326   7452   -481   2513  -2061       O  
ATOM   1684  CB  ALA A 292      27.629  -8.331  10.043  1.00 66.54           C  
ANISOU 1684  CB  ALA A 292    12462   6685   6135   -395   3410  -2160       C  
ATOM   1685  N   ARG A 293      29.575  -7.477   7.615  1.00 82.76           N  
ANISOU 1685  N   ARG A 293    14015   8852   8576   -456   2788  -2211       N  
ATOM   1686  CA  ARG A 293      30.017  -7.623   6.235  1.00 74.37           C  
ANISOU 1686  CA  ARG A 293    12619   7871   7767   -424   2575  -2126       C  
ATOM   1687  C   ARG A 293      31.485  -8.030   6.153  1.00 78.60           C  
ANISOU 1687  C   ARG A 293    13154   8580   8131   -547   2135  -2192       C  
ATOM   1688  O   ARG A 293      31.895  -8.699   5.193  1.00 75.13           O  
ANISOU 1688  O   ARG A 293    12463   8269   7814   -524   1922  -2094       O  
ATOM   1689  CB  ARG A 293      29.797  -6.302   5.502  1.00 61.85           C  
ANISOU 1689  CB  ARG A 293    10922   6102   6476   -381   2728  -2160       C  
ATOM   1690  CG  ARG A 293      28.359  -6.002   5.082  1.00 55.89           C  
ANISOU 1690  CG  ARG A 293    10009   5199   6026   -226   3110  -2020       C  
ATOM   1691  CD  ARG A 293      28.340  -4.806   4.129  1.00 57.74           C  
ANISOU 1691  CD  ARG A 293    10078   5285   6574   -184   3178  -2019       C  
ATOM   1692  NE  ARG A 293      27.084  -4.672   3.396  1.00 66.40           N  
ANISOU 1692  NE  ARG A 293    10919   6285   8027    -29   3451  -1828       N  
ATOM   1693  CZ  ARG A 293      26.695  -3.566   2.766  1.00 71.28           C  
ANISOU 1693  CZ  ARG A 293    11415   6729   8938     38   3616  -1791       C  
ATOM   1694  NH1 ARG A 293      27.453  -2.476   2.788  1.00 71.95           N  
ANISOU 1694  NH1 ARG A 293    11628   6708   9001    -39   3560  -1946       N  
ATOM   1695  NH2 ARG A 293      25.537  -3.546   2.120  1.00 71.72           N  
ANISOU 1695  NH2 ARG A 293    11215   6715   9322    179   3831  -1587       N  
ATOM   1696  N   ARG A 294      32.293  -7.640   7.142  1.00 83.46           N  
ANISOU 1696  N   ARG A 294    14042   9198   8473   -681   1992  -2354       N  
ATOM   1697  CA  ARG A 294      33.691  -8.064   7.145  1.00 71.11           C  
ANISOU 1697  CA  ARG A 294    12455   7803   6762   -798   1563  -2396       C  
ATOM   1698  C   ARG A 294      33.814  -9.570   7.324  1.00 66.97           C  
ANISOU 1698  C   ARG A 294    11881   7479   6087   -781   1395  -2263       C  
ATOM   1699  O   ARG A 294      34.666 -10.208   6.700  1.00 66.29           O  
ANISOU 1699  O   ARG A 294    11601   7541   6045   -800   1090  -2202       O  
ATOM   1700  CB  ARG A 294      34.460  -7.352   8.259  1.00 62.13           C  
ANISOU 1700  CB  ARG A 294    11627   6624   5357   -955   1445  -2588       C  
ATOM   1701  CG  ARG A 294      34.853  -5.914   7.986  1.00 61.64           C  
ANISOU 1701  CG  ARG A 294    11594   6395   5431  -1019   1465  -2740       C  
ATOM   1702  CD  ARG A 294      35.333  -5.298   9.282  1.00 66.62           C  
ANISOU 1702  CD  ARG A 294    12593   6965   5755  -1174   1418  -2931       C  
ATOM   1703  NE  ARG A 294      35.848  -3.945   9.121  1.00 68.57           N  
ANISOU 1703  NE  ARG A 294    12898   7051   6104  -1265   1397  -3094       N  
ATOM   1704  CZ  ARG A 294      36.657  -3.361   9.997  1.00 80.32           C  
ANISOU 1704  CZ  ARG A 294    14645   8508   7364  -1440   1230  -3274       C  
ATOM   1705  NH1 ARG A 294      37.039  -4.019  11.084  1.00 91.81           N  
ANISOU 1705  NH1 ARG A 294    16322  10094   8470  -1539   1064  -3303       N  
ATOM   1706  NH2 ARG A 294      37.094  -2.127   9.787  1.00 87.18           N  
ANISOU 1706  NH2 ARG A 294    15557   9214   8352  -1525   1219  -3420       N  
ATOM   1707  N   LYS A 295      32.951 -10.151   8.155  1.00 66.25           N  
ANISOU 1707  N   LYS A 295    11960   7381   5831   -741   1607  -2208       N  
ATOM   1708  CA  LYS A 295      33.038 -11.568   8.471  1.00 62.76           C  
ANISOU 1708  CA  LYS A 295    11515   7110   5220   -732   1466  -2079       C  
ATOM   1709  C   LYS A 295      32.633 -12.428   7.284  1.00 62.94           C  
ANISOU 1709  C   LYS A 295    11220   7203   5491   -620   1465  -1907       C  
ATOM   1710  O   LYS A 295      33.125 -13.554   7.128  1.00 66.95           O  
ANISOU 1710  O   LYS A 295    11641   7870   5928   -624   1233  -1805       O  
ATOM   1711  CB  LYS A 295      32.142 -11.834   9.662  1.00 71.33           C  
ANISOU 1711  CB  LYS A 295    12880   8139   6083   -721   1737  -2069       C  
ATOM   1712  CG  LYS A 295      32.637 -11.103  10.897  1.00 85.27           C  
ANISOU 1712  CG  LYS A 295    14999   9851   7547   -852   1704  -2245       C  
ATOM   1713  CD  LYS A 295      31.712 -11.281  12.095  1.00 95.53           C  
ANISOU 1713  CD  LYS A 295    16606  11073   8617   -842   2011  -2246       C  
ATOM   1714  CE  LYS A 295      32.162 -10.365  13.220  1.00106.00           C  
ANISOU 1714  CE  LYS A 295    18302  12315   9659   -978   2007  -2446       C  
ATOM   1715  NZ  LYS A 295      31.157 -10.295  14.314  1.00110.16           N  
ANISOU 1715  NZ  LYS A 295    19145  12719   9992   -960   2379  -2471       N  
ATOM   1716  N   THR A 296      31.734 -11.917   6.442  1.00 63.52           N  
ANISOU 1716  N   THR A 296    11122   7155   5859   -520   1722  -1865       N  
ATOM   1717  CA  THR A 296      31.373 -12.618   5.217  1.00 59.92           C  
ANISOU 1717  CA  THR A 296    10362   6756   5650   -428   1711  -1714       C  
ATOM   1718  C   THR A 296      32.432 -12.443   4.137  1.00 65.95           C  
ANISOU 1718  C   THR A 296    10916   7588   6556   -459   1418  -1736       C  
ATOM   1719  O   THR A 296      32.751 -13.394   3.415  1.00 73.76           O  
ANISOU 1719  O   THR A 296    11730   8699   7597   -437   1240  -1635       O  
ATOM   1720  CB  THR A 296      30.023 -12.112   4.717  1.00 62.77           C  
ANISOU 1720  CB  THR A 296    10596   6964   6291   -312   2080  -1643       C  
ATOM   1721  OG1 THR A 296      29.151 -11.910   5.838  1.00 78.50           O  
ANISOU 1721  OG1 THR A 296    12812   8852   8163   -295   2378  -1661       O  
ATOM   1722  CG2 THR A 296      29.398 -13.117   3.768  1.00 52.50           C  
ANISOU 1722  CG2 THR A 296     9035   5732   5181   -224   2108  -1462       C  
ATOM   1723  N   ALA A 297      32.979 -11.232   4.005  1.00 69.06           N  
ANISOU 1723  N   ALA A 297    11331   7891   7019   -513   1377  -1866       N  
ATOM   1724  CA  ALA A 297      34.042 -11.012   3.032  1.00 64.44           C  
ANISOU 1724  CA  ALA A 297    10554   7360   6572   -554   1105  -1888       C  
ATOM   1725  C   ALA A 297      35.273 -11.842   3.368  1.00 73.37           C  
ANISOU 1725  C   ALA A 297    11699   8669   7509   -638    738  -1891       C  
ATOM   1726  O   ALA A 297      35.950 -12.352   2.468  1.00 77.80           O  
ANISOU 1726  O   ALA A 297    12048   9327   8185   -632    523  -1828       O  
ATOM   1727  CB  ALA A 297      34.393  -9.526   2.959  1.00 61.00           C  
ANISOU 1727  CB  ALA A 297    10166   6776   6235   -610   1141  -2027       C  
ATOM   1728  N   LYS A 298      35.578 -11.994   4.659  1.00 76.37           N  
ANISOU 1728  N   LYS A 298    12324   9091   7603   -714    667  -1953       N  
ATOM   1729  CA  LYS A 298      36.695 -12.843   5.059  1.00 76.72           C  
ANISOU 1729  CA  LYS A 298    12369   9309   7472   -785    323  -1925       C  
ATOM   1730  C   LYS A 298      36.448 -14.292   4.662  1.00 76.24           C  
ANISOU 1730  C   LYS A 298    12179   9372   7418   -703    274  -1750       C  
ATOM   1731  O   LYS A 298      37.342 -14.971   4.145  1.00 84.77           O  
ANISOU 1731  O   LYS A 298    13088  10576   8546   -710      6  -1683       O  
ATOM   1732  CB  LYS A 298      36.927 -12.725   6.566  1.00 82.46           C  
ANISOU 1732  CB  LYS A 298    13407  10048   7875   -883    282  -2010       C  
ATOM   1733  CG  LYS A 298      38.166 -13.443   7.074  1.00 84.10           C  
ANISOU 1733  CG  LYS A 298    13618  10430   7907   -970    -93  -1979       C  
ATOM   1734  CD  LYS A 298      38.210 -13.401   8.594  1.00 97.02           C  
ANISOU 1734  CD  LYS A 298    15593  12075   9196  -1064   -106  -2044       C  
ATOM   1735  CE  LYS A 298      39.475 -14.049   9.137  1.00101.19           C  
ANISOU 1735  CE  LYS A 298    16119  12775   9554  -1157   -495  -1999       C  
ATOM   1736  NZ  LYS A 298      39.525 -14.056  10.629  1.00102.30           N  
ANISOU 1736  NZ  LYS A 298    16607  12932   9330  -1258   -528  -2051       N  
ATOM   1737  N   MET A 299      35.231 -14.785   4.903  1.00 66.36           N  
ANISOU 1737  N   MET A 299    11006   8077   6132   -626    543  -1670       N  
ATOM   1738  CA  MET A 299      34.906 -16.163   4.554  1.00 60.63           C  
ANISOU 1738  CA  MET A 299    10181   7447   5411   -557    518  -1504       C  
ATOM   1739  C   MET A 299      34.947 -16.376   3.046  1.00 57.53           C  
ANISOU 1739  C   MET A 299     9499   7067   5294   -495    472  -1439       C  
ATOM   1740  O   MET A 299      35.521 -17.357   2.561  1.00 62.27           O  
ANISOU 1740  O   MET A 299     9973   7778   5907   -482    263  -1346       O  
ATOM   1741  CB  MET A 299      33.528 -16.528   5.105  1.00 61.86           C  
ANISOU 1741  CB  MET A 299    10468   7531   5504   -497    846  -1434       C  
ATOM   1742  CG  MET A 299      33.179 -17.998   4.976  1.00 60.32           C  
ANISOU 1742  CG  MET A 299    10223   7424   5272   -446    824  -1263       C  
ATOM   1743  SD  MET A 299      31.413 -18.308   5.155  1.00 58.91           S  
ANISOU 1743  SD  MET A 299    10081   7139   5165   -361   1256  -1161       S  
ATOM   1744  CE  MET A 299      30.824 -17.855   3.526  1.00 58.71           C  
ANISOU 1744  CE  MET A 299     9739   7042   5526   -281   1385  -1131       C  
ATOM   1745  N   LEU A 300      34.341 -15.461   2.285  1.00 54.32           N  
ANISOU 1745  N   LEU A 300     8989   6538   5111   -456    672  -1479       N  
ATOM   1746  CA  LEU A 300      34.276 -15.644   0.839  1.00 44.44           C  
ANISOU 1746  CA  LEU A 300     7483   5291   4112   -402    652  -1413       C  
ATOM   1747  C   LEU A 300      35.652 -15.554   0.192  1.00 43.48           C  
ANISOU 1747  C   LEU A 300     7220   5247   4054   -456    339  -1449       C  
ATOM   1748  O   LEU A 300      35.908 -16.233  -0.809  1.00 36.95           O  
ANISOU 1748  O   LEU A 300     6214   4482   3344   -426    229  -1370       O  
ATOM   1749  CB  LEU A 300      33.325 -14.617   0.223  1.00 38.43           C  
ANISOU 1749  CB  LEU A 300     6636   4376   3588   -347    936  -1430       C  
ATOM   1750  CG  LEU A 300      31.854 -14.786   0.606  1.00 40.57           C  
ANISOU 1750  CG  LEU A 300     6955   4568   3890   -269   1273  -1352       C  
ATOM   1751  CD1 LEU A 300      31.065 -13.526   0.286  1.00 47.69           C  
ANISOU 1751  CD1 LEU A 300     7793   5303   5024   -217   1539  -1376       C  
ATOM   1752  CD2 LEU A 300      31.256 -15.993  -0.103  1.00 38.56           C  
ANISOU 1752  CD2 LEU A 300     6552   4380   3721   -209   1304  -1200       C  
ATOM   1753  N   MET A 301      36.546 -14.726   0.739  1.00 45.04           N  
ANISOU 1753  N   MET A 301     7493   5436   4186   -540    200  -1567       N  
ATOM   1754  CA  MET A 301      37.890 -14.636   0.177  1.00 49.36           C  
ANISOU 1754  CA  MET A 301     7882   6056   4818   -595    -89  -1590       C  
ATOM   1755  C   MET A 301      38.668 -15.923   0.410  1.00 53.28           C  
ANISOU 1755  C   MET A 301     8328   6718   5198   -598   -340  -1496       C  
ATOM   1756  O   MET A 301      39.451 -16.349  -0.448  1.00 57.88           O  
ANISOU 1756  O   MET A 301     8705   7373   5914   -590   -516  -1442       O  
ATOM   1757  CB  MET A 301      38.631 -13.439   0.773  1.00 57.07           C  
ANISOU 1757  CB  MET A 301     8953   6975   5759   -698   -174  -1737       C  
ATOM   1758  CG  MET A 301      38.146 -12.096   0.240  1.00 61.89           C  
ANISOU 1758  CG  MET A 301     9554   7408   6553   -697     30  -1814       C  
ATOM   1759  SD  MET A 301      38.711 -10.689   1.220  1.00 64.24           S  
ANISOU 1759  SD  MET A 301    10053   7599   6757   -824     -2  -2001       S  
ATOM   1760  CE  MET A 301      37.534  -9.423   0.738  1.00 66.77           C  
ANISOU 1760  CE  MET A 301    10406   7691   7272   -764    370  -2038       C  
ATOM   1761  N   VAL A 302      38.471 -16.552   1.569  1.00 56.42           N  
ANISOU 1761  N   VAL A 302     8913   7169   5355   -607   -346  -1464       N  
ATOM   1762  CA  VAL A 302      39.118 -17.831   1.819  1.00 51.34           C  
ANISOU 1762  CA  VAL A 302     8230   6667   4609   -597   -564  -1343       C  
ATOM   1763  C   VAL A 302      38.565 -18.903   0.895  1.00 50.23           C  
ANISOU 1763  C   VAL A 302     7966   6544   4577   -501   -504  -1207       C  
ATOM   1764  O   VAL A 302      39.287 -19.827   0.499  1.00 50.20           O  
ANISOU 1764  O   VAL A 302     7829   6631   4613   -476   -696  -1105       O  
ATOM   1765  CB  VAL A 302      38.955 -18.221   3.296  1.00 43.30           C  
ANISOU 1765  CB  VAL A 302     7470   5685   3299   -632   -570  -1327       C  
ATOM   1766  CG1 VAL A 302      39.611 -19.565   3.556  1.00 41.55           C  
ANISOU 1766  CG1 VAL A 302     7208   5593   2984   -611   -795  -1175       C  
ATOM   1767  CG2 VAL A 302      39.550 -17.142   4.176  1.00 43.27           C  
ANISOU 1767  CG2 VAL A 302     7607   5660   3175   -744   -649  -1474       C  
ATOM   1768  N   VAL A 303      37.284 -18.810   0.544  1.00 43.59           N  
ANISOU 1768  N   VAL A 303     7164   5607   3792   -448   -232  -1196       N  
ATOM   1769  CA  VAL A 303      36.699 -19.782  -0.371  1.00 41.52           C  
ANISOU 1769  CA  VAL A 303     6796   5349   3631   -374   -174  -1076       C  
ATOM   1770  C   VAL A 303      37.305 -19.642  -1.759  1.00 45.80           C  
ANISOU 1770  C   VAL A 303     7103   5902   4398   -364   -287  -1079       C  
ATOM   1771  O   VAL A 303      37.710 -20.631  -2.381  1.00 49.04           O  
ANISOU 1771  O   VAL A 303     7406   6371   4857   -325   -426   -982       O  
ATOM   1772  CB  VAL A 303      35.171 -19.630  -0.405  1.00 36.25           C  
ANISOU 1772  CB  VAL A 303     6202   4579   2994   -333    159  -1060       C  
ATOM   1773  CG1 VAL A 303      34.599 -20.451  -1.548  1.00 26.12           C  
ANISOU 1773  CG1 VAL A 303     4786   3290   1848   -279    214   -957       C  
ATOM   1774  CG2 VAL A 303      34.583 -20.061   0.920  1.00 40.04           C  
ANISOU 1774  CG2 VAL A 303     6905   5058   3251   -336    276  -1020       C  
ATOM   1775  N   VAL A 304      37.369 -18.412  -2.269  1.00 42.50           N  
ANISOU 1775  N   VAL A 304     6613   5412   4125   -395   -220  -1183       N  
ATOM   1776  CA  VAL A 304      37.947 -18.196  -3.591  1.00 38.09           C  
ANISOU 1776  CA  VAL A 304     5839   4857   3778   -399   -308  -1183       C  
ATOM   1777  C   VAL A 304      39.421 -18.576  -3.598  1.00 46.56           C  
ANISOU 1777  C   VAL A 304     6794   6039   4856   -425   -594  -1163       C  
ATOM   1778  O   VAL A 304      39.945 -19.076  -4.602  1.00 57.39           O  
ANISOU 1778  O   VAL A 304     7993   7450   6364   -395   -694  -1097       O  
ATOM   1779  CB  VAL A 304      37.744 -16.737  -4.030  1.00 36.41           C  
ANISOU 1779  CB  VAL A 304     5582   4529   3721   -433   -167  -1282       C  
ATOM   1780  CG1 VAL A 304      38.348 -16.523  -5.403  1.00 24.48           C  
ANISOU 1780  CG1 VAL A 304     3825   3035   2441   -436   -241  -1254       C  
ATOM   1781  CG2 VAL A 304      36.266 -16.391  -4.025  1.00 40.94           C  
ANISOU 1781  CG2 VAL A 304     6223   4995   4338   -386    144  -1279       C  
ATOM   1782  N   LEU A 305      40.115 -18.341  -2.484  1.00 51.64           N  
ANISOU 1782  N   LEU A 305     7522   6734   5364   -482   -716  -1210       N  
ATOM   1783  CA  LEU A 305      41.534 -18.669  -2.420  1.00 53.04           C  
ANISOU 1783  CA  LEU A 305     7561   7027   5563   -528   -965  -1170       C  
ATOM   1784  C   LEU A 305      41.752 -20.176  -2.473  1.00 58.89           C  
ANISOU 1784  C   LEU A 305     8264   7845   6266   -451  -1076  -1006       C  
ATOM   1785  O   LEU A 305      42.648 -20.658  -3.177  1.00 63.74           O  
ANISOU 1785  O   LEU A 305     8690   8506   7022   -422  -1212   -922       O  
ATOM   1786  CB  LEU A 305      42.151 -18.076  -1.154  1.00 51.56           C  
ANISOU 1786  CB  LEU A 305     7494   6872   5225   -617  -1080  -1254       C  
ATOM   1787  CG  LEU A 305      43.671 -18.159  -1.006  1.00 46.81           C  
ANISOU 1787  CG  LEU A 305     6738   6384   4663   -687  -1342  -1220       C  
ATOM   1788  CD1 LEU A 305      44.350 -17.452  -2.166  1.00 47.72           C  
ANISOU 1788  CD1 LEU A 305     6620   6484   5027   -740  -1350  -1247       C  
ATOM   1789  CD2 LEU A 305      44.114 -17.560   0.319  1.00 43.01           C  
ANISOU 1789  CD2 LEU A 305     6417   5924   4001   -784  -1457  -1313       C  
ATOM   1790  N   VAL A 306      40.945 -20.938  -1.733  1.00 52.92           N  
ANISOU 1790  N   VAL A 306     7689   7083   5335   -404  -1009   -949       N  
ATOM   1791  CA  VAL A 306      41.081 -22.390  -1.767  1.00 44.27           C  
ANISOU 1791  CA  VAL A 306     6579   6030   4212   -319  -1106   -791       C  
ATOM   1792  C   VAL A 306      40.690 -22.939  -3.132  1.00 45.92           C  
ANISOU 1792  C   VAL A 306     6659   6189   4601   -229  -1040   -738       C  
ATOM   1793  O   VAL A 306      41.326 -23.865  -3.650  1.00 48.52           O  
ANISOU 1793  O   VAL A 306     6868   6543   5026   -150  -1164   -639       O  
ATOM   1794  CB  VAL A 306      40.252 -23.027  -0.643  1.00 37.39           C  
ANISOU 1794  CB  VAL A 306     5947   5150   3109   -305  -1027   -736       C  
ATOM   1795  CG1 VAL A 306      40.221 -24.531  -0.827  1.00 35.59           C  
ANISOU 1795  CG1 VAL A 306     5714   4929   2880   -210  -1094   -570       C  
ATOM   1796  CG2 VAL A 306      40.847 -22.657   0.699  1.00 41.26           C  
ANISOU 1796  CG2 VAL A 306     6565   5703   3411   -383  -1144   -773       C  
ATOM   1797  N   PHE A 307      39.639 -22.383  -3.736  1.00 41.87           N  
ANISOU 1797  N   PHE A 307     6170   5595   4142   -229   -843   -804       N  
ATOM   1798  CA  PHE A 307      39.241 -22.820  -5.070  1.00 37.46           C  
ANISOU 1798  CA  PHE A 307     5435   5003   3793   -155   -745   -737       C  
ATOM   1799  C   PHE A 307      40.356 -22.581  -6.081  1.00 34.04           C  
ANISOU 1799  C   PHE A 307     4780   4600   3552   -139   -854   -748       C  
ATOM   1800  O   PHE A 307      40.642 -23.441  -6.920  1.00 34.90           O  
ANISOU 1800  O   PHE A 307     4773   4713   3775    -61   -875   -667       O  
ATOM   1801  CB  PHE A 307      37.961 -22.098  -5.495  1.00 47.38           C  
ANISOU 1801  CB  PHE A 307     6692   6186   5125   -171   -502   -770       C  
ATOM   1802  CG  PHE A 307      37.447 -22.511  -6.844  1.00 51.55           C  
ANISOU 1802  CG  PHE A 307     7059   6687   5840   -121   -423   -692       C  
ATOM   1803  CD1 PHE A 307      37.966 -21.952  -8.000  1.00 53.48           C  
ANISOU 1803  CD1 PHE A 307     7131   6933   6254   -121   -442   -716       C  
ATOM   1804  CD2 PHE A 307      36.440 -23.456  -6.955  1.00 57.53           C  
ANISOU 1804  CD2 PHE A 307     7850   7416   6592    -92   -333   -592       C  
ATOM   1805  CE1 PHE A 307      37.489 -22.326  -9.242  1.00 56.31           C  
ANISOU 1805  CE1 PHE A 307     7382   7272   6741    -92   -381   -647       C  
ATOM   1806  CE2 PHE A 307      35.959 -23.834  -8.197  1.00 58.92           C  
ANISOU 1806  CE2 PHE A 307     7902   7568   6917    -75   -290   -528       C  
ATOM   1807  CZ  PHE A 307      36.485 -23.269  -9.342  1.00 56.28           C  
ANISOU 1807  CZ  PHE A 307     7424   7242   6717    -75   -319   -559       C  
ATOM   1808  N   ALA A 308      40.991 -21.407  -6.022  1.00 29.45           N  
ANISOU 1808  N   ALA A 308     4150   4027   3012   -217   -906   -851       N  
ATOM   1809  CA  ALA A 308      42.106 -21.127  -6.920  1.00 21.94           C  
ANISOU 1809  CA  ALA A 308     2977   3105   2253   -213   -994   -852       C  
ATOM   1810  C   ALA A 308      43.229 -22.140  -6.733  1.00 37.15           C  
ANISOU 1810  C   ALA A 308     4814   5102   4198   -152  -1190   -759       C  
ATOM   1811  O   ALA A 308      43.783 -22.656  -7.710  1.00 50.36           O  
ANISOU 1811  O   ALA A 308     6315   6781   6039    -71  -1185   -698       O  
ATOM   1812  CB  ALA A 308      42.620 -19.704  -6.699  1.00 25.30           C  
ANISOU 1812  CB  ALA A 308     3381   3513   2720   -335  -1009   -951       C  
ATOM   1813  N   LEU A 309      43.585 -22.433  -5.479  1.00 42.46           N  
ANISOU 1813  N   LEU A 309     5600   5822   4710   -190  -1317   -718       N  
ATOM   1814  CA  LEU A 309      44.667 -23.380  -5.225  1.00 42.39           C  
ANISOU 1814  CA  LEU A 309     5489   5877   4741   -123  -1505   -598       C  
ATOM   1815  C   LEU A 309      44.283 -24.799  -5.630  1.00 43.56           C  
ANISOU 1815  C   LEU A 309     5659   5990   4901     27  -1492   -499       C  
ATOM   1816  O   LEU A 309      45.115 -25.543  -6.160  1.00 49.90           O  
ANISOU 1816  O   LEU A 309     6299   6801   5861    134  -1566   -413       O  
ATOM   1817  CB  LEU A 309      45.063 -23.341  -3.748  1.00 41.65           C  
ANISOU 1817  CB  LEU A 309     5518   5854   4452   -205  -1645   -572       C  
ATOM   1818  CG  LEU A 309      45.790 -22.089  -3.252  1.00 35.33           C  
ANISOU 1818  CG  LEU A 309     4677   5105   3642   -355  -1720   -664       C  
ATOM   1819  CD1 LEU A 309      45.533 -21.859  -1.765  1.00 33.53           C  
ANISOU 1819  CD1 LEU A 309     4675   4919   3147   -438  -1768   -714       C  
ATOM   1820  CD2 LEU A 309      47.278 -22.202  -3.527  1.00 35.10           C  
ANISOU 1820  CD2 LEU A 309     4390   5148   3798   -345  -1901   -581       C  
ATOM   1821  N   CYS A 310      43.029 -25.194  -5.393  1.00 39.97           N  
ANISOU 1821  N   CYS A 310     5398   5484   4306     36  -1359   -497       N  
ATOM   1822  CA  CYS A 310      42.633 -26.572  -5.669  1.00 46.37           C  
ANISOU 1822  CA  CYS A 310     6247   6241   5132    146  -1301   -380       C  
ATOM   1823  C   CYS A 310      42.645 -26.870  -7.163  1.00 46.39           C  
ANISOU 1823  C   CYS A 310     6095   6185   5344    215  -1169   -379       C  
ATOM   1824  O   CYS A 310      43.105 -27.937  -7.586  1.00 50.74           O  
ANISOU 1824  O   CYS A 310     6593   6697   5989    324  -1185   -294       O  
ATOM   1825  CB  CYS A 310      41.249 -26.848  -5.084  1.00 51.35           C  
ANISOU 1825  CB  CYS A 310     7098   6825   5588    112  -1164   -369       C  
ATOM   1826  SG  CYS A 310      41.233 -27.065  -3.294  1.00 49.26           S  
ANISOU 1826  SG  CYS A 310     7084   6610   5024     66  -1298   -320       S  
ATOM   1827  N   TYR A 311      42.141 -25.949  -7.977  1.00 37.57           N  
ANISOU 1827  N   TYR A 311     4925   5054   4297    156  -1031   -469       N  
ATOM   1828  CA  TYR A 311      42.054 -26.164  -9.414  1.00 30.07           C  
ANISOU 1828  CA  TYR A 311     3873   4055   3498    198   -905   -470       C  
ATOM   1829  C   TYR A 311      43.287 -25.689 -10.169  1.00 30.26           C  
ANISOU 1829  C   TYR A 311     3694   4111   3691    224   -934   -493       C  
ATOM   1830  O   TYR A 311      43.370 -25.903 -11.383  1.00 33.07           O  
ANISOU 1830  O   TYR A 311     3982   4428   4154    266   -821   -494       O  
ATOM   1831  CB  TYR A 311      40.806 -25.472  -9.968  1.00 38.13           C  
ANISOU 1831  CB  TYR A 311     4937   5043   4507    123   -749   -519       C  
ATOM   1832  CG  TYR A 311      39.510 -26.127  -9.545  1.00 44.80           C  
ANISOU 1832  CG  TYR A 311     5934   5841   5245    107   -677   -471       C  
ATOM   1833  CD1 TYR A 311      38.986 -25.925  -8.274  1.00 50.34           C  
ANISOU 1833  CD1 TYR A 311     6767   6558   5803     66   -683   -471       C  
ATOM   1834  CD2 TYR A 311      38.810 -26.947 -10.419  1.00 39.92           C  
ANISOU 1834  CD2 TYR A 311     5340   5160   4669    119   -598   -425       C  
ATOM   1835  CE1 TYR A 311      37.802 -26.523  -7.887  1.00 51.16           C  
ANISOU 1835  CE1 TYR A 311     6992   6617   5831     50   -589   -412       C  
ATOM   1836  CE2 TYR A 311      37.624 -27.547 -10.042  1.00 36.45           C  
ANISOU 1836  CE2 TYR A 311     5012   4675   4162     85   -536   -368       C  
ATOM   1837  CZ  TYR A 311      37.125 -27.332  -8.775  1.00 45.37           C  
ANISOU 1837  CZ  TYR A 311     6241   5822   5173     57   -522   -354       C  
ATOM   1838  OH  TYR A 311      35.944 -27.929  -8.395  1.00 50.00           O  
ANISOU 1838  OH  TYR A 311     6924   6362   5714     22   -434   -283       O  
ATOM   1839  N   LEU A 312      44.240 -25.053  -9.490  1.00 26.74           N  
ANISOU 1839  N   LEU A 312     3158   3734   3267    189  -1081   -511       N  
ATOM   1840  CA  LEU A 312      45.461 -24.630 -10.171  1.00 26.91           C  
ANISOU 1840  CA  LEU A 312     2954   3786   3484    208  -1104   -513       C  
ATOM   1841  C   LEU A 312      46.226 -25.797 -10.780  1.00 42.05           C  
ANISOU 1841  C   LEU A 312     4764   5674   5538    356  -1081   -422       C  
ATOM   1842  O   LEU A 312      46.603 -25.711 -11.962  1.00 50.58           O  
ANISOU 1842  O   LEU A 312     5731   6727   6761    396   -940   -434       O  
ATOM   1843  CB  LEU A 312      46.346 -23.839  -9.203  1.00 32.19           C  
ANISOU 1843  CB  LEU A 312     3541   4533   4156    121  -1306   -535       C  
ATOM   1844  CG  LEU A 312      47.680 -23.344  -9.772  1.00 30.05           C  
ANISOU 1844  CG  LEU A 312     2999   4302   4118    119  -1350   -521       C  
ATOM   1845  CD1 LEU A 312      47.476 -22.165 -10.715  1.00 24.89           C  
ANISOU 1845  CD1 LEU A 312     2287   3619   3551     34  -1190   -607       C  
ATOM   1846  CD2 LEU A 312      48.648 -22.988  -8.653  1.00 33.56           C  
ANISOU 1846  CD2 LEU A 312     3381   4820   4549     33  -1571   -480       C  
ATOM   1847  N   PRO A 313      46.495 -26.891 -10.060  1.00 39.15           N  
ANISOU 1847  N   PRO A 313     4438   5297   5138    449  -1193   -326       N  
ATOM   1848  CA  PRO A 313      47.297 -27.973 -10.665  1.00 34.35           C  
ANISOU 1848  CA  PRO A 313     3718   4634   4701    612  -1143   -237       C  
ATOM   1849  C   PRO A 313      46.651 -28.597 -11.891  1.00 39.42           C  
ANISOU 1849  C   PRO A 313     4460   5166   5353    665   -911   -272       C  
ATOM   1850  O   PRO A 313      47.313 -28.759 -12.925  1.00 41.14           O  
ANISOU 1850  O   PRO A 313     4561   5343   5727    744   -775   -276       O  
ATOM   1851  CB  PRO A 313      47.444 -28.981  -9.513  1.00 24.28           C  
ANISOU 1851  CB  PRO A 313     2518   3353   3353    687  -1315   -117       C  
ATOM   1852  CG  PRO A 313      47.151 -28.202  -8.267  1.00 24.57           C  
ANISOU 1852  CG  PRO A 313     2649   3485   3201    548  -1498   -144       C  
ATOM   1853  CD  PRO A 313      46.146 -27.172  -8.658  1.00 27.44           C  
ANISOU 1853  CD  PRO A 313     3112   3847   3468    416  -1358   -284       C  
ATOM   1854  N   ILE A 314      45.365 -28.944 -11.810  1.00 45.48           N  
ANISOU 1854  N   ILE A 314     5446   5881   5955    613   -857   -298       N  
ATOM   1855  CA  ILE A 314      44.715 -29.596 -12.941  1.00 47.97           C  
ANISOU 1855  CA  ILE A 314     5875   6090   6262    635   -676   -330       C  
ATOM   1856  C   ILE A 314      44.603 -28.650 -14.130  1.00 40.87           C  
ANISOU 1856  C   ILE A 314     4920   5213   5398    563   -545   -415       C  
ATOM   1857  O   ILE A 314      44.684 -29.084 -15.286  1.00 39.61           O  
ANISOU 1857  O   ILE A 314     4794   4980   5275    603   -396   -440       O  
ATOM   1858  CB  ILE A 314      43.336 -30.137 -12.524  1.00 49.26           C  
ANISOU 1858  CB  ILE A 314     6256   6201   6262    569   -674   -321       C  
ATOM   1859  CG1 ILE A 314      42.793 -31.076 -13.601  1.00 48.52           C  
ANISOU 1859  CG1 ILE A 314     6291   5978   6166    587   -532   -342       C  
ATOM   1860  CG2 ILE A 314      42.371 -28.993 -12.265  1.00 46.99           C  
ANISOU 1860  CG2 ILE A 314     5999   5985   5872    426   -679   -376       C  
ATOM   1861  CD1 ILE A 314      43.726 -32.226 -13.913  1.00 50.70           C  
ANISOU 1861  CD1 ILE A 314     6560   6145   6558    745   -480   -300       C  
ATOM   1862  N   SER A 315      44.420 -27.352 -13.877  1.00 38.72           N  
ANISOU 1862  N   SER A 315     4583   5026   5101    453   -590   -457       N  
ATOM   1863  CA  SER A 315      44.273 -26.402 -14.974  1.00 34.63           C  
ANISOU 1863  CA  SER A 315     4019   4523   4617    383   -472   -513       C  
ATOM   1864  C   SER A 315      45.589 -26.209 -15.714  1.00 50.82           C  
ANISOU 1864  C   SER A 315     5889   6584   6834    450   -396   -508       C  
ATOM   1865  O   SER A 315      45.633 -26.261 -16.949  1.00 61.79           O  
ANISOU 1865  O   SER A 315     7301   7934   8243    462   -235   -529       O  
ATOM   1866  CB  SER A 315      43.750 -25.066 -14.447  1.00 27.60           C  
ANISOU 1866  CB  SER A 315     3112   3693   3683    261   -526   -553       C  
ATOM   1867  OG  SER A 315      42.466 -25.221 -13.871  1.00 40.16           O  
ANISOU 1867  OG  SER A 315     4856   5264   5139    208   -544   -550       O  
ATOM   1868  N   VAL A 316      46.675 -25.987 -14.973  1.00 46.56           N  
ANISOU 1868  N   VAL A 316     5173   6102   6417    485   -511   -473       N  
ATOM   1869  CA  VAL A 316      47.975 -25.811 -15.611  1.00 39.71           C  
ANISOU 1869  CA  VAL A 316     4088   5247   5752    550   -431   -446       C  
ATOM   1870  C   VAL A 316      48.425 -27.104 -16.277  1.00 39.48           C  
ANISOU 1870  C   VAL A 316     4078   5127   5796    713   -289   -407       C  
ATOM   1871  O   VAL A 316      48.983 -27.088 -17.382  1.00 39.07           O  
ANISOU 1871  O   VAL A 316     3962   5041   5843    763    -92   -417       O  
ATOM   1872  CB  VAL A 316      49.008 -25.314 -14.586  1.00 31.39           C  
ANISOU 1872  CB  VAL A 316     2818   4279   4828    533   -627   -401       C  
ATOM   1873  CG1 VAL A 316      50.370 -25.159 -15.249  1.00 25.23           C  
ANISOU 1873  CG1 VAL A 316     1768   3513   4304    600   -535   -350       C  
ATOM   1874  CG2 VAL A 316      48.546 -24.004 -13.981  1.00 27.24           C  
ANISOU 1874  CG2 VAL A 316     2320   3814   4217    361   -738   -468       C  
ATOM   1875  N   LEU A 317      48.194 -28.242 -15.619  1.00 41.77           N  
ANISOU 1875  N   LEU A 317     4473   5361   6037    798   -366   -362       N  
ATOM   1876  CA  LEU A 317      48.579 -29.521 -16.205  1.00 40.45           C  
ANISOU 1876  CA  LEU A 317     4352   5070   5946    960   -217   -331       C  
ATOM   1877  C   LEU A 317      47.819 -29.788 -17.497  1.00 34.81           C  
ANISOU 1877  C   LEU A 317     3853   4263   5109    926     -5   -421       C  
ATOM   1878  O   LEU A 317      48.369 -30.364 -18.443  1.00 38.00           O  
ANISOU 1878  O   LEU A 317     4273   4574   5591   1031    202   -437       O  
ATOM   1879  CB  LEU A 317      48.334 -30.650 -15.202  1.00 39.93           C  
ANISOU 1879  CB  LEU A 317     4388   4945   5838   1041   -349   -256       C  
ATOM   1880  CG  LEU A 317      49.382 -30.847 -14.106  1.00 40.31           C  
ANISOU 1880  CG  LEU A 317     4227   5050   6040   1137   -541   -127       C  
ATOM   1881  CD1 LEU A 317      49.025 -32.044 -13.240  1.00 42.83           C  
ANISOU 1881  CD1 LEU A 317     4695   5289   6291   1220   -646    -39       C  
ATOM   1882  CD2 LEU A 317      50.761 -31.016 -14.720  1.00 41.60           C  
ANISOU 1882  CD2 LEU A 317     4133   5188   6484   1289   -418    -67       C  
ATOM   1883  N   ASN A 318      46.548 -29.379 -17.557  1.00 33.82           N  
ANISOU 1883  N   ASN A 318     3901   4160   4790    777    -50   -476       N  
ATOM   1884  CA  ASN A 318      45.765 -29.595 -18.770  1.00 43.70           C  
ANISOU 1884  CA  ASN A 318     5358   5338   5907    714     99   -547       C  
ATOM   1885  C   ASN A 318      46.268 -28.730 -19.918  1.00 54.69           C  
ANISOU 1885  C   ASN A 318     6677   6767   7334    684    258   -582       C  
ATOM   1886  O   ASN A 318      46.292 -29.172 -21.073  1.00 58.12           O  
ANISOU 1886  O   ASN A 318     7253   7121   7710    703    442   -630       O  
ATOM   1887  CB  ASN A 318      44.287 -29.319 -18.491  1.00 53.46           C  
ANISOU 1887  CB  ASN A 318     6744   6600   6967    562    -12   -564       C  
ATOM   1888  CG  ASN A 318      43.367 -30.012 -19.480  1.00 67.76           C  
ANISOU 1888  CG  ASN A 318     8797   8313   8635    497     72   -613       C  
ATOM   1889  OD1 ASN A 318      42.550 -29.372 -20.142  1.00 79.21           O  
ANISOU 1889  OD1 ASN A 318    10315   9802   9981    368     72   -634       O  
ATOM   1890  ND2 ASN A 318      43.498 -31.330 -19.584  1.00 61.65           N  
ANISOU 1890  ND2 ASN A 318     8161   7404   7860    582    133   -624       N  
ATOM   1891  N   VAL A 319      46.674 -27.494 -19.622  1.00 54.06           N  
ANISOU 1891  N   VAL A 319     6400   6799   7340    627    197   -561       N  
ATOM   1892  CA  VAL A 319      47.165 -26.609 -20.672  1.00 43.57           C  
ANISOU 1892  CA  VAL A 319     4996   5503   6057    590    353   -574       C  
ATOM   1893  C   VAL A 319      48.540 -27.050 -21.154  1.00 49.85           C  
ANISOU 1893  C   VAL A 319     5647   6258   7037    737    537   -550       C  
ATOM   1894  O   VAL A 319      48.829 -27.024 -22.357  1.00 59.47           O  
ANISOU 1894  O   VAL A 319     6928   7434   8233    751    764   -576       O  
ATOM   1895  CB  VAL A 319      47.184 -25.154 -20.173  1.00 38.87           C  
ANISOU 1895  CB  VAL A 319     4238   5013   5519    477    239   -557       C  
ATOM   1896  CG1 VAL A 319      48.180 -24.340 -20.981  1.00 43.67           C  
ANISOU 1896  CG1 VAL A 319     4679   5648   6267    473    396   -538       C  
ATOM   1897  CG2 VAL A 319      45.793 -24.552 -20.264  1.00 44.14           C  
ANISOU 1897  CG2 VAL A 319     5061   5695   6013    340    170   -578       C  
ATOM   1898  N   LEU A 320      49.415 -27.456 -20.229  1.00 37.02           N  
ANISOU 1898  N   LEU A 320     3825   4643   5600    850    447   -488       N  
ATOM   1899  CA  LEU A 320      50.732 -27.935 -20.635  1.00 41.35           C  
ANISOU 1899  CA  LEU A 320     4194   5143   6373   1013    629   -440       C  
ATOM   1900  C   LEU A 320      50.636 -29.226 -21.435  1.00 49.83           C  
ANISOU 1900  C   LEU A 320     5490   6060   7384   1138    850   -484       C  
ATOM   1901  O   LEU A 320      51.477 -29.479 -22.304  1.00 62.37           O  
ANISOU 1901  O   LEU A 320     7026   7582   9090   1249   1118   -484       O  
ATOM   1902  CB  LEU A 320      51.625 -28.136 -19.410  1.00 54.83           C  
ANISOU 1902  CB  LEU A 320     5631   6900   8304   1104    439   -337       C  
ATOM   1903  CG  LEU A 320      51.894 -26.907 -18.540  1.00 54.26           C  
ANISOU 1903  CG  LEU A 320     5343   6970   8304    971    207   -303       C  
ATOM   1904  CD1 LEU A 320      52.632 -27.304 -17.271  1.00 54.68           C  
ANISOU 1904  CD1 LEU A 320     5192   7069   8517   1047    -31   -197       C  
ATOM   1905  CD2 LEU A 320      52.681 -25.863 -19.318  1.00 52.24           C  
ANISOU 1905  CD2 LEU A 320     4881   6762   8206    917    359   -295       C  
ATOM   1906  N   LYS A 321      49.629 -30.053 -21.155  1.00 50.75           N  
ANISOU 1906  N   LYS A 321     5860   6101   7321   1118    759   -525       N  
ATOM   1907  CA  LYS A 321      49.453 -31.298 -21.893  1.00 52.10           C  
ANISOU 1907  CA  LYS A 321     6285   6097   7415   1210    955   -586       C  
ATOM   1908  C   LYS A 321      48.835 -31.048 -23.264  1.00 54.84           C  
ANISOU 1908  C   LYS A 321     6889   6411   7536   1091   1130   -692       C  
ATOM   1909  O   LYS A 321      49.380 -31.463 -24.291  1.00 58.34           O  
ANISOU 1909  O   LYS A 321     7431   6752   7983   1174   1411   -742       O  
ATOM   1910  CB  LYS A 321      48.586 -32.266 -21.085  1.00 50.93           C  
ANISOU 1910  CB  LYS A 321     6315   5870   7166   1206    784   -582       C  
ATOM   1911  CG  LYS A 321      48.234 -33.546 -21.824  1.00 57.14           C  
ANISOU 1911  CG  LYS A 321     7408   6451   7850   1260    962   -663       C  
ATOM   1912  CD  LYS A 321      47.260 -34.395 -21.019  1.00 60.98           C  
ANISOU 1912  CD  LYS A 321     8070   6864   8238   1216    782   -649       C  
ATOM   1913  CE  LYS A 321      46.839 -35.635 -21.794  1.00 70.13           C  
ANISOU 1913  CE  LYS A 321     9561   7799   9288   1232    947   -745       C  
ATOM   1914  NZ  LYS A 321      46.180 -36.652 -20.928  1.00 76.54           N  
ANISOU 1914  NZ  LYS A 321    10503   8498  10080   1235    807   -704       N  
ATOM   1915  N   ARG A 322      47.686 -30.371 -23.293  1.00 53.50           N  
ANISOU 1915  N   ARG A 322     6837   6324   7166    899    970   -718       N  
ATOM   1916  CA  ARG A 322      46.957 -30.191 -24.543  1.00 58.91           C  
ANISOU 1916  CA  ARG A 322     7786   6986   7611    768   1075   -795       C  
ATOM   1917  C   ARG A 322      47.617 -29.139 -25.426  1.00 71.32           C  
ANISOU 1917  C   ARG A 322     9256   8634   9210    743   1245   -782       C  
ATOM   1918  O   ARG A 322      47.998 -29.416 -26.568  1.00 80.17           O  
ANISOU 1918  O   ARG A 322    10533   9679  10250    773   1501   -835       O  
ATOM   1919  CB  ARG A 322      45.506 -29.812 -24.246  1.00 52.59           C  
ANISOU 1919  CB  ARG A 322     7101   6250   6631    582    835   -792       C  
ATOM   1920  CG  ARG A 322      44.804 -30.770 -23.303  1.00 55.50           C  
ANISOU 1920  CG  ARG A 322     7553   6552   6983    589    672   -787       C  
ATOM   1921  CD  ARG A 322      44.243 -31.980 -24.041  1.00 65.07           C  
ANISOU 1921  CD  ARG A 322     9091   7601   8032    558    754   -872       C  
ATOM   1922  NE  ARG A 322      43.848 -33.052 -23.128  1.00 74.01           N  
ANISOU 1922  NE  ARG A 322    10287   8633   9201    599    648   -855       N  
ATOM   1923  CZ  ARG A 322      43.366 -34.230 -23.517  1.00 75.49           C  
ANISOU 1923  CZ  ARG A 322    10749   8650   9285    573    695   -923       C  
ATOM   1924  NH1 ARG A 322      43.212 -34.496 -24.807  1.00 75.86           N  
ANISOU 1924  NH1 ARG A 322    11044   8616   9165    497    833  -1023       N  
ATOM   1925  NH2 ARG A 322      43.037 -35.146 -22.614  1.00 70.45           N  
ANISOU 1925  NH2 ARG A 322    10150   7918   8701    610    600   -887       N  
ATOM   1926  N   VAL A 323      47.758 -27.918 -24.914  1.00 70.48           N  
ANISOU 1926  N   VAL A 323     8907   8665   9209    680   1120   -713       N  
ATOM   1927  CA  VAL A 323      48.219 -26.821 -25.757  1.00 64.24           C  
ANISOU 1927  CA  VAL A 323     8036   7941   8431    623   1265   -687       C  
ATOM   1928  C   VAL A 323      49.707 -26.945 -26.056  1.00 72.23           C  
ANISOU 1928  C   VAL A 323     8852   8922   9671    776   1519   -659       C  
ATOM   1929  O   VAL A 323      50.145 -26.729 -27.192  1.00 83.08           O  
ANISOU 1929  O   VAL A 323    10300  10271  10994    779   1781   -671       O  
ATOM   1930  CB  VAL A 323      47.892 -25.476 -25.093  1.00 51.64           C  
ANISOU 1930  CB  VAL A 323     6254   6470   6896    503   1061   -626       C  
ATOM   1931  CG1 VAL A 323      48.136 -24.346 -26.072  1.00 41.30           C  
ANISOU 1931  CG1 VAL A 323     4920   5208   5565    418   1204   -590       C  
ATOM   1932  CG2 VAL A 323      46.458 -25.479 -24.606  1.00 58.58           C  
ANISOU 1932  CG2 VAL A 323     7284   7367   7608    390    828   -639       C  
ATOM   1933  N   PHE A 324      50.509 -27.292 -25.054  1.00 71.15           N  
ANISOU 1933  N   PHE A 324     8456   8787   9789    905   1449   -609       N  
ATOM   1934  CA  PHE A 324      51.957 -27.300 -25.205  1.00 74.64           C  
ANISOU 1934  CA  PHE A 324     8640   9228  10492   1033   1625   -540       C  
ATOM   1935  C   PHE A 324      52.535 -28.676 -25.517  1.00 82.94           C  
ANISOU 1935  C   PHE A 324     9793  10155  11564   1189   1765   -546       C  
ATOM   1936  O   PHE A 324      53.752 -28.795 -25.684  1.00 88.17           O  
ANISOU 1936  O   PHE A 324    10264  10818  12418   1279   1878   -474       O  
ATOM   1937  CB  PHE A 324      52.606 -26.730 -23.942  1.00 66.31           C  
ANISOU 1937  CB  PHE A 324     7217   8276   9703   1042   1398   -446       C  
ATOM   1938  CG  PHE A 324      52.347 -25.261 -23.743  1.00 56.44           C  
ANISOU 1938  CG  PHE A 324     5841   7141   8464    869   1274   -432       C  
ATOM   1939  CD1 PHE A 324      52.982 -24.314 -24.531  1.00 49.43           C  
ANISOU 1939  CD1 PHE A 324     4856   6294   7629    798   1423   -387       C  
ATOM   1940  CD2 PHE A 324      51.467 -24.829 -22.765  1.00 50.10           C  
ANISOU 1940  CD2 PHE A 324     5079   6399   7556    751    969   -448       C  
ATOM   1941  CE1 PHE A 324      52.744 -22.963 -24.344  1.00 43.73           C  
ANISOU 1941  CE1 PHE A 324     4032   5651   6932    638   1316   -371       C  
ATOM   1942  CE2 PHE A 324      51.226 -23.483 -22.574  1.00 38.33           C  
ANISOU 1942  CE2 PHE A 324     3508   4989   6065    591    857   -439       C  
ATOM   1943  CZ  PHE A 324      51.865 -22.549 -23.363  1.00 39.35           C  
ANISOU 1943  CZ  PHE A 324     3509   5141   6301    536   1031   -403       C  
ATOM   1944  N   GLY A 325      51.703 -29.712 -25.600  1.00 83.20           N  
ANISOU 1944  N   GLY A 325    10121  10073  11418   1210   1760   -630       N  
ATOM   1945  CA  GLY A 325      52.182 -31.026 -25.999  1.00 86.94           C  
ANISOU 1945  CA  GLY A 325    10725  10404  11903   1336   1908   -650       C  
ATOM   1946  C   GLY A 325      53.201 -31.651 -25.071  1.00 87.18           C  
ANISOU 1946  C   GLY A 325    10483  10415  12226   1511   1850   -547       C  
ATOM   1947  O   GLY A 325      54.081 -32.383 -25.535  1.00 91.41           O  
ANISOU 1947  O   GLY A 325    11004  10863  12866   1628   2035   -525       O  
ATOM   1948  N   MET A 326      53.113 -31.383 -23.769  1.00 78.43           N  
ANISOU 1948  N   MET A 326     9163   9386  11251   1528   1593   -476       N  
ATOM   1949  CA  MET A 326      54.037 -31.946 -22.795  1.00 69.30           C  
ANISOU 1949  CA  MET A 326     7751   8230  10348   1676   1479   -355       C  
ATOM   1950  C   MET A 326      53.564 -33.316 -22.306  1.00 64.62           C  
ANISOU 1950  C   MET A 326     7348   7488   9718   1782   1426   -367       C  
ATOM   1951  O   MET A 326      52.482 -33.796 -22.652  1.00 66.37           O  
ANISOU 1951  O   MET A 326     7893   7608   9718   1722   1458   -475       O  
ATOM   1952  CB  MET A 326      54.219 -30.988 -21.618  1.00 58.51           C  
ANISOU 1952  CB  MET A 326     6084   7029   9117   1617   1194   -260       C  
ATOM   1953  CG  MET A 326      54.814 -29.641 -21.988  1.00 61.80           C  
ANISOU 1953  CG  MET A 326     6290   7582   9608   1500   1223   -232       C  
ATOM   1954  SD  MET A 326      55.363 -28.723 -20.534  1.00 78.11           S  
ANISOU 1954  SD  MET A 326     8001   9823  11855   1422    866   -113       S  
ATOM   1955  CE  MET A 326      55.747 -27.130 -21.255  1.00 85.71           C  
ANISOU 1955  CE  MET A 326     8833  10891  12843   1246    954   -124       C  
ATOM   1956  N   PHE A 327      54.400 -33.945 -21.473  1.00 61.91           N  
ANISOU 1956  N   PHE A 327     6800   7130   9593   1928   1329   -243       N  
ATOM   1957  CA  PHE A 327      54.084 -35.218 -20.817  1.00 67.00           C  
ANISOU 1957  CA  PHE A 327     7577   7634  10245   2039   1247   -213       C  
ATOM   1958  C   PHE A 327      53.787 -36.333 -21.819  1.00 82.93           C  
ANISOU 1958  C   PHE A 327     9921   9446  12143   2075   1499   -326       C  
ATOM   1959  O   PHE A 327      52.898 -37.161 -21.603  1.00 96.64           O  
ANISOU 1959  O   PHE A 327    11914  11052  13752   2064   1450   -376       O  
ATOM   1960  CB  PHE A 327      52.911 -35.055 -19.846  1.00 61.78           C  
ANISOU 1960  CB  PHE A 327     7016   7000   9456   1961    993   -214       C  
ATOM   1961  CG  PHE A 327      52.872 -33.726 -19.139  1.00 53.37           C  
ANISOU 1961  CG  PHE A 327     5714   6137   8427   1852    772   -163       C  
ATOM   1962  CD1 PHE A 327      53.912 -33.331 -18.311  1.00 50.56           C  
ANISOU 1962  CD1 PHE A 327     5026   5918   8266   1886    588    -22       C  
ATOM   1963  CD2 PHE A 327      51.777 -32.891 -19.270  1.00 51.17           C  
ANISOU 1963  CD2 PHE A 327     5579   5927   7937   1665    704   -262       C  
ATOM   1964  CE1 PHE A 327      53.867 -32.115 -17.645  1.00 40.46           C  
ANISOU 1964  CE1 PHE A 327     3562   4818   6994   1744    360      7       C  
ATOM   1965  CE2 PHE A 327      51.723 -31.680 -18.608  1.00 50.02           C  
ANISOU 1965  CE2 PHE A 327     5261   5971   7772   1515    474   -235       C  
ATOM   1966  CZ  PHE A 327      52.770 -31.290 -17.794  1.00 43.08           C  
ANISOU 1966  CZ  PHE A 327     4041   5197   7131   1569    314   -109       C  
ATOM   1967  N   ARG A 328      54.527 -36.362 -22.929  1.00 85.56           N  
ANISOU 1967  N   ARG A 328    10256   9742  12509   2103   1770   -363       N  
ATOM   1968  CA  ARG A 328      54.366 -37.417 -23.918  1.00 92.15           C  
ANISOU 1968  CA  ARG A 328    11400  10383  13230   2130   2016   -467       C  
ATOM   1969  C   ARG A 328      55.538 -38.390 -23.966  1.00 98.92           C  
ANISOU 1969  C   ARG A 328    12136  11117  14330   2330   2182   -385       C  
ATOM   1970  O   ARG A 328      55.409 -39.465 -24.564  1.00100.79           O  
ANISOU 1970  O   ARG A 328    12629  11162  14503   2376   2365   -459       O  
ATOM   1971  CB  ARG A 328      54.162 -36.800 -25.308  1.00 92.89           C  
ANISOU 1971  CB  ARG A 328    11676  10500  13119   1996   2229   -585       C  
ATOM   1972  CG  ARG A 328      52.866 -35.999 -25.437  1.00 93.85           C  
ANISOU 1972  CG  ARG A 328    12033  10683  12944   1789   2099   -691       C  
ATOM   1973  CD  ARG A 328      52.732 -35.313 -26.799  1.00102.72           C  
ANISOU 1973  CD  ARG A 328    13267  11876  13887   1654   2260   -761       C  
ATOM   1974  NE  ARG A 328      52.642 -36.273 -27.902  1.00112.63           N  
ANISOU 1974  NE  ARG A 328    14799  13159  14836   1455   2146   -861       N  
ATOM   1975  CZ  ARG A 328      52.634 -35.935 -29.187  1.00117.65           C  
ANISOU 1975  CZ  ARG A 328    15368  13905  15428   1364   1915   -846       C  
ATOM   1976  NH1 ARG A 328      52.555 -36.867 -30.129  1.00113.59           N  
ANISOU 1976  NH1 ARG A 328    15106  13411  14643   1179   1818   -925       N  
ATOM   1977  NH2 ARG A 328      52.692 -34.657 -29.531  1.00120.75           N  
ANISOU 1977  NH2 ARG A 328    15441  14387  16051   1453   1770   -743       N  
ATOM   1978  N   GLN A 329      56.673 -38.045 -23.364  1.00 99.78           N  
ANISOU 1978  N   GLN A 329    11867  11327  14719   2441   2121   -231       N  
ATOM   1979  CA  GLN A 329      57.821 -38.944 -23.301  1.00 97.47           C  
ANISOU 1979  CA  GLN A 329    11418  10923  14692   2641   2260   -124       C  
ATOM   1980  C   GLN A 329      57.671 -39.898 -22.116  1.00 91.40           C  
ANISOU 1980  C   GLN A 329    10628  10075  14024   2755   2045    -26       C  
ATOM   1981  O   GLN A 329      57.481 -39.455 -20.976  1.00 80.92           O  
ANISOU 1981  O   GLN A 329     9136   8880  12729   2728   1732     70       O  
ATOM   1982  CB  GLN A 329      59.123 -38.153 -23.216  1.00101.98           C  
ANISOU 1982  CB  GLN A 329    11585  11638  15524   2690   2279     11       C  
ATOM   1983  CG  GLN A 329      60.347 -39.043 -23.166  1.00114.88           C  
ANISOU 1983  CG  GLN A 329    13030  13159  17459   2901   2431    139       C  
ATOM   1984  CD  GLN A 329      60.378 -40.047 -24.304  1.00116.65           C  
ANISOU 1984  CD  GLN A 329    13544  13153  17626   2981   2803     32       C  
ATOM   1985  OE1 GLN A 329      60.246 -39.684 -25.473  1.00118.40           O  
ANISOU 1985  OE1 GLN A 329    13946  13352  17688   2894   3048    -87       O  
ATOM   1986  NE2 GLN A 329      60.551 -41.320 -23.965  1.00110.67           N  
ANISOU 1986  NE2 GLN A 329    12845  12215  16987   3143   2843     80       N  
ATOM   1987  N   ALA A 330      57.724 -41.207 -22.387  1.00 97.68           N  
ANISOU 1987  N   ALA A 330    11611  10648  14855   2875   2212    -47       N  
ATOM   1988  CA  ALA A 330      57.454 -42.217 -21.371  1.00 94.39           C  
ANISOU 1988  CA  ALA A 330    11239  10120  14504   2974   2033     38       C  
ATOM   1989  C   ALA A 330      58.614 -42.412 -20.407  1.00 94.86           C  
ANISOU 1989  C   ALA A 330    10926  10234  14883   3150   1895    262       C  
ATOM   1990  O   ALA A 330      58.607 -43.377 -19.631  1.00 92.21           O  
ANISOU 1990  O   ALA A 330    10612   9784  14638   3267   1781    362       O  
ATOM   1991  CB  ALA A 330      57.123 -43.558 -22.036  1.00 95.82           C  
ANISOU 1991  CB  ALA A 330    11758  10029  14620   3030   2269    -64       C  
ATOM   1992  N   SER A 331      59.622 -41.536 -20.439  1.00102.16           N  
ANISOU 1992  N   SER A 331    11509  11325  15981   3163   1895    353       N  
ATOM   1993  CA  SER A 331      60.698 -41.631 -19.457  1.00107.60           C  
ANISOU 1993  CA  SER A 331    11829  12093  16961   3297   1711    577       C  
ATOM   1994  C   SER A 331      60.206 -41.185 -18.086  1.00104.61           C  
ANISOU 1994  C   SER A 331    11366  11876  16505   3217   1284    670       C  
ATOM   1995  O   SER A 331      60.492 -41.832 -17.073  1.00103.61           O  
ANISOU 1995  O   SER A 331    11142  11728  16497   3327   1080    831       O  
ATOM   1996  CB  SER A 331      61.896 -40.794 -19.893  1.00109.66           C  
ANISOU 1996  CB  SER A 331    11751  12485  17431   3303   1824    647       C  
ATOM   1997  OG  SER A 331      61.619 -39.417 -19.719  1.00107.69           O  
ANISOU 1997  OG  SER A 331    11396  12458  17062   3112   1642    614       O  
ATOM   1998  N   ASP A 332      59.457 -40.086 -18.032  1.00104.42           N  
ANISOU 1998  N   ASP A 332    11391  12009  16273   3026   1148    578       N  
ATOM   1999  CA  ASP A 332      58.840 -39.648 -16.785  1.00105.65           C  
ANISOU 1999  CA  ASP A 332    11526  12305  16311   2933    768    646       C  
ATOM   2000  C   ASP A 332      57.350 -39.938 -16.714  1.00104.04           C  
ANISOU 2000  C   ASP A 332    11696  11990  15844   2858    741    527       C  
ATOM   2001  O   ASP A 332      56.555 -39.082 -16.316  1.00101.62           O  
ANISOU 2001  O   ASP A 332    11458  11802  15353   2706    568    477       O  
ATOM   2002  CB  ASP A 332      58.988 -38.139 -16.643  1.00108.72           C  
ANISOU 2002  CB  ASP A 332    11707  12937  16664   2765    621    638       C  
ATOM   2003  CG  ASP A 332      58.503 -37.405 -17.872  1.00104.04           C  
ANISOU 2003  CG  ASP A 332    11253  12346  15931   2642    867    453       C  
ATOM   2004  OD1 ASP A 332      58.831 -37.862 -18.988  1.00105.09           O  
ANISOU 2004  OD1 ASP A 332    11473  12344  16110   2712   1195    380       O  
ATOM   2005  OD2 ASP A 332      57.780 -36.398 -17.732  1.00 97.85           O  
ANISOU 2005  OD2 ASP A 332    10508  11690  14979   2474    739    383       O  
ATOM   2006  N   ARG A 333      56.966 -41.159 -17.104  1.00103.95           N  
ANISOU 2006  N   ARG A 333    11929  11741  15826   2957    917    484       N  
ATOM   2007  CA  ARG A 333      55.562 -41.563 -17.082  1.00100.73           C  
ANISOU 2007  CA  ARG A 333    11888  11197  15186   2872    908    373       C  
ATOM   2008  C   ARG A 333      55.006 -41.735 -15.665  1.00 94.68           C  
ANISOU 2008  C   ARG A 333    11133  10490  14350   2846    563    502       C  
ATOM   2009  O   ARG A 333      53.820 -41.508 -15.405  1.00 95.51           O  
ANISOU 2009  O   ARG A 333    11440  10605  14244   2707    468    431       O  
ATOM   2010  CB  ARG A 333      55.415 -42.906 -17.807  1.00115.92           C  
ANISOU 2010  CB  ARG A 333    14050  12847  17146   2977   1159    315       C  
ATOM   2011  CG  ARG A 333      54.003 -43.487 -17.896  1.00123.84           C  
ANISOU 2011  CG  ARG A 333    15463  13694  17896   2838   1282    124       C  
ATOM   2012  CD  ARG A 333      53.981 -44.796 -18.710  1.00137.11           C  
ANISOU 2012  CD  ARG A 333    17371  15111  19612   2926   1348    142       C  
ATOM   2013  NE  ARG A 333      52.632 -45.354 -18.825  1.00148.97           N  
ANISOU 2013  NE  ARG A 333    18868  16607  21128   2949   1059    299       N  
ATOM   2014  CZ  ARG A 333      52.301 -46.364 -19.624  1.00153.99           C  
ANISOU 2014  CZ  ARG A 333    19782  17133  21593   2830    974    261       C  
ATOM   2015  NH1 ARG A 333      53.223 -46.945 -20.379  1.00154.27           N  
ANISOU 2015  NH1 ARG A 333    20119  17065  21433   2673   1137     63       N  
ATOM   2016  NH2 ARG A 333      51.047 -46.798 -19.670  1.00154.74           N  
ANISOU 2016  NH2 ARG A 333    19862  17231  21701   2854    720    430       N  
ATOM   2017  N   GLU A 334      55.879 -42.110 -14.724  1.00 93.50           N  
ANISOU 2017  N   GLU A 334    10775  10385  14366   2972    371    703       N  
ATOM   2018  CA  GLU A 334      55.423 -42.417 -13.369  1.00 87.62           C  
ANISOU 2018  CA  GLU A 334    10086   9682  13524   2953     52    844       C  
ATOM   2019  C   GLU A 334      55.082 -41.095 -12.689  1.00 78.41           C  
ANISOU 2019  C   GLU A 334     8810   8774  12207   2791   -208    862       C  
ATOM   2020  O   GLU A 334      54.009 -40.951 -12.092  1.00 72.04           O  
ANISOU 2020  O   GLU A 334     8192   7984  11196   2684   -359    860       O  
ATOM   2021  CB  GLU A 334      56.448 -43.199 -12.548  1.00101.30           C  
ANISOU 2021  CB  GLU A 334    11639  11395  15456   3129    -79   1061       C  
ATOM   2022  CG  GLU A 334      55.946 -43.749 -11.225  1.00109.55           C  
ANISOU 2022  CG  GLU A 334    12809  12429  16387   3135   -364   1219       C  
ATOM   2023  CD  GLU A 334      57.088 -44.046 -10.273  1.00118.69           C  
ANISOU 2023  CD  GLU A 334    13712  13675  17710   3266   -575   1453       C  
ATOM   2024  OE1 GLU A 334      57.724 -43.082  -9.799  1.00123.50           O  
ANISOU 2024  OE1 GLU A 334    14060  14531  18333   3201   -770   1520       O  
ATOM   2025  OE2 GLU A 334      57.364 -45.237 -10.014  1.00121.86           O  
ANISOU 2025  OE2 GLU A 334    14173  13897  18233   3424   -547   1568       O  
ATOM   2026  N   ALA A 335      55.987 -40.115 -12.766  1.00 83.25           N  
ANISOU 2026  N   ALA A 335     9122   9587  12924   2758   -255    883       N  
ATOM   2027  CA  ALA A 335      55.751 -38.836 -12.102  1.00 79.33           C  
ANISOU 2027  CA  ALA A 335     8515   9335  12292   2583   -506    894       C  
ATOM   2028  C   ALA A 335      54.578 -38.081 -12.711  1.00 78.35           C  
ANISOU 2028  C   ALA A 335     8573   9216  11980   2426   -411    717       C  
ATOM   2029  O   ALA A 335      53.862 -37.368 -11.999  1.00 83.77           O  
ANISOU 2029  O   ALA A 335     9306  10030  12494   2278   -626    722       O  
ATOM   2030  CB  ALA A 335      57.014 -37.976 -12.161  1.00 78.18           C  
ANISOU 2030  CB  ALA A 335     8014   9371  12320   2558   -554    942       C  
ATOM   2031  N   VAL A 336      54.366 -38.225 -14.018  1.00 71.97           N  
ANISOU 2031  N   VAL A 336     7882   8272  11191   2442    -94    558       N  
ATOM   2032  CA  VAL A 336      53.251 -37.545 -14.661  1.00 63.02           C  
ANISOU 2032  CA  VAL A 336     6931   7135   9880   2295      4    392       C  
ATOM   2033  C   VAL A 336      51.927 -38.137 -14.209  1.00 66.20           C  
ANISOU 2033  C   VAL A 336     7638   7411  10105   2255    -63    384       C  
ATOM   2034  O   VAL A 336      50.947 -37.417 -13.985  1.00 64.55           O  
ANISOU 2034  O   VAL A 336     7553   7308   9667   2057   -177    302       O  
ATOM   2035  CB  VAL A 336      53.401 -37.630 -16.189  1.00 60.22           C  
ANISOU 2035  CB  VAL A 336     6667   6672   9543   2306    361    230       C  
ATOM   2036  CG1 VAL A 336      52.071 -37.334 -16.868  1.00 55.93           C  
ANISOU 2036  CG1 VAL A 336     6414   6065   8770   2166    474     60       C  
ATOM   2037  CG2 VAL A 336      54.488 -36.688 -16.667  1.00 60.26           C  
ANISOU 2037  CG2 VAL A 336     6379   6833   9686   2288    427    235       C  
ATOM   2038  N   TYR A 337      51.866 -39.457 -14.095  1.00 78.21           N  
ANISOU 2038  N   TYR A 337     9329   8736  11652   2366     -3    429       N  
ATOM   2039  CA  TYR A 337      50.623 -40.085 -13.674  1.00 87.94           C  
ANISOU 2039  CA  TYR A 337    10867   9835  12709   2312    -48    434       C  
ATOM   2040  C   TYR A 337      50.315 -39.782 -12.216  1.00 84.81           C  
ANISOU 2040  C   TYR A 337    10434   9599  12190   2232   -389    580       C  
ATOM   2041  O   TYR A 337      49.149 -39.592 -11.850  1.00 87.25           O  
ANISOU 2041  O   TYR A 337    10962   9954  12235   2041   -475    515       O  
ATOM   2042  CB  TYR A 337      50.709 -41.574 -13.947  1.00103.83           C  
ANISOU 2042  CB  TYR A 337    13060  11595  14796   2412    100    435       C  
ATOM   2043  CG  TYR A 337      50.818 -41.791 -15.427  1.00121.98           C  
ANISOU 2043  CG  TYR A 337    15469  13775  17103   2400    417    239       C  
ATOM   2044  CD1 TYR A 337      50.333 -40.844 -16.320  1.00125.30           C  
ANISOU 2044  CD1 TYR A 337    15949  14277  17380   2261    532     73       C  
ATOM   2045  CD2 TYR A 337      51.477 -42.888 -15.936  1.00138.99           C  
ANISOU 2045  CD2 TYR A 337    17662  15752  19397   2526    598    230       C  
ATOM   2046  CE1 TYR A 337      50.461 -41.022 -17.681  1.00133.82           C  
ANISOU 2046  CE1 TYR A 337    17149  15271  18424   2228    802    -95       C  
ATOM   2047  CE2 TYR A 337      51.607 -43.070 -17.278  1.00146.81           C  
ANISOU 2047  CE2 TYR A 337    18770  16651  20361   2504    884     60       C  
ATOM   2048  CZ  TYR A 337      51.105 -42.145 -18.154  1.00145.51           C  
ANISOU 2048  CZ  TYR A 337    18683  16579  20026   2349    979   -100       C  
ATOM   2049  OH  TYR A 337      51.262 -42.372 -19.499  1.00151.64           O  
ANISOU 2049  OH  TYR A 337    19602  17271  20744   2317   1251   -255       O  
ATOM   2050  N   ALA A 338      51.340 -39.736 -11.362  1.00 76.80           N  
ANISOU 2050  N   ALA A 338     9167   8695  11319   2337   -589    761       N  
ATOM   2051  CA  ALA A 338      51.092 -39.370  -9.972  1.00 69.05           C  
ANISOU 2051  CA  ALA A 338     8172   7880  10181   2238   -919    896       C  
ATOM   2052  C   ALA A 338      50.657 -37.916  -9.852  1.00 65.93           C  
ANISOU 2052  C   ALA A 338     7738   7710   9604   2006  -1045    762       C  
ATOM   2053  O   ALA A 338      49.884 -37.574  -8.950  1.00 65.14           O  
ANISOU 2053  O   ALA A 338     7788   7711   9249   1849  -1224    764       O  
ATOM   2054  CB  ALA A 338      52.336 -39.630  -9.118  1.00 75.45           C  
ANISOU 2054  CB  ALA A 338     8769   8811  11086   2346  -1085   1082       C  
ATOM   2055  N   ALA A 339      51.161 -37.044 -10.730  1.00 64.16           N  
ANISOU 2055  N   ALA A 339     7324   7562   9491   1978   -927    648       N  
ATOM   2056  CA  ALA A 339      50.763 -35.641 -10.690  1.00 53.55           C  
ANISOU 2056  CA  ALA A 339     5954   6412   7979   1755  -1012    516       C  
ATOM   2057  C   ALA A 339      49.299 -35.471 -11.072  1.00 55.03           C  
ANISOU 2057  C   ALA A 339     6445   6564   7900   1585   -894    350       C  
ATOM   2058  O   ALA A 339      48.529 -34.828 -10.349  1.00 63.94           O  
ANISOU 2058  O   ALA A 339     7681   7806   8809   1418  -1036    314       O  
ATOM   2059  CB  ALA A 339      51.659 -34.812 -11.612  1.00 44.92           C  
ANISOU 2059  CB  ALA A 339     4592   5385   7091   1770   -888    451       C  
ATOM   2060  N   PHE A 340      48.901 -36.031 -12.215  1.00 47.79           N  
ANISOU 2060  N   PHE A 340     5670   5486   7001   1622   -632    249       N  
ATOM   2061  CA  PHE A 340      47.519 -35.893 -12.660  1.00 46.58           C  
ANISOU 2061  CA  PHE A 340     5776   5302   6621   1451   -542    109       C  
ATOM   2062  C   PHE A 340      46.556 -36.550 -11.680  1.00 48.22           C  
ANISOU 2062  C   PHE A 340     6199   5464   6660   1394   -658    179       C  
ATOM   2063  O   PHE A 340      45.447 -36.050 -11.459  1.00 47.96           O  
ANISOU 2063  O   PHE A 340     6297   5495   6431   1220   -692    113       O  
ATOM   2064  CB  PHE A 340      47.355 -36.494 -14.055  1.00 57.74           C  
ANISOU 2064  CB  PHE A 340     7323   6540   8074   1493   -268     -3       C  
ATOM   2065  CG  PHE A 340      47.818 -35.594 -15.164  1.00 62.90           C  
ANISOU 2065  CG  PHE A 340     7852   7262   8787   1465   -119   -112       C  
ATOM   2066  CD1 PHE A 340      47.040 -34.525 -15.569  1.00 59.22           C  
ANISOU 2066  CD1 PHE A 340     7430   6911   8158   1272   -127   -221       C  
ATOM   2067  CD2 PHE A 340      49.023 -35.822 -15.809  1.00 68.94           C  
ANISOU 2067  CD2 PHE A 340     8450   7964   9779   1639     47    -90       C  
ATOM   2068  CE1 PHE A 340      47.457 -33.692 -16.591  1.00 59.29           C  
ANISOU 2068  CE1 PHE A 340     7340   6977   8211   1242     12   -303       C  
ATOM   2069  CE2 PHE A 340      49.447 -34.992 -16.837  1.00 67.04           C  
ANISOU 2069  CE2 PHE A 340     8105   7783   9583   1607    208   -180       C  
ATOM   2070  CZ  PHE A 340      48.661 -33.925 -17.228  1.00 65.05           C  
ANISOU 2070  CZ  PHE A 340     7919   7649   9147   1403    184   -284       C  
ATOM   2071  N   THR A 341      46.969 -37.662 -11.067  1.00 52.76           N  
ANISOU 2071  N   THR A 341     6802   5922   7322   1546   -710    329       N  
ATOM   2072  CA  THR A 341      46.117 -38.318 -10.080  1.00 46.00           C  
ANISOU 2072  CA  THR A 341     6152   5016   6308   1495   -812    422       C  
ATOM   2073  C   THR A 341      45.832 -37.394  -8.906  1.00 43.29           C  
ANISOU 2073  C   THR A 341     5786   4881   5782   1364  -1030    459       C  
ATOM   2074  O   THR A 341      44.676 -37.221  -8.502  1.00 53.39           O  
ANISOU 2074  O   THR A 341     7242   6185   6861   1213  -1032    423       O  
ATOM   2075  CB  THR A 341      46.767 -39.611  -9.599  1.00 47.34           C  
ANISOU 2075  CB  THR A 341     6336   5024   6627   1699   -842    606       C  
ATOM   2076  OG1 THR A 341      46.825 -40.544 -10.683  1.00 58.27           O  
ANISOU 2076  OG1 THR A 341     7817   6171   8152   1804   -600    543       O  
ATOM   2077  CG2 THR A 341      45.955 -40.213  -8.466  1.00 46.44           C  
ANISOU 2077  CG2 THR A 341     6432   4876   6339   1639   -961    730       C  
ATOM   2078  N   PHE A 342      46.880 -36.792  -8.343  1.00 41.42           N  
ANISOU 2078  N   PHE A 342     5333   4789   5617   1412  -1208    532       N  
ATOM   2079  CA  PHE A 342      46.691 -35.855  -7.242  1.00 48.31           C  
ANISOU 2079  CA  PHE A 342     6211   5849   6294   1273  -1416    543       C  
ATOM   2080  C   PHE A 342      45.879 -34.643  -7.680  1.00 52.86           C  
ANISOU 2080  C   PHE A 342     6821   6519   6744   1087  -1327    354       C  
ATOM   2081  O   PHE A 342      45.091 -34.098  -6.899  1.00 57.68           O  
ANISOU 2081  O   PHE A 342     7564   7210   7140    949  -1389    325       O  
ATOM   2082  CB  PHE A 342      48.054 -35.430  -6.693  1.00 50.76           C  
ANISOU 2082  CB  PHE A 342     6268   6288   6729   1340  -1642    648       C  
ATOM   2083  CG  PHE A 342      47.999 -34.272  -5.742  1.00 49.31           C  
ANISOU 2083  CG  PHE A 342     6089   6298   6350   1170  -1851    611       C  
ATOM   2084  CD1 PHE A 342      47.609 -34.459  -4.428  1.00 43.90           C  
ANISOU 2084  CD1 PHE A 342     5592   5666   5421   1101  -2013    705       C  
ATOM   2085  CD2 PHE A 342      48.355 -32.997  -6.156  1.00 50.38           C  
ANISOU 2085  CD2 PHE A 342     6058   6549   6534   1066  -1858    477       C  
ATOM   2086  CE1 PHE A 342      47.566 -33.399  -3.545  1.00 47.46           C  
ANISOU 2086  CE1 PHE A 342     6079   6282   5670    914  -2125    641       C  
ATOM   2087  CE2 PHE A 342      48.314 -31.932  -5.276  1.00 49.19           C  
ANISOU 2087  CE2 PHE A 342     5940   6548   6201    894  -2024    425       C  
ATOM   2088  CZ  PHE A 342      47.919 -32.135  -3.969  1.00 50.49           C  
ANISOU 2088  CZ  PHE A 342     6308   6763   6111    810  -2130    496       C  
ATOM   2089  N   SER A 343      46.060 -34.205  -8.928  1.00 54.41           N  
ANISOU 2089  N   SER A 343     6904   6698   7072   1088  -1167    232       N  
ATOM   2090  CA  SER A 343      45.284 -33.076  -9.430  1.00 58.58           C  
ANISOU 2090  CA  SER A 343     7457   7298   7501    925  -1081     76       C  
ATOM   2091  C   SER A 343      43.803 -33.419  -9.535  1.00 60.98           C  
ANISOU 2091  C   SER A 343     7991   7526   7651    826   -969     34       C  
ATOM   2092  O   SER A 343      42.944 -32.564  -9.287  1.00 60.97           O  
ANISOU 2092  O   SER A 343     8047   7600   7519    687   -962    -34       O  
ATOM   2093  CB  SER A 343      45.826 -32.626 -10.787  1.00 62.41           C  
ANISOU 2093  CB  SER A 343     7790   7772   8151    953   -931    -18       C  
ATOM   2094  OG  SER A 343      47.199 -32.289 -10.693  1.00 67.44           O  
ANISOU 2094  OG  SER A 343     8178   8480   8966   1037  -1021     36       O  
ATOM   2095  N   HIS A 344      43.480 -34.664  -9.898  1.00 62.02           N  
ANISOU 2095  N   HIS A 344     8251   7497   7817    894   -876     78       N  
ATOM   2096  CA  HIS A 344      42.074 -35.055  -9.960  1.00 53.46           C  
ANISOU 2096  CA  HIS A 344     7366   6337   6611    781   -790     56       C  
ATOM   2097  C   HIS A 344      41.457 -35.100  -8.571  1.00 53.48           C  
ANISOU 2097  C   HIS A 344     7482   6388   6449    721   -888    147       C  
ATOM   2098  O   HIS A 344      40.313 -34.672  -8.377  1.00 53.29           O  
ANISOU 2098  O   HIS A 344     7543   6395   6310    588   -835    110       O  
ATOM   2099  CB  HIS A 344      41.925 -36.414 -10.647  1.00 49.99           C  
ANISOU 2099  CB  HIS A 344     7054   5692   6249    848   -676     75       C  
ATOM   2100  CG  HIS A 344      42.560 -36.488 -11.999  1.00 45.06           C  
ANISOU 2100  CG  HIS A 344     6366   4997   5756    915   -547    -19       C  
ATOM   2101  ND1 HIS A 344      43.142 -37.640 -12.477  1.00 44.34           N  
ANISOU 2101  ND1 HIS A 344     6334   4723   5791   1058   -452      7       N  
ATOM   2102  CD2 HIS A 344      42.697 -35.565 -12.979  1.00 42.49           C  
ANISOU 2102  CD2 HIS A 344     5944   4747   5451    863   -474   -136       C  
ATOM   2103  CE1 HIS A 344      43.621 -37.426 -13.688  1.00 46.42           C  
ANISOU 2103  CE1 HIS A 344     6548   4956   6133   1090   -312   -101       C  
ATOM   2104  NE2 HIS A 344      43.362 -36.173 -14.017  1.00 45.83           N  
ANISOU 2104  NE2 HIS A 344     6380   5044   5990    969   -331   -182       N  
ATOM   2105  N   TRP A 345      42.205 -35.615  -7.592  1.00 54.35           N  
ANISOU 2105  N   TRP A 345     7597   6505   6550    823  -1025    279       N  
ATOM   2106  CA  TRP A 345      41.708 -35.664  -6.222  1.00 53.63           C  
ANISOU 2106  CA  TRP A 345     7646   6465   6265    766  -1119    376       C  
ATOM   2107  C   TRP A 345      41.528 -34.266  -5.646  1.00 57.03           C  
ANISOU 2107  C   TRP A 345     8048   7068   6553    647  -1177    290       C  
ATOM   2108  O   TRP A 345      40.571 -34.012  -4.907  1.00 58.80           O  
ANISOU 2108  O   TRP A 345     8419   7321   6601    544  -1135    292       O  
ATOM   2109  CB  TRP A 345      42.665 -36.475  -5.357  1.00 49.51           C  
ANISOU 2109  CB  TRP A 345     7131   5923   5759    903  -1286    553       C  
ATOM   2110  CG  TRP A 345      42.316 -36.460  -3.911  1.00 46.92           C  
ANISOU 2110  CG  TRP A 345     6966   5667   5194    843  -1404    661       C  
ATOM   2111  CD1 TRP A 345      41.437 -37.281  -3.270  1.00 49.83           C  
ANISOU 2111  CD1 TRP A 345     7552   5946   5436    812  -1344    769       C  
ATOM   2112  CD2 TRP A 345      42.838 -35.573  -2.916  1.00 50.56           C  
ANISOU 2112  CD2 TRP A 345     7411   6302   5499    792  -1596    670       C  
ATOM   2113  NE1 TRP A 345      41.385 -36.965  -1.933  1.00 59.95           N  
ANISOU 2113  NE1 TRP A 345     8964   7339   6475    756  -1470    849       N  
ATOM   2114  CE2 TRP A 345      42.236 -35.918  -1.691  1.00 59.88           C  
ANISOU 2114  CE2 TRP A 345     8828   7492   6432    737  -1636    782       C  
ATOM   2115  CE3 TRP A 345      43.758 -34.522  -2.944  1.00 43.90           C  
ANISOU 2115  CE3 TRP A 345     6387   5599   4695    771  -1738    593       C  
ATOM   2116  CZ2 TRP A 345      42.525 -35.249  -0.504  1.00 57.13           C  
ANISOU 2116  CZ2 TRP A 345     8516   7301   5890    640  -1750    784       C  
ATOM   2117  CZ3 TRP A 345      44.044 -33.860  -1.767  1.00 43.72           C  
ANISOU 2117  CZ3 TRP A 345     6411   5720   4480    671  -1888    605       C  
ATOM   2118  CH2 TRP A 345      43.430 -34.225  -0.562  1.00 48.98           C  
ANISOU 2118  CH2 TRP A 345     7301   6401   4908    603  -1875    689       C  
ATOM   2119  N   LEU A 346      42.438 -33.346  -5.975  1.00 58.78           N  
ANISOU 2119  N   LEU A 346     8085   7389   6858    657  -1253    213       N  
ATOM   2120  CA  LEU A 346      42.337 -31.984  -5.465  1.00 54.39           C  
ANISOU 2120  CA  LEU A 346     7513   6969   6182    537  -1305    116       C  
ATOM   2121  C   LEU A 346      41.033 -31.324  -5.886  1.00 56.54           C  
ANISOU 2121  C   LEU A 346     7852   7229   6403    420  -1118      6       C  
ATOM   2122  O   LEU A 346      40.476 -30.513  -5.135  1.00 61.84           O  
ANISOU 2122  O   LEU A 346     8614   7963   6921    322  -1105    -43       O  
ATOM   2123  CB  LEU A 346      43.532 -31.162  -5.949  1.00 44.02           C  
ANISOU 2123  CB  LEU A 346     5970   5738   5018    558  -1398     55       C  
ATOM   2124  CG  LEU A 346      44.213 -30.241  -4.937  1.00 36.09           C  
ANISOU 2124  CG  LEU A 346     4937   4867   3908    484  -1604     40       C  
ATOM   2125  CD1 LEU A 346      44.485 -30.980  -3.634  1.00 39.79           C  
ANISOU 2125  CD1 LEU A 346     5540   5361   4216    515  -1796    191       C  
ATOM   2126  CD2 LEU A 346      45.506 -29.676  -5.509  1.00 27.00           C  
ANISOU 2126  CD2 LEU A 346     3517   3775   2967    514  -1700     16       C  
ATOM   2127  N   VAL A 347      40.536 -31.646  -7.079  1.00 53.86           N  
ANISOU 2127  N   VAL A 347     7473   6804   6189    426   -974    -31       N  
ATOM   2128  CA  VAL A 347      39.271 -31.074  -7.527  1.00 48.22           C  
ANISOU 2128  CA  VAL A 347     6790   6078   5451    316   -823   -102       C  
ATOM   2129  C   VAL A 347      38.142 -31.467  -6.585  1.00 56.88           C  
ANISOU 2129  C   VAL A 347     8060   7147   6405    257   -760    -33       C  
ATOM   2130  O   VAL A 347      37.304 -30.639  -6.206  1.00 57.23           O  
ANISOU 2130  O   VAL A 347     8137   7232   6377    171   -673    -75       O  
ATOM   2131  CB  VAL A 347      38.970 -31.509  -8.969  1.00 40.61           C  
ANISOU 2131  CB  VAL A 347     5778   5028   4624    320   -721   -134       C  
ATOM   2132  CG1 VAL A 347      37.568 -31.084  -9.359  1.00 42.49           C  
ANISOU 2132  CG1 VAL A 347     6042   5255   4848    201   -602   -162       C  
ATOM   2133  CG2 VAL A 347      40.001 -30.918  -9.909  1.00 38.98           C  
ANISOU 2133  CG2 VAL A 347     5409   4860   4541    366   -735   -208       C  
ATOM   2134  N   TYR A 348      38.102 -32.740  -6.196  1.00 58.82           N  
ANISOU 2134  N   TYR A 348     8417   7308   6624    307   -782     84       N  
ATOM   2135  CA  TYR A 348      37.080 -33.203  -5.270  1.00 50.09           C  
ANISOU 2135  CA  TYR A 348     7479   6167   5385    250   -708    173       C  
ATOM   2136  C   TYR A 348      37.359 -32.769  -3.838  1.00 45.70           C  
ANISOU 2136  C   TYR A 348     7041   5704   4620    242   -786    205       C  
ATOM   2137  O   TYR A 348      36.417 -32.585  -3.058  1.00 59.02           O  
ANISOU 2137  O   TYR A 348     8858   7399   6169    169   -672    229       O  
ATOM   2138  CB  TYR A 348      36.955 -34.720  -5.358  1.00 54.34           C  
ANISOU 2138  CB  TYR A 348     8112   6563   5970    297   -700    294       C  
ATOM   2139  CG  TYR A 348      36.587 -35.195  -6.742  1.00 50.03           C  
ANISOU 2139  CG  TYR A 348     7506   5910   5594    275   -622    245       C  
ATOM   2140  CD1 TYR A 348      35.306 -35.003  -7.239  1.00 46.26           C  
ANISOU 2140  CD1 TYR A 348     7020   5408   5150    148   -501    218       C  
ATOM   2141  CD2 TYR A 348      37.519 -35.828  -7.556  1.00 48.16           C  
ANISOU 2141  CD2 TYR A 348     7226   5594   5481    377   -667    229       C  
ATOM   2142  CE1 TYR A 348      34.957 -35.432  -8.501  1.00 48.03           C  
ANISOU 2142  CE1 TYR A 348     7212   5539   5496    100   -463    172       C  
ATOM   2143  CE2 TYR A 348      37.178 -36.262  -8.825  1.00 47.72           C  
ANISOU 2143  CE2 TYR A 348     7164   5431   5537    341   -589    166       C  
ATOM   2144  CZ  TYR A 348      35.894 -36.060  -9.291  1.00 50.82           C  
ANISOU 2144  CZ  TYR A 348     7569   5810   5929    191   -505    135       C  
ATOM   2145  OH  TYR A 348      35.538 -36.485 -10.550  1.00 54.93           O  
ANISOU 2145  OH  TYR A 348     8109   6232   6532    127   -462     73       O  
ATOM   2146  N   ALA A 349      38.633 -32.611  -3.466  1.00 36.68           N  
ANISOU 2146  N   ALA A 349     5858   4631   3447    308   -976    212       N  
ATOM   2147  CA  ALA A 349      38.943 -32.118  -2.129  1.00 35.45           C  
ANISOU 2147  CA  ALA A 349     5835   4573   3060    271  -1088    229       C  
ATOM   2148  C   ALA A 349      38.345 -30.740  -1.896  1.00 48.65           C  
ANISOU 2148  C   ALA A 349     7535   6311   4638    161   -978     83       C  
ATOM   2149  O   ALA A 349      37.982 -30.402  -0.762  1.00 55.63           O  
ANISOU 2149  O   ALA A 349     8613   7234   5288     99   -953     83       O  
ATOM   2150  CB  ALA A 349      40.459 -32.085  -1.916  1.00 26.98           C  
ANISOU 2150  CB  ALA A 349     4664   3575   2013    342  -1346    262       C  
ATOM   2151  N   ASN A 350      38.232 -29.933  -2.951  1.00 51.24           N  
ANISOU 2151  N   ASN A 350     7690   6640   5138    140   -899    -38       N  
ATOM   2152  CA  ASN A 350      37.606 -28.624  -2.812  1.00 47.39           C  
ANISOU 2152  CA  ASN A 350     7219   6183   4603     52   -769   -167       C  
ATOM   2153  C   ASN A 350      36.142 -28.747  -2.408  1.00 54.83           C  
ANISOU 2153  C   ASN A 350     8288   7071   5475      5   -538   -130       C  
ATOM   2154  O   ASN A 350      35.626 -27.914  -1.655  1.00 55.66           O  
ANISOU 2154  O   ASN A 350     8511   7192   5444    -53   -421   -197       O  
ATOM   2155  CB  ASN A 350      37.738 -27.848  -4.123  1.00 33.92           C  
ANISOU 2155  CB  ASN A 350     5297   4474   3118     49   -728   -266       C  
ATOM   2156  CG  ASN A 350      37.177 -26.450  -4.030  1.00 37.30           C  
ANISOU 2156  CG  ASN A 350     5728   4912   3532    -26   -598   -388       C  
ATOM   2157  OD1 ASN A 350      37.811 -25.549  -3.480  1.00 50.54           O  
ANISOU 2157  OD1 ASN A 350     7443   6636   5124    -70   -679   -482       O  
ATOM   2158  ND2 ASN A 350      35.977 -26.258  -4.565  1.00 35.56           N  
ANISOU 2158  ND2 ASN A 350     5465   4637   3410    -46   -401   -381       N  
ATOM   2159  N   SER A 351      35.452 -29.782  -2.900  1.00 57.97           N  
ANISOU 2159  N   SER A 351     8662   7391   5974     25   -456    -26       N  
ATOM   2160  CA  SER A 351      34.050 -29.965  -2.536  1.00 51.97           C  
ANISOU 2160  CA  SER A 351     7982   6578   5186    -28   -235     35       C  
ATOM   2161  C   SER A 351      33.882 -30.221  -1.045  1.00 47.16           C  
ANISOU 2161  C   SER A 351     7622   5984   4312    -45   -194    101       C  
ATOM   2162  O   SER A 351      32.868 -29.827  -0.459  1.00 41.57           O  
ANISOU 2162  O   SER A 351     7005   5260   3531    -94     25    101       O  
ATOM   2163  CB  SER A 351      33.445 -31.117  -3.338  1.00 51.90           C  
ANISOU 2163  CB  SER A 351     7904   6477   5339    -29   -196    140       C  
ATOM   2164  OG  SER A 351      33.573 -30.885  -4.730  1.00 49.36           O  
ANISOU 2164  OG  SER A 351     7392   6142   5220    -27   -233     75       O  
ATOM   2165  N   ALA A 352      34.851 -30.890  -0.420  1.00 52.59           N  
ANISOU 2165  N   ALA A 352     8425   6700   4857     -2   -392    171       N  
ATOM   2166  CA  ALA A 352      34.787 -31.120   1.018  1.00 60.30           C  
ANISOU 2166  CA  ALA A 352     9671   7703   5537    -26   -385    245       C  
ATOM   2167  C   ALA A 352      35.309 -29.932   1.810  1.00 59.89           C  
ANISOU 2167  C   ALA A 352     9677   7743   5336    -73   -436    107       C  
ATOM   2168  O   ALA A 352      34.907 -29.734   2.962  1.00 57.33           O  
ANISOU 2168  O   ALA A 352     9516   7435   4831   -119   -327    109       O  
ATOM   2169  CB  ALA A 352      35.570 -32.381   1.387  1.00 62.75           C  
ANISOU 2169  CB  ALA A 352    10047   7997   5796     41   -586    408       C  
ATOM   2170  N   ALA A 353      36.207 -29.144   1.217  1.00 56.64           N  
ANISOU 2170  N   ALA A 353     9108   7384   5029    -69   -589    -13       N  
ATOM   2171  CA  ALA A 353      36.810 -28.030   1.939  1.00 54.53           C  
ANISOU 2171  CA  ALA A 353     8859   7191   4669   -130   -655   -142       C  
ATOM   2172  C   ALA A 353      35.788 -26.943   2.248  1.00 54.93           C  
ANISOU 2172  C   ALA A 353     9003   7204   4665   -190   -388   -267       C  
ATOM   2173  O   ALA A 353      35.752 -26.415   3.365  1.00 58.77           O  
ANISOU 2173  O   ALA A 353     9642   7712   4976   -243   -342   -321       O  
ATOM   2174  CB  ALA A 353      37.980 -27.458   1.139  1.00 48.84           C  
ANISOU 2174  CB  ALA A 353     7922   6521   4115   -120   -857   -225       C  
ATOM   2175  N   ASN A 354      34.954 -26.586   1.270  1.00 47.44           N  
ANISOU 2175  N   ASN A 354     7967   6191   3868   -180   -204   -311       N  
ATOM   2176  CA  ASN A 354      34.037 -25.459   1.442  1.00 44.40           C  
ANISOU 2176  CA  ASN A 354     7625   5754   3491   -216     64   -425       C  
ATOM   2177  C   ASN A 354      33.142 -25.580   2.666  1.00 47.60           C  
ANISOU 2177  C   ASN A 354     8236   6127   3724   -236    287   -382       C  
ATOM   2178  O   ASN A 354      33.066 -24.612   3.443  1.00 60.31           O  
ANISOU 2178  O   ASN A 354     9948   7724   5244   -273    381   -495       O  
ATOM   2179  CB  ASN A 354      33.196 -25.292   0.172  1.00 45.82           C  
ANISOU 2179  CB  ASN A 354     7604   5872   3933   -187    228   -417       C  
ATOM   2180  CG  ASN A 354      34.025 -24.861  -1.013  1.00 54.78           C  
ANISOU 2180  CG  ASN A 354     8501   7031   5281   -171     48   -480       C  
ATOM   2181  OD1 ASN A 354      34.997 -24.126  -0.860  1.00 61.57           O  
ANISOU 2181  OD1 ASN A 354     9384   7930   6078   -202   -102   -595       O  
ATOM   2182  ND2 ASN A 354      33.646 -25.311  -2.203  1.00 61.59           N  
ANISOU 2182  ND2 ASN A 354     9143   7869   6390   -136     63   -405       N  
ATOM   2183  N   PRO A 355      32.449 -26.693   2.906  1.00 42.44           N  
ANISOU 2183  N   PRO A 355     7653   5447   3025   -218    391   -224       N  
ATOM   2184  CA  PRO A 355      31.662 -26.795   4.144  1.00 48.05           C  
ANISOU 2184  CA  PRO A 355     8555   6129   3574   -240    606   -181       C  
ATOM   2185  C   PRO A 355      32.502 -26.636   5.393  1.00 52.56           C  
ANISOU 2185  C   PRO A 355     9306   6764   3900   -278    440   -224       C  
ATOM   2186  O   PRO A 355      32.020 -26.102   6.402  1.00 53.01           O  
ANISOU 2186  O   PRO A 355     9533   6795   3812   -310    617   -279       O  
ATOM   2187  CB  PRO A 355      31.033 -28.195   4.053  1.00 53.19           C  
ANISOU 2187  CB  PRO A 355     9216   6746   4247   -222    676     21       C  
ATOM   2188  CG  PRO A 355      31.113 -28.564   2.611  1.00 50.33           C  
ANISOU 2188  CG  PRO A 355     8664   6366   4092   -196    592     59       C  
ATOM   2189  CD  PRO A 355      32.328 -27.893   2.064  1.00 46.98           C  
ANISOU 2189  CD  PRO A 355     8145   6002   3703   -183    328    -77       C  
ATOM   2190  N   ILE A 356      33.751 -27.100   5.360  1.00 54.84           N  
ANISOU 2190  N   ILE A 356     9558   7133   4146   -274    108   -190       N  
ATOM   2191  CA  ILE A 356      34.634 -26.898   6.503  1.00 51.92           C  
ANISOU 2191  CA  ILE A 356     9334   6840   3555   -321    -77   -223       C  
ATOM   2192  C   ILE A 356      34.944 -25.421   6.687  1.00 57.52           C  
ANISOU 2192  C   ILE A 356    10058   7552   4246   -380    -69   -425       C  
ATOM   2193  O   ILE A 356      35.043 -24.931   7.819  1.00 63.88           O  
ANISOU 2193  O   ILE A 356    11063   8372   4836   -440    -54   -491       O  
ATOM   2194  CB  ILE A 356      35.918 -27.723   6.334  1.00 48.18           C  
ANISOU 2194  CB  ILE A 356     8762   6448   3096   -292   -428   -119       C  
ATOM   2195  CG1 ILE A 356      35.564 -29.203   6.195  1.00 53.31           C  
ANISOU 2195  CG1 ILE A 356     9422   7063   3772   -230   -417     87       C  
ATOM   2196  CG2 ILE A 356      36.844 -27.500   7.515  1.00 46.98           C  
ANISOU 2196  CG2 ILE A 356     8743   6388   2720   -351   -635   -137       C  
ATOM   2197  CD1 ILE A 356      36.693 -30.040   5.669  1.00 53.00           C  
ANISOU 2197  CD1 ILE A 356     9232   7062   3844   -166   -712    196       C  
ATOM   2198  N   ILE A 357      35.114 -24.689   5.583  1.00 54.64           N  
ANISOU 2198  N   ILE A 357     9494   7166   4100   -367    -79   -525       N  
ATOM   2199  CA  ILE A 357      35.391 -23.260   5.682  1.00 57.03           C  
ANISOU 2199  CA  ILE A 357     9802   7448   4416   -422    -60   -712       C  
ATOM   2200  C   ILE A 357      34.220 -22.526   6.321  1.00 62.91           C  
ANISOU 2200  C   ILE A 357    10721   8092   5092   -436    281   -789       C  
ATOM   2201  O   ILE A 357      34.413 -21.603   7.123  1.00 66.84           O  
ANISOU 2201  O   ILE A 357    11372   8569   5457   -498    303   -916       O  
ATOM   2202  CB  ILE A 357      35.733 -22.681   4.298  1.00 50.76           C  
ANISOU 2202  CB  ILE A 357     8754   6641   3892   -400   -117   -782       C  
ATOM   2203  CG1 ILE A 357      37.047 -23.267   3.785  1.00 48.87           C  
ANISOU 2203  CG1 ILE A 357     8344   6499   3724   -390   -452   -721       C  
ATOM   2204  CG2 ILE A 357      35.809 -21.168   4.374  1.00 52.45           C  
ANISOU 2204  CG2 ILE A 357     8984   6799   4144   -452    -41   -965       C  
ATOM   2205  CD1 ILE A 357      37.248 -23.106   2.301  1.00 41.22           C  
ANISOU 2205  CD1 ILE A 357     7126   5515   3022   -350   -485   -740       C  
ATOM   2206  N   TYR A 358      32.990 -22.908   5.968  1.00 59.80           N  
ANISOU 2206  N   TYR A 358    10298   7624   4800   -379    560   -710       N  
ATOM   2207  CA  TYR A 358      31.825 -22.262   6.565  1.00 58.16           C  
ANISOU 2207  CA  TYR A 358    10219   7311   4569   -374    915   -759       C  
ATOM   2208  C   TYR A 358      31.766 -22.506   8.067  1.00 64.23           C  
ANISOU 2208  C   TYR A 358    11276   8093   5036   -421    955   -746       C  
ATOM   2209  O   TYR A 358      31.336 -21.635   8.831  1.00 69.15           O  
ANISOU 2209  O   TYR A 358    12068   8641   5566   -448   1153   -853       O  
ATOM   2210  CB  TYR A 358      30.537 -22.762   5.910  1.00 55.66           C  
ANISOU 2210  CB  TYR A 358     9774   6926   4450   -306   1195   -642       C  
ATOM   2211  CG  TYR A 358      30.510 -22.713   4.399  1.00 59.69           C  
ANISOU 2211  CG  TYR A 358    10014   7429   5235   -265   1158   -628       C  
ATOM   2212  CD1 TYR A 358      31.084 -21.660   3.701  1.00 61.45           C  
ANISOU 2212  CD1 TYR A 358    10120   7641   5588   -272   1063   -762       C  
ATOM   2213  CD2 TYR A 358      29.887 -23.719   3.672  1.00 61.72           C  
ANISOU 2213  CD2 TYR A 358    10143   7687   5621   -228   1226   -475       C  
ATOM   2214  CE1 TYR A 358      31.046 -21.614   2.315  1.00 54.73           C  
ANISOU 2214  CE1 TYR A 358     9036   6783   4976   -237   1037   -748       C  
ATOM   2215  CE2 TYR A 358      29.844 -23.684   2.291  1.00 62.35           C  
ANISOU 2215  CE2 TYR A 358    10000   7762   5929   -202   1197   -463       C  
ATOM   2216  CZ  TYR A 358      30.424 -22.631   1.616  1.00 58.98           C  
ANISOU 2216  CZ  TYR A 358     9466   7329   5616   -203   1103   -602       C  
ATOM   2217  OH  TYR A 358      30.382 -22.594   0.239  1.00 62.31           O  
ANISOU 2217  OH  TYR A 358     9632   7747   6294   -177   1052   -577       O  
ATOM   2218  N   ASN A 359      32.195 -23.691   8.507  1.00 65.25           N  
ANISOU 2218  N   ASN A 359    11474   8308   5011   -429    774   -610       N  
ATOM   2219  CA  ASN A 359      32.105 -24.040   9.920  1.00 70.54           C  
ANISOU 2219  CA  ASN A 359    12423   8996   5382   -472    812   -572       C  
ATOM   2220  C   ASN A 359      32.987 -23.143  10.779  1.00 77.03           C  
ANISOU 2220  C   ASN A 359    13425   9855   5990   -559    648   -723       C  
ATOM   2221  O   ASN A 359      32.628 -22.813  11.916  1.00 83.42           O  
ANISOU 2221  O   ASN A 359    14500  10628   6569   -606    797   -775       O  
ATOM   2222  CB  ASN A 359      32.484 -25.509  10.111  1.00 67.73           C  
ANISOU 2222  CB  ASN A 359    12078   8723   4932   -456    620   -377       C  
ATOM   2223  CG  ASN A 359      32.480 -25.927  11.564  1.00 70.75           C  
ANISOU 2223  CG  ASN A 359    12752   9138   4992   -503    628   -320       C  
ATOM   2224  OD1 ASN A 359      31.422 -26.075  12.173  1.00 76.35           O  
ANISOU 2224  OD1 ASN A 359    13605   9780   5625   -497    932   -280       O  
ATOM   2225  ND2 ASN A 359      33.667 -26.128  12.128  1.00 69.27           N  
ANISOU 2225  ND2 ASN A 359    12644   9056   4618   -551    295   -305       N  
ATOM   2226  N   PHE A 360      34.145 -22.740  10.260  1.00 72.26           N  
ANISOU 2226  N   PHE A 360    12682   9318   5457   -589    346   -794       N  
ATOM   2227  CA  PHE A 360      35.085 -21.946  11.042  1.00 75.99           C  
ANISOU 2227  CA  PHE A 360    13303   9832   5738   -689    151   -926       C  
ATOM   2228  C   PHE A 360      34.965 -20.445  10.810  1.00 79.20           C  
ANISOU 2228  C   PHE A 360    13709  10140   6242   -725    282  -1131       C  
ATOM   2229  O   PHE A 360      35.204 -19.666  11.739  1.00 81.65           O  
ANISOU 2229  O   PHE A 360    14250  10426   6348   -814    280  -1260       O  
ATOM   2230  CB  PHE A 360      36.522 -22.391  10.744  1.00 72.83           C  
ANISOU 2230  CB  PHE A 360    12745   9567   5361   -711   -271   -870       C  
ATOM   2231  CG  PHE A 360      36.816 -23.803  11.170  1.00 77.36           C  
ANISOU 2231  CG  PHE A 360    13351  10231   5809   -681   -436   -665       C  
ATOM   2232  CD1 PHE A 360      36.916 -24.821  10.235  1.00 82.97           C  
ANISOU 2232  CD1 PHE A 360    13836  10967   6719   -592   -519   -512       C  
ATOM   2233  CD2 PHE A 360      36.979 -24.114  12.509  1.00 81.45           C  
ANISOU 2233  CD2 PHE A 360    14142  10799   6006   -742   -503   -621       C  
ATOM   2234  CE1 PHE A 360      37.187 -26.121  10.629  1.00 81.31           C  
ANISOU 2234  CE1 PHE A 360    13661  10820   6412   -556   -662   -315       C  
ATOM   2235  CE2 PHE A 360      37.249 -25.410  12.909  1.00 84.65           C  
ANISOU 2235  CE2 PHE A 360    14578  11281   6304   -708   -654   -417       C  
ATOM   2236  CZ  PHE A 360      37.353 -26.415  11.970  1.00 81.36           C  
ANISOU 2236  CZ  PHE A 360    13925  10878   6110   -611   -730   -260       C  
ATOM   2237  N   LEU A 361      34.601 -20.016   9.603  1.00 73.19           N  
ANISOU 2237  N   LEU A 361    12711   9315   5783   -662    396  -1161       N  
ATOM   2238  CA  LEU A 361      34.518 -18.600   9.275  1.00 64.61           C  
ANISOU 2238  CA  LEU A 361    11599   8124   4825   -685    514  -1336       C  
ATOM   2239  C   LEU A 361      33.086 -18.080   9.237  1.00 70.21           C  
ANISOU 2239  C   LEU A 361    12358   8678   5641   -621    943  -1362       C  
ATOM   2240  O   LEU A 361      32.866 -16.933   8.835  1.00 76.77           O  
ANISOU 2240  O   LEU A 361    13141   9400   6629   -616   1080  -1481       O  
ATOM   2241  CB  LEU A 361      35.215 -18.328   7.940  1.00 50.81           C  
ANISOU 2241  CB  LEU A 361     9547   6407   3353   -664    328  -1355       C  
ATOM   2242  CG  LEU A 361      36.742 -18.419   7.987  1.00 46.99           C  
ANISOU 2242  CG  LEU A 361     8992   6050   2814   -739    -75  -1372       C  
ATOM   2243  CD1 LEU A 361      37.334 -18.640   6.597  1.00 48.20           C  
ANISOU 2243  CD1 LEU A 361     8817   6252   3246   -691   -240  -1324       C  
ATOM   2244  CD2 LEU A 361      37.328 -17.169   8.628  1.00 49.94           C  
ANISOU 2244  CD2 LEU A 361     9512   6381   3080   -852   -142  -1555       C  
ATOM   2245  N   SER A 362      32.112 -18.891   9.641  1.00 66.58           N  
ANISOU 2245  N   SER A 362    11976   8199   5121   -569   1163  -1240       N  
ATOM   2246  CA  SER A 362      30.720 -18.455   9.717  1.00 66.10           C  
ANISOU 2246  CA  SER A 362    11947   7992   5177   -504   1587  -1242       C  
ATOM   2247  C   SER A 362      30.116 -19.019  10.994  1.00 70.08           C  
ANISOU 2247  C   SER A 362    12723   8483   5421   -519   1765  -1185       C  
ATOM   2248  O   SER A 362      29.931 -20.234  11.111  1.00 73.62           O  
ANISOU 2248  O   SER A 362    13159   9006   5809   -497   1729  -1027       O  
ATOM   2249  CB  SER A 362      29.927 -18.907   8.489  1.00 63.31           C  
ANISOU 2249  CB  SER A 362    11296   7614   5145   -403   1723  -1117       C  
ATOM   2250  OG  SER A 362      28.533 -18.903   8.748  1.00 62.34           O  
ANISOU 2250  OG  SER A 362    11190   7379   5118   -336   2116  -1053       O  
ATOM   2251  N   GLY A 363      29.810 -18.139  11.949  1.00 71.16           N  
ANISOU 2251  N   GLY A 363    13118   8517   5403   -559   1966  -1312       N  
ATOM   2252  CA  GLY A 363      29.192 -18.593  13.181  1.00 74.40           C  
ANISOU 2252  CA  GLY A 363    13807   8902   5558   -573   2169  -1267       C  
ATOM   2253  C   GLY A 363      27.773 -19.082  12.996  1.00 77.05           C  
ANISOU 2253  C   GLY A 363    14036   9154   6084   -469   2544  -1131       C  
ATOM   2254  O   GLY A 363      27.292 -19.880  13.807  1.00 80.43           O  
ANISOU 2254  O   GLY A 363    14622   9599   6339   -470   2669  -1030       O  
ATOM   2255  N   LYS A 364      27.089 -18.614  11.950  1.00 77.65           N  
ANISOU 2255  N   LYS A 364    13836   9142   6524   -382   2722  -1115       N  
ATOM   2256  CA  LYS A 364      25.739 -19.097  11.686  1.00 81.14           C  
ANISOU 2256  CA  LYS A 364    14119   9512   7197   -284   3054   -965       C  
ATOM   2257  C   LYS A 364      25.764 -20.514  11.129  1.00 80.43           C  
ANISOU 2257  C   LYS A 364    13850   9546   7164   -268   2894   -778       C  
ATOM   2258  O   LYS A 364      24.951 -21.357  11.528  1.00 83.78           O  
ANISOU 2258  O   LYS A 364    14290   9963   7580   -241   3083   -637       O  
ATOM   2259  CB  LYS A 364      25.021 -18.142  10.732  1.00 79.91           C  
ANISOU 2259  CB  LYS A 364    13706   9227   7428   -196   3268   -987       C  
ATOM   2260  CG  LYS A 364      24.499 -16.871  11.399  1.00 85.44           C  
ANISOU 2260  CG  LYS A 364    14584   9750   8128   -180   3576  -1120       C  
ATOM   2261  CD  LYS A 364      24.451 -15.718  10.411  1.00 90.32           C  
ANISOU 2261  CD  LYS A 364    14988  10270   9061   -130   3611  -1188       C  
ATOM   2262  CE  LYS A 364      23.942 -14.442  11.055  1.00 92.73           C  
ANISOU 2262  CE  LYS A 364    15476  10379   9380   -109   3927  -1313       C  
ATOM   2263  NZ  LYS A 364      22.467 -14.459  11.245  1.00 90.42           N  
ANISOU 2263  NZ  LYS A 364    15097   9948   9310      4   4355  -1193       N  
ATOM   2264  N   PHE A 365      26.688 -20.798  10.205  1.00 74.03           N  
ANISOU 2264  N   PHE A 365    12870   8840   6417   -286   2557   -771       N  
ATOM   2265  CA  PHE A 365      26.851 -22.170   9.734  1.00 68.15           C  
ANISOU 2265  CA  PHE A 365    12000   8203   5691   -281   2382   -601       C  
ATOM   2266  C   PHE A 365      27.393 -23.064  10.840  1.00 66.02           C  
ANISOU 2266  C   PHE A 365    11990   8022   5074   -342   2226   -542       C  
ATOM   2267  O   PHE A 365      26.950 -24.210  10.993  1.00 70.06           O  
ANISOU 2267  O   PHE A 365    12492   8562   5566   -329   2275   -373       O  
ATOM   2268  CB  PHE A 365      27.775 -22.206   8.518  1.00 73.17           C  
ANISOU 2268  CB  PHE A 365    12420   8916   6464   -283   2066   -619       C  
ATOM   2269  CG  PHE A 365      27.069 -21.978   7.209  1.00 73.73           C  
ANISOU 2269  CG  PHE A 365    12180   8932   6903   -214   2203   -574       C  
ATOM   2270  CD1 PHE A 365      26.218 -22.939   6.684  1.00 73.00           C  
ANISOU 2270  CD1 PHE A 365    11913   8839   6985   -176   2325   -396       C  
ATOM   2271  CD2 PHE A 365      27.267 -20.807   6.497  1.00 67.58           C  
ANISOU 2271  CD2 PHE A 365    11276   8101   6301   -197   2198   -699       C  
ATOM   2272  CE1 PHE A 365      25.574 -22.728   5.476  1.00 66.63           C  
ANISOU 2272  CE1 PHE A 365    10805   7991   6520   -124   2431   -341       C  
ATOM   2273  CE2 PHE A 365      26.628 -20.592   5.292  1.00 60.16           C  
ANISOU 2273  CE2 PHE A 365    10045   7116   5699   -133   2310   -641       C  
ATOM   2274  CZ  PHE A 365      25.781 -21.552   4.780  1.00 62.32           C  
ANISOU 2274  CZ  PHE A 365    10138   7400   6140    -98   2421   -462       C  
ATOM   2275  N   ARG A 366      28.350 -22.559  11.623  1.00 67.09           N  
ANISOU 2275  N   ARG A 366    12352   8200   4938   -416   2031   -669       N  
ATOM   2276  CA  ARG A 366      28.835 -23.318  12.770  1.00 70.63           C  
ANISOU 2276  CA  ARG A 366    13061   8732   5045   -476   1889   -607       C  
ATOM   2277  C   ARG A 366      27.680 -23.686  13.690  1.00 74.22           C  
ANISOU 2277  C   ARG A 366    13690   9114   5397   -459   2247   -527       C  
ATOM   2278  O   ARG A 366      27.570 -24.832  14.140  1.00 74.37           O  
ANISOU 2278  O   ARG A 366    13781   9189   5289   -464   2219   -366       O  
ATOM   2279  CB  ARG A 366      29.906 -22.528  13.527  1.00 77.05           C  
ANISOU 2279  CB  ARG A 366    14094   9587   5594   -568   1663   -769       C  
ATOM   2280  CG  ARG A 366      30.527 -23.308  14.679  1.00 87.55           C  
ANISOU 2280  CG  ARG A 366    15680  11021   6564   -636   1464   -692       C  
ATOM   2281  CD  ARG A 366      31.385 -22.447  15.600  1.00 96.73           C  
ANISOU 2281  CD  ARG A 366    17101  12210   7441   -744   1296   -857       C  
ATOM   2282  NE  ARG A 366      32.686 -22.111  15.025  1.00100.60           N  
ANISOU 2282  NE  ARG A 366    17437  12790   7997   -786    905   -923       N  
ATOM   2283  CZ  ARG A 366      32.997 -20.939  14.483  1.00106.02           C  
ANISOU 2283  CZ  ARG A 366    18030  13424   8831   -809    883  -1095       C  
ATOM   2284  NH1 ARG A 366      32.101 -19.964  14.430  1.00106.43           N  
ANISOU 2284  NH1 ARG A 366    18129  13325   8985   -786   1228  -1216       N  
ATOM   2285  NH2 ARG A 366      34.214 -20.742  13.993  1.00107.05           N  
ANISOU 2285  NH2 ARG A 366    18007  13645   9023   -851    522  -1134       N  
ATOM   2286  N   GLU A 367      26.812 -22.718  13.979  1.00 79.72           N  
ANISOU 2286  N   GLU A 367    14453   9678   6161   -434   2596   -630       N  
ATOM   2287  CA  GLU A 367      25.665 -22.969  14.837  1.00 83.27           C  
ANISOU 2287  CA  GLU A 367    15052  10044   6544   -409   2975   -560       C  
ATOM   2288  C   GLU A 367      24.724 -24.007  14.240  1.00 73.08           C  
ANISOU 2288  C   GLU A 367    13513   8748   5506   -342   3133   -352       C  
ATOM   2289  O   GLU A 367      24.136 -24.811  14.975  1.00 70.54           O  
ANISOU 2289  O   GLU A 367    13308   8426   5067   -345   3298   -223       O  
ATOM   2290  CB  GLU A 367      24.924 -21.647  15.047  1.00 90.96           C  
ANISOU 2290  CB  GLU A 367    16085  10855   7621   -375   3322   -708       C  
ATOM   2291  CG  GLU A 367      23.709 -21.680  15.955  1.00101.76           C  
ANISOU 2291  CG  GLU A 367    17610  12109   8944   -339   3762   -661       C  
ATOM   2292  CD  GLU A 367      23.068 -20.310  16.078  1.00109.73           C  
ANISOU 2292  CD  GLU A 367    18666  12940  10087   -294   4090   -809       C  
ATOM   2293  OE1 GLU A 367      21.923 -20.121  15.599  1.00111.26           O  
ANISOU 2293  OE1 GLU A 367    18629  13020  10623   -192   4412   -734       O  
ATOM   2294  OE2 GLU A 367      23.733 -19.413  16.622  1.00112.83           O  
ANISOU 2294  OE2 GLU A 367    19311  13302  10258   -361   4012   -993       O  
ATOM   2295  N   GLN A 368      24.576 -24.014  12.916  1.00 70.76           N  
ANISOU 2295  N   GLN A 368    12878   8451   5555   -290   3081   -312       N  
ATOM   2296  CA  GLN A 368      23.715 -24.996  12.264  1.00 72.51           C  
ANISOU 2296  CA  GLN A 368    12845   8670   6035   -245   3200   -114       C  
ATOM   2297  C   GLN A 368      24.363 -26.375  12.204  1.00 75.05           C  
ANISOU 2297  C   GLN A 368    13182   9108   6227   -286   2914     35       C  
ATOM   2298  O   GLN A 368      23.679 -27.397  12.337  1.00 73.23           O  
ANISOU 2298  O   GLN A 368    12902   8873   6050   -284   3037    214       O  
ATOM   2299  CB  GLN A 368      23.354 -24.513  10.859  1.00 73.89           C  
ANISOU 2299  CB  GLN A 368    12662   8803   6609   -186   3227   -119       C  
ATOM   2300  CG  GLN A 368      22.347 -23.365  10.853  1.00 75.19           C  
ANISOU 2300  CG  GLN A 368    12741   8826   7000   -117   3580   -189       C  
ATOM   2301  CD  GLN A 368      20.985 -23.760  11.386  1.00 70.77           C  
ANISOU 2301  CD  GLN A 368    12141   8187   6560    -75   3953    -53       C  
ATOM   2302  OE1 GLN A 368      20.357 -24.697  10.892  1.00 76.52           O  
ANISOU 2302  OE1 GLN A 368    12641   8942   7489    -67   3988    128       O  
ATOM   2303  NE2 GLN A 368      20.516 -23.036  12.395  1.00 64.55           N  
ANISOU 2303  NE2 GLN A 368    11573   7296   5659    -56   4237   -139       N  
ATOM   2304  N   PHE A 369      25.682 -26.418  12.004  1.00 75.29           N  
ANISOU 2304  N   PHE A 369    13266   9233   6109   -323   2530    -26       N  
ATOM   2305  CA  PHE A 369      26.392 -27.691  12.022  1.00 71.46           C  
ANISOU 2305  CA  PHE A 369    12809   8843   5500   -350   2244    120       C  
ATOM   2306  C   PHE A 369      26.429 -28.284  13.419  1.00 79.28           C  
ANISOU 2306  C   PHE A 369    14100   9864   6158   -392   2271    196       C  
ATOM   2307  O   PHE A 369      26.540 -29.506  13.570  1.00 80.88           O  
ANISOU 2307  O   PHE A 369    14320  10108   6302   -400   2166    376       O  
ATOM   2308  CB  PHE A 369      27.810 -27.515  11.482  1.00 69.42           C  
ANISOU 2308  CB  PHE A 369    12507   8674   5196   -367   1832     40       C  
ATOM   2309  CG  PHE A 369      27.870 -26.997  10.076  1.00 65.47           C  
ANISOU 2309  CG  PHE A 369    11724   8153   4998   -330   1785    -26       C  
ATOM   2310  CD1 PHE A 369      26.881 -27.315   9.158  1.00 63.96           C  
ANISOU 2310  CD1 PHE A 369    11296   7901   5105   -288   1985     71       C  
ATOM   2311  CD2 PHE A 369      28.917 -26.190   9.670  1.00 57.81           C  
ANISOU 2311  CD2 PHE A 369    10717   7228   4020   -345   1535   -177       C  
ATOM   2312  CE1 PHE A 369      26.939 -26.835   7.859  1.00 53.37           C  
ANISOU 2312  CE1 PHE A 369     9707   6546   4024   -260   1938     18       C  
ATOM   2313  CE2 PHE A 369      28.981 -25.708   8.377  1.00 53.43           C  
ANISOU 2313  CE2 PHE A 369     9914   6656   3731   -313   1498   -233       C  
ATOM   2314  CZ  PHE A 369      27.993 -26.030   7.470  1.00 49.18           C  
ANISOU 2314  CZ  PHE A 369     9163   6059   3463   -268   1700   -137       C  
ATOM   2315  N   LYS A 370      26.342 -27.437  14.443  1.00 87.10           N  
ANISOU 2315  N   LYS A 370    15341  10826   6926   -422   2413     65       N  
ATOM   2316  CA  LYS A 370      26.258 -27.932  15.811  1.00 86.22           C  
ANISOU 2316  CA  LYS A 370    15541  10738   6481   -466   2484    135       C  
ATOM   2317  C   LYS A 370      24.958 -28.695  16.030  1.00 84.74           C  
ANISOU 2317  C   LYS A 370    15311  10482   6402   -436   2834    304       C  
ATOM   2318  O   LYS A 370      24.961 -29.813  16.559  1.00 81.64           O  
ANISOU 2318  O   LYS A 370    15017  10134   5868   -458   2789    480       O  
ATOM   2319  CB  LYS A 370      26.345 -26.757  16.784  1.00 90.96           C  
ANISOU 2319  CB  LYS A 370    16426  11300   6835   -509   2600    -61       C  
ATOM   2320  CG  LYS A 370      27.718 -26.460  17.348  1.00 97.64           C  
ANISOU 2320  CG  LYS A 370    17477  12249   7372   -589   2223   -159       C  
ATOM   2321  CD  LYS A 370      27.591 -25.426  18.459  1.00104.57           C  
ANISOU 2321  CD  LYS A 370    18686  13066   7977   -648   2399   -334       C  
ATOM   2322  CE  LYS A 370      28.858 -24.604  18.630  1.00105.17           C  
ANISOU 2322  CE  LYS A 370    18872  13207   7881   -730   2059   -504       C  
ATOM   2323  NZ  LYS A 370      28.630 -23.432  19.524  1.00110.98           N  
ANISOU 2323  NZ  LYS A 370    19912  13848   8408   -789   2269   -703       N  
ATOM   2324  N   ALA A 371      23.834 -28.103  15.618  1.00 86.10           N  
ANISOU 2324  N   ALA A 371    15317  10545   6852   -385   3184    267       N  
ATOM   2325  CA  ALA A 371      22.537 -28.733  15.834  1.00 92.45           C  
ANISOU 2325  CA  ALA A 371    16045  11282   7801   -360   3536    427       C  
ATOM   2326  C   ALA A 371      22.378 -30.014  15.021  1.00 99.98           C  
ANISOU 2326  C   ALA A 371    16748  12270   8971   -361   3418    638       C  
ATOM   2327  O   ALA A 371      21.784 -30.985  15.505  1.00107.05           O  
ANISOU 2327  O   ALA A 371    17678  13157   9841   -381   3555    816       O  
ATOM   2328  CB  ALA A 371      21.414 -27.749  15.504  1.00 90.98           C  
ANISOU 2328  CB  ALA A 371    15688  10969   7909   -294   3909    348       C  
ATOM   2329  N   ALA A 372      22.888 -30.044  13.785  1.00 97.50           N  
ANISOU 2329  N   ALA A 372    16188  11984   8873   -346   3172    624       N  
ATOM   2330  CA  ALA A 372      22.717 -31.250  12.978  1.00 90.89           C  
ANISOU 2330  CA  ALA A 372    15130  11158   8248   -357   3068    817       C  
ATOM   2331  C   ALA A 372      23.465 -32.436  13.569  1.00 91.79           C  
ANISOU 2331  C   ALA A 372    15433  11335   8108   -397   2828    958       C  
ATOM   2332  O   ALA A 372      23.039 -33.585  13.402  1.00 89.76           O  
ANISOU 2332  O   ALA A 372    15084  11054   7966   -419   2852   1154       O  
ATOM   2333  CB  ALA A 372      23.181 -30.992  11.541  1.00 81.06           C  
ANISOU 2333  CB  ALA A 372    13619   9926   7255   -335   2853    761       C  
ATOM   2334  N   PHE A 373      24.580 -32.177  14.248  1.00 97.20           N  
ANISOU 2334  N   PHE A 373    16367  12096   8469   -411   2585    870       N  
ATOM   2335  CA  PHE A 373      25.378 -33.222  14.878  1.00101.71           C  
ANISOU 2335  CA  PHE A 373    17116  12735   8794   -437   2332   1012       C  
ATOM   2336  C   PHE A 373      24.850 -33.653  16.239  1.00115.53           C  
ANISOU 2336  C   PHE A 373    19132  14482  10284   -472   2542   1116       C  
ATOM   2337  O   PHE A 373      25.219 -34.730  16.719  1.00121.72           O  
ANISOU 2337  O   PHE A 373    20027  15302  10921   -491   2396   1295       O  
ATOM   2338  CB  PHE A 373      26.839 -32.779  14.958  1.00 98.08           C  
ANISOU 2338  CB  PHE A 373    16760  12372   8135   -440   1946    894       C  
ATOM   2339  CG  PHE A 373      27.619 -33.102  13.718  1.00 93.05           C  
ANISOU 2339  CG  PHE A 373    15885  11755   7715   -406   1644    910       C  
ATOM   2340  CD1 PHE A 373      27.789 -34.424  13.331  1.00 90.13           C  
ANISOU 2340  CD1 PHE A 373    15428  11369   7447   -389   1504   1114       C  
ATOM   2341  CD2 PHE A 373      28.136 -32.100  12.914  1.00 81.44           C  
ANISOU 2341  CD2 PHE A 373    14281  10302   6362   -389   1521    726       C  
ATOM   2342  CE1 PHE A 373      28.495 -34.745  12.187  1.00 74.13           C  
ANISOU 2342  CE1 PHE A 373    13202   9343   5623   -351   1247   1127       C  
ATOM   2343  CE2 PHE A 373      28.841 -32.414  11.764  1.00 68.03           C  
ANISOU 2343  CE2 PHE A 373    12372   8617   4858   -355   1262    744       C  
ATOM   2344  CZ  PHE A 373      29.020 -33.738  11.401  1.00 64.96           C  
ANISOU 2344  CZ  PHE A 373    11913   8210   4560   -333   1128    940       C  
ATOM   2345  N   SER A 374      23.991 -32.851  16.865  1.00122.39           N  
ANISOU 2345  N   SER A 374    20106  15299  11099   -475   2889   1018       N  
ATOM   2346  CA  SER A 374      23.393 -33.274  18.125  1.00127.14           C  
ANISOU 2346  CA  SER A 374    20960  15888  11461   -508   3132   1123       C  
ATOM   2347  C   SER A 374      22.234 -34.228  17.874  1.00130.89           C  
ANISOU 2347  C   SER A 374    21248  16291  12193   -509   3391   1330       C  
ATOM   2348  O   SER A 374      22.046 -35.198  18.616  1.00136.23           O  
ANISOU 2348  O   SER A 374    22068  16977  12718   -544   3441   1515       O  
ATOM   2349  CB  SER A 374      22.925 -32.054  18.919  1.00126.30           C  
ANISOU 2349  CB  SER A 374    21055  15734  11197   -507   3423    936       C  
ATOM   2350  OG  SER A 374      24.021 -31.318  19.431  1.00123.92           O  
ANISOU 2350  OG  SER A 374    20994  15501  10588   -540   3173    769       O  
ATOM   2351  N   TRP A 375      21.448 -33.951  16.834  1.00121.31           N  
ANISOU 2351  N   TRP A 375    19707  15008  11376   -478   3550   1310       N  
ATOM   2352  CA  TRP A 375      20.326 -34.805  16.469  1.00120.71           C  
ANISOU 2352  CA  TRP A 375    19399  14866  11600   -497   3769   1503       C  
ATOM   2353  C   TRP A 375      20.783 -36.221  16.142  1.00125.61           C  
ANISOU 2353  C   TRP A 375    19971  15504  12250   -539   3509   1709       C  
ATOM   2354  O   TRP A 375      20.039 -37.184  16.360  1.00135.18           O  
ANISOU 2354  O   TRP A 375    21133  16670  13559   -585   3662   1906       O  
ATOM   2355  CB  TRP A 375      19.594 -34.186  15.282  1.00116.19           C  
ANISOU 2355  CB  TRP A 375    18458  14236  11454   -462   3896   1437       C  
ATOM   2356  CG  TRP A 375      18.520 -35.035  14.705  1.00116.48           C  
ANISOU 2356  CG  TRP A 375    18196  14214  11848   -500   4047   1630       C  
ATOM   2357  CD1 TRP A 375      18.612 -35.830  13.602  1.00116.35           C  
ANISOU 2357  CD1 TRP A 375    17927  14188  12091   -540   3837   1739       C  
ATOM   2358  CD2 TRP A 375      17.173 -35.148  15.173  1.00119.41           C  
ANISOU 2358  CD2 TRP A 375    18476  14520  12373   -512   4437   1735       C  
ATOM   2359  NE1 TRP A 375      17.409 -36.446  13.362  1.00120.12           N  
ANISOU 2359  NE1 TRP A 375    18164  14605  12873   -594   4048   1904       N  
ATOM   2360  CE2 TRP A 375      16.508 -36.043  14.312  1.00123.19           C  
ANISOU 2360  CE2 TRP A 375    18631  14964  13211   -574   4417   1910       C  
ATOM   2361  CE3 TRP A 375      16.465 -34.586  16.240  1.00120.08           C  
ANISOU 2361  CE3 TRP A 375    18727  14567  12332   -480   4803   1698       C  
ATOM   2362  CZ2 TRP A 375      15.171 -36.390  14.485  1.00125.12           C  
ANISOU 2362  CZ2 TRP A 375    18688  15148  13702   -610   4731   2055       C  
ATOM   2363  CZ3 TRP A 375      15.137 -34.932  16.409  1.00123.20           C  
ANISOU 2363  CZ3 TRP A 375    18942  14896  12974   -497   5141   1844       C  
ATOM   2364  CH2 TRP A 375      14.504 -35.825  15.536  1.00124.11           C  
ANISOU 2364  CH2 TRP A 375    18710  14990  13457   -564   5095   2024       C  
ATOM   2365  N   TRP A 376      22.004 -36.358  15.629  1.00120.48           N  
ANISOU 2365  N   TRP A 376    19333  14910  11535   -523   3121   1668       N  
ATOM   2366  CA  TRP A 376      22.559 -37.639  15.205  1.00117.98           C  
ANISOU 2366  CA  TRP A 376    18963  14587  11278   -543   2851   1848       C  
ATOM   2367  C   TRP A 376      23.167 -38.432  16.353  1.00119.86           C  
ANISOU 2367  C   TRP A 376    19499  14871  11172   -559   2724   1989       C  
ATOM   2368  O   TRP A 376      23.103 -39.667  16.342  1.00120.23           O  
ANISOU 2368  O   TRP A 376    19523  14871  11286   -586   2664   2204       O  
ATOM   2369  CB  TRP A 376      23.590 -37.403  14.105  1.00116.76           C  
ANISOU 2369  CB  TRP A 376    18671  14459  11232   -502   2508   1745       C  
ATOM   2370  CG  TRP A 376      24.582 -38.504  13.929  1.00122.56           C  
ANISOU 2370  CG  TRP A 376    19444  15199  11923   -491   2170   1885       C  
ATOM   2371  CD1 TRP A 376      24.377 -39.733  13.377  1.00123.57           C  
ANISOU 2371  CD1 TRP A 376    19445  15239  12267   -514   2117   2073       C  
ATOM   2372  CD2 TRP A 376      25.970 -38.440  14.267  1.00125.39           C  
ANISOU 2372  CD2 TRP A 376    19961  15646  12035   -450   1828   1846       C  
ATOM   2373  NE1 TRP A 376      25.551 -40.454  13.382  1.00124.61           N  
ANISOU 2373  NE1 TRP A 376    19660  15386  12299   -472   1783   2156       N  
ATOM   2374  CE2 TRP A 376      26.545 -39.677  13.920  1.00126.65           C  
ANISOU 2374  CE2 TRP A 376    20077  15763  12282   -429   1595   2027       C  
ATOM   2375  CE3 TRP A 376      26.781 -37.457  14.842  1.00125.86           C  
ANISOU 2375  CE3 TRP A 376    20185  15811  11827   -434   1691   1680       C  
ATOM   2376  CZ2 TRP A 376      27.894 -39.956  14.129  1.00129.17           C  
ANISOU 2376  CZ2 TRP A 376    20487  16149  12444   -377   1239   2060       C  
ATOM   2377  CZ3 TRP A 376      28.114 -37.733  15.048  1.00126.88           C  
ANISOU 2377  CZ3 TRP A 376    20398  16019  11793   -403   1320   1710       C  
ATOM   2378  CH2 TRP A 376      28.660 -38.972  14.694  1.00128.86           C  
ANISOU 2378  CH2 TRP A 376    20579  16233  12150   -366   1100   1906       C  
ATOM   2379  N   LEU A 377      23.762 -37.767  17.333  1.00121.08           N  
ANISOU 2379  N   LEU A 377    19929  15108  10966   -550   2670   1882       N  
ATOM   2380  CA  LEU A 377      24.383 -38.479  18.437  1.00118.74           C  
ANISOU 2380  CA  LEU A 377    19916  14873  10328   -569   2523   2026       C  
ATOM   2381  C   LEU A 377      23.351 -38.771  19.520  1.00117.18           C  
ANISOU 2381  C   LEU A 377    19897  14643   9983   -616   2886   2140       C  
ATOM   2382  O   LEU A 377      23.566 -39.622  20.381  1.00117.43           O  
ANISOU 2382  O   LEU A 377    20131  14701   9785   -642   2832   2326       O  
ATOM   2383  CB  LEU A 377      25.536 -37.662  19.022  1.00121.50           C  
ANISOU 2383  CB  LEU A 377    20484  15337  10346   -559   2265   1869       C  
ATOM   2384  CG  LEU A 377      26.903 -37.667  18.344  1.00119.40           C  
ANISOU 2384  CG  LEU A 377    20116  15135  10115   -518   1820   1826       C  
ATOM   2385  CD1 LEU A 377      27.622 -36.350  18.599  1.00119.66           C  
ANISOU 2385  CD1 LEU A 377    20260  15251   9954   -526   1687   1579       C  
ATOM   2386  CD2 LEU A 377      27.722 -38.820  18.885  1.00120.65           C  
ANISOU 2386  CD2 LEU A 377    20393  15341  10106   -508   1543   2055       C  
TER    2387      LEU A 377                                                      
ATOM   2388  N   ALA B  25      55.913  23.576 -66.076  1.00120.82           N  
ANISOU 2388  N   ALA B  25    17454  12810  15642    281   5074   3505       N  
ATOM   2389  CA  ALA B  25      56.489  23.779 -67.400  1.00121.71           C  
ANISOU 2389  CA  ALA B  25    17828  12820  15598    395   5366   3589       C  
ATOM   2390  C   ALA B  25      56.777  22.453 -68.082  1.00133.76           C  
ANISOU 2390  C   ALA B  25    19475  14398  16949    558   5488   3571       C  
ATOM   2391  O   ALA B  25      55.863  21.754 -68.517  1.00136.08           O  
ANISOU 2391  O   ALA B  25    20053  14716  16935    694   5330   3543       O  
ATOM   2392  CB  ALA B  25      57.764  24.602 -67.309  1.00112.93           C  
ANISOU 2392  CB  ALA B  25    16490  11647  14770    237   5618   3645       C  
ATOM   2393  N   ALA B  26      58.059  22.114 -68.189  1.00138.41           N  
ANISOU 2393  N   ALA B  26    19860  15000  17730    544   5766   3596       N  
ATOM   2394  CA  ALA B  26      58.418  20.914 -68.932  1.00136.12           C  
ANISOU 2394  CA  ALA B  26    19733  14717  17270    731   5943   3586       C  
ATOM   2395  C   ALA B  26      58.151  19.664 -68.107  1.00132.60           C  
ANISOU 2395  C   ALA B  26    19104  14416  16863    742   5759   3489       C  
ATOM   2396  O   ALA B  26      57.614  18.671 -68.613  1.00130.88           O  
ANISOU 2396  O   ALA B  26    19181  14198  16349    893   5712   3440       O  
ATOM   2397  CB  ALA B  26      59.884  20.985 -69.366  1.00135.30           C  
ANISOU 2397  CB  ALA B  26    19471  14566  17371    748   6326   3673       C  
ATOM   2398  N   SER B  27      58.504  19.702 -66.827  1.00132.88           N  
ANISOU 2398  N   SER B  27    18674  14570  17243    570   5637   3456       N  
ATOM   2399  CA  SER B  27      58.404  18.529 -65.970  1.00131.58           C  
ANISOU 2399  CA  SER B  27    18286  14548  17162    575   5487   3372       C  
ATOM   2400  C   SER B  27      57.156  18.633 -65.096  1.00127.43           C  
ANISOU 2400  C   SER B  27    17740  14085  16592    484   5111   3296       C  
ATOM   2401  O   SER B  27      57.208  18.915 -63.897  1.00120.32           O  
ANISOU 2401  O   SER B  27    16483  13268  15967    310   4941   3255       O  
ATOM   2402  CB  SER B  27      59.671  18.376 -65.141  1.00128.50           C  
ANISOU 2402  CB  SER B  27    17385  14262  17176    458   5585   3394       C  
ATOM   2403  OG  SER B  27      59.609  17.194 -64.367  1.00118.80           O  
ANISOU 2403  OG  SER B  27    15951  13168  16020    486   5454   3319       O  
ATOM   2404  N   GLU B  28      56.010  18.413 -65.740  1.00130.48           N  
ANISOU 2404  N   GLU B  28    18536  14426  16613    604   4967   3286       N  
ATOM   2405  CA  GLU B  28      54.745  18.261 -65.033  1.00128.37           C  
ANISOU 2405  CA  GLU B  28    18282  14227  16265    567   4608   3236       C  
ATOM   2406  C   GLU B  28      54.596  16.889 -64.395  1.00129.34           C  
ANISOU 2406  C   GLU B  28    18275  14474  16396    591   4488   3153       C  
ATOM   2407  O   GLU B  28      53.689  16.704 -63.577  1.00125.05           O  
ANISOU 2407  O   GLU B  28    17644  14005  15866    537   4196   3113       O  
ATOM   2408  CB  GLU B  28      53.576  18.508 -65.989  1.00130.11           C  
ANISOU 2408  CB  GLU B  28    18970  14378  16089    680   4453   3281       C  
ATOM   2409  CG  GLU B  28      53.687  19.809 -66.763  1.00137.63           C  
ANISOU 2409  CG  GLU B  28    20103  15198  16993    689   4587   3372       C  
ATOM   2410  CD  GLU B  28      52.872  19.807 -68.035  1.00141.43           C  
ANISOU 2410  CD  GLU B  28    21079  15614  17043    833   4509   3426       C  
ATOM   2411  OE1 GLU B  28      51.690  19.410 -67.987  1.00141.81           O  
ANISOU 2411  OE1 GLU B  28    21280  15729  16874    869   4183   3423       O  
ATOM   2412  OE2 GLU B  28      53.422  20.198 -69.085  1.00142.52           O  
ANISOU 2412  OE2 GLU B  28    21447  15640  17062    902   4759   3478       O  
ATOM   2413  N   ASP B  29      55.469  15.938 -64.731  1.00133.00           N  
ANISOU 2413  N   ASP B  29    18722  14952  16861    682   4716   3134       N  
ATOM   2414  CA  ASP B  29      55.358  14.597 -64.166  1.00125.57           C  
ANISOU 2414  CA  ASP B  29    17685  14112  15912    721   4626   3056       C  
ATOM   2415  C   ASP B  29      55.418  14.631 -62.645  1.00113.35           C  
ANISOU 2415  C   ASP B  29    15642  12698  14726    558   4441   3010       C  
ATOM   2416  O   ASP B  29      54.611  13.986 -61.966  1.00109.15           O  
ANISOU 2416  O   ASP B  29    15076  12245  14151    538   4195   2951       O  
ATOM   2417  CB  ASP B  29      56.473  13.702 -64.705  1.00131.17           C  
ANISOU 2417  CB  ASP B  29    18411  14795  16632    862   4952   3058       C  
ATOM   2418  CG  ASP B  29      56.432  13.555 -66.203  1.00136.80           C  
ANISOU 2418  CG  ASP B  29    19652  15356  16968   1029   5143   3081       C  
ATOM   2419  OD1 ASP B  29      55.327  13.684 -66.773  1.00138.12           O  
ANISOU 2419  OD1 ASP B  29    20217  15476  16786   1043   4937   3066       O  
ATOM   2420  OD2 ASP B  29      57.494  13.309 -66.810  1.00140.29           O  
ANISOU 2420  OD2 ASP B  29    20112  15724  17465   1146   5482   3122       O  
ATOM   2421  N   GLU B  30      56.367  15.384 -62.088  1.00109.41           N  
ANISOU 2421  N   GLU B  30    14768  12225  14578    425   4534   3034       N  
ATOM   2422  CA  GLU B  30      56.561  15.341 -60.643  1.00105.96           C  
ANISOU 2422  CA  GLU B  30    13871  11918  14471    256   4342   2972       C  
ATOM   2423  C   GLU B  30      55.602  16.278 -59.917  1.00102.96           C  
ANISOU 2423  C   GLU B  30    13467  11517  14134    111   4071   2942       C  
ATOM   2424  O   GLU B  30      55.125  15.955 -58.823  1.00104.73           O  
ANISOU 2424  O   GLU B  30    13481  11832  14481     26   3832   2867       O  
ATOM   2425  CB  GLU B  30      58.014  15.688 -60.298  1.00109.27           C  
ANISOU 2425  CB  GLU B  30    13908  12386  15223    150   4497   3010       C  
ATOM   2426  CG  GLU B  30      58.515  15.129 -58.967  1.00112.05           C  
ANISOU 2426  CG  GLU B  30    13799  12906  15870     31   4324   2945       C  
ATOM   2427  CD  GLU B  30      59.833  15.763 -58.525  1.00117.03           C  
ANISOU 2427  CD  GLU B  30    14064  13594  16810   -138   4381   2999       C  
ATOM   2428  OE1 GLU B  30      60.038  15.949 -57.303  1.00116.39           O  
ANISOU 2428  OE1 GLU B  30    13659  13621  16944   -338   4140   2936       O  
ATOM   2429  OE2 GLU B  30      60.662  16.086 -59.401  1.00119.34           O  
ANISOU 2429  OE2 GLU B  30    14411  13821  17113    -81   4656   3108       O  
ATOM   2430  N   PHE B  31      55.315  17.443 -60.502  1.00 98.51           N  
ANISOU 2430  N   PHE B  31    13126  10827  13477     95   4114   3001       N  
ATOM   2431  CA  PHE B  31      54.453  18.410 -59.829  1.00 92.32           C  
ANISOU 2431  CA  PHE B  31    12339   9995  12744    -15   3891   2983       C  
ATOM   2432  C   PHE B  31      53.044  17.860 -59.642  1.00 88.02           C  
ANISOU 2432  C   PHE B  31    11961   9480  12003     82   3634   2969       C  
ATOM   2433  O   PHE B  31      52.393  18.130 -58.627  1.00 88.65           O  
ANISOU 2433  O   PHE B  31    11894   9580  12208     -3   3411   2925       O  
ATOM   2434  CB  PHE B  31      54.420  19.715 -60.620  1.00 94.94           C  
ANISOU 2434  CB  PHE B  31    12917  10172  12985    -12   4014   3064       C  
ATOM   2435  CG  PHE B  31      53.291  20.626 -60.239  1.00 92.47           C  
ANISOU 2435  CG  PHE B  31    12730   9778  12625    -32   3810   3071       C  
ATOM   2436  CD1 PHE B  31      53.325  21.332 -59.049  1.00 92.37           C  
ANISOU 2436  CD1 PHE B  31    12491   9748  12858   -215   3690   3007       C  
ATOM   2437  CD2 PHE B  31      52.200  20.783 -61.075  1.00 93.95           C  
ANISOU 2437  CD2 PHE B  31    13279   9907  12512    140   3728   3147       C  
ATOM   2438  CE1 PHE B  31      52.288  22.174 -58.698  1.00 93.14           C  
ANISOU 2438  CE1 PHE B  31    12727   9749  12913   -199   3538   3017       C  
ATOM   2439  CE2 PHE B  31      51.162  21.622 -60.733  1.00 94.98           C  
ANISOU 2439  CE2 PHE B  31    13502   9970  12616    160   3548   3177       C  
ATOM   2440  CZ  PHE B  31      51.204  22.320 -59.542  1.00 93.41           C  
ANISOU 2440  CZ  PHE B  31    13083   9734  12675      4   3475   3111       C  
ATOM   2441  N   LEU B  32      52.561  17.071 -60.606  1.00 88.81           N  
ANISOU 2441  N   LEU B  32    12380   9580  11783    254   3646   3007       N  
ATOM   2442  CA  LEU B  32      51.247  16.456 -60.465  1.00 83.72           C  
ANISOU 2442  CA  LEU B  32    11883   8994  10933    334   3339   2988       C  
ATOM   2443  C   LEU B  32      51.250  15.321 -59.450  1.00 78.19           C  
ANISOU 2443  C   LEU B  32    10882   8460  10368    291   3134   2822       C  
ATOM   2444  O   LEU B  32      50.189  14.979 -58.918  1.00 78.21           O  
ANISOU 2444  O   LEU B  32    10849   8555  10311    302   2782   2730       O  
ATOM   2445  CB  LEU B  32      50.756  15.959 -61.825  1.00 81.71           C  
ANISOU 2445  CB  LEU B  32    12093   8698  10255    495   3347   3049       C  
ATOM   2446  CG  LEU B  32      50.343  17.049 -62.815  1.00 84.66           C  
ANISOU 2446  CG  LEU B  32    12778   8956  10431    559   3374   3158       C  
ATOM   2447  CD1 LEU B  32      50.474  16.549 -64.241  1.00 92.78           C  
ANISOU 2447  CD1 LEU B  32    14225   9935  11093    680   3491   3179       C  
ATOM   2448  CD2 LEU B  32      48.917  17.486 -62.530  1.00 78.01           C  
ANISOU 2448  CD2 LEU B  32    12002   8139   9500    593   3031   3221       C  
ATOM   2449  N   ARG B  33      52.420  14.744 -59.161  1.00 73.06           N  
ANISOU 2449  N   ARG B  33    10000   7852   9909    248   3355   2803       N  
ATOM   2450  CA  ARG B  33      52.515  13.717 -58.131  1.00 76.95           C  
ANISOU 2450  CA  ARG B  33    10188   8495  10554    209   3178   2662       C  
ATOM   2451  C   ARG B  33      52.611  14.316 -56.735  1.00 80.76           C  
ANISOU 2451  C   ARG B  33    10282   9032  11371     27   3023   2602       C  
ATOM   2452  O   ARG B  33      52.078  13.738 -55.782  1.00 83.52           O  
ANISOU 2452  O   ARG B  33    10458   9494  11780     -4   2738   2470       O  
ATOM   2453  CB  ARG B  33      53.720  12.810 -58.391  1.00 84.42           C  
ANISOU 2453  CB  ARG B  33    11040   9468  11568    267   3483   2695       C  
ATOM   2454  CG  ARG B  33      53.491  11.779 -59.486  1.00 96.38           C  
ANISOU 2454  CG  ARG B  33    12960  10942  12720    453   3569   2687       C  
ATOM   2455  CD  ARG B  33      54.684  10.849 -59.653  1.00105.67           C  
ANISOU 2455  CD  ARG B  33    14039  12128  13981    547   3908   2728       C  
ATOM   2456  NE  ARG B  33      54.268   9.451 -59.733  1.00108.40           N  
ANISOU 2456  NE  ARG B  33    14573  12509  14104    661   3787   2608       N  
ATOM   2457  CZ  ARG B  33      53.915   8.834 -60.857  1.00108.66           C  
ANISOU 2457  CZ  ARG B  33    15114  12432  13739    797   3868   2603       C  
ATOM   2458  NH1 ARG B  33      53.926   9.487 -62.011  1.00105.02           N  
ANISOU 2458  NH1 ARG B  33    15019  11832  13052    852   4071   2717       N  
ATOM   2459  NH2 ARG B  33      53.549   7.559 -60.826  1.00111.71           N  
ANISOU 2459  NH2 ARG B  33    15673  12836  13934    867   3743   2483       N  
ATOM   2460  N   TYR B  34      53.289  15.456 -56.591  1.00 84.57           N  
ANISOU 2460  N   TYR B  34    10651   9423  12059   -109   3207   2696       N  
ATOM   2461  CA  TYR B  34      53.341  16.118 -55.293  1.00 83.84           C  
ANISOU 2461  CA  TYR B  34    10271   9345  12239   -309   3052   2634       C  
ATOM   2462  C   TYR B  34      52.070  16.901 -55.001  1.00 76.45           C  
ANISOU 2462  C   TYR B  34     9503   8337  11207   -296   2816   2594       C  
ATOM   2463  O   TYR B  34      51.701  17.056 -53.830  1.00 73.38           O  
ANISOU 2463  O   TYR B  34     8940   7982  10958   -399   2601   2492       O  
ATOM   2464  CB  TYR B  34      54.566  17.029 -55.217  1.00 98.66           C  
ANISOU 2464  CB  TYR B  34    11994  11190  14300   -463   3187   2634       C  
ATOM   2465  CG  TYR B  34      55.852  16.278 -54.952  1.00120.94           C  
ANISOU 2465  CG  TYR B  34    14506  14152  17294   -501   3259   2612       C  
ATOM   2466  CD1 TYR B  34      56.134  15.089 -55.615  1.00129.26           C  
ANISOU 2466  CD1 TYR B  34    15595  15268  18248   -315   3410   2649       C  
ATOM   2467  CD2 TYR B  34      56.784  16.758 -54.044  1.00133.19           C  
ANISOU 2467  CD2 TYR B  34    15760  15767  19081   -716   3171   2564       C  
ATOM   2468  CE1 TYR B  34      57.306  14.398 -55.377  1.00136.83           C  
ANISOU 2468  CE1 TYR B  34    16273  16345  19371   -311   3486   2651       C  
ATOM   2469  CE2 TYR B  34      57.961  16.074 -53.801  1.00141.83           C  
ANISOU 2469  CE2 TYR B  34    16562  17001  20324   -734   3211   2575       C  
ATOM   2470  CZ  TYR B  34      58.217  14.896 -54.470  1.00141.98           C  
ANISOU 2470  CZ  TYR B  34    16597  17077  20274   -515   3376   2624       C  
ATOM   2471  OH  TYR B  34      59.387  14.213 -54.230  1.00141.52           O  
ANISOU 2471  OH  TYR B  34    16253  17146  20372   -499   3428   2658       O  
ATOM   2472  N   LEU B  35      51.388  17.399 -56.037  1.00 77.24           N  
ANISOU 2472  N   LEU B  35     9946   8335  11066   -159   2862   2688       N  
ATOM   2473  CA  LEU B  35      50.083  18.016 -55.824  1.00 74.86           C  
ANISOU 2473  CA  LEU B  35     9789   7989  10666    -93   2634   2684       C  
ATOM   2474  C   LEU B  35      49.081  17.007 -55.285  1.00 67.81           C  
ANISOU 2474  C   LEU B  35     8817   7256   9690    -13   2298   2565       C  
ATOM   2475  O   LEU B  35      48.191  17.364 -54.507  1.00 70.86           O  
ANISOU 2475  O   LEU B  35     9147   7648  10129    -11   2092   2526       O  
ATOM   2476  CB  LEU B  35      49.574  18.626 -57.132  1.00 82.25           C  
ANISOU 2476  CB  LEU B  35    11098   8810  11344     57   2735   2839       C  
ATOM   2477  CG  LEU B  35      48.132  19.134 -57.170  1.00 83.08           C  
ANISOU 2477  CG  LEU B  35    11365   8895  11307    186   2499   2892       C  
ATOM   2478  CD1 LEU B  35      48.049  20.565 -56.663  1.00 86.64           C  
ANISOU 2478  CD1 LEU B  35    11835   9170  11916    124   2596   2952       C  
ATOM   2479  CD2 LEU B  35      47.566  19.019 -58.577  1.00 84.52           C  
ANISOU 2479  CD2 LEU B  35    11894   9065  11153    358   2490   3026       C  
ATOM   2480  N   TRP B  36      49.215  15.743 -55.679  1.00 63.82           N  
ANISOU 2480  N   TRP B  36     8324   6868   9057     54   2259   2513       N  
ATOM   2481  CA  TRP B  36      48.342  14.707 -55.145  1.00 59.04           C  
ANISOU 2481  CA  TRP B  36     7639   6411   8383     98   1947   2398       C  
ATOM   2482  C   TRP B  36      48.754  14.303 -53.736  1.00 58.06           C  
ANISOU 2482  C   TRP B  36     7163   6373   8523    -28   1857   2262       C  
ATOM   2483  O   TRP B  36      47.907  14.170 -52.846  1.00 56.86           O  
ANISOU 2483  O   TRP B  36     6899   6286   8419    -38   1607   2183       O  
ATOM   2484  CB  TRP B  36      48.356  13.498 -56.078  1.00 60.08           C  
ANISOU 2484  CB  TRP B  36     7968   6602   8259    198   1947   2386       C  
ATOM   2485  CG  TRP B  36      47.820  12.243 -55.467  1.00 53.75           C  
ANISOU 2485  CG  TRP B  36     7055   5942   7423    202   1684   2251       C  
ATOM   2486  CD1 TRP B  36      48.530  11.283 -54.804  1.00 52.27           C  
ANISOU 2486  CD1 TRP B  36     6656   5832   7370    159   1716   2142       C  
ATOM   2487  CD2 TRP B  36      46.461  11.800 -55.479  1.00 48.79           C  
ANISOU 2487  CD2 TRP B  36     6520   5398   6619    247   1351   2232       C  
ATOM   2488  NE1 TRP B  36      47.692  10.273 -54.396  1.00 54.41           N  
ANISOU 2488  NE1 TRP B  36     6912   6212   7550    174   1434   2040       N  
ATOM   2489  CE2 TRP B  36      46.416  10.567 -54.799  1.00 51.08           C  
ANISOU 2489  CE2 TRP B  36     6664   5800   6942    215   1203   2093       C  
ATOM   2490  CE3 TRP B  36      45.275  12.329 -55.997  1.00 47.82           C  
ANISOU 2490  CE3 TRP B  36     6570   5275   6325    311   1160   2340       C  
ATOM   2491  CZ2 TRP B  36      45.232   9.855 -54.623  1.00 48.04           C  
ANISOU 2491  CZ2 TRP B  36     6308   5519   6427    222    876   2051       C  
ATOM   2492  CZ3 TRP B  36      44.102  11.622 -55.821  1.00 52.09           C  
ANISOU 2492  CZ3 TRP B  36     7105   5939   6749    321    823   2316       C  
ATOM   2493  CH2 TRP B  36      44.088  10.399 -55.141  1.00 52.29           C  
ANISOU 2493  CH2 TRP B  36     6988   6067   6812    265    685   2168       C  
ATOM   2494  N   ARG B  37      50.053  14.088 -53.519  1.00 56.83           N  
ANISOU 2494  N   ARG B  37     6824   6226   8542   -123   2060   2251       N  
ATOM   2495  CA  ARG B  37      50.504  13.589 -52.225  1.00 54.57           C  
ANISOU 2495  CA  ARG B  37     6206   6041   8487   -243   1954   2138       C  
ATOM   2496  C   ARG B  37      50.298  14.622 -51.125  1.00 56.62           C  
ANISOU 2496  C   ARG B  37     6342   6239   8930   -393   1855   2103       C  
ATOM   2497  O   ARG B  37      49.982  14.267 -49.983  1.00 50.62           O  
ANISOU 2497  O   ARG B  37     5412   5555   8268   -453   1649   1989       O  
ATOM   2498  CB  ARG B  37      51.972  13.174 -52.306  1.00 62.66           C  
ANISOU 2498  CB  ARG B  37     7037   7102   9670   -302   2197   2182       C  
ATOM   2499  CG  ARG B  37      52.532  12.624 -51.005  1.00 67.94           C  
ANISOU 2499  CG  ARG B  37     7346   7891  10575   -427   2078   2095       C  
ATOM   2500  CD  ARG B  37      53.747  13.424 -50.562  1.00 77.81           C  
ANISOU 2500  CD  ARG B  37     8359   9116  12091   -630   2225   2167       C  
ATOM   2501  NE  ARG B  37      54.986  12.976 -51.194  1.00 91.34           N  
ANISOU 2501  NE  ARG B  37     9985  10885  13834   -569   2439   2230       N  
ATOM   2502  CZ  ARG B  37      56.022  13.772 -51.446  1.00105.43           C  
ANISOU 2502  CZ  ARG B  37    11714  12638  15707   -663   2571   2283       C  
ATOM   2503  NH1 ARG B  37      55.958  15.061 -51.141  1.00108.61           N  
ANISOU 2503  NH1 ARG B  37    12169  12944  16153   -836   2517   2269       N  
ATOM   2504  NH2 ARG B  37      57.116  13.285 -52.016  1.00109.39           N  
ANISOU 2504  NH2 ARG B  37    12120  13194  16251   -582   2770   2362       N  
ATOM   2505  N   ASP B  38      50.459  15.903 -51.449  1.00 60.49           N  
ANISOU 2505  N   ASP B  38     6957   6572   9453   -452   2012   2198       N  
ATOM   2506  CA  ASP B  38      50.428  16.951 -50.439  1.00 62.46           C  
ANISOU 2506  CA  ASP B  38     7148   6716   9867   -617   1970   2166       C  
ATOM   2507  C   ASP B  38      49.088  17.665 -50.340  1.00 61.71           C  
ANISOU 2507  C   ASP B  38     7262   6525   9660   -506   1853   2177       C  
ATOM   2508  O   ASP B  38      48.868  18.398 -49.370  1.00 62.23           O  
ANISOU 2508  O   ASP B  38     7319   6493   9835   -609   1802   2128       O  
ATOM   2509  CB  ASP B  38      51.528  17.985 -50.708  1.00 73.35           C  
ANISOU 2509  CB  ASP B  38     8530   7956  11383   -792   2231   2267       C  
ATOM   2510  CG  ASP B  38      52.923  17.440 -50.458  1.00 81.33           C  
ANISOU 2510  CG  ASP B  38     9265   9103  12533   -921   2271   2221       C  
ATOM   2511  OD1 ASP B  38      53.059  16.406 -49.767  1.00 78.58           O  
ANISOU 2511  OD1 ASP B  38     8696   8911  12250   -925   2120   2135       O  
ATOM   2512  OD2 ASP B  38      53.890  18.061 -50.948  1.00 83.88           O  
ANISOU 2512  OD2 ASP B  38     9595   9386  12889  -1004   2434   2270       O  
ATOM   2513  N   TYR B  39      48.188  17.470 -51.300  1.00 63.72           N  
ANISOU 2513  N   TYR B  39     7712   6801   9698   -298   1809   2252       N  
ATOM   2514  CA  TYR B  39      46.923  18.190 -51.252  1.00 58.73           C  
ANISOU 2514  CA  TYR B  39     7241   6091   8983   -170   1710   2312       C  
ATOM   2515  C   TYR B  39      45.748  17.318 -51.661  1.00 65.24           C  
ANISOU 2515  C   TYR B  39     8101   7066   9622     15   1479   2332       C  
ATOM   2516  O   TYR B  39      44.818  17.116 -50.873  1.00 69.27           O  
ANISOU 2516  O   TYR B  39     8518   7638  10163     64   1283   2289       O  
ATOM   2517  CB  TYR B  39      46.968  19.427 -52.148  1.00 54.19           C  
ANISOU 2517  CB  TYR B  39     6922   5326   8341   -122   1925   2471       C  
ATOM   2518  CG  TYR B  39      45.622  20.105 -52.292  1.00 57.95           C  
ANISOU 2518  CG  TYR B  39     7568   5737   8714     66   1838   2582       C  
ATOM   2519  CD1 TYR B  39      45.029  20.749 -51.214  1.00 59.21           C  
ANISOU 2519  CD1 TYR B  39     7702   5803   8991     65   1792   2550       C  
ATOM   2520  CD2 TYR B  39      44.944  20.103 -53.506  1.00 60.05           C  
ANISOU 2520  CD2 TYR B  39     8028   6030   8760    254   1807   2736       C  
ATOM   2521  CE1 TYR B  39      43.801  21.372 -51.338  1.00 52.49           C  
ANISOU 2521  CE1 TYR B  39     6982   4893   8068    272   1746   2686       C  
ATOM   2522  CE2 TYR B  39      43.715  20.725 -53.639  1.00 59.00           C  
ANISOU 2522  CE2 TYR B  39     8006   5857   8552    439   1718   2878       C  
ATOM   2523  CZ  TYR B  39      43.149  21.357 -52.552  1.00 57.14           C  
ANISOU 2523  CZ  TYR B  39     7710   5536   8465    462   1702   2861       C  
ATOM   2524  OH  TYR B  39      41.925  21.976 -52.681  1.00 64.06           O  
ANISOU 2524  OH  TYR B  39     8676   6375   9289    681   1646   3034       O  
ATOM   2525  N   LEU B  40      45.768  16.814 -52.897  1.00 65.22           N  
ANISOU 2525  N   LEU B  40     8251   7114   9417    106   1502   2406       N  
ATOM   2526  CA  LEU B  40      44.590  16.126 -53.409  1.00 58.89           C  
ANISOU 2526  CA  LEU B  40     7532   6437   8407    248   1258   2453       C  
ATOM   2527  C   LEU B  40      44.252  14.906 -52.563  1.00 55.12           C  
ANISOU 2527  C   LEU B  40     6844   6126   7975    211   1027   2309       C  
ATOM   2528  O   LEU B  40      43.080  14.651 -52.271  1.00 53.13           O  
ANISOU 2528  O   LEU B  40     6542   5964   7680    284    791   2333       O  
ATOM   2529  CB  LEU B  40      44.808  15.720 -54.868  1.00 63.60           C  
ANISOU 2529  CB  LEU B  40     8381   7038   8744    314   1325   2537       C  
ATOM   2530  CG  LEU B  40      44.964  16.832 -55.910  1.00 74.62           C  
ANISOU 2530  CG  LEU B  40    10040   8279  10033    381   1532   2707       C  
ATOM   2531  CD1 LEU B  40      45.394  16.238 -57.241  1.00 81.16           C  
ANISOU 2531  CD1 LEU B  40    11130   9108  10600    423   1630   2754       C  
ATOM   2532  CD2 LEU B  40      43.673  17.621 -56.069  1.00 76.28           C  
ANISOU 2532  CD2 LEU B  40    10344   8469  10168    517   1378   2863       C  
ATOM   2533  N   TYR B  41      45.265  14.147 -52.140  1.00 42.27           N  
ANISOU 2533  N   TYR B  41     5074   4543   6445    103   1097   2178       N  
ATOM   2534  CA  TYR B  41      44.964  12.924 -51.397  1.00 56.15           C  
ANISOU 2534  CA  TYR B  41     6661   6448   8225     79    888   2047       C  
ATOM   2535  C   TYR B  41      44.535  13.223 -49.971  1.00 55.64           C  
ANISOU 2535  C   TYR B  41     6388   6395   8358     27    775   1973       C  
ATOM   2536  O   TYR B  41      43.484  12.713 -49.541  1.00 54.69           O  
ANISOU 2536  O   TYR B  41     6203   6372   8206     79    551   1955       O  
ATOM   2537  CB  TYR B  41      46.162  11.976 -51.437  1.00 40.13           C  
ANISOU 2537  CB  TYR B  41     4557   4461   6229     15   1012   1957       C  
ATOM   2538  CG  TYR B  41      46.016  10.805 -50.498  1.00 45.86           C  
ANISOU 2538  CG  TYR B  41     5093   5314   7016    -20    830   1819       C  
ATOM   2539  CD1 TYR B  41      45.133   9.772 -50.778  1.00 52.18           C  
ANISOU 2539  CD1 TYR B  41     5981   6209   7635     38    618   1790       C  
ATOM   2540  CD2 TYR B  41      46.749  10.742 -49.323  1.00 52.23           C  
ANISOU 2540  CD2 TYR B  41     5646   6144   8056   -129    857   1727       C  
ATOM   2541  CE1 TYR B  41      44.989   8.705 -49.917  1.00 61.23           C  
ANISOU 2541  CE1 TYR B  41     6971   7456   8836      3    465   1669       C  
ATOM   2542  CE2 TYR B  41      46.614   9.680 -48.456  1.00 59.47           C  
ANISOU 2542  CE2 TYR B  41     6404   7171   9021   -152    695   1611       C  
ATOM   2543  CZ  TYR B  41      45.733   8.664 -48.756  1.00 64.13           C  
ANISOU 2543  CZ  TYR B  41     7091   7842   9436    -78    513   1581       C  
ATOM   2544  OH  TYR B  41      45.596   7.603 -47.892  1.00 66.92           O  
ANISOU 2544  OH  TYR B  41     7302   8290   9835   -104    366   1470       O  
ATOM   2545  N   PRO B  42      45.278  14.012 -49.190  1.00 55.04           N  
ANISOU 2545  N   PRO B  42     6216   6218   8477    -87    915   1933       N  
ATOM   2546  CA  PRO B  42      44.853  14.278 -47.815  1.00 44.89           C  
ANISOU 2546  CA  PRO B  42     4796   4919   7341   -139    813   1854       C  
ATOM   2547  C   PRO B  42      43.469  14.900 -47.725  1.00 44.85           C  
ANISOU 2547  C   PRO B  42     4876   4876   7289      2    723   1948       C  
ATOM   2548  O   PRO B  42      42.728  14.610 -46.779  1.00 45.55           O  
ANISOU 2548  O   PRO B  42     4854   5018   7435     26    582   1897       O  
ATOM   2549  CB  PRO B  42      45.951  15.211 -47.282  1.00 46.85           C  
ANISOU 2549  CB  PRO B  42     5018   5027   7756   -311    997   1826       C  
ATOM   2550  CG  PRO B  42      46.631  15.757 -48.512  1.00 58.72           C  
ANISOU 2550  CG  PRO B  42     6666   6446   9199   -306   1212   1941       C  
ATOM   2551  CD  PRO B  42      46.538  14.679 -49.534  1.00 60.41           C  
ANISOU 2551  CD  PRO B  42     6924   6788   9241   -190   1170   1967       C  
ATOM   2552  N   LYS B  43      43.082  15.730 -48.694  1.00 46.39           N  
ANISOU 2552  N   LYS B  43     5257   4984   7383    112    811   2106       N  
ATOM   2553  CA  LYS B  43      41.707  16.217 -48.724  1.00 51.01           C  
ANISOU 2553  CA  LYS B  43     5891   5564   7924    283    716   2242       C  
ATOM   2554  C   LYS B  43      40.740  15.082 -49.023  1.00 50.63           C  
ANISOU 2554  C   LYS B  43     5757   5723   7758    364    451   2273       C  
ATOM   2555  O   LYS B  43      39.719  14.925 -48.345  1.00 51.75           O  
ANISOU 2555  O   LYS B  43     5774   5934   7955    437    310   2303       O  
ATOM   2556  CB  LYS B  43      41.554  17.331 -49.763  1.00 59.03           C  
ANISOU 2556  CB  LYS B  43     7131   6447   8850    392    864   2428       C  
ATOM   2557  CG  LYS B  43      42.298  18.611 -49.430  1.00 65.09           C  
ANISOU 2557  CG  LYS B  43     8018   6978   9733    313   1126   2423       C  
ATOM   2558  CD  LYS B  43      41.349  19.708 -48.965  1.00 81.56           C  
ANISOU 2558  CD  LYS B  43    10198   8919  11873    460   1189   2540       C  
ATOM   2559  CE  LYS B  43      40.489  20.228 -50.110  1.00 93.89           C  
ANISOU 2559  CE  LYS B  43    11907  10475  13294    680   1186   2783       C  
ATOM   2560  NZ  LYS B  43      39.608  21.355 -49.683  1.00 99.49           N  
ANISOU 2560  NZ  LYS B  43    12709  11022  14069    860   1296   2929       N  
ATOM   2561  N   GLN B  44      41.053  14.272 -50.036  1.00 51.10           N  
ANISOU 2561  N   GLN B  44     5895   5871   7649    341    391   2272       N  
ATOM   2562  CA  GLN B  44      40.172  13.165 -50.399  1.00 52.77           C  
ANISOU 2562  CA  GLN B  44     6075   6260   7716    373    123   2297       C  
ATOM   2563  C   GLN B  44      40.111  12.114 -49.296  1.00 54.67           C  
ANISOU 2563  C   GLN B  44     6104   6607   8059    291    -10   2135       C  
ATOM   2564  O   GLN B  44      39.062  11.500 -49.074  1.00 60.33           O  
ANISOU 2564  O   GLN B  44     6721   7453   8748    320   -237   2173       O  
ATOM   2565  CB  GLN B  44      40.636  12.554 -51.720  1.00 63.94           C  
ANISOU 2565  CB  GLN B  44     7700   7698   8894    350    123   2312       C  
ATOM   2566  CG  GLN B  44      39.825  11.371 -52.219  1.00 80.89           C  
ANISOU 2566  CG  GLN B  44     9889  10001  10844    337   -161   2327       C  
ATOM   2567  CD  GLN B  44      40.521  10.644 -53.354  1.00 92.90           C  
ANISOU 2567  CD  GLN B  44    11673  11501  12123    293   -108   2287       C  
ATOM   2568  OE1 GLN B  44      40.955   9.503 -53.200  1.00 98.84           O  
ANISOU 2568  OE1 GLN B  44    12428  12294  12831    218   -135   2144       O  
ATOM   2569  NE2 GLN B  44      40.644  11.310 -54.497  1.00 93.10           N  
ANISOU 2569  NE2 GLN B  44    11948  11445  11981    352     -8   2419       N  
ATOM   2570  N   TYR B  45      41.217  11.908 -48.579  1.00 52.12           N  
ANISOU 2570  N   TYR B  45     5701   6238   7863    182    121   1972       N  
ATOM   2571  CA  TYR B  45      41.202  11.001 -47.434  1.00 45.29           C  
ANISOU 2571  CA  TYR B  45     4644   5460   7103    111      7   1826       C  
ATOM   2572  C   TYR B  45      40.295  11.533 -46.336  1.00 48.11           C  
ANISOU 2572  C   TYR B  45     4880   5804   7597    160    -48   1850       C  
ATOM   2573  O   TYR B  45      39.461  10.802 -45.787  1.00 52.55           O  
ANISOU 2573  O   TYR B  45     5317   6478   8172    177   -225   1835       O  
ATOM   2574  CB  TYR B  45      42.623  10.822 -46.897  1.00 51.44           C  
ANISOU 2574  CB  TYR B  45     5352   6194   8000    -12    159   1684       C  
ATOM   2575  CG  TYR B  45      42.736  10.045 -45.606  1.00 52.16           C  
ANISOU 2575  CG  TYR B  45     5252   6354   8211    -86     59   1542       C  
ATOM   2576  CD1 TYR B  45      42.552  10.666 -44.374  1.00 56.84           C  
ANISOU 2576  CD1 TYR B  45     5756   6888   8953   -123     66   1498       C  
ATOM   2577  CD2 TYR B  45      43.089   8.702 -45.617  1.00 49.28           C  
ANISOU 2577  CD2 TYR B  45     4835   6093   7795   -118    -19   1451       C  
ATOM   2578  CE1 TYR B  45      42.666   9.962 -43.189  1.00 57.34           C  
ANISOU 2578  CE1 TYR B  45     5672   7010   9105   -193    -27   1373       C  
ATOM   2579  CE2 TYR B  45      43.213   7.992 -44.435  1.00 45.64           C  
ANISOU 2579  CE2 TYR B  45     4210   5692   7438   -178   -107   1333       C  
ATOM   2580  CZ  TYR B  45      43.000   8.628 -43.227  1.00 51.27           C  
ANISOU 2580  CZ  TYR B  45     4827   6360   8293   -219   -119   1295       C  
ATOM   2581  OH  TYR B  45      43.122   7.928 -42.050  1.00 52.45           O  
ANISOU 2581  OH  TYR B  45     4840   6564   8526   -280   -209   1183       O  
ATOM   2582  N   ALA B  46      40.440  12.819 -46.015  1.00 52.65           N  
ANISOU 2582  N   ALA B  46     5511   6224   8270    185    123   1896       N  
ATOM   2583  CA  ALA B  46      39.670  13.410 -44.929  1.00 52.29           C  
ANISOU 2583  CA  ALA B  46     5404   6118   8345    248    134   1917       C  
ATOM   2584  C   ALA B  46      38.185  13.442 -45.254  1.00 55.51           C  
ANISOU 2584  C   ALA B  46     5768   6614   8709    422      5   2104       C  
ATOM   2585  O   ALA B  46      37.349  13.217 -44.373  1.00 61.94           O  
ANISOU 2585  O   ALA B  46     6450   7478   9606    478    -68   2116       O  
ATOM   2586  CB  ALA B  46      40.189  14.818 -44.633  1.00 55.37           C  
ANISOU 2586  CB  ALA B  46     5937   6284   8816    229    369   1930       C  
ATOM   2587  N   TRP B  47      37.835  13.728 -46.509  1.00 54.09           N  
ANISOU 2587  N   TRP B  47     5690   6460   8402    509    -26   2271       N  
ATOM   2588  CA  TRP B  47      36.424  13.841 -46.848  1.00 56.30           C  
ANISOU 2588  CA  TRP B  47     5898   6839   8653    671   -169   2494       C  
ATOM   2589  C   TRP B  47      35.729  12.489 -46.761  1.00 63.55           C  
ANISOU 2589  C   TRP B  47     6645   7974   9527    617   -447   2479       C  
ATOM   2590  O   TRP B  47      34.602  12.391 -46.256  1.00 73.24           O  
ANISOU 2590  O   TRP B  47     7697   9292  10837    707   -553   2600       O  
ATOM   2591  CB  TRP B  47      36.276  14.401 -48.259  1.00 66.83           C  
ANISOU 2591  CB  TRP B  47     7397   8161   9834    755   -171   2683       C  
ATOM   2592  CG  TRP B  47      34.862  14.634 -48.656  1.00 79.12           C  
ANISOU 2592  CG  TRP B  47     8861   9830  11371    924   -328   2956       C  
ATOM   2593  CD1 TRP B  47      34.112  15.741 -48.388  1.00 80.34           C  
ANISOU 2593  CD1 TRP B  47     8998   9907  11623   1110   -197   3120       C  
ATOM   2594  CD2 TRP B  47      33.989  13.706 -49.310  1.00 91.36           C  
ANISOU 2594  CD2 TRP B  47    10322  11604  12786    889   -637   3047       C  
ATOM   2595  NE1 TRP B  47      32.842  15.584 -48.887  1.00 83.73           N  
ANISOU 2595  NE1 TRP B  47     9327  10526  11960   1157   -378   3222       N  
ATOM   2596  CE2 TRP B  47      32.738  14.339 -49.450  1.00 92.15           C  
ANISOU 2596  CE2 TRP B  47    10352  11774  12885   1006   -656   3172       C  
ATOM   2597  CE3 TRP B  47      34.149  12.410 -49.808  1.00 96.40           C  
ANISOU 2597  CE3 TRP B  47    10977  12379  13271    731   -873   2970       C  
ATOM   2598  CZ2 TRP B  47      31.652  13.719 -50.068  1.00 96.94           C  
ANISOU 2598  CZ2 TRP B  47    10881  12583  13367    952   -915   3232       C  
ATOM   2599  CZ3 TRP B  47      33.070  11.795 -50.421  1.00 97.06           C  
ANISOU 2599  CZ3 TRP B  47    11028  12646  13206    670  -1129   3011       C  
ATOM   2600  CH2 TRP B  47      31.839  12.450 -50.546  1.00 98.90           C  
ANISOU 2600  CH2 TRP B  47    11167  12946  13463    771  -1152   3142       C  
ATOM   2601  N   VAL B  48      36.380  11.435 -47.258  1.00 63.12           N  
ANISOU 2601  N   VAL B  48     6648   7993   9343    474   -550   2344       N  
ATOM   2602  CA  VAL B  48      35.801  10.099 -47.159  1.00 57.99           C  
ANISOU 2602  CA  VAL B  48     5882   7518   8635    393   -805   2308       C  
ATOM   2603  C   VAL B  48      35.697   9.660 -45.706  1.00 57.31           C  
ANISOU 2603  C   VAL B  48     5606   7447   8721    360   -797   2179       C  
ATOM   2604  O   VAL B  48      34.748   8.968 -45.319  1.00 62.52           O  
ANISOU 2604  O   VAL B  48     6186   8218   9351    317   -922   2144       O  
ATOM   2605  CB  VAL B  48      36.620   9.098 -47.993  1.00 49.31           C  
ANISOU 2605  CB  VAL B  48     4949   6442   7342    262   -863   2180       C  
ATOM   2606  CG1 VAL B  48      36.038   7.702 -47.848  1.00 34.73           C  
ANISOU 2606  CG1 VAL B  48     3029   4744   5425    159  -1117   2130       C  
ATOM   2607  CG2 VAL B  48      36.643   9.529 -49.446  1.00 47.22           C  
ANISOU 2607  CG2 VAL B  48     4912   6154   6876    298   -870   2318       C  
ATOM   2608  N   LEU B  49      36.667  10.058 -44.881  1.00 45.93           N  
ANISOU 2608  N   LEU B  49     4187   5873   7392    323   -595   2021       N  
ATOM   2609  CA  LEU B  49      36.641   9.689 -43.470  1.00 35.96           C  
ANISOU 2609  CA  LEU B  49     2787   4609   6268    286   -583   1894       C  
ATOM   2610  C   LEU B  49      35.457  10.327 -42.756  1.00 41.48           C  
ANISOU 2610  C   LEU B  49     3423   5290   7046    406   -535   1999       C  
ATOM   2611  O   LEU B  49      34.679   9.643 -42.080  1.00 41.97           O  
ANISOU 2611  O   LEU B  49     3467   5426   7055    359   -587   1906       O  
ATOM   2612  CB  LEU B  49      37.960  10.101 -42.807  1.00 32.91           C  
ANISOU 2612  CB  LEU B  49     2468   4080   5957    194   -395   1720       C  
ATOM   2613  CG  LEU B  49      38.375   9.467 -41.479  1.00 45.20           C  
ANISOU 2613  CG  LEU B  49     3927   5642   7605     98   -409   1544       C  
ATOM   2614  CD1 LEU B  49      39.824   9.820 -41.182  1.00 49.65           C  
ANISOU 2614  CD1 LEU B  49     4554   6099   8214    -27   -271   1410       C  
ATOM   2615  CD2 LEU B  49      37.469   9.920 -40.349  1.00 54.57           C  
ANISOU 2615  CD2 LEU B  49     5056   6781   8897    182   -371   1583       C  
ATOM   2616  N   ILE B  50      35.299  11.643 -42.902  1.00 47.16           N  
ANISOU 2616  N   ILE B  50     4187   5881   7850    556   -382   2164       N  
ATOM   2617  CA  ILE B  50      34.199  12.326 -42.230  1.00 49.79           C  
ANISOU 2617  CA  ILE B  50     4504   6178   8238    686   -271   2253       C  
ATOM   2618  C   ILE B  50      32.859  11.907 -42.817  1.00 55.70           C  
ANISOU 2618  C   ILE B  50     5196   7108   8858    699   -411   2346       C  
ATOM   2619  O   ILE B  50      31.869  11.754 -42.091  1.00 55.45           O  
ANISOU 2619  O   ILE B  50     5098   7123   8846    724   -389   2348       O  
ATOM   2620  CB  ILE B  50      34.397  13.849 -42.298  1.00 49.10           C  
ANISOU 2620  CB  ILE B  50     4540   5867   8250    855    -37   2406       C  
ATOM   2621  CG1 ILE B  50      35.808  14.202 -41.828  1.00 51.38           C  
ANISOU 2621  CG1 ILE B  50     5007   5976   8539    689    117   2173       C  
ATOM   2622  CG2 ILE B  50      33.349  14.555 -41.452  1.00 46.72           C  
ANISOU 2622  CG2 ILE B  50     4247   5503   8000    998    129   2471       C  
ATOM   2623  CD1 ILE B  50      36.270  15.558 -42.288  1.00 60.37           C  
ANISOU 2623  CD1 ILE B  50     6372   6902   9664    734    336   2236       C  
ATOM   2624  N   ALA B  51      32.800  11.722 -44.137  1.00 59.53           N  
ANISOU 2624  N   ALA B  51     5712   7686   9220    680   -557   2441       N  
ATOM   2625  CA  ALA B  51      31.551  11.312 -44.767  1.00 51.58           C  
ANISOU 2625  CA  ALA B  51     4646   6845   8107    667   -720   2538       C  
ATOM   2626  C   ALA B  51      31.106   9.940 -44.277  1.00 57.70           C  
ANISOU 2626  C   ALA B  51     5365   7731   8826    510   -861   2385       C  
ATOM   2627  O   ALA B  51      29.920   9.728 -43.999  1.00 67.02           O  
ANISOU 2627  O   ALA B  51     6455   8994  10016    518   -895   2444       O  
ATOM   2628  CB  ALA B  51      31.704  11.315 -46.287  1.00 40.75           C  
ANISOU 2628  CB  ALA B  51     3362   5534   6588    656   -871   2658       C  
ATOM   2629  N   ALA B  52      32.039   8.990 -44.172  1.00 60.15           N  
ANISOU 2629  N   ALA B  52     5736   8036   9083    376   -927   2200       N  
ATOM   2630  CA  ALA B  52      31.669   7.664 -43.687  1.00 54.20           C  
ANISOU 2630  CA  ALA B  52     4977   7353   8262    243  -1029   2044       C  
ATOM   2631  C   ALA B  52      31.258   7.706 -42.221  1.00 53.94           C  
ANISOU 2631  C   ALA B  52     4895   7271   8331    278   -892   1966       C  
ATOM   2632  O   ALA B  52      30.316   7.016 -41.815  1.00 58.94           O  
ANISOU 2632  O   ALA B  52     5485   7971   8941    238   -943   1952       O  
ATOM   2633  CB  ALA B  52      32.824   6.683 -43.899  1.00 45.45           C  
ANISOU 2633  CB  ALA B  52     3963   6233   7071    121  -1098   1873       C  
ATOM   2634  N   TYR B  53      31.950   8.510 -41.412  1.00 49.76           N  
ANISOU 2634  N   TYR B  53     4375   6615   7917    350   -719   1931       N  
ATOM   2635  CA  TYR B  53      31.591   8.615 -40.002  1.00 45.07           C  
ANISOU 2635  CA  TYR B  53     3757   5959   7407    390   -592   1876       C  
ATOM   2636  C   TYR B  53      30.248   9.303 -39.810  1.00 54.96           C  
ANISOU 2636  C   TYR B  53     4917   7235   8729    524   -511   2073       C  
ATOM   2637  O   TYR B  53      29.513   8.977 -38.870  1.00 65.29           O  
ANISOU 2637  O   TYR B  53     6182   8555  10069    536   -464   2061       O  
ATOM   2638  CB  TYR B  53      32.686   9.354 -39.236  1.00 48.47           C  
ANISOU 2638  CB  TYR B  53     4229   6234   7956    423   -441   1809       C  
ATOM   2639  CG  TYR B  53      33.658   8.432 -38.535  1.00 47.42           C  
ANISOU 2639  CG  TYR B  53     4154   6083   7782    287   -482   1576       C  
ATOM   2640  CD1 TYR B  53      33.352   7.880 -37.298  1.00 49.63           C  
ANISOU 2640  CD1 TYR B  53     4448   6353   8055    264   -456   1468       C  
ATOM   2641  CD2 TYR B  53      34.882   8.113 -39.109  1.00 46.29           C  
ANISOU 2641  CD2 TYR B  53     4050   5935   7604    195   -536   1479       C  
ATOM   2642  CE1 TYR B  53      34.237   7.038 -36.651  1.00 50.75           C  
ANISOU 2642  CE1 TYR B  53     4659   6485   8136    157   -492   1264       C  
ATOM   2643  CE2 TYR B  53      35.774   7.271 -38.469  1.00 55.19           C  
ANISOU 2643  CE2 TYR B  53     5236   7054   8678     88   -557   1274       C  
ATOM   2644  CZ  TYR B  53      35.445   6.737 -37.240  1.00 55.12           C  
ANISOU 2644  CZ  TYR B  53     5258   7041   8643     72   -540   1165       C  
ATOM   2645  OH  TYR B  53      36.320   5.898 -36.588  1.00 49.10           O  
ANISOU 2645  OH  TYR B  53     4567   6282   7807    -13   -557    977       O  
ATOM   2646  N   VAL B  54      29.912  10.257 -40.680  1.00 57.32           N  
ANISOU 2646  N   VAL B  54     5186   7540   9053    636   -480   2267       N  
ATOM   2647  CA  VAL B  54      28.625  10.933 -40.565  1.00 48.94           C  
ANISOU 2647  CA  VAL B  54     4027   6510   8060    779   -389   2475       C  
ATOM   2648  C   VAL B  54      27.492  10.006 -40.984  1.00 51.09           C  
ANISOU 2648  C   VAL B  54     4190   6955   8269    691   -571   2537       C  
ATOM   2649  O   VAL B  54      26.423   9.992 -40.364  1.00 52.90           O  
ANISOU 2649  O   VAL B  54     4310   7222   8566    745   -509   2641       O  
ATOM   2650  CB  VAL B  54      28.627  12.230 -41.390  1.00 40.70           C  
ANISOU 2650  CB  VAL B  54     3003   5413   7047    939   -292   2665       C  
ATOM   2651  CG1 VAL B  54      27.210  12.764 -41.531  1.00 43.77           C  
ANISOU 2651  CG1 VAL B  54     3267   5879   7484   1075   -239   2901       C  
ATOM   2652  CG2 VAL B  54      29.531  13.260 -40.741  1.00 40.06           C  
ANISOU 2652  CG2 VAL B  54     3044   5116   7062   1051    -52   2631       C  
ATOM   2653  N   ALA B  55      27.700   9.230 -42.052  1.00 50.71           N  
ANISOU 2653  N   ALA B  55     4171   7003   8095    555   -790   2493       N  
ATOM   2654  CA  ALA B  55      26.656   8.322 -42.517  1.00 48.49           C  
ANISOU 2654  CA  ALA B  55     3802   6867   7754    451   -978   2558       C  
ATOM   2655  C   ALA B  55      26.333   7.258 -41.474  1.00 57.09           C  
ANISOU 2655  C   ALA B  55     4877   7963   8851    359   -979   2425       C  
ATOM   2656  O   ALA B  55      25.159   6.964 -41.222  1.00 66.07           O  
ANISOU 2656  O   ALA B  55     5886   9181  10038    353  -1006   2548       O  
ATOM   2657  CB  ALA B  55      27.073   7.675 -43.837  1.00 41.50           C  
ANISOU 2657  CB  ALA B  55     2999   6052   6715    317  -1204   2524       C  
ATOM   2658  N   VAL B  56      27.357   6.671 -40.853  1.00 52.00           N  
ANISOU 2658  N   VAL B  56     4358   7237   8162    291   -946   2189       N  
ATOM   2659  CA  VAL B  56      27.104   5.672 -39.817  1.00 53.87           C  
ANISOU 2659  CA  VAL B  56     4603   7471   8395    222   -936   2059       C  
ATOM   2660  C   VAL B  56      26.406   6.309 -38.624  1.00 66.88           C  
ANISOU 2660  C   VAL B  56     6159   9073  10178    349   -753   2158       C  
ATOM   2661  O   VAL B  56      25.571   5.678 -37.964  1.00 82.13           O  
ANISOU 2661  O   VAL B  56     8021  11046  12139    324   -753   2184       O  
ATOM   2662  CB  VAL B  56      28.414   4.979 -39.405  1.00 45.62           C  
ANISOU 2662  CB  VAL B  56     3712   6350   7270    144   -929   1798       C  
ATOM   2663  CG1 VAL B  56      28.904   4.083 -40.524  1.00 37.11           C  
ANISOU 2663  CG1 VAL B  56     2719   5324   6058     18  -1101   1722       C  
ATOM   2664  CG2 VAL B  56      29.458   6.016 -39.051  1.00 54.28           C  
ANISOU 2664  CG2 VAL B  56     4861   7333   8431    228   -787   1759       C  
ATOM   2665  N   PHE B  57      26.738   7.566 -38.325  1.00 56.42           N  
ANISOU 2665  N   PHE B  57     4839   7654   8943    493   -579   2229       N  
ATOM   2666  CA  PHE B  57      26.118   8.251 -37.195  1.00 56.26           C  
ANISOU 2666  CA  PHE B  57     4756   7566   9053    638   -369   2341       C  
ATOM   2667  C   PHE B  57      24.612   8.393 -37.391  1.00 63.80           C  
ANISOU 2667  C   PHE B  57     5532   8628  10081    706   -361   2596       C  
ATOM   2668  O   PHE B  57      23.823   8.038 -36.509  1.00 62.99           O  
ANISOU 2668  O   PHE B  57     5351   8540  10043    727   -291   2655       O  
ATOM   2669  CB  PHE B  57      26.776   9.619 -36.999  1.00 54.69           C  
ANISOU 2669  CB  PHE B  57     4622   7223   8933    789   -169   2385       C  
ATOM   2670  CG  PHE B  57      26.344  10.334 -35.749  1.00 55.52           C  
ANISOU 2670  CG  PHE B  57     4723   7212   9159    951     91   2471       C  
ATOM   2671  CD1 PHE B  57      26.809   9.935 -34.505  1.00 55.19           C  
ANISOU 2671  CD1 PHE B  57     4758   7078   9134    920    164   2316       C  
ATOM   2672  CD2 PHE B  57      25.481  11.415 -35.819  1.00 52.93           C  
ANISOU 2672  CD2 PHE B  57     4330   6858   8922   1147    281   2714       C  
ATOM   2673  CE1 PHE B  57      26.419  10.601 -33.353  1.00 53.89           C  
ANISOU 2673  CE1 PHE B  57     4619   6785   9072   1082    428   2400       C  
ATOM   2674  CE2 PHE B  57      25.087  12.083 -34.672  1.00 54.96           C  
ANISOU 2674  CE2 PHE B  57     4623   6985   9276   1317    566   2797       C  
ATOM   2675  CZ  PHE B  57      25.557  11.675 -33.438  1.00 56.10           C  
ANISOU 2675  CZ  PHE B  57     4860   7024   9431   1284    644   2637       C  
ATOM   2676  N   VAL B  58      24.194   8.912 -38.546  1.00 69.06           N  
ANISOU 2676  N   VAL B  58     6121   9375  10745    743   -434   2770       N  
ATOM   2677  CA  VAL B  58      22.768   9.107 -38.800  1.00 61.74           C  
ANISOU 2677  CA  VAL B  58     4994   8564   9901    809   -436   3046       C  
ATOM   2678  C   VAL B  58      22.052   7.768 -38.926  1.00 52.83           C  
ANISOU 2678  C   VAL B  58     3777   7565   8733    633   -641   3039       C  
ATOM   2679  O   VAL B  58      21.009   7.542 -38.302  1.00 57.79           O  
ANISOU 2679  O   VAL B  58     4257   8242   9456    661   -585   3188       O  
ATOM   2680  CB  VAL B  58      22.561   9.975 -40.052  1.00 60.09           C  
ANISOU 2680  CB  VAL B  58     4730   8414   9688    888   -486   3234       C  
ATOM   2681  CG1 VAL B  58      23.029  11.383 -39.781  1.00 50.56           C  
ANISOU 2681  CG1 VAL B  58     3601   7063   8547   1099   -228   3291       C  
ATOM   2682  CG2 VAL B  58      23.310   9.377 -41.232  1.00 69.20           C  
ANISOU 2682  CG2 VAL B  58     5984   9619  10689    724   -735   3099       C  
ATOM   2683  N   VAL B  59      22.594   6.865 -39.744  1.00 46.19           N  
ANISOU 2683  N   VAL B  59     3029   6770   7752    454   -867   2882       N  
ATOM   2684  CA  VAL B  59      21.907   5.604 -40.002  1.00 47.12           C  
ANISOU 2684  CA  VAL B  59     3083   6998   7823    281  -1066   2889       C  
ATOM   2685  C   VAL B  59      21.748   4.798 -38.719  1.00 45.91           C  
ANISOU 2685  C   VAL B  59     2937   6801   7707    245   -986   2786       C  
ATOM   2686  O   VAL B  59      20.682   4.229 -38.456  1.00 48.17           O  
ANISOU 2686  O   VAL B  59     3062   7170   8069    189  -1032   2958       O  
ATOM   2687  CB  VAL B  59      22.650   4.800 -41.081  1.00 45.92           C  
ANISOU 2687  CB  VAL B  59     3076   6871   7503    110  -1287   2729       C  
ATOM   2688  CG1 VAL B  59      21.982   3.453 -41.266  1.00 47.10           C  
ANISOU 2688  CG1 VAL B  59     3182   7108   7606    -80  -1477   2743       C  
ATOM   2689  CG2 VAL B  59      22.676   5.577 -42.382  1.00 47.67           C  
ANISOU 2689  CG2 VAL B  59     3277   7148   7686    143  -1384   2872       C  
ATOM   2690  N   ALA B  60      22.804   4.728 -37.904  1.00 52.59           N  
ANISOU 2690  N   ALA B  60     3950   7521   8511    267   -874   2546       N  
ATOM   2691  CA  ALA B  60      22.721   3.962 -36.663  1.00 45.83           C  
ANISOU 2691  CA  ALA B  60     3105   6619   7689    234   -803   2469       C  
ATOM   2692  C   ALA B  60      21.703   4.563 -35.700  1.00 51.56           C  
ANISOU 2692  C   ALA B  60     3680   7340   8570    382   -615   2670       C  
ATOM   2693  O   ALA B  60      20.941   3.831 -35.057  1.00 50.22           O  
ANISOU 2693  O   ALA B  60     3411   7209   8463    337   -615   2758       O  
ATOM   2694  CB  ALA B  60      24.097   3.884 -36.002  1.00 41.05           C  
ANISOU 2694  CB  ALA B  60     2701   5887   7008    237   -727   2186       C  
ATOM   2695  N   LEU B  61      21.677   5.893 -35.583  1.00 64.55           N  
ANISOU 2695  N   LEU B  61     5300   8930  10297    563   -434   2788       N  
ATOM   2696  CA  LEU B  61      20.721   6.538 -34.688  1.00 68.74           C  
ANISOU 2696  CA  LEU B  61     5695   9439  10984    731   -207   3019       C  
ATOM   2697  C   LEU B  61      19.299   6.387 -35.207  1.00 70.11           C  
ANISOU 2697  C   LEU B  61     5625   9767  11247    726   -280   3317       C  
ATOM   2698  O   LEU B  61      18.404   5.935 -34.482  1.00 70.20           O  
ANISOU 2698  O   LEU B  61     5507   9815  11350    736   -221   3449       O  
ATOM   2699  CB  LEU B  61      21.072   8.017 -34.513  1.00 65.41           C  
ANISOU 2699  CB  LEU B  61     5326   8900  10627    938     32   3099       C  
ATOM   2700  CG  LEU B  61      22.404   8.331 -33.828  1.00 61.54           C  
ANISOU 2700  CG  LEU B  61     5052   8241  10087    961    140   2856       C  
ATOM   2701  CD1 LEU B  61      22.726   9.817 -33.923  1.00 67.13           C  
ANISOU 2701  CD1 LEU B  61     5824   8831  10852   1153    360   2952       C  
ATOM   2702  CD2 LEU B  61      22.380   7.871 -32.382  1.00 51.57           C  
ANISOU 2702  CD2 LEU B  61     3836   6898   8862    978    272   2778       C  
ATOM   2703  N   VAL B  62      19.070   6.756 -36.468  1.00 70.03           N  
ANISOU 2703  N   VAL B  62     5538   9854  11217    708   -415   3442       N  
ATOM   2704  CA  VAL B  62      17.735   6.627 -37.046  1.00 69.24           C  
ANISOU 2704  CA  VAL B  62     5185   9918  11205    686   -516   3747       C  
ATOM   2705  C   VAL B  62      17.272   5.175 -37.004  1.00 73.18           C  
ANISOU 2705  C   VAL B  62     5611  10507  11686    468   -718   3745       C  
ATOM   2706  O   VAL B  62      16.144   4.875 -36.594  1.00 82.00           O  
ANISOU 2706  O   VAL B  62     6517  11709  12932    470   -693   3991       O  
ATOM   2707  CB  VAL B  62      17.714   7.179 -38.481  1.00 61.85           C  
ANISOU 2707  CB  VAL B  62     4203   9072  10225    677   -667   3860       C  
ATOM   2708  CG1 VAL B  62      16.448   6.729 -39.184  1.00 62.02           C  
ANISOU 2708  CG1 VAL B  62     3973   9284  10308    579   -860   4140       C  
ATOM   2709  CG2 VAL B  62      17.820   8.688 -38.460  1.00 64.60           C  
ANISOU 2709  CG2 VAL B  62     4550   9347  10649    922   -427   3997       C  
ATOM   2710  N   GLY B  63      18.137   4.253 -37.432  1.00 68.82           N  
ANISOU 2710  N   GLY B  63     5233   9935  10980    281   -908   3489       N  
ATOM   2711  CA  GLY B  63      17.758   2.848 -37.455  1.00 61.02           C  
ANISOU 2711  CA  GLY B  63     4209   9016   9960     68  -1099   3483       C  
ATOM   2712  C   GLY B  63      17.471   2.283 -36.076  1.00 56.56           C  
ANISOU 2712  C   GLY B  63     3618   8398   9475     90   -961   3467       C  
ATOM   2713  O   GLY B  63      16.419   1.684 -35.843  1.00 57.01           O  
ANISOU 2713  O   GLY B  63     3488   8546   9627     23  -1013   3673       O  
ATOM   2714  N   ASN B  64      18.409   2.460 -35.141  1.00 65.94           N  
ANISOU 2714  N   ASN B  64     4990   9439  10624    180   -792   3228       N  
ATOM   2715  CA  ASN B  64      18.251   1.847 -33.824  1.00 64.90           C  
ANISOU 2715  CA  ASN B  64     4864   9250  10545    193   -676   3181       C  
ATOM   2716  C   ASN B  64      17.080   2.442 -33.054  1.00 62.61           C  
ANISOU 2716  C   ASN B  64     4365   8986  10440    357   -473   3471       C  
ATOM   2717  O   ASN B  64      16.463   1.748 -32.237  1.00 64.48           O  
ANISOU 2717  O   ASN B  64     4513   9236  10751    334   -432   3549       O  
ATOM   2718  CB  ASN B  64      19.544   1.984 -33.019  1.00 57.71           C  
ANISOU 2718  CB  ASN B  64     4194   8185   9549    251   -553   2873       C  
ATOM   2719  CG  ASN B  64      20.608   1.011 -33.475  1.00 44.47           C  
ANISOU 2719  CG  ASN B  64     2705   6483   7708     81   -732   2604       C  
ATOM   2720  OD1 ASN B  64      20.416  -0.205 -33.409  1.00 43.79           O  
ANISOU 2720  OD1 ASN B  64     2619   6432   7586    -63   -856   2571       O  
ATOM   2721  ND2 ASN B  64      21.732   1.534 -33.946  1.00 41.48           N  
ANISOU 2721  ND2 ASN B  64     2486   6042   7233    103   -734   2423       N  
ATOM   2722  N   THR B  65      16.750   3.709 -33.295  1.00 57.32           N  
ANISOU 2722  N   THR B  65     3614   8318   9847    535   -328   3645       N  
ATOM   2723  CA  THR B  65      15.558   4.263 -32.666  1.00 64.66           C  
ANISOU 2723  CA  THR B  65     4331   9277  10958    705   -117   3965       C  
ATOM   2724  C   THR B  65      14.296   3.634 -33.237  1.00 62.59           C  
ANISOU 2724  C   THR B  65     3786   9199  10797    589   -288   4274       C  
ATOM   2725  O   THR B  65      13.334   3.378 -32.501  1.00 67.76           O  
ANISOU 2725  O   THR B  65     4262   9890  11592    640   -179   4495       O  
ATOM   2726  CB  THR B  65      15.519   5.779 -32.834  1.00 59.87           C  
ANISOU 2726  CB  THR B  65     3718   8621  10409    936     97   4096       C  
ATOM   2727  OG1 THR B  65      16.800   6.334 -32.508  1.00 56.46           O  
ANISOU 2727  OG1 THR B  65     3546   8026   9880    999    207   3828       O  
ATOM   2728  CG2 THR B  65      14.465   6.373 -31.918  1.00 63.38           C  
ANISOU 2728  CG2 THR B  65     3996   9045  11041   1154    403   4420       C  
ATOM   2729  N   LEU B  66      14.279   3.376 -34.547  1.00 68.91           N  
ANISOU 2729  N   LEU B  66     4541  10116  11526    429   -559   4303       N  
ATOM   2730  CA  LEU B  66      13.139   2.699 -35.152  1.00 74.86           C  
ANISOU 2730  CA  LEU B  66     5037  11050  12357    275   -768   4585       C  
ATOM   2731  C   LEU B  66      13.025   1.259 -34.675  1.00 84.19           C  
ANISOU 2731  C   LEU B  66     6236  12242  13511     77   -901   4495       C  
ATOM   2732  O   LEU B  66      11.919   0.711 -34.618  1.00 99.47           O  
ANISOU 2732  O   LEU B  66     7931  14299  15564     -6   -980   4763       O  
ATOM   2733  CB  LEU B  66      13.248   2.744 -36.678  1.00 68.29           C  
ANISOU 2733  CB  LEU B  66     4197  10325  11426    134  -1040   4607       C  
ATOM   2734  CG  LEU B  66      13.209   4.136 -37.312  1.00 77.53           C  
ANISOU 2734  CG  LEU B  66     5312  11515  12632    320   -942   4744       C  
ATOM   2735  CD1 LEU B  66      13.204   4.039 -38.830  1.00 83.55           C  
ANISOU 2735  CD1 LEU B  66     6050  12399  13295    161  -1243   4788       C  
ATOM   2736  CD2 LEU B  66      12.001   4.919 -36.817  1.00 73.84           C  
ANISOU 2736  CD2 LEU B  66     4561  11114  12382    526   -725   5135       C  
ATOM   2737  N   VAL B  67      14.150   0.629 -34.333  1.00 62.52           N  
ANISOU 2737  N   VAL B  67     3764   9374  10616      1   -926   4133       N  
ATOM   2738  CA  VAL B  67      14.091  -0.741 -33.840  1.00 70.74           C  
ANISOU 2738  CA  VAL B  67     4840  10413  11625   -170  -1034   4037       C  
ATOM   2739  C   VAL B  67      13.374  -0.794 -32.500  1.00 75.67           C  
ANISOU 2739  C   VAL B  67     5329  11013  12409    -44   -814   4183       C  
ATOM   2740  O   VAL B  67      12.634  -1.742 -32.210  1.00 72.89           O  
ANISOU 2740  O   VAL B  67     4842  10731  12122   -165   -900   4308       O  
ATOM   2741  CB  VAL B  67      15.505  -1.335 -33.748  1.00 58.52           C  
ANISOU 2741  CB  VAL B  67     3612   8737   9887   -248  -1081   3631       C  
ATOM   2742  CG1 VAL B  67      15.458  -2.692 -33.070  1.00 56.60           C  
ANISOU 2742  CG1 VAL B  67     3412   8475   9619   -385  -1144   3533       C  
ATOM   2743  CG2 VAL B  67      16.115  -1.447 -35.133  1.00 56.54           C  
ANISOU 2743  CG2 VAL B  67     3483   8517   9482   -386  -1304   3517       C  
ATOM   2744  N   CYS B  68      13.585   0.218 -31.658  1.00 76.85           N  
ANISOU 2744  N   CYS B  68     5525  11055  12621    200   -521   4171       N  
ATOM   2745  CA  CYS B  68      12.873   0.276 -30.389  1.00 76.68           C  
ANISOU 2745  CA  CYS B  68     5386  10996  12751    347   -277   4330       C  
ATOM   2746  C   CYS B  68      11.409   0.632 -30.598  1.00 87.44           C  
ANISOU 2746  C   CYS B  68     6408  12501  14316    415   -232   4779       C  
ATOM   2747  O   CYS B  68      10.525   0.067 -29.943  1.00 98.07           O  
ANISOU 2747  O   CYS B  68     7574  13895  15793    409   -181   4976       O  
ATOM   2748  CB  CYS B  68      13.544   1.285 -29.458  1.00 75.85           C  
ANISOU 2748  CB  CYS B  68     5462  10719  12637    585     31   4189       C  
ATOM   2749  SG  CYS B  68      15.269   0.912 -29.067  1.00 68.44           S  
ANISOU 2749  SG  CYS B  68     4893   9626  11486    513    -10   3693       S  
ATOM   2750  N   LEU B  69      11.135   1.576 -31.500  1.00 89.41           N  
ANISOU 2750  N   LEU B  69     6550  12822  14598    487   -245   4960       N  
ATOM   2751  CA  LEU B  69       9.753   1.962 -31.764  1.00 91.93           C  
ANISOU 2751  CA  LEU B  69     6521  13291  15116    559   -208   5416       C  
ATOM   2752  C   LEU B  69       8.961   0.813 -32.374  1.00 94.34           C  
ANISOU 2752  C   LEU B  69     6612  13776  15457    291   -523   5589       C  
ATOM   2753  O   LEU B  69       7.765   0.662 -32.101  1.00106.55           O  
ANISOU 2753  O   LEU B  69     7858  15436  17192    313   -482   5949       O  
ATOM   2754  CB  LEU B  69       9.716   3.184 -32.680  1.00 94.88           C  
ANISOU 2754  CB  LEU B  69     6840  13710  15499    683   -178   5555       C  
ATOM   2755  CG  LEU B  69      10.168   4.513 -32.069  1.00102.40           C  
ANISOU 2755  CG  LEU B  69     7942  14499  16465    983    179   5503       C  
ATOM   2756  CD1 LEU B  69      10.902   5.354 -33.102  1.00104.66           C  
ANISOU 2756  CD1 LEU B  69     8357  14775  16635   1006    103   5378       C  
ATOM   2757  CD2 LEU B  69       8.971   5.267 -31.515  1.00112.26           C  
ANISOU 2757  CD2 LEU B  69     8940  15779  17935   1233    478   5927       C  
ATOM   2758  N   ALA B  70       9.608  -0.006 -33.207  1.00 86.07           N  
ANISOU 2758  N   ALA B  70     5719  12754  14231     34   -832   5348       N  
ATOM   2759  CA  ALA B  70       8.900  -1.108 -33.852  1.00 90.40           C  
ANISOU 2759  CA  ALA B  70     6102  13459  14786   -247  -1148   5498       C  
ATOM   2760  C   ALA B  70       8.469  -2.158 -32.837  1.00 93.03           C  
ANISOU 2760  C   ALA B  70     6374  13779  15193   -318  -1115   5516       C  
ATOM   2761  O   ALA B  70       7.365  -2.707 -32.931  1.00100.58           O  
ANISOU 2761  O   ALA B  70     7052  14883  16281   -441  -1238   5822       O  
ATOM   2762  CB  ALA B  70       9.777  -1.738 -34.933  1.00 91.47           C  
ANISOU 2762  CB  ALA B  70     6474  13588  14692   -488  -1450   5214       C  
ATOM   2763  N   VAL B  71       9.331  -2.458 -31.864  1.00 88.62           N  
ANISOU 2763  N   VAL B  71     6065  13053  14553   -251   -959   5197       N  
ATOM   2764  CA  VAL B  71       8.966  -3.419 -30.827  1.00 79.33           C  
ANISOU 2764  CA  VAL B  71     4843  11855  13445   -297   -904   5200       C  
ATOM   2765  C   VAL B  71       7.973  -2.816 -29.848  1.00 80.02           C  
ANISOU 2765  C   VAL B  71     4683  11954  13769    -62   -605   5525       C  
ATOM   2766  O   VAL B  71       7.123  -3.526 -29.296  1.00 82.77           O  
ANISOU 2766  O   VAL B  71     4833  12366  14249   -118   -601   5718       O  
ATOM   2767  CB  VAL B  71      10.228  -3.922 -30.102  1.00 71.44           C  
ANISOU 2767  CB  VAL B  71     4186  10678  12280   -296   -835   4763       C  
ATOM   2768  CG1 VAL B  71       9.845  -4.863 -28.975  1.00 71.82           C  
ANISOU 2768  CG1 VAL B  71     4184  10701  12403   -324   -756   4769       C  
ATOM   2769  CG2 VAL B  71      11.169  -4.601 -31.088  1.00 68.74           C  
ANISOU 2769  CG2 VAL B  71     4079  10324  11714   -520  -1113   4474       C  
ATOM   2770  N   TRP B  72       8.061  -1.506 -29.611  1.00 79.97           N  
ANISOU 2770  N   TRP B  72     4690  11877  13819    210   -336   5597       N  
ATOM   2771  CA  TRP B  72       7.162  -0.860 -28.661  1.00 90.69           C  
ANISOU 2771  CA  TRP B  72     5850  13216  15392    469     -2   5911       C  
ATOM   2772  C   TRP B  72       5.733  -0.791 -29.186  1.00 97.28           C  
ANISOU 2772  C   TRP B  72     6269  14256  16436    445    -76   6408       C  
ATOM   2773  O   TRP B  72       4.782  -1.046 -28.439  1.00 98.16           O  
ANISOU 2773  O   TRP B  72     6152  14408  16737    518     69   6687       O  
ATOM   2774  CB  TRP B  72       7.678   0.540 -28.336  1.00 96.41           C  
ANISOU 2774  CB  TRP B  72     6736  13796  16101    760    310   5851       C  
ATOM   2775  CG  TRP B  72       6.809   1.326 -27.403  1.00105.74           C  
ANISOU 2775  CG  TRP B  72     7765  14928  17485   1058    699   6176       C  
ATOM   2776  CD1 TRP B  72       6.680   1.147 -26.056  1.00105.34           C  
ANISOU 2776  CD1 TRP B  72     7774  14748  17504   1202    979   6175       C  
ATOM   2777  CD2 TRP B  72       5.979   2.445 -27.741  1.00115.74           C  
ANISOU 2777  CD2 TRP B  72     8812  16258  18907   1268    880   6566       C  
ATOM   2778  NE1 TRP B  72       5.807   2.076 -25.538  1.00113.41           N  
ANISOU 2778  NE1 TRP B  72     8632  15736  18723   1493   1341   6569       N  
ATOM   2779  CE2 TRP B  72       5.365   2.885 -26.552  1.00120.07           C  
ANISOU 2779  CE2 TRP B  72     9299  16699  19621   1542   1289   6812       C  
ATOM   2780  CE3 TRP B  72       5.691   3.112 -28.935  1.00125.83           C  
ANISOU 2780  CE3 TRP B  72     9934  17669  20206   1259    749   6762       C  
ATOM   2781  CZ2 TRP B  72       4.479   3.962 -26.523  1.00132.54           C  
ANISOU 2781  CZ2 TRP B  72    10677  18297  21385   1815   1584   7245       C  
ATOM   2782  CZ3 TRP B  72       4.813   4.181 -28.905  1.00135.36           C  
ANISOU 2782  CZ3 TRP B  72    10929  18910  21593   1522   1020   7169       C  
ATOM   2783  CH2 TRP B  72       4.217   4.595 -27.707  1.00138.05           C  
ANISOU 2783  CH2 TRP B  72    11216  19137  22097   1801   1442   7416       C  
ATOM   2784  N   ARG B  73       5.559  -0.439 -30.463  1.00 93.71           N  
ANISOU 2784  N   ARG B  73     5706  13940  15960    345   -298   6538       N  
ATOM   2785  CA  ARG B  73       4.212  -0.314 -31.011  1.00 97.49           C  
ANISOU 2785  CA  ARG B  73     5771  14631  16640    317   -385   7034       C  
ATOM   2786  C   ARG B  73       3.574  -1.677 -31.252  1.00103.85           C  
ANISOU 2786  C   ARG B  73     6395  15586  17479      1   -701   7142       C  
ATOM   2787  O   ARG B  73       2.382  -1.864 -30.978  1.00124.42           O  
ANISOU 2787  O   ARG B  73     8649  18321  20303     11   -668   7546       O  
ATOM   2788  CB  ARG B  73       4.234   0.519 -32.292  1.00101.82           C  
ANISOU 2788  CB  ARG B  73     6259  15281  17146    311   -527   7143       C  
ATOM   2789  CG  ARG B  73       4.369   2.006 -32.036  1.00114.57           C  
ANISOU 2789  CG  ARG B  73     7916  16798  18818    661   -172   7224       C  
ATOM   2790  CD  ARG B  73       3.986   2.833 -33.254  1.00127.44           C  
ANISOU 2790  CD  ARG B  73     9364  18577  20479    680   -291   7477       C  
ATOM   2791  NE  ARG B  73       4.053   4.262 -32.963  1.00138.39           N  
ANISOU 2791  NE  ARG B  73    10789  19865  21929   1030     78   7577       N  
ATOM   2792  CZ  ARG B  73       5.158   4.992 -33.070  1.00145.66           C  
ANISOU 2792  CZ  ARG B  73    12031  20626  22685   1137    182   7249       C  
ATOM   2793  NH1 ARG B  73       6.292   4.427 -33.462  1.00143.33           N  
ANISOU 2793  NH1 ARG B  73    12030  20263  22165    932    -50   6812       N  
ATOM   2794  NH2 ARG B  73       5.133   6.286 -32.780  1.00149.17           N  
ANISOU 2794  NH2 ARG B  73    12508  20977  23192   1454    529   7369       N  
ATOM   2795  N   ASN B  74       4.339  -2.638 -31.765  1.00 96.70           N  
ANISOU 2795  N   ASN B  74     5723  14659  16359   -279   -999   6801       N  
ATOM   2796  CA  ASN B  74       3.799  -3.961 -32.065  1.00 99.04           C  
ANISOU 2796  CA  ASN B  74     5893  15082  16656   -605  -1313   6878       C  
ATOM   2797  C   ASN B  74       3.969  -4.860 -30.847  1.00 99.48           C  
ANISOU 2797  C   ASN B  74     6051  15025  16720   -611  -1185   6698       C  
ATOM   2798  O   ASN B  74       5.087  -5.256 -30.498  1.00107.74           O  
ANISOU 2798  O   ASN B  74     7444  15911  17580   -630  -1161   6272       O  
ATOM   2799  CB  ASN B  74       4.477  -4.576 -33.286  1.00 97.19           C  
ANISOU 2799  CB  ASN B  74     5873  14873  16180   -908  -1689   6627       C  
ATOM   2800  CG  ASN B  74       4.271  -3.755 -34.537  1.00103.84           C  
ANISOU 2800  CG  ASN B  74     6608  15836  17009   -925  -1841   6812       C  
ATOM   2801  OD1 ASN B  74       4.378  -2.528 -34.509  1.00108.42           O  
ANISOU 2801  OD1 ASN B  74     7164  16384  17649   -657  -1615   6884       O  
ATOM   2802  ND2 ASN B  74       3.969  -4.422 -35.643  1.00102.11           N  
ANISOU 2802  ND2 ASN B  74     6336  15755  16708  -1245  -2224   6892       N  
ATOM   2803  N   HIS B  75       2.845  -5.189 -30.219  1.00101.38           N  
ANISOU 2803  N   HIS B  75     5974  15361  17185   -595  -1106   7039       N  
ATOM   2804  CA  HIS B  75       2.842  -6.056 -29.050  1.00100.23           C  
ANISOU 2804  CA  HIS B  75     5877  15130  17077   -600   -979   6921       C  
ATOM   2805  C   HIS B  75       3.166  -7.500 -29.425  1.00109.60           C  
ANISOU 2805  C   HIS B  75     7203  16340  18101   -964  -1316   6686       C  
ATOM   2806  O   HIS B  75       3.716  -8.246 -28.604  1.00107.28           O  
ANISOU 2806  O   HIS B  75     7110  15923  17731   -986  -1239   6403       O  
ATOM   2807  CB  HIS B  75       1.505  -5.929 -28.325  1.00118.07           C  
ANISOU 2807  CB  HIS B  75     7736  17488  19639   -466   -781   7386       C  
ATOM   2808  CG  HIS B  75       1.363  -4.640 -27.576  1.00118.24           C  
ANISOU 2808  CG  HIS B  75     7720  17409  19798    -60   -349   7540       C  
ATOM   2809  ND1 HIS B  75       1.103  -3.439 -28.201  1.00119.75           N  
ANISOU 2809  ND1 HIS B  75     7793  17656  20053    109   -271   7776       N  
ATOM   2810  CD2 HIS B  75       1.497  -4.352 -26.261  1.00116.58           C  
ANISOU 2810  CD2 HIS B  75     7611  17030  19653    211     40   7477       C  
ATOM   2811  CE1 HIS B  75       1.056  -2.472 -27.304  1.00119.08           C  
ANISOU 2811  CE1 HIS B  75     7740  17436  20070    468    155   7861       C  
ATOM   2812  NE2 HIS B  75       1.292  -3.000 -26.117  1.00117.80           N  
ANISOU 2812  NE2 HIS B  75     7720  17133  19908    534    349   7682       N  
ATOM   2813  N   HIS B  76       2.821  -7.921 -30.646  1.00115.74           N  
ANISOU 2813  N   HIS B  76     7886  17271  18820  -1255  -1685   6807       N  
ATOM   2814  CA  HIS B  76       3.146  -9.269 -31.100  1.00123.18           C  
ANISOU 2814  CA  HIS B  76     9001  18218  19584  -1610  -2005   6586       C  
ATOM   2815  C   HIS B  76       4.621  -9.430 -31.420  1.00115.46           C  
ANISOU 2815  C   HIS B  76     8481  17070  18318  -1638  -2051   6089       C  
ATOM   2816  O   HIS B  76       5.122 -10.561 -31.442  1.00118.04           O  
ANISOU 2816  O   HIS B  76     9027  17336  18488  -1855  -2206   5830       O  
ATOM   2817  CB  HIS B  76       2.370  -9.598 -32.375  1.00144.93           C  
ANISOU 2817  CB  HIS B  76    11555  21175  22339  -1922  -2391   6866       C  
ATOM   2818  CG  HIS B  76       2.672  -8.662 -33.501  1.00159.91           C  
ANISOU 2818  CG  HIS B  76    13504  23109  24145  -1885  -2492   6886       C  
ATOM   2819  ND1 HIS B  76       3.782  -8.805 -34.306  1.00160.12           N  
ANISOU 2819  ND1 HIS B  76    13903  23036  23900  -1994  -2648   6521       N  
ATOM   2820  CD2 HIS B  76       2.031  -7.557 -33.940  1.00167.39           C  
ANISOU 2820  CD2 HIS B  76    14181  24178  25241  -1736  -2442   7230       C  
ATOM   2821  CE1 HIS B  76       3.808  -7.835 -35.200  1.00161.23           C  
ANISOU 2821  CE1 HIS B  76    14000  23236  24023  -1925  -2698   6629       C  
ATOM   2822  NE2 HIS B  76       2.754  -7.064 -35.000  1.00165.14           N  
ANISOU 2822  NE2 HIS B  76    14109  23869  24769  -1770  -2578   7055       N  
ATOM   2823  N   MET B  77       5.316  -8.328 -31.664  1.00108.94           N  
ANISOU 2823  N   MET B  77     7797  16166  17429  -1421  -1911   5967       N  
ATOM   2824  CA  MET B  77       6.739  -8.316 -31.948  1.00 92.52           C  
ANISOU 2824  CA  MET B  77     6123  13929  15102  -1409  -1922   5525       C  
ATOM   2825  C   MET B  77       7.588  -8.352 -30.686  1.00 87.84           C  
ANISOU 2825  C   MET B  77     5750  13150  14473  -1212  -1637   5221       C  
ATOM   2826  O   MET B  77       8.817  -8.381 -30.784  1.00 91.65           O  
ANISOU 2826  O   MET B  77     6561  13499  14764  -1192  -1627   4855       O  
ATOM   2827  CB  MET B  77       7.076  -7.077 -32.793  1.00 87.47           C  
ANISOU 2827  CB  MET B  77     5515  13298  14421  -1275  -1904   5549       C  
ATOM   2828  CG  MET B  77       8.245  -7.251 -33.751  1.00 88.96           C  
ANISOU 2828  CG  MET B  77     6044  13408  14349  -1399  -2081   5207       C  
ATOM   2829  SD  MET B  77       8.496  -5.726 -34.672  1.00 96.85           S  
ANISOU 2829  SD  MET B  77     7028  14433  15336  -1226  -2036   5281       S  
ATOM   2830  CE  MET B  77       7.213  -5.891 -35.914  1.00103.70           C  
ANISOU 2830  CE  MET B  77     7579  15543  16279  -1477  -2375   5703       C  
ATOM   2831  N   ARG B  78       6.966  -8.341 -29.507  1.00 87.22           N  
ANISOU 2831  N   ARG B  78     5498  13063  14578  -1065  -1404   5375       N  
ATOM   2832  CA  ARG B  78       7.699  -8.360 -28.240  1.00 91.46           C  
ANISOU 2832  CA  ARG B  78     6236  13428  15088   -881  -1130   5110       C  
ATOM   2833  C   ARG B  78       8.077  -9.795 -27.876  1.00 90.84           C  
ANISOU 2833  C   ARG B  78     6313  13303  14900  -1091  -1253   4871       C  
ATOM   2834  O   ARG B  78       7.608 -10.389 -26.901  1.00 88.84           O  
ANISOU 2834  O   ARG B  78     5959  13043  14754  -1085  -1138   4932       O  
ATOM   2835  CB  ARG B  78       6.892  -7.681 -27.145  1.00 81.36           C  
ANISOU 2835  CB  ARG B  78     4731  12142  14041   -617   -801   5378       C  
ATOM   2836  CG  ARG B  78       6.735  -6.187 -27.410  1.00 82.37           C  
ANISOU 2836  CG  ARG B  78     4777  12271  14249   -370   -626   5560       C  
ATOM   2837  CD  ARG B  78       5.330  -5.700 -27.146  1.00104.00           C  
ANISOU 2837  CD  ARG B  78     7127  15128  17260   -238   -477   6046       C  
ATOM   2838  NE  ARG B  78       5.196  -4.992 -25.875  1.00106.14           N  
ANISOU 2838  NE  ARG B  78     7401  15270  17655     82    -62   6114       N  
ATOM   2839  CZ  ARG B  78       4.799  -3.727 -25.755  1.00114.45           C  
ANISOU 2839  CZ  ARG B  78     8350  16302  18831    357    200   6356       C  
ATOM   2840  NH1 ARG B  78       4.457  -3.031 -26.829  1.00123.82           N  
ANISOU 2840  NH1 ARG B  78     9388  17608  20050    351     83   6569       N  
ATOM   2841  NH2 ARG B  78       4.707  -3.170 -24.551  1.00114.45           N  
ANISOU 2841  NH2 ARG B  78     8402  16160  18924    640    592   6400       N  
ATOM   2842  N   THR B  79       8.948 -10.351 -28.706  1.00 87.53           N  
ANISOU 2842  N   THR B  79     6151  12848  14261  -1276  -1479   4601       N  
ATOM   2843  CA  THR B  79       9.500 -11.667 -28.472  1.00 83.86           C  
ANISOU 2843  CA  THR B  79     5891  12315  13658  -1463  -1586   4340       C  
ATOM   2844  C   THR B  79      10.702 -11.555 -27.553  1.00 86.93           C  
ANISOU 2844  C   THR B  79     6554  12530  13946  -1285  -1369   3995       C  
ATOM   2845  O   THR B  79      11.289 -10.481 -27.392  1.00 89.15           O  
ANISOU 2845  O   THR B  79     6923  12737  14212  -1065  -1200   3911       O  
ATOM   2846  CB  THR B  79       9.912 -12.315 -29.792  1.00 84.27           C  
ANISOU 2846  CB  THR B  79     6114  12391  13512  -1729  -1905   4220       C  
ATOM   2847  OG1 THR B  79       8.836 -12.209 -30.732  1.00 97.19           O  
ANISOU 2847  OG1 THR B  79     7499  14196  15232  -1890  -2119   4555       O  
ATOM   2848  CG2 THR B  79      10.241 -13.773 -29.583  1.00 86.03           C  
ANISOU 2848  CG2 THR B  79     6513  12557  13616  -1946  -2021   4018       C  
ATOM   2849  N   VAL B  80      11.063 -12.681 -26.935  1.00 87.99           N  
ANISOU 2849  N   VAL B  80     6823  12599  14013  -1391  -1377   3802       N  
ATOM   2850  CA  VAL B  80      12.269 -12.697 -26.113  1.00 77.52           C  
ANISOU 2850  CA  VAL B  80     5762  11117  12574  -1255  -1206   3473       C  
ATOM   2851  C   VAL B  80      13.467 -12.261 -26.946  1.00 65.43           C  
ANISOU 2851  C   VAL B  80     4488   9517  10856  -1230  -1284   3233       C  
ATOM   2852  O   VAL B  80      14.260 -11.406 -26.530  1.00 67.10           O  
ANISOU 2852  O   VAL B  80     4822   9638  11034  -1030  -1113   3089       O  
ATOM   2853  CB  VAL B  80      12.482 -14.086 -25.486  1.00 78.86           C  
ANISOU 2853  CB  VAL B  80     6039  11237  12685  -1406  -1237   3312       C  
ATOM   2854  CG1 VAL B  80      12.527 -15.168 -26.562  1.00 83.69           C  
ANISOU 2854  CG1 VAL B  80     6750  11886  13164  -1701  -1534   3258       C  
ATOM   2855  CG2 VAL B  80      13.756 -14.087 -24.663  1.00 76.37           C  
ANISOU 2855  CG2 VAL B  80     5988  10774  12254  -1269  -1075   2992       C  
ATOM   2856  N   THR B  81      13.605 -12.835 -28.144  1.00 58.98           N  
ANISOU 2856  N   THR B  81     3758   8740   9914  -1442  -1540   3197       N  
ATOM   2857  CA  THR B  81      14.665 -12.425 -29.057  1.00 58.60           C  
ANISOU 2857  CA  THR B  81     3932   8634   9697  -1425  -1613   3002       C  
ATOM   2858  C   THR B  81      14.620 -10.925 -29.316  1.00 61.24           C  
ANISOU 2858  C   THR B  81     4176   8989  10101  -1230  -1504   3111       C  
ATOM   2859  O   THR B  81      15.640 -10.235 -29.220  1.00 64.60           O  
ANISOU 2859  O   THR B  81     4772   9322  10450  -1081  -1391   2915       O  
ATOM   2860  CB  THR B  81      14.547 -13.194 -30.371  1.00 62.05           C  
ANISOU 2860  CB  THR B  81     4440   9124  10012  -1687  -1901   3019       C  
ATOM   2861  OG1 THR B  81      14.752 -14.585 -30.118  1.00 72.93           O  
ANISOU 2861  OG1 THR B  81     5955  10453  11302  -1862  -1982   2880       O  
ATOM   2862  CG2 THR B  81      15.585 -12.704 -31.360  1.00 55.74           C  
ANISOU 2862  CG2 THR B  81     3855   8271   9054  -1657  -1957   2842       C  
ATOM   2863  N   ASN B  82      13.438 -10.402 -29.654  1.00 66.27           N  
ANISOU 2863  N   ASN B  82     4540   9751  10888  -1234  -1539   3436       N  
ATOM   2864  CA  ASN B  82      13.336  -8.983 -29.981  1.00 64.70           C  
ANISOU 2864  CA  ASN B  82     4249   9575  10758  -1054  -1437   3562       C  
ATOM   2865  C   ASN B  82      13.581  -8.103 -28.761  1.00 65.63           C  
ANISOU 2865  C   ASN B  82     4372   9601  10965   -783  -1126   3523       C  
ATOM   2866  O   ASN B  82      14.003  -6.949 -28.905  1.00 63.77           O  
ANISOU 2866  O   ASN B  82     4184   9323  10725   -617  -1008   3496       O  
ATOM   2867  CB  ASN B  82      11.966  -8.678 -30.586  1.00 65.51           C  
ANISOU 2867  CB  ASN B  82     4034   9842  11012  -1118  -1541   3953       C  
ATOM   2868  CG  ASN B  82      11.862  -9.103 -32.031  1.00 67.27           C  
ANISOU 2868  CG  ASN B  82     4283  10153  11123  -1362  -1852   3995       C  
ATOM   2869  OD1 ASN B  82      12.859  -9.120 -32.754  1.00 64.64           O  
ANISOU 2869  OD1 ASN B  82     4198   9753  10610  -1406  -1938   3757       O  
ATOM   2870  ND2 ASN B  82      10.660  -9.459 -32.459  1.00 71.97           N  
ANISOU 2870  ND2 ASN B  82     4625  10899  11822  -1528  -2023   4306       N  
ATOM   2871  N   TYR B  83      13.339  -8.622 -27.557  1.00 58.62           N  
ANISOU 2871  N   TYR B  83     3447   8673  10151   -740   -986   3515       N  
ATOM   2872  CA  TYR B  83      13.705  -7.867 -26.364  1.00 56.71           C  
ANISOU 2872  CA  TYR B  83     3266   8321   9961   -498   -693   3440       C  
ATOM   2873  C   TYR B  83      15.218  -7.759 -26.232  1.00 61.17           C  
ANISOU 2873  C   TYR B  83     4141   8757  10345   -458   -667   3077       C  
ATOM   2874  O   TYR B  83      15.741  -6.709 -25.842  1.00 60.14           O  
ANISOU 2874  O   TYR B  83     4093   8547  10212   -276   -491   3007       O  
ATOM   2875  CB  TYR B  83      13.100  -8.527 -25.128  1.00 72.65           C  
ANISOU 2875  CB  TYR B  83     5183  10329  12093   -475   -553   3514       C  
ATOM   2876  CG  TYR B  83      11.660  -8.148 -24.861  1.00 81.35           C  
ANISOU 2876  CG  TYR B  83     5961  11524  13422   -393   -439   3904       C  
ATOM   2877  CD1 TYR B  83      11.084  -7.036 -25.467  1.00 81.27           C  
ANISOU 2877  CD1 TYR B  83     5789  11579  13511   -280   -398   4155       C  
ATOM   2878  CD2 TYR B  83      10.873  -8.914 -24.012  1.00 86.90           C  
ANISOU 2878  CD2 TYR B  83     6512  12256  14249   -425   -365   4037       C  
ATOM   2879  CE1 TYR B  83       9.763  -6.693 -25.219  1.00 85.49           C  
ANISOU 2879  CE1 TYR B  83     6013  12203  14267   -189   -280   4543       C  
ATOM   2880  CE2 TYR B  83       9.563  -8.583 -23.762  1.00 92.36           C  
ANISOU 2880  CE2 TYR B  83     6894  13036  15163   -340   -247   4416       C  
ATOM   2881  CZ  TYR B  83       9.011  -7.476 -24.364  1.00 91.60           C  
ANISOU 2881  CZ  TYR B  83     6634  13003  15166   -218   -204   4675       C  
ATOM   2882  OH  TYR B  83       7.698  -7.161 -24.103  1.00 96.36           O  
ANISOU 2882  OH  TYR B  83     6912  13698  16004   -119    -73   5082       O  
ATOM   2883  N   PHE B  84      15.934  -8.840 -26.549  1.00 54.78           N  
ANISOU 2883  N   PHE B  84     3503   7924   9386   -628   -837   2857       N  
ATOM   2884  CA  PHE B  84      17.391  -8.785 -26.576  1.00 50.32           C  
ANISOU 2884  CA  PHE B  84     3212   7253   8654   -600   -834   2542       C  
ATOM   2885  C   PHE B  84      17.892  -7.900 -27.711  1.00 59.37           C  
ANISOU 2885  C   PHE B  84     4422   8406   9729   -576   -905   2513       C  
ATOM   2886  O   PHE B  84      18.895  -7.193 -27.558  1.00 72.03           O  
ANISOU 2886  O   PHE B  84     6178   9926  11263   -465   -813   2338       O  
ATOM   2887  CB  PHE B  84      17.962 -10.196 -26.701  1.00 48.84           C  
ANISOU 2887  CB  PHE B  84     3179   7041   8336   -776   -982   2352       C  
ATOM   2888  CG  PHE B  84      17.986 -10.962 -25.406  1.00 50.55           C  
ANISOU 2888  CG  PHE B  84     3418   7210   8580   -766   -871   2277       C  
ATOM   2889  CD1 PHE B  84      18.592 -10.429 -24.281  1.00 47.10           C  
ANISOU 2889  CD1 PHE B  84     3063   6686   8148   -600   -670   2158       C  
ATOM   2890  CD2 PHE B  84      17.393 -12.212 -25.313  1.00 57.58           C  
ANISOU 2890  CD2 PHE B  84     4251   8142   9487   -934   -971   2330       C  
ATOM   2891  CE1 PHE B  84      18.614 -11.130 -23.089  1.00 48.55           C  
ANISOU 2891  CE1 PHE B  84     3268   6827   8350   -595   -566   2094       C  
ATOM   2892  CE2 PHE B  84      17.410 -12.917 -24.123  1.00 58.53           C  
ANISOU 2892  CE2 PHE B  84     4388   8217   9634   -927   -860   2264       C  
ATOM   2893  CZ  PHE B  84      18.020 -12.377 -23.010  1.00 54.56           C  
ANISOU 2893  CZ  PHE B  84     3966   7631   9134   -754   -655   2147       C  
ATOM   2894  N   LEU B  85      17.204  -7.923 -28.856  1.00 58.99           N  
ANISOU 2894  N   LEU B  85     4254   8461   9698   -690  -1074   2690       N  
ATOM   2895  CA  LEU B  85      17.617  -7.084 -29.977  1.00 59.65           C  
ANISOU 2895  CA  LEU B  85     4387   8558   9718   -671  -1141   2678       C  
ATOM   2896  C   LEU B  85      17.435  -5.607 -29.661  1.00 59.54           C  
ANISOU 2896  C   LEU B  85     4283   8529   9809   -458   -946   2791       C  
ATOM   2897  O   LEU B  85      18.203  -4.770 -30.153  1.00 62.62           O  
ANISOU 2897  O   LEU B  85     4785   8877  10133   -385   -921   2684       O  
ATOM   2898  CB  LEU B  85      16.840  -7.460 -31.239  1.00 62.68           C  
ANISOU 2898  CB  LEU B  85     4655   9064  10096   -853  -1376   2863       C  
ATOM   2899  CG  LEU B  85      17.150  -8.830 -31.850  1.00 63.15           C  
ANISOU 2899  CG  LEU B  85     4858   9123  10013  -1082  -1590   2735       C  
ATOM   2900  CD1 LEU B  85      16.278  -9.096 -33.068  1.00 67.64           C  
ANISOU 2900  CD1 LEU B  85     5306   9816  10578  -1276  -1830   2947       C  
ATOM   2901  CD2 LEU B  85      18.626  -8.934 -32.213  1.00 59.20           C  
ANISOU 2901  CD2 LEU B  85     4641   8516   9338  -1066  -1593   2429       C  
ATOM   2902  N   VAL B  86      16.438  -5.265 -28.845  1.00 58.63           N  
ANISOU 2902  N   VAL B  86     3972   8443   9861   -350   -793   3013       N  
ATOM   2903  CA  VAL B  86      16.285  -3.876 -28.431  1.00 59.87           C  
ANISOU 2903  CA  VAL B  86     4070   8562  10116   -126   -567   3120       C  
ATOM   2904  C   VAL B  86      17.404  -3.483 -27.480  1.00 64.13           C  
ANISOU 2904  C   VAL B  86     4829   8956  10583     -2   -393   2856       C  
ATOM   2905  O   VAL B  86      17.926  -2.362 -27.537  1.00 69.84           O  
ANISOU 2905  O   VAL B  86     5629   9618  11290    129   -280   2804       O  
ATOM   2906  CB  VAL B  86      14.899  -3.654 -27.804  1.00 57.10           C  
ANISOU 2906  CB  VAL B  86     3453   8272   9968    -28   -421   3452       C  
ATOM   2907  CG1 VAL B  86      14.872  -2.338 -27.045  1.00 59.94           C  
ANISOU 2907  CG1 VAL B  86     3816   8544  10414    233   -120   3520       C  
ATOM   2908  CG2 VAL B  86      13.830  -3.676 -28.885  1.00 59.47           C  
ANISOU 2908  CG2 VAL B  86     3510   8732  10352   -128   -592   3754       C  
ATOM   2909  N   ASN B  87      17.793  -4.396 -26.589  1.00 59.55           N  
ANISOU 2909  N   ASN B  87     4348   8322   9958    -50   -376   2693       N  
ATOM   2910  CA  ASN B  87      18.932  -4.133 -25.722  1.00 54.89           C  
ANISOU 2910  CA  ASN B  87     3965   7607   9283     36   -251   2437       C  
ATOM   2911  C   ASN B  87      20.208  -3.972 -26.535  1.00 59.50           C  
ANISOU 2911  C   ASN B  87     4739   8156   9711    -22   -376   2206       C  
ATOM   2912  O   ASN B  87      21.084  -3.176 -26.181  1.00 60.43           O  
ANISOU 2912  O   ASN B  87     4986   8191   9784     76   -272   2062       O  
ATOM   2913  CB  ASN B  87      19.081  -5.259 -24.701  1.00 49.91           C  
ANISOU 2913  CB  ASN B  87     3390   6944   8629    -22   -235   2322       C  
ATOM   2914  CG  ASN B  87      20.251  -5.042 -23.769  1.00 44.91           C  
ANISOU 2914  CG  ASN B  87     2957   6200   7907     51   -125   2073       C  
ATOM   2915  OD1 ASN B  87      20.336  -4.021 -23.086  1.00 46.88           O  
ANISOU 2915  OD1 ASN B  87     3214   6369   8229    210     76   2134       O  
ATOM   2916  ND2 ASN B  87      21.167  -6.001 -23.740  1.00 44.77           N  
ANISOU 2916  ND2 ASN B  87     3086   6162   7762    -65   -248   1856       N  
ATOM   2917  N   LEU B  88      20.332  -4.723 -27.632  1.00 56.35           N  
ANISOU 2917  N   LEU B  88     4363   7818   9231   -183   -592   2175       N  
ATOM   2918  CA  LEU B  88      21.476  -4.544 -28.518  1.00 43.59           C  
ANISOU 2918  CA  LEU B  88     2913   6170   7478   -225   -691   1989       C  
ATOM   2919  C   LEU B  88      21.458  -3.168 -29.173  1.00 52.19           C  
ANISOU 2919  C   LEU B  88     3961   7267   8602   -122   -639   2077       C  
ATOM   2920  O   LEU B  88      22.520  -2.581 -29.411  1.00 56.49           O  
ANISOU 2920  O   LEU B  88     4646   7752   9066    -83   -620   1915       O  
ATOM   2921  CB  LEU B  88      21.489  -5.648 -29.575  1.00 41.47           C  
ANISOU 2921  CB  LEU B  88     2680   5958   7118   -409   -910   1964       C  
ATOM   2922  CG  LEU B  88      22.556  -5.621 -30.669  1.00 48.50           C  
ANISOU 2922  CG  LEU B  88     3732   6826   7870   -462  -1016   1804       C  
ATOM   2923  CD1 LEU B  88      23.950  -5.619 -30.069  1.00 46.74           C  
ANISOU 2923  CD1 LEU B  88     3698   6503   7559   -404   -936   1555       C  
ATOM   2924  CD2 LEU B  88      22.374  -6.807 -31.603  1.00 52.76           C  
ANISOU 2924  CD2 LEU B  88     4303   7415   8328   -645  -1215   1808       C  
ATOM   2925  N   SER B  89      20.268  -2.641 -29.471  1.00 58.29           N  
ANISOU 2925  N   SER B  89     4533   8117   9498    -77   -612   2346       N  
ATOM   2926  CA  SER B  89      20.170  -1.288 -30.010  1.00 56.24           C  
ANISOU 2926  CA  SER B  89     4222   7863   9284     43   -537   2454       C  
ATOM   2927  C   SER B  89      20.513  -0.244 -28.957  1.00 57.56           C  
ANISOU 2927  C   SER B  89     4448   7923   9499    233   -292   2407       C  
ATOM   2928  O   SER B  89      21.100   0.797 -29.276  1.00 59.23           O  
ANISOU 2928  O   SER B  89     4733   8085   9685    321   -229   2353       O  
ATOM   2929  CB  SER B  89      18.769  -1.048 -30.565  1.00 59.07           C  
ANISOU 2929  CB  SER B  89     4332   8341   9771     49   -568   2784       C  
ATOM   2930  OG  SER B  89      18.616  -1.652 -31.836  1.00 62.29           O  
ANISOU 2930  OG  SER B  89     4711   8846  10111   -125   -812   2822       O  
ATOM   2931  N   LEU B  90      20.149  -0.500 -27.698  1.00 56.60           N  
ANISOU 2931  N   LEU B  90     4302   7757   9444    298   -145   2429       N  
ATOM   2932  CA  LEU B  90      20.480   0.444 -26.638  1.00 53.57           C  
ANISOU 2932  CA  LEU B  90     3994   7253   9106    474    101   2401       C  
ATOM   2933  C   LEU B  90      21.984   0.555 -26.454  1.00 50.39           C  
ANISOU 2933  C   LEU B  90     3806   6760   8581    444     71   2116       C  
ATOM   2934  O   LEU B  90      22.490   1.629 -26.112  1.00 50.71           O  
ANISOU 2934  O   LEU B  90     3912   6696   8659    568    228   2119       O  
ATOM   2935  CB  LEU B  90      19.815   0.024 -25.328  1.00 65.29           C  
ANISOU 2935  CB  LEU B  90     5412   8699  10698    542    271   2516       C  
ATOM   2936  CG  LEU B  90      18.415   0.569 -25.044  1.00 70.06           C  
ANISOU 2936  CG  LEU B  90     5811   9326  11483    692    469   2869       C  
ATOM   2937  CD1 LEU B  90      17.669  -0.379 -24.124  1.00 67.98           C  
ANISOU 2937  CD1 LEU B  90     5452   9078  11299    674    527   2967       C  
ATOM   2938  CD2 LEU B  90      18.505   1.954 -24.426  1.00 74.53           C  
ANISOU 2938  CD2 LEU B  90     6439   9751  12127    926    785   2978       C  
ATOM   2939  N   ALA B  91      22.715  -0.539 -26.677  1.00 54.80           N  
ANISOU 2939  N   ALA B  91     4472   7347   9002    287   -115   1891       N  
ATOM   2940  CA  ALA B  91      24.170  -0.465 -26.653  1.00 48.97           C  
ANISOU 2940  CA  ALA B  91     3919   6547   8142    251   -162   1637       C  
ATOM   2941  C   ALA B  91      24.698   0.315 -27.850  1.00 57.38           C  
ANISOU 2941  C   ALA B  91     5019   7620   9164    248   -230   1619       C  
ATOM   2942  O   ALA B  91      25.567   1.182 -27.703  1.00 66.20           O  
ANISOU 2942  O   ALA B  91     6220   8658  10275    307   -162   1541       O  
ATOM   2943  CB  ALA B  91      24.774  -1.869 -26.613  1.00 43.21           C  
ANISOU 2943  CB  ALA B  91     3276   5833   7309    104   -311   1478       C  
ATOM   2944  N   ASP B  92      24.194   0.011 -29.049  1.00 62.99           N  
ANISOU 2944  N   ASP B  92     5650   8415   9868    170   -367   1729       N  
ATOM   2945  CA  ASP B  92      24.699   0.673 -30.249  1.00 65.96           C  
ANISOU 2945  CA  ASP B  92     6061   8805  10195    162   -437   1713       C  
ATOM   2946  C   ASP B  92      24.463   2.178 -30.203  1.00 66.09           C  
ANISOU 2946  C   ASP B  92     6033   8784  10295    324   -281   1823       C  
ATOM   2947  O   ASP B  92      25.307   2.957 -30.658  1.00 70.76           O  
ANISOU 2947  O   ASP B  92     6705   9329  10853    354   -270   1750       O  
ATOM   2948  CB  ASP B  92      24.043   0.070 -31.492  1.00 70.94           C  
ANISOU 2948  CB  ASP B  92     6605   9541  10808     51   -611   1836       C  
ATOM   2949  CG  ASP B  92      24.356  -1.399 -31.657  1.00 73.81           C  
ANISOU 2949  CG  ASP B  92     7045   9923  11077   -103   -757   1719       C  
ATOM   2950  OD1 ASP B  92      25.399  -1.843 -31.133  1.00 65.71           O  
ANISOU 2950  OD1 ASP B  92     6164   8830   9973   -122   -742   1515       O  
ATOM   2951  OD2 ASP B  92      23.555  -2.109 -32.304  1.00 80.62           O  
ANISOU 2951  OD2 ASP B  92     7819  10867  11943   -206   -887   1841       O  
ATOM   2952  N   VAL B  93      23.326   2.611 -29.656  1.00 62.15           N  
ANISOU 2952  N   VAL B  93     5394   8290   9930    437   -137   2046       N  
ATOM   2953  CA  VAL B  93      23.071   4.047 -29.585  1.00 61.04           C  
ANISOU 2953  CA  VAL B  93     5205   8084   9904    614     61   2229       C  
ATOM   2954  C   VAL B  93      23.995   4.722 -28.581  1.00 63.98           C  
ANISOU 2954  C   VAL B  93     5712   8296  10302    708    241   2125       C  
ATOM   2955  O   VAL B  93      24.379   5.885 -28.763  1.00 69.53           O  
ANISOU 2955  O   VAL B  93     6461   8911  11047    819    367   2171       O  
ATOM   2956  CB  VAL B  93      21.595   4.314 -29.245  1.00 58.73           C  
ANISOU 2956  CB  VAL B  93     4725   7832   9758    732    209   2532       C  
ATOM   2957  CG1 VAL B  93      21.364   5.806 -29.088  1.00 43.47           C  
ANISOU 2957  CG1 VAL B  93     2778   5807   7931    950    471   2722       C  
ATOM   2958  CG2 VAL B  93      20.695   3.740 -30.326  1.00 55.53           C  
ANISOU 2958  CG2 VAL B  93     4163   7590   9348    628     12   2664       C  
ATOM   2959  N   LEU B  94      24.356   4.022 -27.506  1.00 66.36           N  
ANISOU 2959  N   LEU B  94     6080   8547  10585    670    263   1995       N  
ATOM   2960  CA  LEU B  94      25.298   4.590 -26.549  1.00 66.87           C  
ANISOU 2960  CA  LEU B  94     6273   8454  10680    742    415   1893       C  
ATOM   2961  C   LEU B  94      26.667   4.788 -27.182  1.00 55.72           C  
ANISOU 2961  C   LEU B  94     4967   7019   9186    648    274   1699       C  
ATOM   2962  O   LEU B  94      27.347   5.784 -26.909  1.00 56.96           O  
ANISOU 2962  O   LEU B  94     5198   7036   9407    736    411   1688       O  
ATOM   2963  CB  LEU B  94      25.403   3.690 -25.319  1.00 81.09           C  
ANISOU 2963  CB  LEU B  94     8109  10222  12479    707    443   1802       C  
ATOM   2964  CG  LEU B  94      26.629   3.897 -24.427  1.00 86.33           C  
ANISOU 2964  CG  LEU B  94     8909  10744  13150    714    508   1635       C  
ATOM   2965  CD1 LEU B  94      26.397   5.026 -23.435  1.00 88.83           C  
ANISOU 2965  CD1 LEU B  94     9309  10856  13587    941    869   1754       C  
ATOM   2966  CD2 LEU B  94      26.995   2.606 -23.705  1.00 84.62           C  
ANISOU 2966  CD2 LEU B  94     8715  10565  12870    591    385   1487       C  
ATOM   2967  N   ALA B  95      27.093   3.844 -28.026  1.00 50.78           N  
ANISOU 2967  N   ALA B  95     4365   6508   8419    481     29   1551       N  
ATOM   2968  CA  ALA B  95      28.373   3.986 -28.710  1.00 43.73           C  
ANISOU 2968  CA  ALA B  95     3571   5602   7442    397    -87   1389       C  
ATOM   2969  C   ALA B  95      28.307   5.066 -29.781  1.00 49.23           C  
ANISOU 2969  C   ALA B  95     4233   6294   8179    462    -60   1507       C  
ATOM   2970  O   ALA B  95      29.197   5.920 -29.874  1.00 49.53           O  
ANISOU 2970  O   ALA B  95     4323   6235   8262    491     -8   1476       O  
ATOM   2971  CB  ALA B  95      28.795   2.649 -29.321  1.00 33.62           C  
ANISOU 2971  CB  ALA B  95     2360   4430   5985    242   -288   1212       C  
ATOM   2972  N   THR B  96      27.257   5.041 -30.604  1.00 54.28           N  
ANISOU 2972  N   THR B  96     4773   7032   8817    482    -99   1658       N  
ATOM   2973  CA  THR B  96      27.152   5.996 -31.701  1.00 52.12           C  
ANISOU 2973  CA  THR B  96     4460   6770   8572    542    -90   1785       C  
ATOM   2974  C   THR B  96      27.053   7.426 -31.187  1.00 58.61           C  
ANISOU 2974  C   THR B  96     5279   7456   9535    731    161   1934       C  
ATOM   2975  O   THR B  96      27.777   8.315 -31.649  1.00 70.39           O  
ANISOU 2975  O   THR B  96     6827   8868  11050    775    207   1932       O  
ATOM   2976  CB  THR B  96      25.942   5.654 -32.569  1.00 46.74           C  
ANISOU 2976  CB  THR B  96     3650   6227   7883    526   -184   1946       C  
ATOM   2977  OG1 THR B  96      26.125   4.353 -33.139  1.00 39.39           O  
ANISOU 2977  OG1 THR B  96     2760   5389   6818    360   -392   1799       O  
ATOM   2978  CG2 THR B  96      25.778   6.675 -33.682  1.00 43.13           C  
ANISOU 2978  CG2 THR B  96     3140   5789   7457    601   -174   2103       C  
ATOM   2979  N   ALA B  97      26.163   7.666 -30.223  1.00 56.00           N  
ANISOU 2979  N   ALA B  97     4902   7077   9298    860    356   2072       N  
ATOM   2980  CA  ALA B  97      25.916   9.030 -29.766  1.00 61.91           C  
ANISOU 2980  CA  ALA B  97     5695   7672  10157   1078    658   2229       C  
ATOM   2981  C   ALA B  97      27.128   9.611 -29.047  1.00 64.19           C  
ANISOU 2981  C   ALA B  97     6164   7754  10472   1117    789   2080       C  
ATOM   2982  O   ALA B  97      27.542  10.742 -29.323  1.00 72.62           O  
ANISOU 2982  O   ALA B  97     7336   8680  11576   1226    937   2118       O  
ATOM   2983  CB  ALA B  97      24.690   9.060 -28.854  1.00 69.27           C  
ANISOU 2983  CB  ALA B  97     6564   8588  11168   1216    872   2411       C  
ATOM   2984  N   ILE B  98      27.709   8.860 -28.119  1.00 62.74           N  
ANISOU 2984  N   ILE B  98     6031   7530  10276   1029    743   1913       N  
ATOM   2985  CA  ILE B  98      28.759   9.398 -27.259  1.00 62.12           C  
ANISOU 2985  CA  ILE B  98     6132   7219  10253   1077    889   1787       C  
ATOM   2986  C   ILE B  98      30.146   9.106 -27.814  1.00 56.65           C  
ANISOU 2986  C   ILE B  98     5435   6544   9547    897    652   1607       C  
ATOM   2987  O   ILE B  98      30.966  10.015 -27.975  1.00 51.28           O  
ANISOU 2987  O   ILE B  98     4874   5675   8935    941    735   1579       O  
ATOM   2988  CB  ILE B  98      28.601   8.843 -25.828  1.00 64.34           C  
ANISOU 2988  CB  ILE B  98     6481   7415  10552   1109   1007   1728       C  
ATOM   2989  CG1 ILE B  98      27.313   9.371 -25.194  1.00 60.27           C  
ANISOU 2989  CG1 ILE B  98     6016   6829  10055   1317   1322   1922       C  
ATOM   2990  CG2 ILE B  98      29.811   9.203 -24.985  1.00 60.07           C  
ANISOU 2990  CG2 ILE B  98     6179   6591  10052   1116   1094   1556       C  
ATOM   2991  CD1 ILE B  98      26.856   8.586 -23.986  1.00 62.55           C  
ANISOU 2991  CD1 ILE B  98     6316   7104  10345   1334   1411   1909       C  
ATOM   2992  N   CYS B  99      30.437   7.838 -28.110  1.00 61.37           N  
ANISOU 2992  N   CYS B  99     5944   7335  10038    693    373   1478       N  
ATOM   2993  CA  CYS B  99      31.804   7.462 -28.455  1.00 56.49           C  
ANISOU 2993  CA  CYS B  99     5346   6737   9382    515    175   1295       C  
ATOM   2994  C   CYS B  99      32.158   7.773 -29.903  1.00 46.81           C  
ANISOU 2994  C   CYS B  99     4107   5585   8093    464     67   1313       C  
ATOM   2995  O   CYS B  99      33.318   8.092 -30.189  1.00 46.09           O  
ANISOU 2995  O   CYS B  99     4035   5433   8042    382     14   1228       O  
ATOM   2996  CB  CYS B  99      32.031   5.977 -28.177  1.00 57.68           C  
ANISOU 2996  CB  CYS B  99     5512   7029   9375    350    -23   1132       C  
ATOM   2997  SG  CYS B  99      31.490   5.438 -26.545  1.00 57.63           S  
ANISOU 2997  SG  CYS B  99     5501   6964   9433    405     87   1131       S  
ATOM   2998  N   LEU B 100      31.201   7.682 -30.825  1.00 47.06           N  
ANISOU 2998  N   LEU B 100     4094   5741   8046    502     33   1429       N  
ATOM   2999  CA  LEU B 100      31.519   7.934 -32.229  1.00 41.02           C  
ANISOU 2999  CA  LEU B 100     3322   5039   7224    464    -65   1454       C  
ATOM   3000  C   LEU B 100      32.119   9.317 -32.454  1.00 37.91           C  
ANISOU 3000  C   LEU B 100     2946   4484   6974    562     78   1539       C  
ATOM   3001  O   LEU B 100      33.156   9.413 -33.135  1.00 37.59           O  
ANISOU 3001  O   LEU B 100     2921   4436   6927    470     -9   1468       O  
ATOM   3002  CB  LEU B 100      30.271   7.732 -33.092  1.00 45.66           C  
ANISOU 3002  CB  LEU B 100     3837   5763   7751    503   -114   1596       C  
ATOM   3003  CG  LEU B 100      30.504   7.747 -34.607  1.00 41.36           C  
ANISOU 3003  CG  LEU B 100     3287   5301   7128    452   -244   1619       C  
ATOM   3004  CD1 LEU B 100      29.528   6.820 -35.314  1.00 45.80           C  
ANISOU 3004  CD1 LEU B 100     3796   6018   7590    394   -386   1659       C  
ATOM   3005  CD2 LEU B 100      30.402   9.162 -35.163  1.00 31.94           C  
ANISOU 3005  CD2 LEU B 100     2064   4032   6039    595   -114   1805       C  
ATOM   3006  N   PRO B 101      31.541  10.410 -31.942  1.00 43.10           N  
ANISOU 3006  N   PRO B 101     3637   4988   7751    759    324   1689       N  
ATOM   3007  CA  PRO B 101      32.158  11.721 -32.190  1.00 37.03           C  
ANISOU 3007  CA  PRO B 101     2979   3998   7091    871    493   1751       C  
ATOM   3008  C   PRO B 101      33.596  11.820 -31.700  1.00 40.59           C  
ANISOU 3008  C   PRO B 101     3608   4298   7517    683    466   1524       C  
ATOM   3009  O   PRO B 101      34.428  12.446 -32.366  1.00 45.81           O  
ANISOU 3009  O   PRO B 101     4387   4885   8136    591    465   1477       O  
ATOM   3010  CB  PRO B 101      31.223  12.686 -31.438  1.00 44.16           C  
ANISOU 3010  CB  PRO B 101     4027   4723   8030   1100    809   1886       C  
ATOM   3011  CG  PRO B 101      29.902  11.968 -31.435  1.00 46.24           C  
ANISOU 3011  CG  PRO B 101     4120   5220   8229   1113    748   1985       C  
ATOM   3012  CD  PRO B 101      30.279  10.534 -31.196  1.00 52.24           C  
ANISOU 3012  CD  PRO B 101     4786   6135   8926    904    493   1813       C  
ATOM   3013  N   ALA B 102      33.910  11.221 -30.546  1.00 43.66           N  
ANISOU 3013  N   ALA B 102     4064   4659   7864    568    435   1359       N  
ATOM   3014  CA  ALA B 102      35.291  11.186 -30.085  1.00 41.53           C  
ANISOU 3014  CA  ALA B 102     3968   4310   7503    313    349   1124       C  
ATOM   3015  C   ALA B 102      36.164  10.355 -31.009  1.00 47.32           C  
ANISOU 3015  C   ALA B 102     4501   5246   8232    152    102   1058       C  
ATOM   3016  O   ALA B 102      37.360  10.638 -31.163  1.00 47.24           O  
ANISOU 3016  O   ALA B 102     4584   5182   8181    -28     55    942       O  
ATOM   3017  CB  ALA B 102      35.360  10.626 -28.663  1.00 45.18           C  
ANISOU 3017  CB  ALA B 102     4532   4724   7911    238    342    988       C  
ATOM   3018  N   SER B 103      35.579   9.333 -31.633  1.00 54.71           N  
ANISOU 3018  N   SER B 103     5174   6406   9208    211    -47   1142       N  
ATOM   3019  CA  SER B 103      36.334   8.481 -32.541  1.00 48.01           C  
ANISOU 3019  CA  SER B 103     4305   5714   8224     71   -233   1044       C  
ATOM   3020  C   SER B 103      36.796   9.250 -33.764  1.00 56.91           C  
ANISOU 3020  C   SER B 103     5397   6819   9409     79   -209   1133       C  
ATOM   3021  O   SER B 103      37.924   9.063 -34.230  1.00 64.24           O  
ANISOU 3021  O   SER B 103     6349   7771  10287    -57   -274   1035       O  
ATOM   3022  CB  SER B 103      35.479   7.288 -32.964  1.00 55.11           C  
ANISOU 3022  CB  SER B 103     5255   6786   8899     91   -328   1021       C  
ATOM   3023  OG  SER B 103      35.205   6.446 -31.860  1.00 63.74           O  
ANISOU 3023  OG  SER B 103     6383   7905   9931     68   -347    928       O  
ATOM   3024  N   LEU B 104      35.932  10.117 -34.298  1.00 53.84           N  
ANISOU 3024  N   LEU B 104     4987   6379   9088    254    -95   1326       N  
ATOM   3025  CA  LEU B 104      36.255  10.823 -35.531  1.00 50.61           C  
ANISOU 3025  CA  LEU B 104     4627   5946   8656    273    -62   1410       C  
ATOM   3026  C   LEU B 104      37.405  11.805 -35.325  1.00 49.34           C  
ANISOU 3026  C   LEU B 104     4687   5586   8475    146     68   1299       C  
ATOM   3027  O   LEU B 104      38.361  11.825 -36.108  1.00 62.61           O  
ANISOU 3027  O   LEU B 104     6372   7290  10128     32     29   1258       O  
ATOM   3028  CB  LEU B 104      35.007  11.536 -36.055  1.00 56.78           C  
ANISOU 3028  CB  LEU B 104     5379   6714   9479    504     34   1652       C  
ATOM   3029  CG  LEU B 104      35.162  12.518 -37.216  1.00 55.45           C  
ANISOU 3029  CG  LEU B 104     5310   6477   9283    570    115   1775       C  
ATOM   3030  CD1 LEU B 104      35.480  11.790 -38.512  1.00 48.55           C  
ANISOU 3030  CD1 LEU B 104     4329   5784   8335    496    -81   1796       C  
ATOM   3031  CD2 LEU B 104      33.900  13.353 -37.363  1.00 58.29           C  
ANISOU 3031  CD2 LEU B 104     5660   6787   9700    828    254   2025       C  
ATOM   3032  N   LEU B 105      37.337  12.629 -34.274  1.00 44.30           N  
ANISOU 3032  N   LEU B 105     4250   4739   7843    153    233   1255       N  
ATOM   3033  CA  LEU B 105      38.414  13.590 -34.041  1.00 47.88           C  
ANISOU 3033  CA  LEU B 105     4938   4987   8265    -13    336   1152       C  
ATOM   3034  C   LEU B 105      39.725  12.904 -33.670  1.00 57.37           C  
ANISOU 3034  C   LEU B 105     6080   6265   9453   -276    176    974       C  
ATOM   3035  O   LEU B 105      40.802  13.394 -34.030  1.00 59.83           O  
ANISOU 3035  O   LEU B 105     6454   6516   9764   -443    188    930       O  
ATOM   3036  CB  LEU B 105      38.003  14.596 -32.965  1.00 52.76           C  
ANISOU 3036  CB  LEU B 105     5849   5337   8860     40    548   1138       C  
ATOM   3037  CG  LEU B 105      37.012  15.680 -33.402  1.00 61.45           C  
ANISOU 3037  CG  LEU B 105     7080   6286   9983    296    782   1333       C  
ATOM   3038  CD1 LEU B 105      35.663  15.097 -33.807  1.00 64.92           C  
ANISOU 3038  CD1 LEU B 105     7261   6916  10491    558    750   1530       C  
ATOM   3039  CD2 LEU B 105      36.847  16.712 -32.301  1.00 62.97           C  
ANISOU 3039  CD2 LEU B 105     7644   6158  10125    320   1028   1289       C  
ATOM   3040  N   VAL B 106      39.665  11.783 -32.953  1.00 60.58           N  
ANISOU 3040  N   VAL B 106     6353   6806   9858   -312     33    891       N  
ATOM   3041  CA  VAL B 106      40.903  11.093 -32.611  1.00 51.69           C  
ANISOU 3041  CA  VAL B 106     5142   5767   8729   -533   -121    755       C  
ATOM   3042  C   VAL B 106      41.549  10.524 -33.864  1.00 41.99           C  
ANISOU 3042  C   VAL B 106     3724   4703   7525   -556   -202    794       C  
ATOM   3043  O   VAL B 106      42.774  10.568 -34.027  1.00 36.01           O  
ANISOU 3043  O   VAL B 106     2952   3963   6768   -714   -232    739       O  
ATOM   3044  CB  VAL B 106      40.643  10.002 -31.561  1.00 47.08           C  
ANISOU 3044  CB  VAL B 106     4478   5279   8130   -542   -243    672       C  
ATOM   3045  CG1 VAL B 106      41.912   9.207 -31.319  1.00 40.85           C  
ANISOU 3045  CG1 VAL B 106     3643   4623   7256   -691   -393    550       C  
ATOM   3046  CG2 VAL B 106      40.161  10.640 -30.278  1.00 63.99           C  
ANISOU 3046  CG2 VAL B 106     6864   7226  10223   -536   -133    625       C  
ATOM   3047  N   ASP B 107      40.733   9.987 -34.772  1.00 44.16           N  
ANISOU 3047  N   ASP B 107     3883   5103   7791   -390   -233    894       N  
ATOM   3048  CA  ASP B 107      41.247   9.464 -36.028  1.00 46.23           C  
ANISOU 3048  CA  ASP B 107     4102   5489   7974   -376   -278    912       C  
ATOM   3049  C   ASP B 107      41.679  10.578 -36.970  1.00 47.66           C  
ANISOU 3049  C   ASP B 107     4326   5567   8218   -403   -149   1011       C  
ATOM   3050  O   ASP B 107      42.461  10.325 -37.892  1.00 54.15           O  
ANISOU 3050  O   ASP B 107     5095   6451   9028   -448   -148   1027       O  
ATOM   3051  CB  ASP B 107      40.196   8.577 -36.695  1.00 59.26           C  
ANISOU 3051  CB  ASP B 107     5754   7271   9492   -227   -356    960       C  
ATOM   3052  CG  ASP B 107      40.014   7.254 -35.977  1.00 72.65           C  
ANISOU 3052  CG  ASP B 107     7538   9065  11001   -225   -439    813       C  
ATOM   3053  OD1 ASP B 107      41.001   6.750 -35.399  1.00 75.52           O  
ANISOU 3053  OD1 ASP B 107     7948   9452  11294   -303   -454    683       O  
ATOM   3054  OD2 ASP B 107      38.884   6.723 -35.984  1.00 73.39           O  
ANISOU 3054  OD2 ASP B 107     7649   9217  11017   -147   -477    841       O  
ATOM   3055  N   ILE B 108      41.173  11.796 -36.774  1.00 51.09           N  
ANISOU 3055  N   ILE B 108     4929   5826   8659   -346     -9   1070       N  
ATOM   3056  CA  ILE B 108      41.554  12.927 -37.612  1.00 52.10           C  
ANISOU 3056  CA  ILE B 108     5192   5823   8782   -354    138   1149       C  
ATOM   3057  C   ILE B 108      42.798  13.595 -37.043  1.00 54.35           C  
ANISOU 3057  C   ILE B 108     5575   5970   9105   -589    198   1051       C  
ATOM   3058  O   ILE B 108      43.858  13.604 -37.679  1.00 47.59           O  
ANISOU 3058  O   ILE B 108     4660   5147   8274   -713    210   1053       O  
ATOM   3059  CB  ILE B 108      40.404  13.947 -37.720  1.00 47.11           C  
ANISOU 3059  CB  ILE B 108     4712   5050   8137   -162    278   1283       C  
ATOM   3060  CG1 ILE B 108      39.270  13.402 -38.592  1.00 47.80           C  
ANISOU 3060  CG1 ILE B 108     4669   5299   8193     45    196   1435       C  
ATOM   3061  CG2 ILE B 108      40.923  15.273 -38.252  1.00 46.49           C  
ANISOU 3061  CG2 ILE B 108     4837   4772   8055   -204    460   1337       C  
ATOM   3062  CD1 ILE B 108      38.081  14.342 -38.718  1.00 41.59           C  
ANISOU 3062  CD1 ILE B 108     3975   4409   7421    267    327   1616       C  
ATOM   3063  N   THR B 109      42.673  14.162 -35.841  1.00 57.06           N  
ANISOU 3063  N   THR B 109     6079   6154   9447   -662    239    977       N  
ATOM   3064  CA  THR B 109      43.786  14.856 -35.206  1.00 48.40           C  
ANISOU 3064  CA  THR B 109     5111   4911   8367   -929    262    887       C  
ATOM   3065  C   THR B 109      44.833  13.912 -34.628  1.00 55.80           C  
ANISOU 3065  C   THR B 109     5852   6004   9345  -1133     77    785       C  
ATOM   3066  O   THR B 109      45.987  14.320 -34.460  1.00 62.53           O  
ANISOU 3066  O   THR B 109     6728   6828  10204  -1361     56    743       O  
ATOM   3067  CB  THR B 109      43.273  15.776 -34.098  1.00 53.72           C  
ANISOU 3067  CB  THR B 109     6092   5332   8987   -948    369    837       C  
ATOM   3068  OG1 THR B 109      42.900  14.987 -32.962  1.00 55.01           O  
ANISOU 3068  OG1 THR B 109     6219   5560   9123   -941    255    745       O  
ATOM   3069  CG2 THR B 109      42.070  16.577 -34.578  1.00 59.81           C  
ANISOU 3069  CG2 THR B 109     7027   5965   9733   -678    568    970       C  
ATOM   3070  N   GLU B 110      44.460  12.672 -34.316  1.00 62.46           N  
ANISOU 3070  N   GLU B 110     6518   7030  10183  -1039    -60    749       N  
ATOM   3071  CA  GLU B 110      45.362  11.720 -33.667  1.00 55.74           C  
ANISOU 3071  CA  GLU B 110     5600   6375   9203  -1105   -216    622       C  
ATOM   3072  C   GLU B 110      45.793  12.205 -32.285  1.00 48.21           C  
ANISOU 3072  C   GLU B 110     4807   5312   8198  -1309   -269    519       C  
ATOM   3073  O   GLU B 110      46.876  11.863 -31.804  1.00 34.79           O  
ANISOU 3073  O   GLU B 110     3086   3743   6389  -1425   -362    442       O  
ATOM   3074  CB  GLU B 110      46.587  11.421 -34.536  1.00 56.59           C  
ANISOU 3074  CB  GLU B 110     5611   6631   9258  -1132   -215    630       C  
ATOM   3075  CG  GLU B 110      46.871   9.933 -34.712  1.00 63.75           C  
ANISOU 3075  CG  GLU B 110     6420   7760  10042   -994   -295    584       C  
ATOM   3076  CD  GLU B 110      45.799   9.227 -35.522  1.00 72.48           C  
ANISOU 3076  CD  GLU B 110     7493   8911  11136   -794   -288    636       C  
ATOM   3077  OE1 GLU B 110      45.380   9.779 -36.560  1.00 82.70           O  
ANISOU 3077  OE1 GLU B 110     8757  10141  12524   -750   -207    748       O  
ATOM   3078  OE2 GLU B 110      45.368   8.126 -35.117  1.00 74.51           O  
ANISOU 3078  OE2 GLU B 110     7768   9265  11276   -694   -360    572       O  
ATOM   3079  N   SER B 111      44.953  13.011 -31.636  1.00 55.44           N  
ANISOU 3079  N   SER B 111     5912   5964   9187  -1350   -188    528       N  
ATOM   3080  CA  SER B 111      45.214  13.486 -30.284  1.00 56.41           C  
ANISOU 3080  CA  SER B 111     6276   5930   9227  -1548   -231    420       C  
ATOM   3081  C   SER B 111      43.892  13.608 -29.536  1.00 58.77           C  
ANISOU 3081  C   SER B 111     6780   6072   9480  -1376   -127    406       C  
ATOM   3082  O   SER B 111      42.819  13.671 -30.142  1.00 66.11           O  
ANISOU 3082  O   SER B 111     7693   7001  10427  -1107     12    498       O  
ATOM   3083  CB  SER B 111      45.955  14.829 -30.293  1.00 64.24           C  
ANISOU 3083  CB  SER B 111     7513   6714  10182  -1781   -151    408       C  
ATOM   3084  OG  SER B 111      45.168  15.840 -30.896  1.00 71.72           O  
ANISOU 3084  OG  SER B 111     8658   7424  11168  -1648     79    492       O  
ATOM   3085  N   TRP B 112      43.982  13.646 -28.207  1.00 55.45           N  
ANISOU 3085  N   TRP B 112     6567   5540   8960  -1515   -189    297       N  
ATOM   3086  CA  TRP B 112      42.814  13.714 -27.335  1.00 59.33           C  
ANISOU 3086  CA  TRP B 112     7291   5893   9358  -1337    -61    273       C  
ATOM   3087  C   TRP B 112      42.563  15.159 -26.913  1.00 65.88           C  
ANISOU 3087  C   TRP B 112     8580   6369  10083  -1377    158    252       C  
ATOM   3088  O   TRP B 112      43.416  15.778 -26.269  1.00 72.91           O  
ANISOU 3088  O   TRP B 112     9728   7095  10881  -1677     95    155       O  
ATOM   3089  CB  TRP B 112      43.006  12.823 -26.107  1.00 56.42           C  
ANISOU 3089  CB  TRP B 112     6924   5599   8915  -1442   -237    168       C  
ATOM   3090  CG  TRP B 112      41.797  12.732 -25.243  1.00 53.53           C  
ANISOU 3090  CG  TRP B 112     6759   5116   8463  -1239    -89    157       C  
ATOM   3091  CD1 TRP B 112      41.596  13.351 -24.045  1.00 52.23           C  
ANISOU 3091  CD1 TRP B 112     7019   4689   8137  -1312      9     71       C  
ATOM   3092  CD2 TRP B 112      40.605  11.988 -25.517  1.00 53.27           C  
ANISOU 3092  CD2 TRP B 112     6525   5215   8500   -934     -8    250       C  
ATOM   3093  NE1 TRP B 112      40.356  13.031 -23.550  1.00 55.63           N  
ANISOU 3093  NE1 TRP B 112     7511   5082   8543  -1042    177    112       N  
ATOM   3094  CE2 TRP B 112      39.727  12.196 -24.437  1.00 56.17           C  
ANISOU 3094  CE2 TRP B 112     7175   5402   8765   -817    159    230       C  
ATOM   3095  CE3 TRP B 112      40.198  11.164 -26.570  1.00 52.29           C  
ANISOU 3095  CE3 TRP B 112     6026   5339   8504   -764    -62    354       C  
ATOM   3096  CZ2 TRP B 112      38.464  11.610 -24.378  1.00 64.20           C  
ANISOU 3096  CZ2 TRP B 112     8057   6498   9838   -536    276    329       C  
ATOM   3097  CZ3 TRP B 112      38.944  10.583 -26.511  1.00 53.01           C  
ANISOU 3097  CZ3 TRP B 112     6005   5504   8633   -516     19    441       C  
ATOM   3098  CH2 TRP B 112      38.093  10.808 -25.423  1.00 62.80           C  
ANISOU 3098  CH2 TRP B 112     7479   6581   9802   -403    188    438       C  
ATOM   3099  N   LEU B 113      41.394  15.691 -27.278  1.00 66.48           N  
ANISOU 3099  N   LEU B 113     8766   6323  10170  -1081    414    356       N  
ATOM   3100  CA  LEU B 113      41.036  17.071 -26.977  1.00 66.84           C  
ANISOU 3100  CA  LEU B 113     9267   6008  10120  -1051    681    363       C  
ATOM   3101  C   LEU B 113      39.847  17.187 -26.023  1.00 72.37           C  
ANISOU 3101  C   LEU B 113    10229   6534  10735   -813    900    375       C  
ATOM   3102  O   LEU B 113      39.232  18.253 -25.942  1.00 85.37           O  
ANISOU 3102  O   LEU B 113    12219   7891  12328   -661   1195    435       O  
ATOM   3103  CB  LEU B 113      40.744  17.831 -28.271  1.00 71.58           C  
ANISOU 3103  CB  LEU B 113     9819   6566  10811   -884    852    513       C  
ATOM   3104  CG  LEU B 113      41.690  17.568 -29.445  1.00 76.20           C  
ANISOU 3104  CG  LEU B 113    10085   7363  11503  -1024    683    546       C  
ATOM   3105  CD1 LEU B 113      41.053  18.004 -30.756  1.00 71.21           C  
ANISOU 3105  CD1 LEU B 113     9354   6752  10952   -764    842    725       C  
ATOM   3106  CD2 LEU B 113      43.015  18.279 -29.224  1.00 82.02           C  
ANISOU 3106  CD2 LEU B 113    11019   7953  12193  -1410    610    446       C  
ATOM   3107  N   PHE B 114      39.501  16.119 -25.302  1.00 72.24           N  
ANISOU 3107  N   PHE B 114    10068   6675  10706   -761    791    335       N  
ATOM   3108  CA  PHE B 114      38.335  16.129 -24.418  1.00 72.63           C  
ANISOU 3108  CA  PHE B 114    10323   6582  10691   -514   1021    370       C  
ATOM   3109  C   PHE B 114      38.686  16.096 -22.930  1.00 68.03           C  
ANISOU 3109  C   PHE B 114    10124   5818   9908   -714    987    199       C  
ATOM   3110  O   PHE B 114      37.778  15.992 -22.095  1.00 68.60           O  
ANISOU 3110  O   PHE B 114    10380   5773   9911   -519   1182    218       O  
ATOM   3111  CB  PHE B 114      37.403  14.954 -24.742  1.00 72.24           C  
ANISOU 3111  CB  PHE B 114     9833   6833  10783   -256    973    493       C  
ATOM   3112  CG  PHE B 114      36.962  14.897 -26.178  1.00 68.95           C  
ANISOU 3112  CG  PHE B 114     9058   6606  10535    -67    976    671       C  
ATOM   3113  CD1 PHE B 114      37.667  14.161 -27.118  1.00 70.82           C  
ANISOU 3113  CD1 PHE B 114     8937   7116  10855   -195    710    660       C  
ATOM   3114  CD2 PHE B 114      35.809  15.549 -26.577  1.00 66.90           C  
ANISOU 3114  CD2 PHE B 114     8825   6249  10343    253   1251    867       C  
ATOM   3115  CE1 PHE B 114      37.240  14.108 -28.438  1.00 68.37           C  
ANISOU 3115  CE1 PHE B 114     8350   6964  10662    -32    707    821       C  
ATOM   3116  CE2 PHE B 114      35.378  15.498 -27.881  1.00 63.79           C  
ANISOU 3116  CE2 PHE B 114     8116   6037  10086    415   1223   1045       C  
ATOM   3117  CZ  PHE B 114      36.091  14.778 -28.815  1.00 61.98           C  
ANISOU 3117  CZ  PHE B 114     7575   6067   9908    261    944   1013       C  
ATOM   3118  N   GLY B 115      39.965  16.166 -22.571  1.00 61.50           N  
ANISOU 3118  N   GLY B 115     9415   4970   8983  -1099    742     48       N  
ATOM   3119  CA  GLY B 115      40.361  16.234 -21.179  1.00 66.98           C  
ANISOU 3119  CA  GLY B 115    10519   5476   9453  -1330    676   -110       C  
ATOM   3120  C   GLY B 115      40.470  14.871 -20.512  1.00 62.23           C  
ANISOU 3120  C   GLY B 115     9676   5128   8842  -1369    435   -162       C  
ATOM   3121  O   GLY B 115      40.073  13.833 -21.046  1.00 71.83           O  
ANISOU 3121  O   GLY B 115    10430   6640  10220  -1183    360    -76       O  
ATOM   3122  N   HIS B 116      41.032  14.885 -19.299  1.00 58.67           N  
ANISOU 3122  N   HIS B 116     9577   4540   8176  -1632    304   -304       N  
ATOM   3123  CA  HIS B 116      41.343  13.638 -18.603  1.00 78.48           C  
ANISOU 3123  CA  HIS B 116    11890   7276  10652  -1719     38   -358       C  
ATOM   3124  C   HIS B 116      40.103  12.899 -18.118  1.00 79.25           C  
ANISOU 3124  C   HIS B 116    11949   7409  10754  -1386    227   -305       C  
ATOM   3125  O   HIS B 116      40.095  11.664 -18.115  1.00 76.10           O  
ANISOU 3125  O   HIS B 116    11181   7291  10444  -1335     50   -282       O  
ATOM   3126  CB  HIS B 116      42.283  13.908 -17.429  1.00 98.36           C  
ANISOU 3126  CB  HIS B 116    14733   9719  12919  -2040   -172   -494       C  
ATOM   3127  CG  HIS B 116      43.668  14.281 -17.843  1.00112.70           C  
ANISOU 3127  CG  HIS B 116    16334  11715  14773  -2301   -429   -506       C  
ATOM   3128  ND1 HIS B 116      44.029  15.560 -18.206  1.00116.89           N  
ANISOU 3128  ND1 HIS B 116    17061  12087  15265  -2396   -332   -509       N  
ATOM   3129  CD2 HIS B 116      44.794  13.537 -17.925  1.00115.89           C  
ANISOU 3129  CD2 HIS B 116    16334  12449  15250  -2451   -744   -498       C  
ATOM   3130  CE1 HIS B 116      45.313  15.585 -18.516  1.00117.96           C  
ANISOU 3130  CE1 HIS B 116    16920  12437  15464  -2616   -583   -504       C  
ATOM   3131  NE2 HIS B 116      45.801  14.369 -18.352  1.00117.87           N  
ANISOU 3131  NE2 HIS B 116    16536  12729  15522  -2630   -816   -491       N  
ATOM   3132  N   ALA B 117      39.053  13.612 -17.706  1.00 78.36           N  
ANISOU 3132  N   ALA B 117    12207   7011  10555  -1153    602   -270       N  
ATOM   3133  CA  ALA B 117      37.880  12.912 -17.189  1.00 69.00           C  
ANISOU 3133  CA  ALA B 117    10968   5862   9389   -846    798   -195       C  
ATOM   3134  C   ALA B 117      37.220  12.078 -18.281  1.00 66.93           C  
ANISOU 3134  C   ALA B 117    10094   5928   9409   -590    785    -31       C  
ATOM   3135  O   ALA B 117      36.883  10.908 -18.063  1.00 73.18           O  
ANISOU 3135  O   ALA B 117    10607   6935  10261   -510    685     -3       O  
ATOM   3136  CB  ALA B 117      36.891  13.909 -16.588  1.00 73.00           C  
ANISOU 3136  CB  ALA B 117    11982   5987   9766   -617   1248   -157       C  
ATOM   3137  N   LEU B 118      37.037  12.662 -19.467  1.00 64.78           N  
ANISOU 3137  N   LEU B 118     9631   5687   9297   -476    874     80       N  
ATOM   3138  CA  LEU B 118      36.453  11.933 -20.587  1.00 63.33           C  
ANISOU 3138  CA  LEU B 118     8903   5807   9354   -271    829    237       C  
ATOM   3139  C   LEU B 118      37.415  10.905 -21.169  1.00 65.84           C  
ANISOU 3139  C   LEU B 118     8825   6440   9752   -473    450    181       C  
ATOM   3140  O   LEU B 118      36.979  10.013 -21.907  1.00 76.42           O  
ANISOU 3140  O   LEU B 118     9750   8038  11247   -342    368    280       O  
ATOM   3141  CB  LEU B 118      36.004  12.915 -21.671  1.00 68.78           C  
ANISOU 3141  CB  LEU B 118     9550   6423  10161    -94   1028    381       C  
ATOM   3142  CG  LEU B 118      34.805  13.785 -21.285  1.00 64.92           C  
ANISOU 3142  CG  LEU B 118     9345   5667   9654    213   1451    511       C  
ATOM   3143  CD1 LEU B 118      34.514  14.821 -22.358  1.00 65.83           C  
ANISOU 3143  CD1 LEU B 118     9443   5697   9872    370   1628    657       C  
ATOM   3144  CD2 LEU B 118      33.583  12.917 -21.028  1.00 54.98           C  
ANISOU 3144  CD2 LEU B 118     7819   4563   8507    487   1564    661       C  
ATOM   3145  N   CYS B 119      38.711  11.012 -20.861  1.00 66.42           N  
ANISOU 3145  N   CYS B 119     9021   6492   9723   -791    222     38       N  
ATOM   3146  CA  CYS B 119      39.662  10.003 -21.320  1.00 67.94           C  
ANISOU 3146  CA  CYS B 119     8841   6976   9997   -955   -105      6       C  
ATOM   3147  C   CYS B 119      39.370   8.643 -20.703  1.00 65.97           C  
ANISOU 3147  C   CYS B 119     8421   6902   9743   -897   -222     -6       C  
ATOM   3148  O   CYS B 119      39.686   7.611 -21.302  1.00 65.88           O  
ANISOU 3148  O   CYS B 119     8039   7150   9842   -899   -410     21       O  
ATOM   3149  CB  CYS B 119      41.092  10.447 -20.990  1.00 66.76           C  
ANISOU 3149  CB  CYS B 119     8849   6767   9750  -1310   -318   -109       C  
ATOM   3150  SG  CYS B 119      42.416   9.258 -21.382  1.00 67.59           S  
ANISOU 3150  SG  CYS B 119     8511   7213   9956  -1510   -698   -122       S  
ATOM   3151  N   LYS B 120      38.778   8.623 -19.512  1.00 64.98           N  
ANISOU 3151  N   LYS B 120     8592   6620   9480   -840    -95    -45       N  
ATOM   3152  CA  LYS B 120      38.376   7.374 -18.881  1.00 60.79           C  
ANISOU 3152  CA  LYS B 120     7931   6228   8940   -765   -164    -44       C  
ATOM   3153  C   LYS B 120      36.928   7.014 -19.181  1.00 63.06           C  
ANISOU 3153  C   LYS B 120     8041   6567   9352   -457     63    101       C  
ATOM   3154  O   LYS B 120      36.611   5.836 -19.386  1.00 69.58           O  
ANISOU 3154  O   LYS B 120     8558   7607  10271   -390    -40    149       O  
ATOM   3155  CB  LYS B 120      38.588   7.451 -17.368  1.00 52.24           C  
ANISOU 3155  CB  LYS B 120     7272   4956   7620   -892   -168   -159       C  
ATOM   3156  CG  LYS B 120      40.047   7.577 -16.951  1.00 43.13           C  
ANISOU 3156  CG  LYS B 120     6243   3804   6339  -1237   -470   -280       C  
ATOM   3157  CD  LYS B 120      40.199   7.646 -15.433  1.00 45.67           C  
ANISOU 3157  CD  LYS B 120     7027   3934   6392  -1375   -497   -388       C  
ATOM   3158  CE  LYS B 120      41.283   6.691 -14.941  1.00 55.33           C  
ANISOU 3158  CE  LYS B 120     8108   5355   7561  -1601   -873   -438       C  
ATOM   3159  NZ  LYS B 120      41.350   6.628 -13.452  1.00 68.94           N  
ANISOU 3159  NZ  LYS B 120    10278   6911   9004  -1723   -919   -528       N  
ATOM   3160  N   VAL B 121      36.039   8.008 -19.201  1.00 53.56           N  
ANISOU 3160  N   VAL B 121     7029   5164   8156   -271    375    186       N  
ATOM   3161  CA  VAL B 121      34.617   7.736 -19.400  1.00 46.56           C  
ANISOU 3161  CA  VAL B 121     5955   4330   7405     25    602    364       C  
ATOM   3162  C   VAL B 121      34.368   7.173 -20.793  1.00 56.72           C  
ANISOU 3162  C   VAL B 121     6758   5893   8900     93    467    488       C  
ATOM   3163  O   VAL B 121      33.865   6.057 -20.953  1.00 68.52           O  
ANISOU 3163  O   VAL B 121     7956   7592  10487    149    376    555       O  
ATOM   3164  CB  VAL B 121      33.786   9.006 -19.157  1.00 47.46           C  
ANISOU 3164  CB  VAL B 121     6377   4163   7492    233    988    459       C  
ATOM   3165  CG1 VAL B 121      32.317   8.726 -19.428  1.00 49.29           C  
ANISOU 3165  CG1 VAL B 121     6339   4486   7905    547   1214    692       C  
ATOM   3166  CG2 VAL B 121      33.999   9.493 -17.741  1.00 51.86           C  
ANISOU 3166  CG2 VAL B 121     7482   4420   7804    157   1133    325       C  
ATOM   3167  N   ILE B 122      34.715   7.943 -21.824  1.00 55.09           N  
ANISOU 3167  N   ILE B 122     6496   5681   8753     77    452    521       N  
ATOM   3168  CA  ILE B 122      34.369   7.542 -23.192  1.00 55.10           C  
ANISOU 3168  CA  ILE B 122     6098   5915   8924    158    352    655       C  
ATOM   3169  C   ILE B 122      34.950   6.188 -23.559  1.00 57.95           C  
ANISOU 3169  C   ILE B 122     6180   6528   9312     17     51    589       C  
ATOM   3170  O   ILE B 122      34.198   5.328 -24.059  1.00 66.20           O  
ANISOU 3170  O   ILE B 122     6939   7755  10459    108     -4    700       O  
ATOM   3171  CB  ILE B 122      34.774   8.646 -24.184  1.00 48.02           C  
ANISOU 3171  CB  ILE B 122     5246   4945   8055    149    392    688       C  
ATOM   3172  CG1 ILE B 122      33.915   9.889 -23.970  1.00 51.08           C  
ANISOU 3172  CG1 ILE B 122     5871   5092   8445    362    731    809       C  
ATOM   3173  CG2 ILE B 122      34.645   8.125 -25.602  1.00 50.13           C  
ANISOU 3173  CG2 ILE B 122     5140   5456   8449    182    235    796       C  
ATOM   3174  CD1 ILE B 122      34.569  11.171 -24.400  1.00 57.67           C  
ANISOU 3174  CD1 ILE B 122     6952   5732   9229    294    813    773       C  
ATOM   3175  N   PRO B 123      36.239   5.912 -23.368  1.00 49.93           N  
ANISOU 3175  N   PRO B 123     5221   5535   8215   -202   -148    433       N  
ATOM   3176  CA  PRO B 123      36.744   4.562 -23.651  1.00 40.99           C  
ANISOU 3176  CA  PRO B 123     3841   4624   7110   -292   -391    390       C  
ATOM   3177  C   PRO B 123      36.043   3.488 -22.841  1.00 48.04           C  
ANISOU 3177  C   PRO B 123     4685   5576   7990   -231   -394    401       C  
ATOM   3178  O   PRO B 123      35.874   2.364 -23.327  1.00 59.47           O  
ANISOU 3178  O   PRO B 123     5998   7201   9396   -209   -495    416       O  
ATOM   3179  CB  PRO B 123      38.238   4.667 -23.301  1.00 48.41           C  
ANISOU 3179  CB  PRO B 123     4892   5539   7965   -518   -555    247       C  
ATOM   3180  CG  PRO B 123      38.538   6.116 -23.491  1.00 55.00           C  
ANISOU 3180  CG  PRO B 123     5936   6191   8772   -565   -436    240       C  
ATOM   3181  CD  PRO B 123      37.329   6.827 -22.973  1.00 53.42           C  
ANISOU 3181  CD  PRO B 123     5940   5808   8548   -384   -167    309       C  
ATOM   3182  N   TYR B 124      35.634   3.808 -21.615  1.00 48.02           N  
ANISOU 3182  N   TYR B 124     4938   5409   7899   -191   -240    375       N  
ATOM   3183  CA  TYR B 124      34.891   2.854 -20.804  1.00 36.48           C  
ANISOU 3183  CA  TYR B 124     3448   3985   6428   -120   -202    403       C  
ATOM   3184  C   TYR B 124      33.515   2.576 -21.399  1.00 37.39           C  
ANISOU 3184  C   TYR B 124     3310   4199   6696     65    -81    592       C  
ATOM   3185  O   TYR B 124      33.094   1.417 -21.506  1.00 46.89           O  
ANISOU 3185  O   TYR B 124     4303   5557   7957     65   -179    637       O  
ATOM   3186  CB  TYR B 124      34.765   3.385 -19.375  1.00 38.30           C  
ANISOU 3186  CB  TYR B 124     4060   3987   6506   -110    -28    340       C  
ATOM   3187  CG  TYR B 124      33.811   2.622 -18.489  1.00 40.15           C  
ANISOU 3187  CG  TYR B 124     4306   4217   6731      4     99    398       C  
ATOM   3188  CD1 TYR B 124      32.534   3.105 -18.236  1.00 35.73           C  
ANISOU 3188  CD1 TYR B 124     3787   3555   6235    221    410    547       C  
ATOM   3189  CD2 TYR B 124      34.189   1.424 -17.897  1.00 37.61           C  
ANISOU 3189  CD2 TYR B 124     3953   3990   6347    -92    -73    324       C  
ATOM   3190  CE1 TYR B 124      31.661   2.417 -17.420  1.00 32.47           C  
ANISOU 3190  CE1 TYR B 124     3372   3138   5828    325    552    620       C  
ATOM   3191  CE2 TYR B 124      33.320   0.729 -17.078  1.00 26.74           C  
ANISOU 3191  CE2 TYR B 124     2601   2600   4960      5     57    384       C  
ATOM   3192  CZ  TYR B 124      32.059   1.230 -16.844  1.00 28.32           C  
ANISOU 3192  CZ  TYR B 124     2830   2701   5229    206    371    531       C  
ATOM   3193  OH  TYR B 124      31.188   0.542 -16.030  1.00 36.75           O  
ANISOU 3193  OH  TYR B 124     3906   3756   6302    303    525    609       O  
ATOM   3194  N   LEU B 125      32.801   3.631 -21.806  1.00 41.42           N  
ANISOU 3194  N   LEU B 125     3835   4623   7278    216    124    721       N  
ATOM   3195  CA  LEU B 125      31.497   3.440 -22.433  1.00 47.16           C  
ANISOU 3195  CA  LEU B 125     4278   5470   8169    385    214    943       C  
ATOM   3196  C   LEU B 125      31.621   2.665 -23.737  1.00 54.18           C  
ANISOU 3196  C   LEU B 125     5108   6576   8903    250    -33    898       C  
ATOM   3197  O   LEU B 125      30.735   1.876 -24.085  1.00 58.89           O  
ANISOU 3197  O   LEU B 125     5688   7295   9391    244    -67    940       O  
ATOM   3198  CB  LEU B 125      30.825   4.793 -22.671  1.00 49.69           C  
ANISOU 3198  CB  LEU B 125     4678   5651   8551    580    481   1092       C  
ATOM   3199  CG  LEU B 125      30.443   5.565 -21.408  1.00 43.17           C  
ANISOU 3199  CG  LEU B 125     4198   4562   7643    711    805   1091       C  
ATOM   3200  CD1 LEU B 125      29.887   6.933 -21.765  1.00 41.64           C  
ANISOU 3200  CD1 LEU B 125     4104   4210   7507    917   1082   1242       C  
ATOM   3201  CD2 LEU B 125      29.445   4.769 -20.581  1.00 41.40           C  
ANISOU 3201  CD2 LEU B 125     3882   4379   7471    819    935   1197       C  
ATOM   3202  N   GLN B 126      32.718   2.883 -24.485  1.00 53.71           N  
ANISOU 3202  N   GLN B 126     5098   6535   8774    143   -171    788       N  
ATOM   3203  CA  GLN B 126      32.959   2.088 -25.685  1.00 52.99           C  
ANISOU 3203  CA  GLN B 126     5082   6602   8448     58   -318    703       C  
ATOM   3204  C   GLN B 126      33.163   0.619 -25.336  1.00 47.69           C  
ANISOU 3204  C   GLN B 126     4489   6025   7606    -14   -406    583       C  
ATOM   3205  O   GLN B 126      32.584  -0.268 -25.973  1.00 49.65           O  
ANISOU 3205  O   GLN B 126     4754   6378   7732    -23   -440    576       O  
ATOM   3206  CB  GLN B 126      34.173   2.638 -26.440  1.00 45.66           C  
ANISOU 3206  CB  GLN B 126     4204   5659   7485    -10   -385    624       C  
ATOM   3207  CG  GLN B 126      34.667   1.750 -27.572  1.00 44.65           C  
ANISOU 3207  CG  GLN B 126     4180   5663   7121    -81   -483    500       C  
ATOM   3208  CD  GLN B 126      33.721   1.695 -28.752  1.00 64.42           C  
ANISOU 3208  CD  GLN B 126     6673   8260   9544    -51   -495    546       C  
ATOM   3209  OE1 GLN B 126      32.712   0.990 -28.727  1.00 75.86           O  
ANISOU 3209  OE1 GLN B 126     8058   9685  11080     -3   -465    657       O  
ATOM   3210  NE2 GLN B 126      34.042   2.448 -29.795  1.00 70.93           N  
ANISOU 3210  NE2 GLN B 126     7527   9129  10294    -92   -559    524       N  
ATOM   3211  N   ALA B 127      33.979   0.340 -24.311  1.00 28.65           N  
ANISOU 3211  N   ALA B 127     2119   3564   5204    -69   -445    495       N  
ATOM   3212  CA  ALA B 127      34.192  -1.040 -23.889  1.00 31.27           C  
ANISOU 3212  CA  ALA B 127     2523   3972   5385   -114   -503    406       C  
ATOM   3213  C   ALA B 127      32.905  -1.668 -23.375  1.00 37.79           C  
ANISOU 3213  C   ALA B 127     3285   4813   6260    -68   -449    490       C  
ATOM   3214  O   ALA B 127      32.614  -2.834 -23.668  1.00 42.11           O  
ANISOU 3214  O   ALA B 127     3870   5449   6681    -93   -484    453       O  
ATOM   3215  CB  ALA B 127      35.275  -1.102 -22.811  1.00 34.66           C  
ANISOU 3215  CB  ALA B 127     2999   4341   5829   -182   -568    321       C  
ATOM   3216  N   VAL B 128      32.122  -0.915 -22.600  1.00 41.19           N  
ANISOU 3216  N   VAL B 128     3607   5146   6897     12   -332    619       N  
ATOM   3217  CA  VAL B 128      30.863  -1.451 -22.090  1.00 38.95           C  
ANISOU 3217  CA  VAL B 128     3247   4879   6672     70   -241    733       C  
ATOM   3218  C   VAL B 128      29.900  -1.747 -23.231  1.00 41.04           C  
ANISOU 3218  C   VAL B 128     3480   5254   6859     72   -263    798       C  
ATOM   3219  O   VAL B 128      29.158  -2.737 -23.198  1.00 42.56           O  
ANISOU 3219  O   VAL B 128     3646   5510   7013     43   -286    823       O  
ATOM   3220  CB  VAL B 128      30.244  -0.478 -21.075  1.00 37.65           C  
ANISOU 3220  CB  VAL B 128     2986   4572   6746    217    -10    886       C  
ATOM   3221  CG1 VAL B 128      28.828  -0.909 -20.753  1.00 37.58           C  
ANISOU 3221  CG1 VAL B 128     2900   4599   6779    297    126   1045       C  
ATOM   3222  CG2 VAL B 128      31.090  -0.432 -19.821  1.00 42.19           C  
ANISOU 3222  CG2 VAL B 128     3597   5014   7418    206     17    801       C  
ATOM   3223  N   SER B 129      29.896  -0.894 -24.258  1.00 41.77           N  
ANISOU 3223  N   SER B 129     3562   5360   6951     96   -266    835       N  
ATOM   3224  CA  SER B 129      29.017  -1.116 -25.399  1.00 45.46           C  
ANISOU 3224  CA  SER B 129     3983   5922   7370     86   -311    903       C  
ATOM   3225  C   SER B 129      29.350  -2.418 -26.111  1.00 47.72           C  
ANISOU 3225  C   SER B 129     4330   6264   7536    -26   -453    818       C  
ATOM   3226  O   SER B 129      28.461  -3.059 -26.684  1.00 53.55           O  
ANISOU 3226  O   SER B 129     5001   7050   8297    -66   -507    919       O  
ATOM   3227  CB  SER B 129      29.116   0.059 -26.372  1.00 59.76           C  
ANISOU 3227  CB  SER B 129     5772   7720   9214    131   -296    965       C  
ATOM   3228  OG  SER B 129      28.097  -0.015 -27.350  1.00 77.70           O  
ANISOU 3228  OG  SER B 129     7963  10072  11489    133   -332   1082       O  
ATOM   3229  N   VAL B 130      30.619  -2.824 -26.087  1.00 48.80           N  
ANISOU 3229  N   VAL B 130     4582   6381   7581    -77   -510    673       N  
ATOM   3230  CA  VAL B 130      31.005  -4.078 -26.726  1.00 41.20           C  
ANISOU 3230  CA  VAL B 130     3677   5439   6539   -157   -611    623       C  
ATOM   3231  C   VAL B 130      30.544  -5.270 -25.902  1.00 42.83           C  
ANISOU 3231  C   VAL B 130     3877   5654   6743   -189   -620    621       C  
ATOM   3232  O   VAL B 130      29.994  -6.240 -26.437  1.00 32.57           O  
ANISOU 3232  O   VAL B 130     2558   4385   5433   -247   -686    663       O  
ATOM   3233  CB  VAL B 130      32.523  -4.123 -26.945  1.00 32.18           C  
ANISOU 3233  CB  VAL B 130     2641   4271   5316   -178   -642    498       C  
ATOM   3234  CG1 VAL B 130      32.901  -5.473 -27.500  1.00 28.91           C  
ANISOU 3234  CG1 VAL B 130     2281   3872   4831   -234   -714    456       C  
ATOM   3235  CG2 VAL B 130      32.940  -3.020 -27.886  1.00 31.57           C  
ANISOU 3235  CG2 VAL B 130     2561   4190   5245   -159   -636    510       C  
ATOM   3236  N   SER B 131      30.780  -5.223 -24.591  1.00 45.07           N  
ANISOU 3236  N   SER B 131     4178   5911   7035   -159   -561    571       N  
ATOM   3237  CA  SER B 131      30.383  -6.331 -23.734  1.00 41.64           C  
ANISOU 3237  CA  SER B 131     3737   5484   6601   -186   -561    569       C  
ATOM   3238  C   SER B 131      28.878  -6.547 -23.770  1.00 39.54           C  
ANISOU 3238  C   SER B 131     3346   5251   6425   -186   -533    714       C  
ATOM   3239  O   SER B 131      28.405  -7.691 -23.789  1.00 26.88           O  
ANISOU 3239  O   SER B 131     1726   3669   4817   -250   -582    740       O  
ATOM   3240  CB  SER B 131      30.854  -6.075 -22.305  1.00 41.16           C  
ANISOU 3240  CB  SER B 131     3705   5398   6537   -150   -499    502       C  
ATOM   3241  OG  SER B 131      30.508  -7.162 -21.469  1.00 52.20           O  
ANISOU 3241  OG  SER B 131     5093   6797   7945   -177   -500    508       O  
ATOM   3242  N   VAL B 132      28.106  -5.461 -23.778  1.00 40.63           N  
ANISOU 3242  N   VAL B 132     3388   5394   6654   -114   -448    825       N  
ATOM   3243  CA  VAL B 132      26.656  -5.598 -23.846  1.00 37.60           C  
ANISOU 3243  CA  VAL B 132     2861   5051   6374   -106   -413   1003       C  
ATOM   3244  C   VAL B 132      26.239  -6.259 -25.152  1.00 40.15           C  
ANISOU 3244  C   VAL B 132     3152   5428   6677   -203   -552   1070       C  
ATOM   3245  O   VAL B 132      25.326  -7.092 -25.182  1.00 49.92           O  
ANISOU 3245  O   VAL B 132     4304   6706   7955   -267   -593   1171       O  
ATOM   3246  CB  VAL B 132      25.985  -4.228 -23.672  1.00 37.35           C  
ANISOU 3246  CB  VAL B 132     2733   5006   6452     17   -274   1136       C  
ATOM   3247  CG1 VAL B 132      24.491  -4.360 -23.883  1.00 41.74           C  
ANISOU 3247  CG1 VAL B 132     3121   5617   7120     28   -242   1355       C  
ATOM   3248  CG2 VAL B 132      26.293  -3.678 -22.299  1.00 29.62           C  
ANISOU 3248  CG2 VAL B 132     1753   3920   5579    110   -118   1167       C  
ATOM   3249  N   ALA B 133      26.898  -5.893 -26.253  1.00 37.17           N  
ANISOU 3249  N   ALA B 133     2838   5051   6235   -224   -625   1020       N  
ATOM   3250  CA  ALA B 133      26.565  -6.468 -27.551  1.00 36.94           C  
ANISOU 3250  CA  ALA B 133     2791   5072   6174   -318   -757   1076       C  
ATOM   3251  C   ALA B 133      26.815  -7.971 -27.570  1.00 45.97           C  
ANISOU 3251  C   ALA B 133     4007   6214   7243   -421   -846    997       C  
ATOM   3252  O   ALA B 133      25.908  -8.766 -27.839  1.00 47.10           O  
ANISOU 3252  O   ALA B 133     4080   6403   7413   -509   -921   1096       O  
ATOM   3253  CB  ALA B 133      27.373  -5.773 -28.647  1.00 27.00           C  
ANISOU 3253  CB  ALA B 133     1600   3806   4853   -309   -797   1020       C  
ATOM   3254  N   VAL B 134      28.053  -8.382 -27.293  1.00 45.62           N  
ANISOU 3254  N   VAL B 134     4100   6121   7111   -414   -840    832       N  
ATOM   3255  CA  VAL B 134      28.392  -9.794 -27.418  1.00 34.48           C  
ANISOU 3255  CA  VAL B 134     2769   4703   5630   -497   -914    759       C  
ATOM   3256  C   VAL B 134      27.622 -10.640 -26.413  1.00 35.95           C  
ANISOU 3256  C   VAL B 134     2900   4895   5864   -533   -896    803       C  
ATOM   3257  O   VAL B 134      27.247 -11.781 -26.711  1.00 49.85           O  
ANISOU 3257  O   VAL B 134     4669   6670   7603   -636   -978    819       O  
ATOM   3258  CB  VAL B 134      29.912  -9.986 -27.271  1.00 30.62           C  
ANISOU 3258  CB  VAL B 134     2413   4166   5053   -461   -894    601       C  
ATOM   3259  CG1 VAL B 134      30.326  -9.828 -25.817  1.00 32.35           C  
ANISOU 3259  CG1 VAL B 134     2651   4353   5289   -398   -808    546       C  
ATOM   3260  CG2 VAL B 134      30.321 -11.342 -27.807  1.00 29.90           C  
ANISOU 3260  CG2 VAL B 134     2404   4069   4889   -538   -972    541       C  
ATOM   3261  N   LEU B 135      27.373 -10.111 -25.210  1.00 34.83           N  
ANISOU 3261  N   LEU B 135     2705   4740   5788   -458   -788    824       N  
ATOM   3262  CA  LEU B 135      26.581 -10.865 -24.242  1.00 26.47           C  
ANISOU 3262  CA  LEU B 135     1578   3691   4788   -488   -754    880       C  
ATOM   3263  C   LEU B 135      25.123 -10.971 -24.669  1.00 30.05           C  
ANISOU 3263  C   LEU B 135     1873   4207   5337   -548   -789   1068       C  
ATOM   3264  O   LEU B 135      24.466 -11.978 -24.380  1.00 30.71           O  
ANISOU 3264  O   LEU B 135     1908   4310   5449   -635   -821   1121       O  
ATOM   3265  CB  LEU B 135      26.679 -10.222 -22.857  1.00 25.79           C  
ANISOU 3265  CB  LEU B 135     1473   3577   4748   -388   -616    861       C  
ATOM   3266  CG  LEU B 135      27.903 -10.592 -22.016  1.00 23.94           C  
ANISOU 3266  CG  LEU B 135     1369   3298   4429   -368   -603    702       C  
ATOM   3267  CD1 LEU B 135      27.983  -9.712 -20.777  1.00 23.70           C  
ANISOU 3267  CD1 LEU B 135     1308   3233   4464   -279   -484    714       C  
ATOM   3268  CD2 LEU B 135      27.859 -12.063 -21.631  1.00 23.97           C  
ANISOU 3268  CD2 LEU B 135     1405   3298   4405   -449   -646    672       C  
ATOM   3269  N   THR B 136      24.603  -9.950 -25.356  1.00 40.44           N  
ANISOU 3269  N   THR B 136     3099   5558   6708   -510   -787   1185       N  
ATOM   3270  CA  THR B 136      23.234 -10.026 -25.854  1.00 44.56           C  
ANISOU 3270  CA  THR B 136     3450   6155   7324   -573   -840   1395       C  
ATOM   3271  C   THR B 136      23.115 -11.059 -26.963  1.00 49.85           C  
ANISOU 3271  C   THR B 136     4157   6861   7922   -737  -1021   1399       C  
ATOM   3272  O   THR B 136      22.164 -11.848 -26.987  1.00 55.66           O  
ANISOU 3272  O   THR B 136     4794   7647   8706   -850  -1092   1518       O  
ATOM   3273  CB  THR B 136      22.775  -8.658 -26.346  1.00 40.04           C  
ANISOU 3273  CB  THR B 136     2773   5615   6827   -484   -793   1531       C  
ATOM   3274  OG1 THR B 136      22.721  -7.749 -25.238  1.00 44.99           O  
ANISOU 3274  OG1 THR B 136     3362   6201   7531   -335   -608   1549       O  
ATOM   3275  CG2 THR B 136      21.398  -8.760 -26.977  1.00 44.35           C  
ANISOU 3275  CG2 THR B 136     3126   6256   7469   -557   -872   1775       C  
ATOM   3276  N   LEU B 137      24.073 -11.067 -27.889  1.00 43.23           N  
ANISOU 3276  N   LEU B 137     3459   5996   6969   -758  -1095   1274       N  
ATOM   3277  CA  LEU B 137      24.069 -12.078 -28.938  1.00 34.13           C  
ANISOU 3277  CA  LEU B 137     2376   4861   5730   -914  -1257   1259       C  
ATOM   3278  C   LEU B 137      24.240 -13.476 -28.359  1.00 35.77           C  
ANISOU 3278  C   LEU B 137     2666   5032   5895  -1000  -1279   1172       C  
ATOM   3279  O   LEU B 137      23.694 -14.445 -28.900  1.00 34.88           O  
ANISOU 3279  O   LEU B 137     2559   4943   5753  -1162  -1408   1222       O  
ATOM   3280  CB  LEU B 137      25.173 -11.781 -29.953  1.00 31.84           C  
ANISOU 3280  CB  LEU B 137     2229   4539   5329   -895  -1295   1135       C  
ATOM   3281  CG  LEU B 137      25.058 -10.454 -30.709  1.00 35.10           C  
ANISOU 3281  CG  LEU B 137     2578   4987   5771   -830  -1290   1215       C  
ATOM   3282  CD1 LEU B 137      26.315 -10.173 -31.526  1.00 30.57           C  
ANISOU 3282  CD1 LEU B 137     2149   4374   5093   -797  -1298   1072       C  
ATOM   3283  CD2 LEU B 137      23.822 -10.436 -31.602  1.00 37.63           C  
ANISOU 3283  CD2 LEU B 137     2768   5396   6133   -944  -1423   1417       C  
ATOM   3284  N   SER B 138      24.995 -13.604 -27.265  1.00 38.94           N  
ANISOU 3284  N   SER B 138     3135   5374   6286   -908  -1164   1046       N  
ATOM   3285  CA  SER B 138      25.177 -14.914 -26.651  1.00 41.01           C  
ANISOU 3285  CA  SER B 138     3470   5599   6513   -982  -1174    969       C  
ATOM   3286  C   SER B 138      23.889 -15.409 -26.010  1.00 47.58           C  
ANISOU 3286  C   SER B 138     4159   6473   7447  -1064  -1173   1110       C  
ATOM   3287  O   SER B 138      23.525 -16.581 -26.161  1.00 51.91           O  
ANISOU 3287  O   SER B 138     4735   7018   7970  -1216  -1260   1118       O  
ATOM   3288  CB  SER B 138      26.301 -14.855 -25.620  1.00 38.90           C  
ANISOU 3288  CB  SER B 138     3297   5270   6213   -864  -1061    822       C  
ATOM   3289  OG  SER B 138      27.528 -14.527 -26.245  1.00 39.12           O  
ANISOU 3289  OG  SER B 138     3445   5266   6153   -805  -1068    706       O  
ATOM   3290  N   PHE B 139      23.192 -14.535 -25.285  1.00 51.56           N  
ANISOU 3290  N   PHE B 139     4509   7012   8070   -970  -1067   1227       N  
ATOM   3291  CA  PHE B 139      21.943 -14.947 -24.660  1.00 55.26           C  
ANISOU 3291  CA  PHE B 139     4812   7528   8657  -1034  -1043   1385       C  
ATOM   3292  C   PHE B 139      20.875 -15.254 -25.699  1.00 53.84           C  
ANISOU 3292  C   PHE B 139     4517   7429   8511  -1191  -1200   1560       C  
ATOM   3293  O   PHE B 139      20.035 -16.138 -25.480  1.00 56.51           O  
ANISOU 3293  O   PHE B 139     4771   7800   8901  -1327  -1250   1655       O  
ATOM   3294  CB  PHE B 139      21.461 -13.866 -23.696  1.00 57.26           C  
ANISOU 3294  CB  PHE B 139     4927   7794   9035   -877   -869   1487       C  
ATOM   3295  CG  PHE B 139      22.251 -13.793 -22.418  1.00 59.72           C  
ANISOU 3295  CG  PHE B 139     5332   8036   9324   -768   -721   1346       C  
ATOM   3296  CD1 PHE B 139      23.530 -14.323 -22.325  1.00 58.85           C  
ANISOU 3296  CD1 PHE B 139     5413   7863   9084   -775   -754   1142       C  
ATOM   3297  CD2 PHE B 139      21.699 -13.198 -21.299  1.00 62.76           C  
ANISOU 3297  CD2 PHE B 139     5602   8416   9830   -660   -548   1451       C  
ATOM   3298  CE1 PHE B 139      24.245 -14.248 -21.136  1.00 53.27           C  
ANISOU 3298  CE1 PHE B 139     4774   7099   8368   -692   -647   1052       C  
ATOM   3299  CE2 PHE B 139      22.404 -13.122 -20.115  1.00 58.80           C  
ANISOU 3299  CE2 PHE B 139     5169   7834   9340   -579   -433   1390       C  
ATOM   3300  CZ  PHE B 139      23.677 -13.646 -20.031  1.00 49.02           C  
ANISOU 3300  CZ  PHE B 139     4113   6542   7971   -605   -499   1190       C  
ATOM   3301  N   ILE B 140      20.887 -14.544 -26.829  1.00 53.05           N  
ANISOU 3301  N   ILE B 140     4411   7365   8382  -1189  -1285   1611       N  
ATOM   3302  CA  ILE B 140      19.952 -14.856 -27.904  1.00 49.78           C  
ANISOU 3302  CA  ILE B 140     3904   7033   7978  -1361  -1466   1778       C  
ATOM   3303  C   ILE B 140      20.202 -16.263 -28.429  1.00 50.13           C  
ANISOU 3303  C   ILE B 140     4107   7042   7900  -1563  -1616   1680       C  
ATOM   3304  O   ILE B 140      19.272 -17.066 -28.570  1.00 62.07           O  
ANISOU 3304  O   ILE B 140     5540   8602   9442  -1747  -1730   1805       O  
ATOM   3305  CB  ILE B 140      20.053 -13.810 -29.026  1.00 48.02           C  
ANISOU 3305  CB  ILE B 140     3668   6847   7731  -1319  -1525   1834       C  
ATOM   3306  CG1 ILE B 140      19.446 -12.487 -28.569  1.00 46.72           C  
ANISOU 3306  CG1 ILE B 140     3310   6728   7712  -1154  -1390   1996       C  
ATOM   3307  CG2 ILE B 140      19.351 -14.309 -30.276  1.00 51.04           C  
ANISOU 3307  CG2 ILE B 140     4020   7303   8071  -1531  -1750   1966       C  
ATOM   3308  CD1 ILE B 140      19.920 -11.298 -29.364  1.00 48.95           C  
ANISOU 3308  CD1 ILE B 140     3625   7010   7964  -1055  -1381   1985       C  
ATOM   3309  N   ALA B 141      21.465 -16.580 -28.729  1.00 43.92           N  
ANISOU 3309  N   ALA B 141     3546   6168   6974  -1536  -1614   1465       N  
ATOM   3310  CA  ALA B 141      21.789 -17.914 -29.220  1.00 42.55           C  
ANISOU 3310  CA  ALA B 141     3555   5938   6676  -1714  -1733   1364       C  
ATOM   3311  C   ALA B 141      21.477 -18.976 -28.173  1.00 43.81           C  
ANISOU 3311  C   ALA B 141     3708   6063   6873  -1789  -1688   1344       C  
ATOM   3312  O   ALA B 141      20.954 -20.047 -28.500  1.00 48.30           O  
ANISOU 3312  O   ALA B 141     4326   6623   7402  -2002  -1813   1379       O  
ATOM   3313  CB  ALA B 141      23.260 -17.983 -29.640  1.00 42.15           C  
ANISOU 3313  CB  ALA B 141     3728   5798   6491  -1635  -1703   1151       C  
ATOM   3314  N   LEU B 142      21.788 -18.696 -26.905  1.00 48.12           N  
ANISOU 3314  N   LEU B 142     4208   6583   7490  -1631  -1513   1289       N  
ATOM   3315  CA  LEU B 142      21.472 -19.650 -25.848  1.00 51.30           C  
ANISOU 3315  CA  LEU B 142     4598   6954   7940  -1699  -1452   1277       C  
ATOM   3316  C   LEU B 142      19.971 -19.864 -25.724  1.00 60.23           C  
ANISOU 3316  C   LEU B 142     5517   8171   9195  -1836  -1504   1495       C  
ATOM   3317  O   LEU B 142      19.523 -20.968 -25.394  1.00 59.81           O  
ANISOU 3317  O   LEU B 142     5480   8095   9151  -2001  -1536   1507       O  
ATOM   3318  CB  LEU B 142      22.053 -19.163 -24.520  1.00 43.84           C  
ANISOU 3318  CB  LEU B 142     3640   5974   7044  -1504  -1257   1196       C  
ATOM   3319  CG  LEU B 142      21.961 -20.081 -23.301  1.00 36.92           C  
ANISOU 3319  CG  LEU B 142     2773   5043   6211  -1555  -1174   1181       C  
ATOM   3320  CD1 LEU B 142      22.825 -21.323 -23.484  1.00 38.92           C  
ANISOU 3320  CD1 LEU B 142     3252   5188   6348  -1667  -1247   1045       C  
ATOM   3321  CD2 LEU B 142      22.373 -19.318 -22.051  1.00 35.17           C  
ANISOU 3321  CD2 LEU B 142     2506   4802   6057  -1367  -1004   1171       C  
ATOM   3322  N   ASP B 143      19.182 -18.817 -25.972  1.00 65.11           N  
ANISOU 3322  N   ASP B 143     5931   8888   9918  -1772  -1507   1680       N  
ATOM   3323  CA  ASP B 143      17.732 -18.947 -25.929  1.00 61.54           C  
ANISOU 3323  CA  ASP B 143     5242   8538   9604  -1895  -1563   1927       C  
ATOM   3324  C   ASP B 143      17.219 -19.779 -27.097  1.00 64.15           C  
ANISOU 3324  C   ASP B 143     5613   8902   9857  -2165  -1808   2001       C  
ATOM   3325  O   ASP B 143      16.390 -20.679 -26.914  1.00 75.90           O  
ANISOU 3325  O   ASP B 143     7027  10418  11393  -2360  -1880   2101       O  
ATOM   3326  CB  ASP B 143      17.091 -17.560 -25.926  1.00 66.58           C  
ANISOU 3326  CB  ASP B 143     5655   9265  10377  -1737  -1491   2121       C  
ATOM   3327  CG  ASP B 143      15.589 -17.621 -25.822  1.00 74.27           C  
ANISOU 3327  CG  ASP B 143     6344  10355  11519  -1836  -1529   2411       C  
ATOM   3328  OD1 ASP B 143      15.088 -18.088 -24.778  1.00 74.88           O  
ANISOU 3328  OD1 ASP B 143     6320  10432  11701  -1843  -1413   2463       O  
ATOM   3329  OD2 ASP B 143      14.911 -17.208 -26.785  1.00 78.64           O  
ANISOU 3329  OD2 ASP B 143     6770  11005  12105  -1911  -1674   2599       O  
ATOM   3330  N   ARG B 144      17.703 -19.493 -28.308  1.00 59.83           N  
ANISOU 3330  N   ARG B 144     5195   8351   9186  -2195  -1938   1954       N  
ATOM   3331  CA  ARG B 144      17.256 -20.242 -29.477  1.00 62.40           C  
ANISOU 3331  CA  ARG B 144     5599   8700   9412  -2466  -2183   2021       C  
ATOM   3332  C   ARG B 144      17.700 -21.697 -29.408  1.00 65.21           C  
ANISOU 3332  C   ARG B 144     6199   8939   9638  -2642  -2233   1856       C  
ATOM   3333  O   ARG B 144      16.983 -22.590 -29.877  1.00 68.80           O  
ANISOU 3333  O   ARG B 144     6681   9409  10052  -2911  -2408   1946       O  
ATOM   3334  CB  ARG B 144      17.799 -19.593 -30.751  1.00 56.60           C  
ANISOU 3334  CB  ARG B 144     4980   7968   8558  -2444  -2284   1987       C  
ATOM   3335  CG  ARG B 144      17.499 -18.109 -30.894  1.00 56.82           C  
ANISOU 3335  CG  ARG B 144     4804   8087   8699  -2263  -2222   2129       C  
ATOM   3336  CD  ARG B 144      16.072 -17.839 -31.340  1.00 64.13           C  
ANISOU 3336  CD  ARG B 144     5468   9158   9740  -2399  -2366   2438       C  
ATOM   3337  NE  ARG B 144      15.107 -18.016 -30.260  1.00 72.67           N  
ANISOU 3337  NE  ARG B 144     6308  10301  11003  -2394  -2279   2599       N  
ATOM   3338  CZ  ARG B 144      14.041 -18.805 -30.334  1.00 72.80           C  
ANISOU 3338  CZ  ARG B 144     6192  10393  11075  -2629  -2427   2782       C  
ATOM   3339  NH1 ARG B 144      13.797 -19.487 -31.444  1.00 66.76           N  
ANISOU 3339  NH1 ARG B 144     5536   9648  10182  -2903  -2684   2823       N  
ATOM   3340  NH2 ARG B 144      13.214 -18.901 -29.302  1.00 64.12           N  
ANISOU 3340  NH2 ARG B 144     4858   9348  10157  -2600  -2316   2930       N  
ATOM   3341  N   TRP B 145      18.869 -21.954 -28.819  1.00 64.71           N  
ANISOU 3341  N   TRP B 145     6320   8758   9510  -2503  -2085   1626       N  
ATOM   3342  CA  TRP B 145      19.387 -23.315 -28.764  1.00 59.14           C  
ANISOU 3342  CA  TRP B 145     5869   7921   8681  -2650  -2111   1466       C  
ATOM   3343  C   TRP B 145      18.554 -24.186 -27.832  1.00 53.08           C  
ANISOU 3343  C   TRP B 145     5007   7149   8011  -2788  -2080   1539       C  
ATOM   3344  O   TRP B 145      18.239 -25.334 -28.163  1.00 56.37           O  
ANISOU 3344  O   TRP B 145     5567   7504   8346  -3049  -2214   1552       O  
ATOM   3345  CB  TRP B 145      20.852 -23.288 -28.334  1.00 53.67           C  
ANISOU 3345  CB  TRP B 145     5361   7114   7917  -2449  -1955   1232       C  
ATOM   3346  CG  TRP B 145      21.539 -24.623 -28.307  1.00 48.31           C  
ANISOU 3346  CG  TRP B 145     4971   6275   7108  -2585  -1987   1104       C  
ATOM   3347  CD1 TRP B 145      22.063 -25.302 -29.370  1.00 47.40           C  
ANISOU 3347  CD1 TRP B 145     5140   6058   6810  -2727  -2115   1026       C  
ATOM   3348  CD2 TRP B 145      21.825 -25.415 -27.148  1.00 56.90           C  
ANISOU 3348  CD2 TRP B 145     6123   7267   8230  -2590  -1881   1050       C  
ATOM   3349  NE1 TRP B 145      22.637 -26.477 -28.947  1.00 52.77           N  
ANISOU 3349  NE1 TRP B 145     6069   6576   7406  -2815  -2090    926       N  
ATOM   3350  CE2 TRP B 145      22.505 -26.569 -27.586  1.00 60.27           C  
ANISOU 3350  CE2 TRP B 145     6880   7528   8492  -2733  -1950    939       C  
ATOM   3351  CE3 TRP B 145      21.561 -25.265 -25.783  1.00 61.88           C  
ANISOU 3351  CE3 TRP B 145     6584   7920   9006  -2493  -1731   1093       C  
ATOM   3352  CZ2 TRP B 145      22.926 -27.567 -26.706  1.00 63.40           C  
ANISOU 3352  CZ2 TRP B 145     7438   7779   8871  -2777  -1873    872       C  
ATOM   3353  CZ3 TRP B 145      21.979 -26.255 -24.912  1.00 59.02           C  
ANISOU 3353  CZ3 TRP B 145     6369   7425   8629  -2547  -1663   1029       C  
ATOM   3354  CH2 TRP B 145      22.653 -27.391 -25.376  1.00 59.17           C  
ANISOU 3354  CH2 TRP B 145     6714   7277   8490  -2685  -1734    919       C  
ATOM   3355  N   TYR B 146      18.185 -23.659 -26.663  1.00 50.77           N  
ANISOU 3355  N   TYR B 146     4492   6912   7887  -2637  -1911   1608       N  
ATOM   3356  CA  TYR B 146      17.298 -24.391 -25.767  1.00 57.45           C  
ANISOU 3356  CA  TYR B 146     5212   7767   8851  -2776  -1877   1729       C  
ATOM   3357  C   TYR B 146      15.868 -24.461 -26.285  1.00 70.44           C  
ANISOU 3357  C   TYR B 146     6639   9541  10585  -2979  -2032   1968       C  
ATOM   3358  O   TYR B 146      15.112 -25.340 -25.860  1.00 76.33           O  
ANISOU 3358  O   TYR B 146     7322  10284  11394  -3181  -2063   2068       O  
ATOM   3359  CB  TYR B 146      17.321 -23.753 -24.378  1.00 53.48           C  
ANISOU 3359  CB  TYR B 146     4542   7280   8497  -2553  -1641   1755       C  
ATOM   3360  CG  TYR B 146      18.468 -24.218 -23.515  1.00 53.60           C  
ANISOU 3360  CG  TYR B 146     4761   7154   8449  -2462  -1510   1570       C  
ATOM   3361  CD1 TYR B 146      18.478 -25.496 -22.974  1.00 52.39           C  
ANISOU 3361  CD1 TYR B 146     4740   6892   8275  -2636  -1502   1538       C  
ATOM   3362  CD2 TYR B 146      19.538 -23.378 -23.234  1.00 55.51           C  
ANISOU 3362  CD2 TYR B 146     5068   7369   8654  -2215  -1399   1442       C  
ATOM   3363  CE1 TYR B 146      19.521 -25.927 -22.180  1.00 50.43           C  
ANISOU 3363  CE1 TYR B 146     4679   6507   7974  -2558  -1389   1395       C  
ATOM   3364  CE2 TYR B 146      20.587 -23.800 -22.439  1.00 50.10           C  
ANISOU 3364  CE2 TYR B 146     4552   6564   7919  -2143  -1303   1303       C  
ATOM   3365  CZ  TYR B 146      20.573 -25.075 -21.915  1.00 51.63           C  
ANISOU 3365  CZ  TYR B 146     4871   6648   8097  -2312  -1300   1286       C  
ATOM   3366  OH  TYR B 146      21.618 -25.495 -21.123  1.00 50.46           O  
ANISOU 3366  OH  TYR B 146     4897   6371   7904  -2243  -1212   1171       O  
ATOM   3367  N   ALA B 147      15.480 -23.556 -27.183  1.00 74.51           N  
ANISOU 3367  N   ALA B 147     7027  10169  11113  -2954  -2150   2110       N  
ATOM   3368  CA  ALA B 147      14.132 -23.586 -27.737  1.00 75.01           C  
ANISOU 3368  CA  ALA B 147     6866  10371  11265  -3163  -2334   2388       C  
ATOM   3369  C   ALA B 147      14.006 -24.617 -28.852  1.00 72.12           C  
ANISOU 3369  C   ALA B 147     6713   9964  10724  -3491  -2598   2375       C  
ATOM   3370  O   ALA B 147      13.065 -25.419 -28.864  1.00 82.34           O  
ANISOU 3370  O   ALA B 147     7929  11297  12058  -3757  -2726   2516       O  
ATOM   3371  CB  ALA B 147      13.747 -22.200 -28.254  1.00 75.71           C  
ANISOU 3371  CB  ALA B 147     6737  10589  11439  -3012  -2357   2570       C  
ATOM   3372  N   ILE B 148      14.939 -24.604 -29.797  1.00 68.10           N  
ANISOU 3372  N   ILE B 148     6485   9374  10017  -3486  -2680   2212       N  
ATOM   3373  CA  ILE B 148      14.864 -25.493 -30.952  1.00 70.00           C  
ANISOU 3373  CA  ILE B 148     6976   9560  10060  -3794  -2928   2200       C  
ATOM   3374  C   ILE B 148      15.484 -26.855 -30.661  1.00 81.48           C  
ANISOU 3374  C   ILE B 148     8758  10827  11375  -3923  -2893   1987       C  
ATOM   3375  O   ILE B 148      14.944 -27.886 -31.067  1.00 97.11           O  
ANISOU 3375  O   ILE B 148    10874  12764  13259  -4243  -3071   2043       O  
ATOM   3376  CB  ILE B 148      15.530 -24.820 -32.166  1.00 65.93           C  
ANISOU 3376  CB  ILE B 148     6620   9037   9395  -3733  -3021   2143       C  
ATOM   3377  CG1 ILE B 148      14.997 -23.395 -32.329  1.00 66.19           C  
ANISOU 3377  CG1 ILE B 148     6333   9236   9581  -3567  -3011   2344       C  
ATOM   3378  CG2 ILE B 148      15.289 -25.642 -33.417  1.00 69.48           C  
ANISOU 3378  CG2 ILE B 148     7326   9441   9634  -4072  -3293   2170       C  
ATOM   3379  CD1 ILE B 148      15.779 -22.560 -33.313  1.00 64.30           C  
ANISOU 3379  CD1 ILE B 148     6225   8980   9227  -3444  -3036   2265       C  
ATOM   3380  N   CYS B 149      16.619 -26.891 -29.962  1.00 75.39           N  
ANISOU 3380  N   CYS B 149     8131   9935  10580  -3703  -2687   1775       N  
ATOM   3381  CA  CYS B 149      17.354 -28.142 -29.816  1.00 68.92           C  
ANISOU 3381  CA  CYS B 149     7669   8916   9602  -3826  -2675   1606       C  
ATOM   3382  C   CYS B 149      16.961 -28.935 -28.575  1.00 76.52           C  
ANISOU 3382  C   CYS B 149     8568   9828  10677  -3897  -2564   1626       C  
ATOM   3383  O   CYS B 149      16.926 -30.171 -28.621  1.00 85.59           O  
ANISOU 3383  O   CYS B 149     9972  10840  11710  -4139  -2632   1583       O  
ATOM   3384  CB  CYS B 149      18.859 -27.868 -29.795  1.00 57.79           C  
ANISOU 3384  CB  CYS B 149     6472   7390   8094  -3579  -2533   1387       C  
ATOM   3385  SG  CYS B 149      19.488 -27.099 -31.300  1.00 57.00           S  
ANISOU 3385  SG  CYS B 149     6513   7308   7838  -3518  -2644   1339       S  
ATOM   3386  N   HIS B 150      16.687 -28.263 -27.460  1.00 70.77           N  
ANISOU 3386  N   HIS B 150     7537   9190  10161  -3694  -2381   1690       N  
ATOM   3387  CA  HIS B 150      16.337 -28.921 -26.199  1.00 65.73           C  
ANISOU 3387  CA  HIS B 150     6827   8503   9645  -3741  -2243   1718       C  
ATOM   3388  C   HIS B 150      15.099 -28.243 -25.624  1.00 73.65           C  
ANISOU 3388  C   HIS B 150     7410   9689  10886  -3710  -2194   1951       C  
ATOM   3389  O   HIS B 150      15.162 -27.517 -24.624  1.00 69.64           O  
ANISOU 3389  O   HIS B 150     6711   9225  10523  -3471  -1988   1973       O  
ATOM   3390  CB  HIS B 150      17.528 -28.896 -25.242  1.00 57.77           C  
ANISOU 3390  CB  HIS B 150     5952   7371   8628  -3505  -2025   1538       C  
ATOM   3391  CG  HIS B 150      18.781 -29.457 -25.843  1.00 56.05           C  
ANISOU 3391  CG  HIS B 150     6124   6980   8192  -3504  -2063   1336       C  
ATOM   3392  ND1 HIS B 150      19.038 -30.810 -25.909  1.00 57.60           N  
ANISOU 3392  ND1 HIS B 150     6652   6986   8245  -3713  -2105   1254       N  
ATOM   3393  CD2 HIS B 150      19.832 -28.848 -26.439  1.00 53.26           C  
ANISOU 3393  CD2 HIS B 150     5892   6608   7736  -3321  -2059   1211       C  
ATOM   3394  CE1 HIS B 150      20.203 -31.011 -26.498  1.00 55.85           C  
ANISOU 3394  CE1 HIS B 150     6746   6632   7841  -3646  -2117   1092       C  
ATOM   3395  NE2 HIS B 150      20.705 -29.836 -26.831  1.00 53.20           N  
ANISOU 3395  NE2 HIS B 150     6274   6404   7535  -3413  -2092   1066       N  
ATOM   3396  N   PRO B 151      13.942 -28.489 -26.243  1.00 76.92           N  
ANISOU 3396  N   PRO B 151     7682  10207  11337  -3961  -2386   2145       N  
ATOM   3397  CA  PRO B 151      12.781 -27.593 -26.078  1.00 80.43           C  
ANISOU 3397  CA  PRO B 151     7708  10855  11996  -3906  -2381   2404       C  
ATOM   3398  C   PRO B 151      12.213 -27.455 -24.673  1.00 84.71           C  
ANISOU 3398  C   PRO B 151     7984  11439  12765  -3799  -2151   2520       C  
ATOM   3399  O   PRO B 151      11.668 -26.386 -24.369  1.00 98.70           O  
ANISOU 3399  O   PRO B 151     9451  13346  14703  -3609  -2056   2684       O  
ATOM   3400  CB  PRO B 151      11.751 -28.220 -27.034  1.00 81.94           C  
ANISOU 3400  CB  PRO B 151     7862  11120  12152  -4269  -2668   2584       C  
ATOM   3401  CG  PRO B 151      12.593 -28.892 -28.082  1.00 79.37           C  
ANISOU 3401  CG  PRO B 151     7959  10652  11546  -4419  -2836   2393       C  
ATOM   3402  CD  PRO B 151      13.720 -29.495 -27.297  1.00 75.97           C  
ANISOU 3402  CD  PRO B 151     7805  10024  11036  -4303  -2641   2145       C  
ATOM   3403  N   LEU B 152      12.314 -28.460 -23.801  1.00 74.88           N  
ANISOU 3403  N   LEU B 152     6850  10069  11531  -3905  -2041   2452       N  
ATOM   3404  CA  LEU B 152      11.551 -28.424 -22.554  1.00 84.52           C  
ANISOU 3404  CA  LEU B 152     7801  11338  12974  -3860  -1835   2611       C  
ATOM   3405  C   LEU B 152      12.421 -28.384 -21.299  1.00 87.45           C  
ANISOU 3405  C   LEU B 152     8288  11581  13357  -3639  -1554   2461       C  
ATOM   3406  O   LEU B 152      11.918 -28.648 -20.199  1.00 86.13           O  
ANISOU 3406  O   LEU B 152     7988  11402  13336  -3643  -1364   2562       O  
ATOM   3407  CB  LEU B 152      10.585 -29.607 -22.476  1.00 97.86           C  
ANISOU 3407  CB  LEU B 152     9445  13017  14720  -4214  -1929   2742       C  
ATOM   3408  CG  LEU B 152       9.417 -29.568 -23.469  1.00104.13           C  
ANISOU 3408  CG  LEU B 152    10018  13980  15567  -4452  -2196   2984       C  
ATOM   3409  CD1 LEU B 152       8.689 -30.910 -23.532  1.00108.47           C  
ANISOU 3409  CD1 LEU B 152    10620  14480  16112  -4855  -2331   3062       C  
ATOM   3410  CD2 LEU B 152       8.455 -28.441 -23.115  1.00103.99           C  
ANISOU 3410  CD2 LEU B 152     9547  14167  15798  -4273  -2102   3264       C  
ATOM   3411  N   LEU B 153      13.707 -28.061 -21.422  1.00 88.88           N  
ANISOU 3411  N   LEU B 153     8711  11669  13390  -3452  -1520   2239       N  
ATOM   3412  CA  LEU B 153      14.543 -27.942 -20.233  1.00 85.06           C  
ANISOU 3412  CA  LEU B 153     8324  11077  12916  -3246  -1276   2124       C  
ATOM   3413  C   LEU B 153      14.316 -26.602 -19.536  1.00 86.19           C  
ANISOU 3413  C   LEU B 153     8204  11333  13209  -2957  -1091   2240       C  
ATOM   3414  O   LEU B 153      13.842 -26.554 -18.396  1.00 84.99           O  
ANISOU 3414  O   LEU B 153     7909  11182  13201  -2895   -879   2359       O  
ATOM   3415  CB  LEU B 153      16.015 -28.121 -20.608  1.00 77.62           C  
ANISOU 3415  CB  LEU B 153     7726   9995  11771  -3164  -1318   1868       C  
ATOM   3416  CG  LEU B 153      16.549 -29.546 -20.460  1.00 74.82           C  
ANISOU 3416  CG  LEU B 153     7700   9436  11293  -3357  -1333   1737       C  
ATOM   3417  CD1 LEU B 153      15.771 -30.511 -21.340  1.00 80.86           C  
ANISOU 3417  CD1 LEU B 153     8530  10191  12003  -3686  -1538   1796       C  
ATOM   3418  CD2 LEU B 153      18.027 -29.583 -20.790  1.00 71.89           C  
ANISOU 3418  CD2 LEU B 153     7635   8937  10743  -3229  -1355   1518       C  
ATOM   3419  N   PHE B 154      14.646 -25.504 -20.209  1.00 84.77           N  
ANISOU 3419  N   PHE B 154     7982  11233  12993  -2775  -1152   2213       N  
ATOM   3420  CA  PHE B 154      14.460 -24.163 -19.677  1.00 82.40           C  
ANISOU 3420  CA  PHE B 154     7473  11018  12817  -2498   -986   2320       C  
ATOM   3421  C   PHE B 154      13.438 -23.421 -20.528  1.00 82.31           C  
ANISOU 3421  C   PHE B 154     7204  11169  12900  -2505  -1103   2525       C  
ATOM   3422  O   PHE B 154      13.419 -23.565 -21.756  1.00 80.72           O  
ANISOU 3422  O   PHE B 154     7065  11006  12599  -2640  -1332   2498       O  
ATOM   3423  CB  PHE B 154      15.787 -23.397 -19.658  1.00 79.21           C  
ANISOU 3423  CB  PHE B 154     7252  10549  12294  -2265   -934   2121       C  
ATOM   3424  CG  PHE B 154      16.851 -24.033 -18.798  1.00 73.31           C  
ANISOU 3424  CG  PHE B 154     6742   9649  11464  -2242   -829   1950       C  
ATOM   3425  CD1 PHE B 154      16.973 -23.705 -17.457  1.00 68.99           C  
ANISOU 3425  CD1 PHE B 154     6150   9057  11008  -2087   -592   1997       C  
ATOM   3426  CD2 PHE B 154      17.730 -24.960 -19.336  1.00 68.95           C  
ANISOU 3426  CD2 PHE B 154     6468   8986  10744  -2371   -961   1762       C  
ATOM   3427  CE1 PHE B 154      17.953 -24.287 -16.671  1.00 62.68           C  
ANISOU 3427  CE1 PHE B 154     5572   8112  10133  -2077   -508   1866       C  
ATOM   3428  CE2 PHE B 154      18.708 -25.546 -18.555  1.00 66.21           C  
ANISOU 3428  CE2 PHE B 154     6337   8491  10330  -2348   -872   1633       C  
ATOM   3429  CZ  PHE B 154      18.820 -25.210 -17.222  1.00 64.12           C  
ANISOU 3429  CZ  PHE B 154     6017   8189  10157  -2208   -656   1688       C  
ATOM   3430  N   LYS B 155      12.590 -22.629 -19.876  1.00 86.03           N  
ANISOU 3430  N   LYS B 155     7397  11727  13565  -2355   -937   2749       N  
ATOM   3431  CA  LYS B 155      11.553 -21.858 -20.549  1.00 94.65           C  
ANISOU 3431  CA  LYS B 155     8212  12971  14779  -2336  -1018   2994       C  
ATOM   3432  C   LYS B 155      11.859 -20.367 -20.455  1.00 91.18           C  
ANISOU 3432  C   LYS B 155     7724  12548  14372  -2023   -882   3015       C  
ATOM   3433  O   LYS B 155      12.127 -19.850 -19.364  1.00 90.85           O  
ANISOU 3433  O   LYS B 155     7681  12443  14394  -1807   -631   3012       O  
ATOM   3434  CB  LYS B 155      10.175 -22.154 -19.954  1.00103.22           C  
ANISOU 3434  CB  LYS B 155     8983  14146  16088  -2422   -934   3293       C  
ATOM   3435  CG  LYS B 155       9.504 -23.407 -20.516  1.00107.92           C  
ANISOU 3435  CG  LYS B 155     9547  14782  16675  -2786  -1156   3359       C  
ATOM   3436  CD  LYS B 155       9.853 -24.657 -19.717  1.00106.71           C  
ANISOU 3436  CD  LYS B 155     9577  14495  16472  -2942  -1072   3217       C  
ATOM   3437  CE  LYS B 155       9.161 -25.888 -20.291  1.00112.36           C  
ANISOU 3437  CE  LYS B 155    10282  15233  17176  -3323  -1293   3285       C  
ATOM   3438  NZ  LYS B 155       9.198 -27.049 -19.357  1.00117.12           N  
ANISOU 3438  NZ  LYS B 155    11002  15711  17790  -3477  -1161   3222       N  
ATOM   3439  N   SER B 156      11.810 -19.685 -21.597  1.00 87.22           N  
ANISOU 3439  N   SER B 156     7197  12119  13822  -2009  -1041   3043       N  
ATOM   3440  CA  SER B 156      12.083 -18.257 -21.685  1.00 85.81           C  
ANISOU 3440  CA  SER B 156     6992  11949  13663  -1742   -933   3062       C  
ATOM   3441  C   SER B 156      10.784 -17.461 -21.663  1.00 86.53           C  
ANISOU 3441  C   SER B 156     6740  12162  13973  -1654   -862   3415       C  
ATOM   3442  O   SER B 156       9.848 -17.769 -22.408  1.00 95.33           O  
ANISOU 3442  O   SER B 156     7665  13399  15159  -1836  -1047   3625       O  
ATOM   3443  CB  SER B 156      12.867 -17.938 -22.956  1.00 89.70           C  
ANISOU 3443  CB  SER B 156     7669  12434  13980  -1771  -1131   2909       C  
ATOM   3444  OG  SER B 156      12.010 -17.914 -24.085  1.00 96.40           O  
ANISOU 3444  OG  SER B 156     8354  13405  14869  -1932  -1354   3132       O  
ATOM   3445  N   THR B 157      10.734 -16.443 -20.807  1.00 81.03           N  
ANISOU 3445  N   THR B 157     5968  11429  13390  -1378   -596   3508       N  
ATOM   3446  CA  THR B 157       9.612 -15.517 -20.709  1.00 86.41           C  
ANISOU 3446  CA  THR B 157     6346  12200  14286  -1227   -469   3854       C  
ATOM   3447  C   THR B 157      10.118 -14.090 -20.892  1.00 94.05           C  
ANISOU 3447  C   THR B 157     7389  13122  15225   -974   -356   3823       C  
ATOM   3448  O   THR B 157      11.326 -13.837 -20.949  1.00100.57           O  
ANISOU 3448  O   THR B 157     8487  13847  15878   -914   -359   3536       O  
ATOM   3449  CB  THR B 157       8.885 -15.644 -19.366  1.00 88.62           C  
ANISOU 3449  CB  THR B 157     6449  12456  14765  -1112   -186   4058       C  
ATOM   3450  OG1 THR B 157       9.845 -15.596 -18.304  1.00 79.49           O  
ANISOU 3450  OG1 THR B 157     5526  11143  13533   -962     30   3842       O  
ATOM   3451  CG2 THR B 157       8.115 -16.951 -19.296  1.00 99.53           C  
ANISOU 3451  CG2 THR B 157     7686  13913  16219  -1381   -301   4163       C  
ATOM   3452  N   ALA B 158       9.173 -13.151 -21.005  1.00 98.22           N  
ANISOU 3452  N   ALA B 158     7666  13724  15930   -829   -255   4138       N  
ATOM   3453  CA  ALA B 158       9.550 -11.746 -21.098  1.00 92.15           C  
ANISOU 3453  CA  ALA B 158     6960  12900  15155   -581   -110   4144       C  
ATOM   3454  C   ALA B 158      10.112 -11.214 -19.791  1.00 89.59           C  
ANISOU 3454  C   ALA B 158     6780  12414  14848   -332    218   4062       C  
ATOM   3455  O   ALA B 158      10.988 -10.341 -19.809  1.00 91.66           O  
ANISOU 3455  O   ALA B 158     7236  12582  15010   -190    294   3900       O  
ATOM   3456  CB  ALA B 158       8.344 -10.905 -21.534  1.00 99.57           C  
ANISOU 3456  CB  ALA B 158     7586  13954  16290   -485    -65   4538       C  
ATOM   3457  N   ARG B 159       9.631 -11.713 -18.652  1.00 90.81           N  
ANISOU 3457  N   ARG B 159     6850  12528  15126   -282    422   4175       N  
ATOM   3458  CA  ARG B 159      10.211 -11.280 -17.384  1.00 92.13           C  
ANISOU 3458  CA  ARG B 159     7190  12525  15291    -55    741   4089       C  
ATOM   3459  C   ARG B 159      11.624 -11.821 -17.223  1.00 89.65           C  
ANISOU 3459  C   ARG B 159     7187  12120  14758   -153    638   3701       C  
ATOM   3460  O   ARG B 159      12.497 -11.144 -16.666  1.00 87.23           O  
ANISOU 3460  O   ARG B 159     7084  11682  14378     12    802   3555       O  
ATOM   3461  CB  ARG B 159       9.350 -11.715 -16.200  1.00100.46           C  
ANISOU 3461  CB  ARG B 159     8096  13548  16526     29   1010   4309       C  
ATOM   3462  CG  ARG B 159      10.005 -11.379 -14.861  1.00101.09           C  
ANISOU 3462  CG  ARG B 159     8403  13430  16576    250   1350   4200       C  
ATOM   3463  CD  ARG B 159       9.696 -12.380 -13.759  1.00101.30           C  
ANISOU 3463  CD  ARG B 159     8414  13410  16667    215   1516   4234       C  
ATOM   3464  NE  ARG B 159       8.329 -12.894 -13.789  1.00105.94           N  
ANISOU 3464  NE  ARG B 159     8678  14118  17456    143   1525   4545       N  
ATOM   3465  CZ  ARG B 159       8.031 -14.178 -13.956  1.00110.86           C  
ANISOU 3465  CZ  ARG B 159     9201  14839  18082   -134   1328   4522       C  
ATOM   3466  NH1 ARG B 159       9.007 -15.065 -14.099  1.00102.56           N  
ANISOU 3466  NH1 ARG B 159     8366  13763  16838   -345   1126   4204       N  
ATOM   3467  NH2 ARG B 159       6.767 -14.581 -13.966  1.00119.73           N  
ANISOU 3467  NH2 ARG B 159    10011  16075  19403   -202   1344   4826       N  
ATOM   3468  N   ARG B 160      11.863 -13.044 -17.702  1.00 92.62           N  
ANISOU 3468  N   ARG B 160     7604  12556  15029   -421    376   3544       N  
ATOM   3469  CA  ARG B 160      13.201 -13.616 -17.630  1.00 91.21           C  
ANISOU 3469  CA  ARG B 160     7711  12296  14648   -513    271   3200       C  
ATOM   3470  C   ARG B 160      14.154 -12.917 -18.589  1.00 88.94           C  
ANISOU 3470  C   ARG B 160     7595  12000  14200   -497    117   3000       C  
ATOM   3471  O   ARG B 160      15.359 -12.849 -18.323  1.00 96.58           O  
ANISOU 3471  O   ARG B 160     8792  12873  15030   -462    125   2754       O  
ATOM   3472  CB  ARG B 160      13.141 -15.114 -17.942  1.00 95.98           C  
ANISOU 3472  CB  ARG B 160     8329  12952  15187   -797     54   3112       C  
ATOM   3473  CG  ARG B 160      12.549 -15.956 -16.826  1.00106.40           C  
ANISOU 3473  CG  ARG B 160     9556  14246  16625   -835    222   3229       C  
ATOM   3474  CD  ARG B 160      13.578 -16.286 -15.758  1.00111.13           C  
ANISOU 3474  CD  ARG B 160    10386  14702  17136   -776    374   3029       C  
ATOM   3475  NE  ARG B 160      12.968 -16.443 -14.439  1.00120.92           N  
ANISOU 3475  NE  ARG B 160    11542  15882  18521   -668    682   3199       N  
ATOM   3476  CZ  ARG B 160      12.400 -17.562 -13.999  1.00126.58           C  
ANISOU 3476  CZ  ARG B 160    12186  16613  19297   -829    703   3272       C  
ATOM   3477  NH1 ARG B 160      12.355 -18.639 -14.771  1.00127.55           N  
ANISOU 3477  NH1 ARG B 160    12312  16803  19347  -1116    426   3190       N  
ATOM   3478  NH2 ARG B 160      11.874 -17.602 -12.782  1.00127.83           N  
ANISOU 3478  NH2 ARG B 160    12289  16701  19579   -702   1023   3427       N  
ATOM   3479  N   ALA B 161      13.633 -12.390 -19.700  1.00 82.65           N  
ANISOU 3479  N   ALA B 161     6680  11300  13422   -524    -20   3115       N  
ATOM   3480  CA  ALA B 161      14.477 -11.661 -20.639  1.00 77.06           C  
ANISOU 3480  CA  ALA B 161     6128  10582  12571   -500   -140   2942       C  
ATOM   3481  C   ALA B 161      14.946 -10.341 -20.044  1.00 78.10           C  
ANISOU 3481  C   ALA B 161     6334  10614  12728   -250     95   2939       C  
ATOM   3482  O   ALA B 161      16.140 -10.021 -20.077  1.00 87.36           O  
ANISOU 3482  O   ALA B 161     7726  11709  13759   -218     76   2696       O  
ATOM   3483  CB  ALA B 161      13.728 -11.423 -21.950  1.00 78.19           C  
ANISOU 3483  CB  ALA B 161     6115  10853  12739   -593   -327   3098       C  
ATOM   3484  N   LEU B 162      14.015  -9.557 -19.490  1.00 73.30           N  
ANISOU 3484  N   LEU B 162     5548   9998  12303    -67    330   3221       N  
ATOM   3485  CA  LEU B 162      14.395  -8.283 -18.889  1.00 70.95           C  
ANISOU 3485  CA  LEU B 162     5343   9581  12034    179    590   3239       C  
ATOM   3486  C   LEU B 162      15.314  -8.481 -17.693  1.00 66.38           C  
ANISOU 3486  C   LEU B 162     4969   8859  11394    249    756   3055       C  
ATOM   3487  O   LEU B 162      16.145  -7.613 -17.400  1.00 74.63           O  
ANISOU 3487  O   LEU B 162     6182   9795  12378    378    877   2940       O  
ATOM   3488  CB  LEU B 162      13.146  -7.494 -18.487  1.00 85.15           C  
ANISOU 3488  CB  LEU B 162     6927  11379  14045    380    852   3605       C  
ATOM   3489  CG  LEU B 162      12.253  -7.041 -19.643  1.00101.49           C  
ANISOU 3489  CG  LEU B 162     8777  13589  16196    349    719   3834       C  
ATOM   3490  CD1 LEU B 162      10.814  -6.908 -19.175  1.00107.35           C  
ANISOU 3490  CD1 LEU B 162     9236  14376  17175    471    920   4233       C  
ATOM   3491  CD2 LEU B 162      12.760  -5.729 -20.222  1.00104.24           C  
ANISOU 3491  CD2 LEU B 162     9225  13893  16487    475    760   3795       C  
ATOM   3492  N   GLY B 163      15.189  -9.609 -16.993  1.00 59.90           N  
ANISOU 3492  N   GLY B 163     4137   8034  10590    157    766   3034       N  
ATOM   3493  CA  GLY B 163      16.131  -9.897 -15.925  1.00 65.61           C  
ANISOU 3493  CA  GLY B 163     5057   8629  11243    199    898   2856       C  
ATOM   3494  C   GLY B 163      17.513 -10.213 -16.459  1.00 73.39           C  
ANISOU 3494  C   GLY B 163     6242   9611  12033     62    656   2540       C  
ATOM   3495  O   GLY B 163      18.524  -9.834 -15.861  1.00 77.04           O  
ANISOU 3495  O   GLY B 163     6877   9967  12429    142    753   2392       O  
ATOM   3496  N   SER B 164      17.577 -10.922 -17.586  1.00 67.19           N  
ANISOU 3496  N   SER B 164     5444   8933  11153   -139    354   2442       N  
ATOM   3497  CA  SER B 164      18.863 -11.158 -18.228  1.00 48.47           C  
ANISOU 3497  CA  SER B 164     3274   6553   8591   -241    146   2157       C  
ATOM   3498  C   SER B 164      19.455  -9.863 -18.768  1.00 55.60           C  
ANISOU 3498  C   SER B 164     4254   7431   9442   -129    154   2091       C  
ATOM   3499  O   SER B 164      20.667  -9.636 -18.666  1.00 57.04           O  
ANISOU 3499  O   SER B 164     4609   7550   9513   -114    123   1888       O  
ATOM   3500  CB  SER B 164      18.710 -12.182 -19.350  1.00 40.72           C  
ANISOU 3500  CB  SER B 164     2289   5665   7516   -455   -123   2088       C  
ATOM   3501  OG  SER B 164      18.037 -13.337 -18.886  1.00 45.26           O  
ANISOU 3501  OG  SER B 164     2775   6265   8158   -573   -127   2177       O  
ATOM   3502  N   ILE B 165      18.617  -9.008 -19.356  1.00 58.70           N  
ANISOU 3502  N   ILE B 165     4510   7874   9920    -56    191   2273       N  
ATOM   3503  CA  ILE B 165      19.118  -7.758 -19.917  1.00 53.72           C  
ANISOU 3503  CA  ILE B 165     3946   7218   9248     43    207   2228       C  
ATOM   3504  C   ILE B 165      19.725  -6.887 -18.828  1.00 55.72           C  
ANISOU 3504  C   ILE B 165     4301   7334   9536    221    453   2204       C  
ATOM   3505  O   ILE B 165      20.719  -6.186 -19.058  1.00 64.11           O  
ANISOU 3505  O   ILE B 165     5499   8347  10514    253    429   2050       O  
ATOM   3506  CB  ILE B 165      17.994  -7.021 -20.669  1.00 48.70           C  
ANISOU 3506  CB  ILE B 165     3124   6659   8722     98    225   2474       C  
ATOM   3507  CG1 ILE B 165      17.723  -7.702 -22.010  1.00 53.07           C  
ANISOU 3507  CG1 ILE B 165     3628   7338   9200    -93    -54   2446       C  
ATOM   3508  CG2 ILE B 165      18.363  -5.561 -20.865  1.00 42.87           C  
ANISOU 3508  CG2 ILE B 165     2440   5859   7989    256    346   2489       C  
ATOM   3509  CD1 ILE B 165      16.307  -7.559 -22.488  1.00 63.59           C  
ANISOU 3509  CD1 ILE B 165     4705   8776  10680    -97    -63   2751       C  
ATOM   3510  N   LEU B 166      19.136  -6.901 -17.629  1.00 51.87           N  
ANISOU 3510  N   LEU B 166     3760   6773   9175    344    715   2363       N  
ATOM   3511  CA  LEU B 166      19.738  -6.163 -16.524  1.00 49.47           C  
ANISOU 3511  CA  LEU B 166     3597   6310   8889    518    990   2331       C  
ATOM   3512  C   LEU B 166      21.009  -6.837 -16.027  1.00 42.95           C  
ANISOU 3512  C   LEU B 166     2928   5439   7953    423    898   2084       C  
ATOM   3513  O   LEU B 166      21.899  -6.162 -15.499  1.00 47.79           O  
ANISOU 3513  O   LEU B 166     3682   5938   8537    516   1025   1982       O  
ATOM   3514  CB  LEU B 166      18.734  -6.003 -15.380  1.00 54.76           C  
ANISOU 3514  CB  LEU B 166     4217   6887   9702    703   1350   2571       C  
ATOM   3515  CG  LEU B 166      17.673  -4.919 -15.581  1.00 57.52           C  
ANISOU 3515  CG  LEU B 166     4462   7218  10173    886   1556   2840       C  
ATOM   3516  CD1 LEU B 166      16.492  -5.139 -14.644  1.00 67.62           C  
ANISOU 3516  CD1 LEU B 166     5649   8447  11598   1025   1847   3101       C  
ATOM   3517  CD2 LEU B 166      18.280  -3.539 -15.371  1.00 55.38           C  
ANISOU 3517  CD2 LEU B 166     4381   6797   9863   1069   1776   2798       C  
ATOM   3518  N   GLY B 167      21.112  -8.157 -16.183  1.00 39.03           N  
ANISOU 3518  N   GLY B 167     2412   5019   7400    242    689   1996       N  
ATOM   3519  CA  GLY B 167      22.348  -8.835 -15.836  1.00 44.00           C  
ANISOU 3519  CA  GLY B 167     3180   5614   7923    145    571   1777       C  
ATOM   3520  C   GLY B 167      23.456  -8.558 -16.831  1.00 55.20           C  
ANISOU 3520  C   GLY B 167     4709   7069   9197     64    326   1565       C  
ATOM   3521  O   GLY B 167      24.631  -8.473 -16.461  1.00 57.15           O  
ANISOU 3521  O   GLY B 167     5072   7257   9387     58    289   1411       O  
ATOM   3522  N   ILE B 168      23.103  -8.433 -18.113  1.00 65.17           N  
ANISOU 3522  N   ILE B 168     5936   8426  10400      2    165   1563       N  
ATOM   3523  CA  ILE B 168      24.115  -8.148 -19.125  1.00 48.09           C  
ANISOU 3523  CA  ILE B 168     3898   6289   8085    -55    -19   1371       C  
ATOM   3524  C   ILE B 168      24.783  -6.810 -18.853  1.00 45.70           C  
ANISOU 3524  C   ILE B 168     3645   5906   7812     67     92   1346       C  
ATOM   3525  O   ILE B 168      25.990  -6.645 -19.070  1.00 49.35           O  
ANISOU 3525  O   ILE B 168     4231   6349   8172     31    -15   1168       O  
ATOM   3526  CB  ILE B 168      23.492  -8.186 -20.531  1.00 41.70           C  
ANISOU 3526  CB  ILE B 168     3037   5581   7227   -124   -155   1404       C  
ATOM   3527  CG1 ILE B 168      23.079  -9.613 -20.881  1.00 41.98           C  
ANISOU 3527  CG1 ILE B 168     3056   5679   7217   -271   -288   1389       C  
ATOM   3528  CG2 ILE B 168      24.471  -7.634 -21.546  1.00 37.67           C  
ANISOU 3528  CG2 ILE B 168     2652   5081   6581   -138   -267   1239       C  
ATOM   3529  CD1 ILE B 168      22.206  -9.699 -22.096  1.00 40.02           C  
ANISOU 3529  CD1 ILE B 168     2708   5518   6979   -343   -398   1494       C  
ATOM   3530  N   TRP B 169      24.012  -5.833 -18.377  1.00 50.92           N  
ANISOU 3530  N   TRP B 169     4218   6510   8618    221    328   1536       N  
ATOM   3531  CA  TRP B 169      24.587  -4.531 -18.066  1.00 50.34           C  
ANISOU 3531  CA  TRP B 169     4209   6330   8590    356    485   1527       C  
ATOM   3532  C   TRP B 169      25.374  -4.553 -16.762  1.00 57.33           C  
ANISOU 3532  C   TRP B 169     5182   7085   9516    419    638   1455       C  
ATOM   3533  O   TRP B 169      26.424  -3.909 -16.659  1.00 70.66           O  
ANISOU 3533  O   TRP B 169     6957   8696  11195    442    628   1334       O  
ATOM   3534  CB  TRP B 169      23.491  -3.470 -18.013  1.00 41.00           C  
ANISOU 3534  CB  TRP B 169     2947   5101   7529    534    741   1761       C  
ATOM   3535  CG  TRP B 169      23.077  -2.990 -19.367  1.00 45.02           C  
ANISOU 3535  CG  TRP B 169     3383   5710   8012    497    599   1814       C  
ATOM   3536  CD1 TRP B 169      22.030  -3.442 -20.116  1.00 45.24           C  
ANISOU 3536  CD1 TRP B 169     3272   5858   8060    435    496   1944       C  
ATOM   3537  CD2 TRP B 169      23.713  -1.967 -20.141  1.00 46.98           C  
ANISOU 3537  CD2 TRP B 169     3692   5940   8218    521    553   1748       C  
ATOM   3538  NE1 TRP B 169      21.971  -2.758 -21.307  1.00 47.99           N  
ANISOU 3538  NE1 TRP B 169     3594   6263   8377    424    395   1964       N  
ATOM   3539  CE2 TRP B 169      22.995  -1.847 -21.347  1.00 39.53           C  
ANISOU 3539  CE2 TRP B 169     2647   5109   7264    478    432   1844       C  
ATOM   3540  CE3 TRP B 169      24.820  -1.139 -19.930  1.00 42.35           C  
ANISOU 3540  CE3 TRP B 169     3229   5247   7617    572    607   1626       C  
ATOM   3541  CZ2 TRP B 169      23.347  -0.932 -22.338  1.00 34.35           C  
ANISOU 3541  CZ2 TRP B 169     2016   4463   6573    493    376   1822       C  
ATOM   3542  CZ3 TRP B 169      25.169  -0.232 -20.913  1.00 34.84           C  
ANISOU 3542  CZ3 TRP B 169     2295   4304   6637    579    544   1605       C  
ATOM   3543  CH2 TRP B 169      24.435  -0.135 -22.102  1.00 36.98           C  
ANISOU 3543  CH2 TRP B 169     2472   4691   6888    543    435   1703       C  
ATOM   3544  N   ALA B 170      24.881  -5.272 -15.751  1.00 50.63           N  
ANISOU 3544  N   ALA B 170     4313   6200   8726    452    795   1535       N  
ATOM   3545  CA  ALA B 170      25.613  -5.357 -14.493  1.00 54.75           C  
ANISOU 3545  CA  ALA B 170     5007   6576   9221    508    955   1438       C  
ATOM   3546  C   ALA B 170      26.986  -5.981 -14.699  1.00 58.11           C  
ANISOU 3546  C   ALA B 170     5573   7031   9477    316    607   1185       C  
ATOM   3547  O   ALA B 170      27.962  -5.581 -14.052  1.00 63.50           O  
ANISOU 3547  O   ALA B 170     6597   7577   9954    302    582   1001       O  
ATOM   3548  CB  ALA B 170      24.808  -6.154 -13.467  1.00 68.71           C  
ANISOU 3548  CB  ALA B 170     6799   8302  11007    547   1167   1550       C  
ATOM   3549  N   VAL B 171      27.081  -6.968 -15.590  1.00 55.55           N  
ANISOU 3549  N   VAL B 171     5054   6870   9183    160    332   1167       N  
ATOM   3550  CA  VAL B 171      28.371  -7.591 -15.874  1.00 42.37           C  
ANISOU 3550  CA  VAL B 171     3482   5233   7382     17     41    963       C  
ATOM   3551  C   VAL B 171      29.234  -6.674 -16.732  1.00 45.66           C  
ANISOU 3551  C   VAL B 171     3972   5660   7715      3    -88    846       C  
ATOM   3552  O   VAL B 171      30.407  -6.431 -16.423  1.00 50.94           O  
ANISOU 3552  O   VAL B 171     4748   6276   8333    -38   -198    711       O  
ATOM   3553  CB  VAL B 171      28.168  -8.960 -16.541  1.00 41.57           C  
ANISOU 3553  CB  VAL B 171     3421   5235   7136   -110   -140    910       C  
ATOM   3554  CG1 VAL B 171      29.510  -9.553 -16.939  1.00 47.99           C  
ANISOU 3554  CG1 VAL B 171     4389   6073   7771   -198   -359    711       C  
ATOM   3555  CG2 VAL B 171      27.424  -9.890 -15.603  1.00 35.84           C  
ANISOU 3555  CG2 VAL B 171     2620   4486   6512   -122    -23   1027       C  
ATOM   3556  N   SER B 172      28.665  -6.144 -17.818  1.00 46.37           N  
ANISOU 3556  N   SER B 172     4044   5815   7759     25    -83    891       N  
ATOM   3557  CA  SER B 172      29.440  -5.300 -18.720  1.00 38.46           C  
ANISOU 3557  CA  SER B 172     3110   4825   6676     12   -177    795       C  
ATOM   3558  C   SER B 172      30.006  -4.082 -17.999  1.00 44.54           C  
ANISOU 3558  C   SER B 172     3858   5460   7603     93    -65    807       C  
ATOM   3559  O   SER B 172      31.156  -3.693 -18.234  1.00 40.35           O  
ANISOU 3559  O   SER B 172     3398   4910   7023     24   -205    677       O  
ATOM   3560  CB  SER B 172      28.575  -4.859 -19.899  1.00 34.89           C  
ANISOU 3560  CB  SER B 172     2613   4447   6198     37   -159    878       C  
ATOM   3561  OG  SER B 172      28.134  -5.971 -20.655  1.00 44.10           O  
ANISOU 3561  OG  SER B 172     3793   5715   7248    -49   -269    849       O  
ATOM   3562  N   LEU B 173      29.209  -3.459 -17.127  1.00 49.79           N  
ANISOU 3562  N   LEU B 173     4548   6004   8366    245    225    931       N  
ATOM   3563  CA  LEU B 173      29.700  -2.307 -16.376  1.00 41.65           C  
ANISOU 3563  CA  LEU B 173     3872   4765   7189    306    382    834       C  
ATOM   3564  C   LEU B 173      30.825  -2.700 -15.425  1.00 45.08           C  
ANISOU 3564  C   LEU B 173     4616   5113   7401    178    246    629       C  
ATOM   3565  O   LEU B 173      31.759  -1.921 -15.203  1.00 42.28           O  
ANISOU 3565  O   LEU B 173     4510   4648   6907    112    190    495       O  
ATOM   3566  CB  LEU B 173      28.554  -1.652 -15.606  1.00 36.42           C  
ANISOU 3566  CB  LEU B 173     3320   3955   6564    512    770    990       C  
ATOM   3567  CG  LEU B 173      27.461  -0.979 -16.444  1.00 37.35           C  
ANISOU 3567  CG  LEU B 173     3150   4135   6904    680    943   1229       C  
ATOM   3568  CD1 LEU B 173      26.184  -0.808 -15.633  1.00 33.85           C  
ANISOU 3568  CD1 LEU B 173     2714   3601   6547    894   1330   1438       C  
ATOM   3569  CD2 LEU B 173      27.942   0.365 -16.972  1.00 34.72           C  
ANISOU 3569  CD2 LEU B 173     2955   3699   6539    728    983   1186       C  
ATOM   3570  N   ALA B 174      30.755  -3.906 -14.856  1.00 47.97           N  
ANISOU 3570  N   ALA B 174     4969   5528   7729    129    181    617       N  
ATOM   3571  CA  ALA B 174      31.753  -4.334 -13.880  1.00 53.07           C  
ANISOU 3571  CA  ALA B 174     5903   6101   8161     25     50    456       C  
ATOM   3572  C   ALA B 174      33.079  -4.688 -14.546  1.00 57.82           C  
ANISOU 3572  C   ALA B 174     6413   6821   8734   -127   -284    333       C  
ATOM   3573  O   ALA B 174      34.133  -4.158 -14.180  1.00 61.49           O  
ANISOU 3573  O   ALA B 174     7088   7220   9057   -218   -400    213       O  
ATOM   3574  CB  ALA B 174      31.225  -5.528 -13.086  1.00 55.09           C  
ANISOU 3574  CB  ALA B 174     6175   6367   8391     39    103    501       C  
ATOM   3575  N   ILE B 175      33.047  -5.594 -15.526  1.00 51.38           N  
ANISOU 3575  N   ILE B 175     5294   6178   8049   -164   -437    374       N  
ATOM   3576  CA  ILE B 175      34.277  -6.140 -16.089  1.00 40.30           C  
ANISOU 3576  CA  ILE B 175     3813   4880   6620   -275   -710    279       C  
ATOM   3577  C   ILE B 175      35.084  -5.122 -16.877  1.00 49.25           C  
ANISOU 3577  C   ILE B 175     4913   6028   7773   -321   -796    228       C  
ATOM   3578  O   ILE B 175      36.259  -5.375 -17.170  1.00 53.99           O  
ANISOU 3578  O   ILE B 175     5621   6699   8193   -365   -896    143       O  
ATOM   3579  CB  ILE B 175      33.966  -7.372 -16.967  1.00 29.11           C  
ANISOU 3579  CB  ILE B 175     2324   3600   5136   -260   -721    302       C  
ATOM   3580  CG1 ILE B 175      33.219  -6.975 -18.243  1.00 40.17           C  
ANISOU 3580  CG1 ILE B 175     3683   5069   6510   -213   -616    352       C  
ATOM   3581  CG2 ILE B 175      33.177  -8.401 -16.175  1.00 22.42           C  
ANISOU 3581  CG2 ILE B 175     1417   2730   4371   -258   -688    374       C  
ATOM   3582  CD1 ILE B 175      33.099  -8.105 -19.225  1.00 40.68           C  
ANISOU 3582  CD1 ILE B 175     3806   5237   6412   -228   -626    317       C  
ATOM   3583  N   MET B 176      34.498  -3.986 -17.237  1.00 54.82           N  
ANISOU 3583  N   MET B 176     5619   6671   8540   -255   -637    282       N  
ATOM   3584  CA  MET B 176      35.224  -2.940 -17.942  1.00 50.88           C  
ANISOU 3584  CA  MET B 176     5119   6160   8053   -302   -693    239       C  
ATOM   3585  C   MET B 176      35.785  -1.871 -17.015  1.00 50.80           C  
ANISOU 3585  C   MET B 176     5437   5973   7891   -356   -639    151       C  
ATOM   3586  O   MET B 176      36.417  -0.922 -17.494  1.00 48.71           O  
ANISOU 3586  O   MET B 176     5210   5672   7625   -419   -676    113       O  
ATOM   3587  CB  MET B 176      34.321  -2.286 -18.993  1.00 47.16           C  
ANISOU 3587  CB  MET B 176     4469   5718   7730   -203   -565    360       C  
ATOM   3588  CG  MET B 176      33.929  -3.217 -20.128  1.00 46.27           C  
ANISOU 3588  CG  MET B 176     4410   5769   7401   -164   -550    367       C  
ATOM   3589  SD  MET B 176      35.344  -4.143 -20.758  1.00 47.54           S  
ANISOU 3589  SD  MET B 176     4725   6047   7290   -229   -654    226       S  
ATOM   3590  CE  MET B 176      34.577  -5.069 -22.086  1.00 52.99           C  
ANISOU 3590  CE  MET B 176     5423   6846   7866   -197   -609    247       C  
ATOM   3591  N   VAL B 177      35.567  -1.999 -15.706  1.00 47.75           N  
ANISOU 3591  N   VAL B 177     5318   5462   7361   -347   -551    118       N  
ATOM   3592  CA  VAL B 177      36.158  -1.053 -14.760  1.00 38.23           C  
ANISOU 3592  CA  VAL B 177     4493   4070   5964   -437   -530     20       C  
ATOM   3593  C   VAL B 177      37.675  -1.037 -14.848  1.00 40.78           C  
ANISOU 3593  C   VAL B 177     4815   4462   6218   -638   -830    -77       C  
ATOM   3594  O   VAL B 177      38.262   0.059 -14.861  1.00 54.37           O  
ANISOU 3594  O   VAL B 177     6706   6079   7874   -748   -852   -132       O  
ATOM   3595  CB  VAL B 177      35.662  -1.345 -13.335  1.00 39.55           C  
ANISOU 3595  CB  VAL B 177     4973   4094   5961   -394   -392      5       C  
ATOM   3596  CG1 VAL B 177      36.481  -0.541 -12.334  1.00 35.25           C  
ANISOU 3596  CG1 VAL B 177     4863   3364   5167   -545   -451   -117       C  
ATOM   3597  CG2 VAL B 177      34.191  -0.992 -13.220  1.00 43.54           C  
ANISOU 3597  CG2 VAL B 177     5507   4494   6544   -185    -34    126       C  
ATOM   3598  N   PRO B 178      38.372  -2.174 -14.899  1.00 39.28           N  
ANISOU 3598  N   PRO B 178     4445   4435   6044   -696  -1056    -86       N  
ATOM   3599  CA  PRO B 178      39.836  -2.129 -15.047  1.00 28.91           C  
ANISOU 3599  CA  PRO B 178     3072   3210   4703   -869  -1329   -134       C  
ATOM   3600  C   PRO B 178      40.279  -1.417 -16.308  1.00 33.94           C  
ANISOU 3600  C   PRO B 178     3542   3927   5427   -866  -1293   -114       C  
ATOM   3601  O   PRO B 178      41.354  -0.803 -16.317  1.00 40.14           O  
ANISOU 3601  O   PRO B 178     4400   4741   6111   -968  -1349   -145       O  
ATOM   3602  CB  PRO B 178      40.223  -3.616 -15.055  1.00 25.05           C  
ANISOU 3602  CB  PRO B 178     2435   2912   4173   -781  -1380    -96       C  
ATOM   3603  CG  PRO B 178      38.982  -4.321 -15.519  1.00 24.62           C  
ANISOU 3603  CG  PRO B 178     2225   2874   4254   -643  -1255    -38       C  
ATOM   3604  CD  PRO B 178      37.860  -3.558 -14.891  1.00 39.96           C  
ANISOU 3604  CD  PRO B 178     4360   4632   6189   -601  -1062    -32       C  
ATOM   3605  N   GLN B 179      39.483  -1.483 -17.376  1.00 37.66           N  
ANISOU 3605  N   GLN B 179     3827   4453   6029   -723  -1149    -49       N  
ATOM   3606  CA  GLN B 179      39.831  -0.755 -18.591  1.00 30.39           C  
ANISOU 3606  CA  GLN B 179     2834   3592   5120   -692  -1070    -27       C  
ATOM   3607  C   GLN B 179      39.825   0.748 -18.357  1.00 41.16           C  
ANISOU 3607  C   GLN B 179     4309   4735   6595   -850  -1104    -64       C  
ATOM   3608  O   GLN B 179      40.722   1.460 -18.828  1.00 58.32           O  
ANISOU 3608  O   GLN B 179     6516   6938   8704   -923  -1121    -82       O  
ATOM   3609  CB  GLN B 179      38.856  -1.115 -19.711  1.00 34.70           C  
ANISOU 3609  CB  GLN B 179     3245   4216   5725   -525   -922     50       C  
ATOM   3610  CG  GLN B 179      39.186  -0.486 -21.050  1.00 44.63           C  
ANISOU 3610  CG  GLN B 179     4468   5531   6960   -493   -856     71       C  
ATOM   3611  CD  GLN B 179      40.429  -1.079 -21.676  1.00 52.04           C  
ANISOU 3611  CD  GLN B 179     5437   6619   7718   -492   -852     35       C  
ATOM   3612  OE1 GLN B 179      40.495  -2.283 -21.933  1.00 46.38           O  
ANISOU 3612  OE1 GLN B 179     4724   5996   6900   -427   -818     33       O  
ATOM   3613  NE2 GLN B 179      41.420  -0.238 -21.931  1.00 58.46           N  
ANISOU 3613  NE2 GLN B 179     6253   7428   8530   -575   -886     16       N  
ATOM   3614  N   ALA B 180      38.822   1.250 -17.634  1.00 38.53           N  
ANISOU 3614  N   ALA B 180     4223   4227   6188   -759   -891    -60       N  
ATOM   3615  CA  ALA B 180      38.790   2.672 -17.317  1.00 37.24           C  
ANISOU 3615  CA  ALA B 180     4375   3841   5933   -806   -748    -97       C  
ATOM   3616  C   ALA B 180      39.939   3.074 -16.404  1.00 47.83           C  
ANISOU 3616  C   ALA B 180     5995   5088   7090  -1054   -928   -207       C  
ATOM   3617  O   ALA B 180      40.448   4.197 -16.510  1.00 65.03           O  
ANISOU 3617  O   ALA B 180     8355   7136   9218  -1190   -924   -249       O  
ATOM   3618  CB  ALA B 180      37.455   3.039 -16.670  1.00 32.35           C  
ANISOU 3618  CB  ALA B 180     3985   3043   5265   -620   -437    -50       C  
ATOM   3619  N   ALA B 181      40.358   2.181 -15.503  1.00 44.49           N  
ANISOU 3619  N   ALA B 181     5618   4726   6559  -1131  -1099   -246       N  
ATOM   3620  CA  ALA B 181      41.445   2.513 -14.589  1.00 53.35           C  
ANISOU 3620  CA  ALA B 181     6997   5779   7493  -1389  -1316   -329       C  
ATOM   3621  C   ALA B 181      42.753   2.749 -15.331  1.00 54.60           C  
ANISOU 3621  C   ALA B 181     6913   6123   7709  -1511  -1478   -311       C  
ATOM   3622  O   ALA B 181      43.547   3.610 -14.940  1.00 63.00           O  
ANISOU 3622  O   ALA B 181     8171   7123   8643  -1681  -1533   -355       O  
ATOM   3623  CB  ALA B 181      41.618   1.401 -13.555  1.00 53.39           C  
ANISOU 3623  CB  ALA B 181     7056   5853   7377  -1408  -1466   -341       C  
ATOM   3624  N   VAL B 182      43.001   1.999 -16.406  1.00 44.30           N  
ANISOU 3624  N   VAL B 182     5222   5082   6531  -1336  -1430   -235       N  
ATOM   3625  CA  VAL B 182      44.272   2.149 -17.109  1.00 42.57           C  
ANISOU 3625  CA  VAL B 182     4828   5049   6299  -1343  -1434   -210       C  
ATOM   3626  C   VAL B 182      44.285   3.331 -18.067  1.00 52.98           C  
ANISOU 3626  C   VAL B 182     6136   6289   7704  -1396  -1355   -207       C  
ATOM   3627  O   VAL B 182      45.368   3.783 -18.457  1.00 64.08           O  
ANISOU 3627  O   VAL B 182     7475   7778   9096  -1470  -1376   -204       O  
ATOM   3628  CB  VAL B 182      44.630   0.865 -17.871  1.00 38.76           C  
ANISOU 3628  CB  VAL B 182     4084   4809   5836  -1141  -1362   -151       C  
ATOM   3629  CG1 VAL B 182      45.068  -0.211 -16.897  1.00 43.97           C  
ANISOU 3629  CG1 VAL B 182     4753   5546   6407  -1125  -1454   -149       C  
ATOM   3630  CG2 VAL B 182      43.441   0.399 -18.685  1.00 45.34           C  
ANISOU 3630  CG2 VAL B 182     4827   5647   6753   -967  -1229   -112       C  
ATOM   3631  N   MET B 183      43.121   3.838 -18.471  1.00 49.51           N  
ANISOU 3631  N   MET B 183     5748   5679   7385  -1357  -1260   -196       N  
ATOM   3632  CA  MET B 183      43.091   4.966 -19.392  1.00 47.78           C  
ANISOU 3632  CA  MET B 183     5529   5358   7265  -1400  -1175   -178       C  
ATOM   3633  C   MET B 183      43.675   6.198 -18.715  1.00 52.97           C  
ANISOU 3633  C   MET B 183     6515   5805   7805  -1647  -1212   -253       C  
ATOM   3634  O   MET B 183      43.252   6.575 -17.619  1.00 61.51           O  
ANISOU 3634  O   MET B 183     7972   6639   8761  -1754  -1213   -320       O  
ATOM   3635  CB  MET B 183      41.662   5.244 -19.856  1.00 50.16           C  
ANISOU 3635  CB  MET B 183     5825   5494   7739  -1254  -1011   -128       C  
ATOM   3636  CG  MET B 183      41.078   4.158 -20.745  1.00 49.08           C  
ANISOU 3636  CG  MET B 183     5341   5575   7732  -1038   -985    -43       C  
ATOM   3637  SD  MET B 183      42.221   3.578 -22.018  1.00 52.65           S  
ANISOU 3637  SD  MET B 183     5619   6343   8044   -932   -970    -10       S  
ATOM   3638  CE  MET B 183      42.225   4.985 -23.128  1.00 46.31           C  
ANISOU 3638  CE  MET B 183     4793   5425   7375   -979   -896     32       C  
ATOM   3639  N   GLU B 184      44.645   6.831 -19.373  1.00 52.74           N  
ANISOU 3639  N   GLU B 184     6398   5858   7783  -1727  -1215   -244       N  
ATOM   3640  CA  GLU B 184      45.280   8.034 -18.849  1.00 62.09           C  
ANISOU 3640  CA  GLU B 184     7869   6861   8860  -1959  -1244   -307       C  
ATOM   3641  C   GLU B 184      45.542   9.001 -19.992  1.00 64.09           C  
ANISOU 3641  C   GLU B 184     8058   7069   9222  -1997  -1144   -272       C  
ATOM   3642  O   GLU B 184      46.031   8.595 -21.051  1.00 57.96           O  
ANISOU 3642  O   GLU B 184     6954   6522   8544  -1894  -1132   -207       O  
ATOM   3643  CB  GLU B 184      46.595   7.705 -18.129  1.00 74.43           C  
ANISOU 3643  CB  GLU B 184     9370   8596  10312  -2069  -1421   -321       C  
ATOM   3644  CG  GLU B 184      46.450   6.758 -16.946  1.00 85.19           C  
ANISOU 3644  CG  GLU B 184    10814  10002  11553  -2044  -1532   -340       C  
ATOM   3645  CD  GLU B 184      45.905   7.441 -15.709  1.00 90.48           C  
ANISOU 3645  CD  GLU B 184    11979  10377  12022  -2192  -1540   -424       C  
ATOM   3646  OE1 GLU B 184      46.047   8.676 -15.602  1.00 91.03           O  
ANISOU 3646  OE1 GLU B 184    12338  10241  12010  -2348  -1492   -467       O  
ATOM   3647  OE2 GLU B 184      45.348   6.738 -14.838  1.00 92.91           O  
ANISOU 3647  OE2 GLU B 184    12427  10647  12228  -2143  -1568   -446       O  
ATOM   3648  N   CYS B 185      45.218  10.275 -19.775  1.00 74.82           N  
ANISOU 3648  N   CYS B 185     9786   8112  10530  -2127  -1043   -314       N  
ATOM   3649  CA  CYS B 185      45.515  11.333 -20.733  1.00 77.84           C  
ANISOU 3649  CA  CYS B 185    10173   8404  10997  -2192   -941   -283       C  
ATOM   3650  C   CYS B 185      46.841  11.976 -20.336  1.00 82.62           C  
ANISOU 3650  C   CYS B 185    10837   9045  11510  -2413  -1062   -325       C  
ATOM   3651  O   CYS B 185      47.012  12.397 -19.187  1.00 85.04           O  
ANISOU 3651  O   CYS B 185    11471   9208  11634  -2559  -1131   -394       O  
ATOM   3652  CB  CYS B 185      44.386  12.363 -20.783  1.00 78.74           C  
ANISOU 3652  CB  CYS B 185    10693   8126  11099  -2157   -707   -278       C  
ATOM   3653  SG  CYS B 185      44.640  13.698 -21.978  1.00 86.40           S  
ANISOU 3653  SG  CYS B 185    11713   8948  12167  -2209   -546   -219       S  
ATOM   3654  N   SER B 186      47.786  12.032 -21.269  1.00 83.08           N  
ANISOU 3654  N   SER B 186    10592   9293  11681  -2438  -1089   -272       N  
ATOM   3655  CA  SER B 186      49.119  12.530 -20.957  1.00 84.87           C  
ANISOU 3655  CA  SER B 186    10807   9575  11864  -2646  -1223   -280       C  
ATOM   3656  C   SER B 186      49.669  13.315 -22.138  1.00 89.72           C  
ANISOU 3656  C   SER B 186    11297  10185  12609  -2704  -1131   -230       C  
ATOM   3657  O   SER B 186      49.370  13.017 -23.298  1.00 92.60           O  
ANISOU 3657  O   SER B 186    11443  10645  13095  -2546  -1011   -171       O  
ATOM   3658  CB  SER B 186      50.074  11.386 -20.590  1.00 85.20           C  
ANISOU 3658  CB  SER B 186    10552   9922  11899  -2611  -1399   -245       C  
ATOM   3659  OG  SER B 186      49.944  10.315 -21.506  1.00 84.59           O  
ANISOU 3659  OG  SER B 186    10142  10072  11925  -2371  -1328   -189       O  
ATOM   3660  N   SER B 187      50.469  14.330 -21.827  1.00 90.87           N  
ANISOU 3660  N   SER B 187    11604  10214  12707  -2941  -1193   -245       N  
ATOM   3661  CA  SER B 187      51.073  15.185 -22.843  1.00 88.11           C  
ANISOU 3661  CA  SER B 187    11170   9831  12477  -3034  -1109   -196       C  
ATOM   3662  C   SER B 187      52.395  14.611 -23.345  1.00 89.54           C  
ANISOU 3662  C   SER B 187    10948  10311  12761  -3055  -1211   -125       C  
ATOM   3663  O   SER B 187      52.755  14.777 -24.511  1.00 89.82           O  
ANISOU 3663  O   SER B 187    10785  10417  12926  -3018  -1103    -63       O  
ATOM   3664  CB  SER B 187      51.297  16.594 -22.288  1.00 90.01           C  
ANISOU 3664  CB  SER B 187    11807   9789  12606  -3287  -1118   -238       C  
ATOM   3665  OG  SER B 187      51.866  17.449 -23.265  1.00 94.11           O  
ANISOU 3665  OG  SER B 187    12253  10256  13247  -3384  -1029   -186       O  
ATOM   3666  N   PHE B 199      49.047  19.374 -26.531  1.00 97.59           N  
ANISOU 3666  N   PHE B 199    13047  10066  13967  -2933   -245      3       N  
ATOM   3667  CA  PHE B 199      48.924  18.154 -27.316  1.00 96.85           C  
ANISOU 3667  CA  PHE B 199    12546  10264  13988  -2767   -249     53       C  
ATOM   3668  C   PHE B 199      49.037  16.940 -26.403  1.00 86.12           C  
ANISOU 3668  C   PHE B 199    11027   9144  12550  -2735   -441    -19       C  
ATOM   3669  O   PHE B 199      50.131  16.437 -26.151  1.00 88.60           O  
ANISOU 3669  O   PHE B 199    11109   9698  12857  -2828   -603    -40       O  
ATOM   3670  CB  PHE B 199      49.988  18.102 -28.414  1.00104.03           C  
ANISOU 3670  CB  PHE B 199    13139  11389  14999  -2832   -240    114       C  
ATOM   3671  CG  PHE B 199      49.869  16.908 -29.316  1.00102.91           C  
ANISOU 3671  CG  PHE B 199    12658  11568  14876  -2635   -260    191       C  
ATOM   3672  CD1 PHE B 199      50.377  15.679 -28.930  1.00100.58           C  
ANISOU 3672  CD1 PHE B 199    12090  11577  14550  -2565   -429    164       C  
ATOM   3673  CD2 PHE B 199      49.249  17.014 -30.549  1.00102.41           C  
ANISOU 3673  CD2 PHE B 199    12553  11484  14876  -2474   -129    321       C  
ATOM   3674  CE1 PHE B 199      50.266  14.579 -29.751  1.00 98.09           C  
ANISOU 3674  CE1 PHE B 199    11494  11514  14262  -2334   -446    242       C  
ATOM   3675  CE2 PHE B 199      49.137  15.917 -31.377  1.00102.63           C  
ANISOU 3675  CE2 PHE B 199    12254  11777  14963  -2241   -173    401       C  
ATOM   3676  CZ  PHE B 199      49.646  14.698 -30.976  1.00 99.44           C  
ANISOU 3676  CZ  PHE B 199    11616  11653  14513  -2175   -323    352       C  
ATOM   3677  N   SER B 200      47.900  16.506 -25.872  1.00 76.21           N  
ANISOU 3677  N   SER B 200     9917   7799  11239  -2590   -411    -38       N  
ATOM   3678  CA  SER B 200      47.816  15.328 -25.024  1.00 78.63           C  
ANISOU 3678  CA  SER B 200    10097   8303  11474  -2528   -570    -92       C  
ATOM   3679  C   SER B 200      47.166  14.176 -25.784  1.00 77.31           C  
ANISOU 3679  C   SER B 200     9628   8359  11388  -2284   -561    -10       C  
ATOM   3680  O   SER B 200      46.370  14.389 -26.703  1.00 78.48           O  
ANISOU 3680  O   SER B 200     9756   8419  11644  -2138   -431     91       O  
ATOM   3681  CB  SER B 200      47.030  15.626 -23.740  1.00 72.77           C  
ANISOU 3681  CB  SER B 200     9770   7298  10582  -2545   -555   -170       C  
ATOM   3682  OG  SER B 200      45.713  16.069 -24.021  1.00 72.89           O  
ANISOU 3682  OG  SER B 200    10046   7039  10609  -2382   -327   -120       O  
ATOM   3683  N   VAL B 201      47.527  12.952 -25.404  1.00 69.33           N  
ANISOU 3683  N   VAL B 201     8376   7631  10335  -2206   -709    -32       N  
ATOM   3684  CA  VAL B 201      46.986  11.743 -26.012  1.00 61.51           C  
ANISOU 3684  CA  VAL B 201     7112   6863   9397  -1947   -721     36       C  
ATOM   3685  C   VAL B 201      46.416  10.860 -24.911  1.00 60.16           C  
ANISOU 3685  C   VAL B 201     6985   6721   9153  -1877   -806    -18       C  
ATOM   3686  O   VAL B 201      46.988  10.758 -23.820  1.00 62.89           O  
ANISOU 3686  O   VAL B 201     7432   7075   9390  -2009   -912    -98       O  
ATOM   3687  CB  VAL B 201      48.050  10.978 -26.824  1.00 57.42           C  
ANISOU 3687  CB  VAL B 201     6289   6649   8879  -1867   -762     78       C  
ATOM   3688  CG1 VAL B 201      48.489  11.796 -28.029  1.00 60.73           C  
ANISOU 3688  CG1 VAL B 201     6659   7031   9386  -1914   -662    148       C  
ATOM   3689  CG2 VAL B 201      49.242  10.632 -25.941  1.00 60.69           C  
ANISOU 3689  CG2 VAL B 201     6656   7186   9215  -1992   -889     17       C  
ATOM   3690  N   CYS B 202      45.283  10.221 -25.209  1.00 60.15           N  
ANISOU 3690  N   CYS B 202     6891   6732   9233  -1662   -761     36       N  
ATOM   3691  CA  CYS B 202      44.586   9.332 -24.283  1.00 62.02           C  
ANISOU 3691  CA  CYS B 202     7147   6986   9431  -1574   -818      2       C  
ATOM   3692  C   CYS B 202      44.887   7.881 -24.649  1.00 60.71           C  
ANISOU 3692  C   CYS B 202     6717   7145   9206  -1385   -871     24       C  
ATOM   3693  O   CYS B 202      44.378   7.371 -25.654  1.00 66.92           O  
ANISOU 3693  O   CYS B 202     7348   8032  10048  -1188   -807     91       O  
ATOM   3694  CB  CYS B 202      43.086   9.618 -24.327  1.00 59.07           C  
ANISOU 3694  CB  CYS B 202     6859   6380   9207  -1435   -677     53       C  
ATOM   3695  SG  CYS B 202      42.034   8.599 -23.267  1.00 53.30           S  
ANISOU 3695  SG  CYS B 202     6171   5679   8400  -1259   -660     25       S  
ATOM   3696  N   ASP B 203      45.714   7.219 -23.838  1.00 50.68           N  
ANISOU 3696  N   ASP B 203     5443   6005   7810  -1439   -969    -30       N  
ATOM   3697  CA  ASP B 203      46.074   5.827 -24.070  1.00 47.52           C  
ANISOU 3697  CA  ASP B 203     4879   5841   7337  -1267   -976    -14       C  
ATOM   3698  C   ASP B 203      46.163   5.081 -22.746  1.00 48.37           C  
ANISOU 3698  C   ASP B 203     5047   5977   7354  -1294  -1070    -64       C  
ATOM   3699  O   ASP B 203      46.097   5.669 -21.661  1.00 59.04           O  
ANISOU 3699  O   ASP B 203     6574   7182   8678  -1460  -1151   -117       O  
ATOM   3700  CB  ASP B 203      47.394   5.715 -24.837  1.00 54.80           C  
ANISOU 3700  CB  ASP B 203     5667   6909   8247  -1277   -965      8       C  
ATOM   3701  CG  ASP B 203      47.440   4.501 -25.727  1.00 63.18           C  
ANISOU 3701  CG  ASP B 203     6612   8126   9268  -1071   -895     42       C  
ATOM   3702  OD1 ASP B 203      46.709   3.527 -25.441  1.00 68.78           O  
ANISOU 3702  OD1 ASP B 203     7348   8868   9919   -944   -882     33       O  
ATOM   3703  OD2 ASP B 203      48.213   4.519 -26.706  1.00 65.13           O  
ANISOU 3703  OD2 ASP B 203     6762   8438   9548  -1052   -856     81       O  
ATOM   3704  N   GLU B 204      46.311   3.762 -22.852  1.00 39.64           N  
ANISOU 3704  N   GLU B 204     3839   5036   6188  -1137  -1053    -49       N  
ATOM   3705  CA  GLU B 204      46.444   2.902 -21.685  1.00 42.91           C  
ANISOU 3705  CA  GLU B 204     4287   5491   6525  -1140  -1135    -79       C  
ATOM   3706  C   GLU B 204      47.820   3.079 -21.050  1.00 44.02           C  
ANISOU 3706  C   GLU B 204     4404   5682   6637  -1284  -1250    -96       C  
ATOM   3707  O   GLU B 204      48.829   3.199 -21.752  1.00 45.35           O  
ANISOU 3707  O   GLU B 204     4448   5941   6843  -1295  -1236    -68       O  
ATOM   3708  CB  GLU B 204      46.240   1.440 -22.087  1.00 58.03           C  
ANISOU 3708  CB  GLU B 204     6119   7535   8396   -943  -1069    -50       C  
ATOM   3709  CG  GLU B 204      44.785   1.061 -22.322  1.00 61.50           C  
ANISOU 3709  CG  GLU B 204     6598   7927   8842   -819   -989    -37       C  
ATOM   3710  CD  GLU B 204      44.636  -0.310 -22.944  1.00 54.63           C  
ANISOU 3710  CD  GLU B 204     5672   7114   7969   -663   -952     14       C  
ATOM   3711  OE1 GLU B 204      45.387  -1.227 -22.554  1.00 54.16           O  
ANISOU 3711  OE1 GLU B 204     5579   7107   7894   -651  -1009     29       O  
ATOM   3712  OE2 GLU B 204      43.770  -0.470 -23.829  1.00 56.85           O  
ANISOU 3712  OE2 GLU B 204     5952   7374   8274   -567   -876     42       O  
ATOM   3713  N   ARG B 205      47.859   3.107 -19.718  1.00 47.34           N  
ANISOU 3713  N   ARG B 205     4952   6036   6999  -1399  -1378   -130       N  
ATOM   3714  CA  ARG B 205      49.107   3.254 -18.965  1.00 59.26           C  
ANISOU 3714  CA  ARG B 205     6453   7587   8477  -1548  -1528   -126       C  
ATOM   3715  C   ARG B 205      49.345   1.999 -18.124  1.00 65.00           C  
ANISOU 3715  C   ARG B 205     7142   8411   9143  -1471  -1607   -106       C  
ATOM   3716  O   ARG B 205      48.749   1.833 -17.055  1.00 63.34           O  
ANISOU 3716  O   ARG B 205     7101   8114   8853  -1515  -1685   -134       O  
ATOM   3717  CB  ARG B 205      49.082   4.513 -18.101  1.00 71.31           C  
ANISOU 3717  CB  ARG B 205     8226   8922   9946  -1794  -1639   -174       C  
ATOM   3718  CG  ARG B 205      50.432   4.876 -17.514  1.00 87.99           C  
ANISOU 3718  CG  ARG B 205    10328  11078  12027  -1981  -1809   -145       C  
ATOM   3719  CD  ARG B 205      50.348   6.144 -16.689  1.00 99.04           C  
ANISOU 3719  CD  ARG B 205    12052  12262  13318  -2240  -1906   -199       C  
ATOM   3720  NE  ARG B 205      49.958   7.290 -17.506  1.00 99.72           N  
ANISOU 3720  NE  ARG B 205    12223  12202  13463  -2299  -1780   -233       N  
ATOM   3721  CZ  ARG B 205      50.050   8.556 -17.113  1.00111.13           C  
ANISOU 3721  CZ  ARG B 205    13955  13443  14826  -2526  -1817   -277       C  
ATOM   3722  NH1 ARG B 205      50.527   8.846 -15.911  1.00119.27           N  
ANISOU 3722  NH1 ARG B 205    15226  14403  15688  -2725  -1989   -291       N  
ATOM   3723  NH2 ARG B 205      49.677   9.534 -17.928  1.00114.11           N  
ANISOU 3723  NH2 ARG B 205    14408  13677  15273  -2557  -1676   -300       N  
ATOM   3724  N   TRP B 206      50.216   1.112 -18.605  1.00 67.89           N  
ANISOU 3724  N   TRP B 206     7313   8919   9564  -1373  -1616    -23       N  
ATOM   3725  CA  TRP B 206      50.584  -0.103 -17.888  1.00 70.68           C  
ANISOU 3725  CA  TRP B 206     7618   9348   9891  -1309  -1709     33       C  
ATOM   3726  C   TRP B 206      51.916   0.082 -17.172  1.00 74.72           C  
ANISOU 3726  C   TRP B 206     8069   9916  10405  -1466  -1904    100       C  
ATOM   3727  O   TRP B 206      52.810   0.772 -17.672  1.00 78.71           O  
ANISOU 3727  O   TRP B 206     8471  10451  10984  -1569  -1941    150       O  
ATOM   3728  CB  TRP B 206      50.662  -1.293 -18.844  1.00 69.78           C  
ANISOU 3728  CB  TRP B 206     7352   9312   9849  -1112  -1611    110       C  
ATOM   3729  CG  TRP B 206      49.377  -1.547 -19.555  1.00 59.13           C  
ANISOU 3729  CG  TRP B 206     6067   7911   8489   -976  -1449     68       C  
ATOM   3730  CD1 TRP B 206      49.027  -1.103 -20.794  1.00 58.97           C  
ANISOU 3730  CD1 TRP B 206     6021   7868   8518   -922  -1327     71       C  
ATOM   3731  CD2 TRP B 206      48.262  -2.302 -19.067  1.00 51.41           C  
ANISOU 3731  CD2 TRP B 206     5185   6898   7449   -886  -1405     32       C  
ATOM   3732  NE1 TRP B 206      47.762  -1.534 -21.111  1.00 57.26           N  
ANISOU 3732  NE1 TRP B 206     5876   7605   8274   -808  -1223     46       N  
ATOM   3733  CE2 TRP B 206      47.271  -2.273 -20.067  1.00 51.18           C  
ANISOU 3733  CE2 TRP B 206     5175   6828   7443   -787  -1264     24       C  
ATOM   3734  CE3 TRP B 206      48.006  -3.000 -17.883  1.00 50.07           C  
ANISOU 3734  CE3 TRP B 206     5088   6729   7208   -886  -1477     14       C  
ATOM   3735  CZ2 TRP B 206      46.044  -2.914 -19.921  1.00 47.95           C  
ANISOU 3735  CZ2 TRP B 206     4836   6381   7002   -696  -1197      5       C  
ATOM   3736  CZ3 TRP B 206      46.786  -3.637 -17.739  1.00 44.46           C  
ANISOU 3736  CZ3 TRP B 206     4450   5978   6462   -791  -1396    -14       C  
ATOM   3737  CH2 TRP B 206      45.821  -3.589 -18.753  1.00 45.99           C  
ANISOU 3737  CH2 TRP B 206     4645   6136   6695   -702  -1258    -14       C  
ATOM   3738  N   ALA B 207      52.043  -0.530 -15.994  1.00 75.25           N  
ANISOU 3738  N   ALA B 207     8199  10002  10391  -1495  -2036    112       N  
ATOM   3739  CA  ALA B 207      53.274  -0.451 -15.218  1.00 76.96           C  
ANISOU 3739  CA  ALA B 207     8361  10283  10597  -1652  -2251    200       C  
ATOM   3740  C   ALA B 207      54.305  -1.511 -15.586  1.00 86.16           C  
ANISOU 3740  C   ALA B 207     9269  11596  11873  -1550  -2290    349       C  
ATOM   3741  O   ALA B 207      55.422  -1.470 -15.060  1.00 97.60           O  
ANISOU 3741  O   ALA B 207    10618  13123  13341  -1676  -2472    455       O  
ATOM   3742  CB  ALA B 207      52.960  -0.557 -13.718  1.00 76.21           C  
ANISOU 3742  CB  ALA B 207     8483  10133  10341  -1748  -2395    151       C  
ATOM   3743  N   ASP B 208      53.971  -2.452 -16.463  1.00 81.34           N  
ANISOU 3743  N   ASP B 208     8557  11019  11332  -1335  -2128    367       N  
ATOM   3744  CA  ASP B 208      54.918  -3.496 -16.825  1.00 75.32           C  
ANISOU 3744  CA  ASP B 208     7572  10375  10671  -1226  -2142    502       C  
ATOM   3745  C   ASP B 208      54.484  -4.130 -18.139  1.00 74.09           C  
ANISOU 3745  C   ASP B 208     7352  10212  10585  -1026  -1929    494       C  
ATOM   3746  O   ASP B 208      53.303  -4.107 -18.494  1.00 75.56           O  
ANISOU 3746  O   ASP B 208     7679  10314  10717   -953  -1797    392       O  
ATOM   3747  CB  ASP B 208      55.035  -4.555 -15.721  1.00 75.39           C  
ANISOU 3747  CB  ASP B 208     7595  10433  10618  -1184  -2261    545       C  
ATOM   3748  CG  ASP B 208      53.744  -5.320 -15.512  1.00 76.83           C  
ANISOU 3748  CG  ASP B 208     7935  10544  10713  -1044  -2148    445       C  
ATOM   3749  OD1 ASP B 208      52.754  -4.698 -15.071  1.00 80.65           O  
ANISOU 3749  OD1 ASP B 208     8618  10928  11097  -1106  -2126    329       O  
ATOM   3750  OD2 ASP B 208      53.720  -6.538 -15.796  1.00 72.92           O  
ANISOU 3750  OD2 ASP B 208     7363  10089  10252   -876  -2077    487       O  
ATOM   3751  N   ASP B 209      55.464  -4.683 -18.862  1.00 71.24           N  
ANISOU 3751  N   ASP B 209     6782   9941  10344   -948  -1901    616       N  
ATOM   3752  CA  ASP B 209      55.194  -5.270 -20.172  1.00 69.55           C  
ANISOU 3752  CA  ASP B 209     6522   9715  10188   -776  -1709    616       C  
ATOM   3753  C   ASP B 209      54.248  -6.461 -20.085  1.00 62.38           C  
ANISOU 3753  C   ASP B 209     5723   8768   9211   -619  -1625    558       C  
ATOM   3754  O   ASP B 209      53.463  -6.699 -21.010  1.00 65.70           O  
ANISOU 3754  O   ASP B 209     6214   9131   9619   -522  -1476    501       O  
ATOM   3755  CB  ASP B 209      56.504  -5.706 -20.828  1.00 80.91           C  
ANISOU 3755  CB  ASP B 209     7714  11258  11770   -717  -1697    772       C  
ATOM   3756  CG  ASP B 209      57.366  -4.538 -21.252  1.00 92.67           C  
ANISOU 3756  CG  ASP B 209     9078  12783  13350   -860  -1736    838       C  
ATOM   3757  OD1 ASP B 209      56.856  -3.402 -21.331  1.00 98.08           O  
ANISOU 3757  OD1 ASP B 209     9883  13397  13987   -980  -1733    744       O  
ATOM   3758  OD2 ASP B 209      58.567  -4.768 -21.505  1.00 98.53           O  
ANISOU 3758  OD2 ASP B 209     9592  13628  14218   -851  -1765    997       O  
ATOM   3759  N   LEU B 210      54.310  -7.225 -18.996  1.00 56.73           N  
ANISOU 3759  N   LEU B 210     5024   8084   8447   -603  -1729    579       N  
ATOM   3760  CA  LEU B 210      53.533  -8.459 -18.926  1.00 52.09           C  
ANISOU 3760  CA  LEU B 210     4518   7467   7806   -455  -1652    542       C  
ATOM   3761  C   LEU B 210      52.039  -8.188 -18.785  1.00 49.67           C  
ANISOU 3761  C   LEU B 210     4422   7055   7397   -470  -1581    412       C  
ATOM   3762  O   LEU B 210      51.219  -8.886 -19.394  1.00 51.54           O  
ANISOU 3762  O   LEU B 210     4722   7244   7615   -363  -1459    373       O  
ATOM   3763  CB  LEU B 210      54.024  -9.323 -17.764  1.00 56.50           C  
ANISOU 3763  CB  LEU B 210     5035   8092   8339   -431  -1788    609       C  
ATOM   3764  CG  LEU B 210      53.431 -10.726 -17.620  1.00 54.47           C  
ANISOU 3764  CG  LEU B 210     4838   7821   8038   -271  -1725    593       C  
ATOM   3765  CD1 LEU B 210      53.850 -11.602 -18.785  1.00 51.21           C  
ANISOU 3765  CD1 LEU B 210     4309   7432   7715   -107  -1595    654       C  
ATOM   3766  CD2 LEU B 210      53.858 -11.354 -16.301  1.00 49.96           C  
ANISOU 3766  CD2 LEU B 210     4250   7310   7421   -269  -1885    654       C  
ATOM   3767  N   ALA B 211      51.662  -7.197 -17.979  1.00 51.72           N  
ANISOU 3767  N   ALA B 211     4789   7272   7591   -606  -1660    352       N  
ATOM   3768  CA  ALA B 211      50.254  -6.968 -17.669  1.00 53.55           C  
ANISOU 3768  CA  ALA B 211     5202   7409   7735   -612  -1598    250       C  
ATOM   3769  C   ALA B 211      49.388  -6.811 -18.914  1.00 56.89           C  
ANISOU 3769  C   ALA B 211     5660   7772   8184   -542  -1432    211       C  
ATOM   3770  O   ALA B 211      48.369  -7.500 -19.049  1.00 56.02           O  
ANISOU 3770  O   ALA B 211     5628   7615   8041   -461  -1350    180       O  
ATOM   3771  CB  ALA B 211      50.103  -5.734 -16.787  1.00 61.43           C  
ANISOU 3771  CB  ALA B 211     6307   8365   8669   -774  -1695    193       C  
ATOM   3772  N   PRO B 212      49.729  -5.900 -19.824  1.00 58.00           N  
ANISOU 3772  N   PRO B 212     5748   7909   8379   -580  -1390    217       N  
ATOM   3773  CA  PRO B 212      48.920  -5.765 -21.047  1.00 53.19           C  
ANISOU 3773  CA  PRO B 212     5177   7247   7786   -513  -1249    192       C  
ATOM   3774  C   PRO B 212      48.846  -7.039 -21.870  1.00 49.70           C  
ANISOU 3774  C   PRO B 212     4701   6817   7364   -383  -1168    222       C  
ATOM   3775  O   PRO B 212      47.804  -7.329 -22.468  1.00 53.70           O  
ANISOU 3775  O   PRO B 212     5290   7267   7848   -330  -1082    190       O  
ATOM   3776  CB  PRO B 212      49.614  -4.626 -21.806  1.00 43.03           C  
ANISOU 3776  CB  PRO B 212     3816   5973   6559   -582  -1241    210       C  
ATOM   3777  CG  PRO B 212      51.017  -4.623 -21.270  1.00 50.77           C  
ANISOU 3777  CG  PRO B 212     4666   7037   7588   -649  -1360    278       C  
ATOM   3778  CD  PRO B 212      50.868  -4.963 -19.818  1.00 53.64           C  
ANISOU 3778  CD  PRO B 212     5097   7404   7879   -695  -1476    258       C  
ATOM   3779  N   LYS B 213      49.931  -7.827 -21.905  1.00 40.83           N  
ANISOU 3779  N   LYS B 213     3456   5768   6288   -333  -1201    289       N  
ATOM   3780  CA  LYS B 213      49.932  -9.047 -22.704  1.00 42.24           C  
ANISOU 3780  CA  LYS B 213     3606   5958   6485   -207  -1121    314       C  
ATOM   3781  C   LYS B 213      48.916 -10.054 -22.183  1.00 49.06           C  
ANISOU 3781  C   LYS B 213     4581   6779   7280   -157  -1110    275       C  
ATOM   3782  O   LYS B 213      48.252 -10.738 -22.971  1.00 48.76           O  
ANISOU 3782  O   LYS B 213     4594   6704   7230    -94  -1030    257       O  
ATOM   3783  CB  LYS B 213      51.334  -9.653 -22.724  1.00 45.06           C  
ANISOU 3783  CB  LYS B 213     3793   6408   6920   -146  -1157    409       C  
ATOM   3784  CG  LYS B 213      52.342  -8.810 -23.487  1.00 48.22           C  
ANISOU 3784  CG  LYS B 213     4057   6851   7412   -182  -1142    469       C  
ATOM   3785  CD  LYS B 213      53.612  -9.586 -23.785  1.00 62.64           C  
ANISOU 3785  CD  LYS B 213     5699   8762   9340    -82  -1132    587       C  
ATOM   3786  CE  LYS B 213      54.784  -8.656 -24.049  1.00 77.78           C  
ANISOU 3786  CE  LYS B 213     7448  10742  11365   -159  -1164    680       C  
ATOM   3787  NZ  LYS B 213      54.749  -8.090 -25.419  1.00 85.34           N  
ANISOU 3787  NZ  LYS B 213     8395  11670  12362   -146  -1040    672       N  
ATOM   3788  N   ILE B 214      48.784 -10.165 -20.859  1.00 47.27           N  
ANISOU 3788  N   ILE B 214     4394   6558   7010   -195  -1197    266       N  
ATOM   3789  CA  ILE B 214      47.809 -11.083 -20.277  1.00 38.71           C  
ANISOU 3789  CA  ILE B 214     3411   5432   5867   -157  -1187    236       C  
ATOM   3790  C   ILE B 214      46.402 -10.507 -20.372  1.00 37.12           C  
ANISOU 3790  C   ILE B 214     3331   5142   5630   -204  -1129    173       C  
ATOM   3791  O   ILE B 214      45.457 -11.196 -20.771  1.00 37.37           O  
ANISOU 3791  O   ILE B 214     3424   5126   5649   -165  -1068    155       O  
ATOM   3792  CB  ILE B 214      48.187 -11.416 -18.820  1.00 37.39           C  
ANISOU 3792  CB  ILE B 214     3242   5306   5660   -175  -1305    256       C  
ATOM   3793  CG1 ILE B 214      49.543 -12.126 -18.770  1.00 40.54           C  
ANISOU 3793  CG1 ILE B 214     3497   5800   6107   -102  -1364    342       C  
ATOM   3794  CG2 ILE B 214      47.111 -12.275 -18.181  1.00 39.49           C  
ANISOU 3794  CG2 ILE B 214     3617   5523   5865   -143  -1291    225       C  
ATOM   3795  CD1 ILE B 214      50.175 -12.132 -17.390  1.00 47.72           C  
ANISOU 3795  CD1 ILE B 214     4380   6767   6983   -145  -1519    381       C  
ATOM   3796  N   TYR B 215      46.249  -9.233 -20.008  1.00 41.89           N  
ANISOU 3796  N   TYR B 215     3964   5728   6225   -289  -1155    145       N  
ATOM   3797  CA  TYR B 215      44.939  -8.592 -20.013  1.00 36.64           C  
ANISOU 3797  CA  TYR B 215     3391   4991   5539   -316  -1101     99       C  
ATOM   3798  C   TYR B 215      44.265  -8.695 -21.376  1.00 39.28           C  
ANISOU 3798  C   TYR B 215     3735   5288   5902   -270  -1003    100       C  
ATOM   3799  O   TYR B 215      43.142  -9.193 -21.496  1.00 44.85           O  
ANISOU 3799  O   TYR B 215     4494   5951   6596   -246   -959     89       O  
ATOM   3800  CB  TYR B 215      45.084  -7.126 -19.604  1.00 42.17           C  
ANISOU 3800  CB  TYR B 215     4105   5684   6232   -409  -1139     72       C  
ATOM   3801  CG  TYR B 215      43.788  -6.355 -19.605  1.00 43.12           C  
ANISOU 3801  CG  TYR B 215     4298   5741   6345   -426  -1079     35       C  
ATOM   3802  CD1 TYR B 215      42.862  -6.505 -18.581  1.00 43.39           C  
ANISOU 3802  CD1 TYR B 215     4399   5748   6338   -439  -1087      6       C  
ATOM   3803  CD2 TYR B 215      43.491  -5.470 -20.631  1.00 46.01           C  
ANISOU 3803  CD2 TYR B 215     4651   6082   6751   -425  -1014     37       C  
ATOM   3804  CE1 TYR B 215      41.677  -5.795 -18.577  1.00 38.13           C  
ANISOU 3804  CE1 TYR B 215     3766   5036   5684   -448  -1025    -14       C  
ATOM   3805  CE2 TYR B 215      42.312  -4.758 -20.636  1.00 45.41           C  
ANISOU 3805  CE2 TYR B 215     4615   5958   6683   -429   -961     20       C  
ATOM   3806  CZ  TYR B 215      41.408  -4.923 -19.608  1.00 41.01           C  
ANISOU 3806  CZ  TYR B 215     4104   5379   6098   -439   -962     -3       C  
ATOM   3807  OH  TYR B 215      40.231  -4.210 -19.618  1.00 46.87           O  
ANISOU 3807  OH  TYR B 215     4847   6054   6907   -436   -920      6       O  
ATOM   3808  N   HIS B 216      44.943  -8.222 -22.423  1.00 43.19           N  
ANISOU 3808  N   HIS B 216     4173   5804   6435   -267   -978    118       N  
ATOM   3809  CA  HIS B 216      44.323  -8.198 -23.743  1.00 38.01           C  
ANISOU 3809  CA  HIS B 216     3533   5116   5793   -237   -904    118       C  
ATOM   3810  C   HIS B 216      44.201  -9.585 -24.358  1.00 41.62           C  
ANISOU 3810  C   HIS B 216     3993   5578   6243   -178   -880    127       C  
ATOM   3811  O   HIS B 216      43.392  -9.773 -25.275  1.00 49.55           O  
ANISOU 3811  O   HIS B 216     5033   6553   7240   -169   -841    120       O  
ATOM   3812  CB  HIS B 216      45.106  -7.262 -24.663  1.00 41.11           C  
ANISOU 3812  CB  HIS B 216     3865   5532   6224   -254   -886    134       C  
ATOM   3813  CG  HIS B 216      44.879  -5.814 -24.362  1.00 48.67           C  
ANISOU 3813  CG  HIS B 216     4840   6465   7189   -319   -895    118       C  
ATOM   3814  ND1 HIS B 216      43.746  -5.143 -24.768  1.00 43.10           N  
ANISOU 3814  ND1 HIS B 216     4186   5709   6482   -319   -850    105       N  
ATOM   3815  CD2 HIS B 216      45.625  -4.914 -23.680  1.00 46.46           C  
ANISOU 3815  CD2 HIS B 216     4527   6206   6919   -393   -951    114       C  
ATOM   3816  CE1 HIS B 216      43.806  -3.889 -24.359  1.00 45.48           C  
ANISOU 3816  CE1 HIS B 216     4489   5996   6795   -378   -865     92       C  
ATOM   3817  NE2 HIS B 216      44.936  -3.724 -23.697  1.00 47.70           N  
ANISOU 3817  NE2 HIS B 216     4729   6318   7078   -436   -930     90       N  
ATOM   3818  N   SER B 217      44.981 -10.559 -23.886  1.00 43.25           N  
ANISOU 3818  N   SER B 217     4158   5826   6450   -139   -912    147       N  
ATOM   3819  CA  SER B 217      44.778 -11.928 -24.344  1.00 36.68           C  
ANISOU 3819  CA  SER B 217     3338   4993   5608    -80   -893    153       C  
ATOM   3820  C   SER B 217      43.480 -12.501 -23.791  1.00 35.77           C  
ANISOU 3820  C   SER B 217     3310   4822   5459   -102   -898    127       C  
ATOM   3821  O   SER B 217      42.732 -13.169 -24.514  1.00 45.61           O  
ANISOU 3821  O   SER B 217     4593   6040   6695   -101   -879    118       O  
ATOM   3822  CB  SER B 217      45.965 -12.802 -23.941  1.00 28.27           C  
ANISOU 3822  CB  SER B 217     2190   3993   4560     -6   -922    195       C  
ATOM   3823  OG  SER B 217      47.151 -12.391 -24.598  1.00 35.67           O  
ANISOU 3823  OG  SER B 217     3018   4988   5546     27   -906    233       O  
ATOM   3824  N   CYS B 218      43.196 -12.249 -22.511  1.00 34.92           N  
ANISOU 3824  N   CYS B 218     3229   4705   5334   -131   -933    119       N  
ATOM   3825  CA  CYS B 218      41.973 -12.771 -21.910  1.00 34.37           C  
ANISOU 3825  CA  CYS B 218     3223   4592   5243   -149   -930    104       C  
ATOM   3826  C   CYS B 218      40.733 -12.120 -22.510  1.00 39.69           C  
ANISOU 3826  C   CYS B 218     3926   5228   5927   -186   -886     95       C  
ATOM   3827  O   CYS B 218      39.715 -12.789 -22.719  1.00 43.21           O  
ANISOU 3827  O   CYS B 218     4396   5650   6371   -201   -876     98       O  
ATOM   3828  CB  CYS B 218      42.003 -12.567 -20.397  1.00 37.43           C  
ANISOU 3828  CB  CYS B 218     3626   4990   5607   -167   -978     99       C  
ATOM   3829  SG  CYS B 218      43.417 -13.329 -19.578  1.00 52.89           S  
ANISOU 3829  SG  CYS B 218     5536   7012   7546   -121  -1057    129       S  
ATOM   3830  N   PHE B 219      40.791 -10.816 -22.792  1.00 44.12           N  
ANISOU 3830  N   PHE B 219     4472   5789   6503   -204   -868     93       N  
ATOM   3831  CA  PHE B 219      39.615 -10.145 -23.333  1.00 45.81           C  
ANISOU 3831  CA  PHE B 219     4694   5978   6733   -223   -831    101       C  
ATOM   3832  C   PHE B 219      39.401 -10.414 -24.816  1.00 39.72           C  
ANISOU 3832  C   PHE B 219     3918   5209   5963   -222   -817    113       C  
ATOM   3833  O   PHE B 219      38.297 -10.180 -25.320  1.00 38.24           O  
ANISOU 3833  O   PHE B 219     3730   5015   5786   -242   -806    134       O  
ATOM   3834  CB  PHE B 219      39.694  -8.640 -23.073  1.00 48.17           C  
ANISOU 3834  CB  PHE B 219     4980   6274   7049   -239   -819     98       C  
ATOM   3835  CG  PHE B 219      38.954  -8.210 -21.842  1.00 59.70           C  
ANISOU 3835  CG  PHE B 219     6449   7722   8512   -255   -816     92       C  
ATOM   3836  CD1 PHE B 219      37.597  -8.461 -21.715  1.00 51.77           C  
ANISOU 3836  CD1 PHE B 219     5434   6707   7528   -250   -782    117       C  
ATOM   3837  CD2 PHE B 219      39.610  -7.566 -20.809  1.00 73.67           C  
ANISOU 3837  CD2 PHE B 219     8227   9501  10264   -284   -854     65       C  
ATOM   3838  CE1 PHE B 219      36.907  -8.073 -20.582  1.00 55.03           C  
ANISOU 3838  CE1 PHE B 219     5835   7119   7956   -258   -765    117       C  
ATOM   3839  CE2 PHE B 219      38.926  -7.176 -19.676  1.00 78.09           C  
ANISOU 3839  CE2 PHE B 219     8798  10053  10819   -307   -854     51       C  
ATOM   3840  CZ  PHE B 219      37.573  -7.429 -19.561  1.00 70.82           C  
ANISOU 3840  CZ  PHE B 219     7857   9123   9931   -285   -798     79       C  
ATOM   3841  N   PHE B 220      40.420 -10.891 -25.530  1.00 38.34           N  
ANISOU 3841  N   PHE B 220     3729   5057   5782   -200   -825    107       N  
ATOM   3842  CA  PHE B 220      40.180 -11.365 -26.889  1.00 31.87           C  
ANISOU 3842  CA  PHE B 220     2913   4244   4950   -206   -825    111       C  
ATOM   3843  C   PHE B 220      39.482 -12.715 -26.864  1.00 35.25           C  
ANISOU 3843  C   PHE B 220     3375   4661   5357   -228   -855    106       C  
ATOM   3844  O   PHE B 220      38.532 -12.951 -27.619  1.00 39.68           O  
ANISOU 3844  O   PHE B 220     3953   5219   5904   -277   -876    114       O  
ATOM   3845  CB  PHE B 220      41.490 -11.457 -27.668  1.00 26.05           C  
ANISOU 3845  CB  PHE B 220     2135   3543   4219   -168   -815    110       C  
ATOM   3846  CG  PHE B 220      41.341 -12.082 -29.027  1.00 25.50           C  
ANISOU 3846  CG  PHE B 220     2072   3489   4126   -172   -823    106       C  
ATOM   3847  CD1 PHE B 220      40.766 -11.376 -30.071  1.00 27.81           C  
ANISOU 3847  CD1 PHE B 220     2371   3787   4408   -206   -824    111       C  
ATOM   3848  CD2 PHE B 220      41.771 -13.377 -29.257  1.00 30.61           C  
ANISOU 3848  CD2 PHE B 220     2718   4152   4759   -141   -841     98       C  
ATOM   3849  CE1 PHE B 220      40.624 -11.954 -31.322  1.00 19.13           C  
ANISOU 3849  CE1 PHE B 220     1286   2710   3272   -228   -854    101       C  
ATOM   3850  CE2 PHE B 220      41.634 -13.958 -30.503  1.00 31.61           C  
ANISOU 3850  CE2 PHE B 220     2847   4224   4940   -163   -910    113       C  
ATOM   3851  CZ  PHE B 220      41.061 -13.247 -31.536  1.00 20.97           C  
ANISOU 3851  CZ  PHE B 220     1518   2892   3558   -219   -920    110       C  
ATOM   3852  N   ILE B 221      39.958 -13.616 -26.005  1.00 37.13           N  
ANISOU 3852  N   ILE B 221     3620   4897   5593   -203   -869     98       N  
ATOM   3853  CA  ILE B 221      39.310 -14.913 -25.839  1.00 34.41           C  
ANISOU 3853  CA  ILE B 221     3311   4533   5230   -233   -901     92       C  
ATOM   3854  C   ILE B 221      37.894 -14.731 -25.310  1.00 42.40           C  
ANISOU 3854  C   ILE B 221     4336   5525   6251   -291   -902    108       C  
ATOM   3855  O   ILE B 221      36.921 -15.230 -25.887  1.00 36.58           O  
ANISOU 3855  O   ILE B 221     3613   4781   5504   -359   -930    118       O  
ATOM   3856  CB  ILE B 221      40.139 -15.810 -24.904  1.00 34.36           C  
ANISOU 3856  CB  ILE B 221     3300   4532   5224   -177   -917     92       C  
ATOM   3857  CG1 ILE B 221      41.541 -16.034 -25.475  1.00 33.73           C  
ANISOU 3857  CG1 ILE B 221     3166   4468   5184    -96   -927    111       C  
ATOM   3858  CG2 ILE B 221      39.431 -17.135 -24.672  1.00 48.70           C  
ANISOU 3858  CG2 ILE B 221     5154   6262   7087   -223   -994    104       C  
ATOM   3859  CD1 ILE B 221      41.552 -16.672 -26.847  1.00 47.64           C  
ANISOU 3859  CD1 ILE B 221     4923   6152   7027   -102   -991    125       C  
ATOM   3860  N   VAL B 222      37.765 -14.014 -24.193  1.00 52.24           N  
ANISOU 3860  N   VAL B 222     5566   6768   7515   -272   -877    117       N  
ATOM   3861  CA  VAL B 222      36.496 -13.967 -23.476  1.00 48.07           C  
ANISOU 3861  CA  VAL B 222     5026   6231   7007   -309   -868    142       C  
ATOM   3862  C   VAL B 222      35.412 -13.266 -24.290  1.00 43.39           C  
ANISOU 3862  C   VAL B 222     4397   5650   6440   -345   -858    182       C  
ATOM   3863  O   VAL B 222      34.255 -13.704 -24.302  1.00 42.97           O  
ANISOU 3863  O   VAL B 222     4317   5600   6408   -399   -871    221       O  
ATOM   3864  CB  VAL B 222      36.690 -13.289 -22.109  1.00 44.55           C  
ANISOU 3864  CB  VAL B 222     4571   5786   6569   -280   -847    136       C  
ATOM   3865  CG1 VAL B 222      35.343 -12.889 -21.526  1.00 40.72           C  
ANISOU 3865  CG1 VAL B 222     4047   5304   6122   -305   -814    171       C  
ATOM   3866  CG2 VAL B 222      37.444 -14.208 -21.172  1.00 42.93           C  
ANISOU 3866  CG2 VAL B 222     4394   5581   6338   -258   -879    116       C  
ATOM   3867  N   THR B 223      35.750 -12.173 -24.974  1.00 40.74           N  
ANISOU 3867  N   THR B 223     4047   5323   6109   -321   -841    184       N  
ATOM   3868  CA  THR B 223      34.738 -11.344 -25.620  1.00 34.24           C  
ANISOU 3868  CA  THR B 223     3176   4515   5318   -341   -834    237       C  
ATOM   3869  C   THR B 223      34.698 -11.457 -27.140  1.00 36.33           C  
ANISOU 3869  C   THR B 223     3447   4797   5559   -374   -876    247       C  
ATOM   3870  O   THR B 223      33.878 -10.780 -27.769  1.00 40.71           O  
ANISOU 3870  O   THR B 223     3956   5372   6141   -392   -887    304       O  
ATOM   3871  CB  THR B 223      34.931  -9.874 -25.231  1.00 28.32           C  
ANISOU 3871  CB  THR B 223     2403   3761   4598   -297   -787    241       C  
ATOM   3872  OG1 THR B 223      36.077  -9.346 -25.910  1.00 34.86           O  
ANISOU 3872  OG1 THR B 223     3255   4588   5402   -275   -788    207       O  
ATOM   3873  CG2 THR B 223      35.114  -9.741 -23.723  1.00 32.32           C  
ANISOU 3873  CG2 THR B 223     2914   4254   5111   -275   -761    218       C  
ATOM   3874  N   TYR B 224      35.542 -12.285 -27.754  1.00 35.72           N  
ANISOU 3874  N   TYR B 224     3417   4718   5437   -382   -904    202       N  
ATOM   3875  CA  TYR B 224      35.431 -12.464 -29.196  1.00 36.41           C  
ANISOU 3875  CA  TYR B 224     3517   4825   5491   -427   -954    206       C  
ATOM   3876  C   TYR B 224      35.485 -13.934 -29.586  1.00 36.95           C  
ANISOU 3876  C   TYR B 224     3645   4884   5512   -492  -1014    171       C  
ATOM   3877  O   TYR B 224      34.498 -14.489 -30.080  1.00 45.78           O  
ANISOU 3877  O   TYR B 224     4779   6003   6613   -588  -1082    198       O  
ATOM   3878  CB  TYR B 224      36.528 -11.693 -29.933  1.00 34.19           C  
ANISOU 3878  CB  TYR B 224     3235   4556   5198   -377   -927    181       C  
ATOM   3879  CG  TYR B 224      36.360 -11.716 -31.438  1.00 32.64           C  
ANISOU 3879  CG  TYR B 224     3052   4386   4963   -425   -981    186       C  
ATOM   3880  CD1 TYR B 224      35.582 -10.763 -32.083  1.00 27.18           C  
ANISOU 3880  CD1 TYR B 224     2325   3714   4287   -444  -1000    242       C  
ATOM   3881  CD2 TYR B 224      36.967 -12.698 -32.212  1.00 31.11           C  
ANISOU 3881  CD2 TYR B 224     2909   4197   4714   -455  -1021    137       C  
ATOM   3882  CE1 TYR B 224      35.420 -10.782 -33.458  1.00 28.30           C  
ANISOU 3882  CE1 TYR B 224     2487   3881   4383   -496  -1068    252       C  
ATOM   3883  CE2 TYR B 224      36.810 -12.726 -33.588  1.00 25.19           C  
ANISOU 3883  CE2 TYR B 224     2194   3459   3916   -517  -1092    137       C  
ATOM   3884  CZ  TYR B 224      36.036 -11.766 -34.205  1.00 33.17           C  
ANISOU 3884  CZ  TYR B 224     3174   4497   4930   -537  -1114    190       C  
ATOM   3885  OH  TYR B 224      35.879 -11.791 -35.572  1.00 39.69           O  
ANISOU 3885  OH  TYR B 224     4050   5322   5709   -614  -1218    214       O  
ATOM   3886  N   LEU B 225      36.635 -14.574 -29.374  1.00 22.95           N  
ANISOU 3886  N   LEU B 225     1903   3099   3719   -449   -997    119       N  
ATOM   3887  CA  LEU B 225      36.808 -15.940 -29.855  1.00 20.15           C  
ANISOU 3887  CA  LEU B 225     1617   2690   3348   -519  -1083     98       C  
ATOM   3888  C   LEU B 225      35.838 -16.895 -29.169  1.00 25.53           C  
ANISOU 3888  C   LEU B 225     2335   3331   4033   -605  -1127    113       C  
ATOM   3889  O   LEU B 225      35.127 -17.657 -29.833  1.00 41.03           O  
ANISOU 3889  O   LEU B 225     4376   5242   5973   -741  -1230    131       O  
ATOM   3890  CB  LEU B 225      38.254 -16.392 -29.639  1.00 32.71           C  
ANISOU 3890  CB  LEU B 225     3198   4222   5008   -436  -1104     93       C  
ATOM   3891  CG  LEU B 225      38.792 -17.468 -30.587  1.00 41.26           C  
ANISOU 3891  CG  LEU B 225     4359   5167   6152   -494  -1269     97       C  
ATOM   3892  CD1 LEU B 225      39.166 -16.862 -31.929  1.00 42.39           C  
ANISOU 3892  CD1 LEU B 225     4503   5312   6289   -505  -1306    102       C  
ATOM   3893  CD2 LEU B 225      39.977 -18.188 -29.964  1.00 40.66           C  
ANISOU 3893  CD2 LEU B 225     4230   5016   6203   -372  -1307    104       C  
ATOM   3894  N   ALA B 226      35.797 -16.873 -27.836  1.00 31.30           N  
ANISOU 3894  N   ALA B 226     3027   4079   4785   -546  -1060    112       N  
ATOM   3895  CA  ALA B 226      34.953 -17.827 -27.117  1.00 30.57           C  
ANISOU 3895  CA  ALA B 226     2959   3939   4717   -629  -1103    137       C  
ATOM   3896  C   ALA B 226      33.472 -17.673 -27.429  1.00 42.13           C  
ANISOU 3896  C   ALA B 226     4393   5448   6169   -725  -1112    174       C  
ATOM   3897  O   ALA B 226      32.830 -18.675 -27.786  1.00 51.19           O  
ANISOU 3897  O   ALA B 226     5602   6537   7310   -866  -1207    202       O  
ATOM   3898  CB  ALA B 226      35.212 -17.709 -25.612  1.00 23.15           C  
ANISOU 3898  CB  ALA B 226     1982   3007   3808   -546  -1040    137       C  
ATOM   3899  N   PRO B 227      32.870 -16.488 -27.312  1.00 36.71           N  
ANISOU 3899  N   PRO B 227     3615   4804   5529   -683  -1079    237       N  
ATOM   3900  CA  PRO B 227      31.436 -16.378 -27.626  1.00 31.12           C  
ANISOU 3900  CA  PRO B 227     2845   4123   4857   -777  -1128    327       C  
ATOM   3901  C   PRO B 227      31.106 -16.718 -29.067  1.00 42.79           C  
ANISOU 3901  C   PRO B 227     4373   5605   6281   -890  -1231    341       C  
ATOM   3902  O   PRO B 227      30.157 -17.470 -29.327  1.00 54.86           O  
ANISOU 3902  O   PRO B 227     5913   7129   7801  -1028  -1314    390       O  
ATOM   3903  CB  PRO B 227      31.123 -14.913 -27.282  1.00 34.63           C  
ANISOU 3903  CB  PRO B 227     3189   4602   5365   -686  -1064    388       C  
ATOM   3904  CG  PRO B 227      32.182 -14.531 -26.287  1.00 41.47           C  
ANISOU 3904  CG  PRO B 227     4080   5445   6230   -575   -982    322       C  
ATOM   3905  CD  PRO B 227      33.413 -15.235 -26.764  1.00 40.88           C  
ANISOU 3905  CD  PRO B 227     4095   5348   6090   -564  -1003    239       C  
ATOM   3906  N   LEU B 228      31.879 -16.193 -30.019  1.00 42.77           N  
ANISOU 3906  N   LEU B 228     4408   5608   6233   -848  -1237    301       N  
ATOM   3907  CA  LEU B 228      31.611 -16.486 -31.422  1.00 37.71           C  
ANISOU 3907  CA  LEU B 228     3840   4965   5522   -963  -1345    308       C  
ATOM   3908  C   LEU B 228      31.829 -17.962 -31.731  1.00 37.80           C  
ANISOU 3908  C   LEU B 228     4016   4887   5461  -1099  -1435    262       C  
ATOM   3909  O   LEU B 228      31.105 -18.546 -32.546  1.00 38.06           O  
ANISOU 3909  O   LEU B 228     4144   4889   5430  -1269  -1565    309       O  
ATOM   3910  CB  LEU B 228      32.483 -15.608 -32.316  1.00 33.89           C  
ANISOU 3910  CB  LEU B 228     3367   4500   5009   -887  -1324    273       C  
ATOM   3911  CG  LEU B 228      31.839 -14.301 -32.786  1.00 38.78           C  
ANISOU 3911  CG  LEU B 228     3887   5175   5673   -861  -1334    370       C  
ATOM   3912  CD1 LEU B 228      31.237 -13.525 -31.623  1.00 40.67           C  
ANISOU 3912  CD1 LEU B 228     4002   5435   6014   -785  -1255    440       C  
ATOM   3913  CD2 LEU B 228      32.857 -13.457 -33.532  1.00 51.02           C  
ANISOU 3913  CD2 LEU B 228     5451   6737   7197   -779  -1295    323       C  
ATOM   3914  N   GLY B 229      32.811 -18.586 -31.081  1.00 31.69           N  
ANISOU 3914  N   GLY B 229     3306   4036   4698  -1055  -1409    208       N  
ATOM   3915  CA  GLY B 229      33.006 -20.014 -31.267  1.00 32.21           C  
ANISOU 3915  CA  GLY B 229     3583   3956   4701  -1207  -1522    190       C  
ATOM   3916  C   GLY B 229      31.828 -20.822 -30.762  1.00 35.95           C  
ANISOU 3916  C   GLY B 229     4072   4415   5171  -1344  -1558    237       C  
ATOM   3917  O   GLY B 229      31.319 -21.707 -31.455  1.00 42.25           O  
ANISOU 3917  O   GLY B 229     5056   5131   5868  -1539  -1673    253       O  
ATOM   3918  N   LEU B 230      31.377 -20.529 -29.538  1.00 34.00           N  
ANISOU 3918  N   LEU B 230     3657   4240   5022  -1258  -1462    263       N  
ATOM   3919  CA  LEU B 230      30.223 -21.233 -28.991  1.00 35.74           C  
ANISOU 3919  CA  LEU B 230     3860   4455   5265  -1388  -1493    325       C  
ATOM   3920  C   LEU B 230      28.961 -20.932 -29.788  1.00 39.53           C  
ANISOU 3920  C   LEU B 230     4272   5014   5735  -1502  -1568    412       C  
ATOM   3921  O   LEU B 230      28.103 -21.807 -29.962  1.00 39.72           O  
ANISOU 3921  O   LEU B 230     4360   5004   5727  -1693  -1666    470       O  
ATOM   3922  CB  LEU B 230      30.030 -20.852 -27.522  1.00 30.44           C  
ANISOU 3922  CB  LEU B 230     3032   3836   4698  -1269  -1375    344       C  
ATOM   3923  CG  LEU B 230      31.083 -21.381 -26.546  1.00 26.77           C  
ANISOU 3923  CG  LEU B 230     2633   3283   4253  -1196  -1340    294       C  
ATOM   3924  CD1 LEU B 230      31.022 -20.631 -25.224  1.00 30.48           C  
ANISOU 3924  CD1 LEU B 230     2957   3821   4803  -1055  -1227    313       C  
ATOM   3925  CD2 LEU B 230      30.903 -22.877 -26.331  1.00 33.86           C  
ANISOU 3925  CD2 LEU B 230     3703   4039   5121  -1371  -1420    301       C  
ATOM   3926  N   MET B 231      28.827 -19.698 -30.279  1.00 45.39           N  
ANISOU 3926  N   MET B 231     4888   5855   6501  -1398  -1533    432       N  
ATOM   3927  CA  MET B 231      27.635 -19.343 -31.044  1.00 45.64           C  
ANISOU 3927  CA  MET B 231     4844   5955   6542  -1513  -1644    565       C  
ATOM   3928  C   MET B 231      27.627 -20.019 -32.409  1.00 47.83           C  
ANISOU 3928  C   MET B 231     5312   6178   6681  -1693  -1795    553       C  
ATOM   3929  O   MET B 231      26.573 -20.458 -32.881  1.00 56.71           O  
ANISOU 3929  O   MET B 231     6446   7323   7778  -1880  -1927    654       O  
ATOM   3930  CB  MET B 231      27.528 -17.823 -31.194  1.00 46.65           C  
ANISOU 3930  CB  MET B 231     4817   6165   6741  -1378  -1599    641       C  
ATOM   3931  CG  MET B 231      26.978 -17.112 -29.966  1.00 56.37           C  
ANISOU 3931  CG  MET B 231     5870   7445   8104  -1269  -1494    719       C  
ATOM   3932  SD  MET B 231      27.324 -15.341 -29.976  1.00 60.40           S  
ANISOU 3932  SD  MET B 231     6279   7997   8674  -1081  -1395    745       S  
ATOM   3933  CE  MET B 231      26.163 -14.785 -31.219  1.00 65.90           C  
ANISOU 3933  CE  MET B 231     6880   8772   9388  -1189  -1530    918       C  
ATOM   3934  N   ALA B 232      28.790 -20.116 -33.060  1.00 44.56           N  
ANISOU 3934  N   ALA B 232     5072   5685   6174  -1667  -1805    463       N  
ATOM   3935  CA  ALA B 232      28.845 -20.781 -34.357  1.00 41.26           C  
ANISOU 3935  CA  ALA B 232     4913   5178   5587  -1863  -1965    466       C  
ATOM   3936  C   ALA B 232      28.418 -22.239 -34.246  1.00 53.54           C  
ANISOU 3936  C   ALA B 232     6682   6615   7044  -2083  -2058    471       C  
ATOM   3937  O   ALA B 232      27.774 -22.778 -35.153  1.00 67.08           O  
ANISOU 3937  O   ALA B 232     8569   8292   8625  -2303  -2211    527       O  
ATOM   3938  CB  ALA B 232      30.252 -20.674 -34.947  1.00 36.39           C  
ANISOU 3938  CB  ALA B 232     4474   4468   4883  -1791  -1944    365       C  
ATOM   3939  N   MET B 233      28.767 -22.897 -33.137  1.00 50.28           N  
ANISOU 3939  N   MET B 233     6285   6136   6684  -2038  -1970    417       N  
ATOM   3940  CA  MET B 233      28.335 -24.275 -32.932  1.00 53.54           C  
ANISOU 3940  CA  MET B 233     6910   6425   7007  -2244  -2037    419       C  
ATOM   3941  C   MET B 233      26.853 -24.343 -32.585  1.00 55.49           C  
ANISOU 3941  C   MET B 233     6960   6784   7339  -2367  -2097    549       C  
ATOM   3942  O   MET B 233      26.163 -25.295 -32.970  1.00 60.67           O  
ANISOU 3942  O   MET B 233     7788   7375   7889  -2611  -2221    595       O  
ATOM   3943  CB  MET B 233      29.177 -24.925 -31.835  1.00 54.27           C  
ANISOU 3943  CB  MET B 233     7086   6401   7135  -2157  -1925    332       C  
ATOM   3944  CG  MET B 233      30.663 -24.943 -32.143  1.00 54.30           C  
ANISOU 3944  CG  MET B 233     7297   6271   7064  -2046  -1878    219       C  
ATOM   3945  SD  MET B 233      31.640 -25.833 -30.920  1.00 62.83           S  
ANISOU 3945  SD  MET B 233     8527   7169   8176  -1965  -1777    137       S  
ATOM   3946  CE  MET B 233      31.716 -24.617 -29.610  1.00 65.03           C  
ANISOU 3946  CE  MET B 233     8341   7663   8704  -1723  -1676    185       C  
ATOM   3947  N   ALA B 234      26.348 -23.352 -31.848  1.00 46.40           N  
ANISOU 3947  N   ALA B 234     5473   5788   6369  -2209  -2007    613       N  
ATOM   3948  CA  ALA B 234      24.936 -23.353 -31.483  1.00 40.75           C  
ANISOU 3948  CA  ALA B 234     4559   5174   5751  -2315  -2056    754       C  
ATOM   3949  C   ALA B 234      24.053 -23.174 -32.710  1.00 43.57           C  
ANISOU 3949  C   ALA B 234     4915   5597   6042  -2491  -2236    872       C  
ATOM   3950  O   ALA B 234      23.080 -23.911 -32.900  1.00 46.65           O  
ANISOU 3950  O   ALA B 234     5334   5990   6401  -2726  -2372    974       O  
ATOM   3951  CB  ALA B 234      24.655 -22.257 -30.454  1.00 38.85           C  
ANISOU 3951  CB  ALA B 234     4014   5055   5693  -2095  -1903    794       C  
ATOM   3952  N   TYR B 235      24.373 -22.192 -33.554  1.00 42.79           N  
ANISOU 3952  N   TYR B 235     4787   5552   5920  -2393  -2249    871       N  
ATOM   3953  CA  TYR B 235      23.569 -21.976 -34.750  1.00 45.63           C  
ANISOU 3953  CA  TYR B 235     5153   5973   6210  -2566  -2434    997       C  
ATOM   3954  C   TYR B 235      23.740 -23.101 -35.762  1.00 48.19           C  
ANISOU 3954  C   TYR B 235     5845   6163   6303  -2832  -2607    968       C  
ATOM   3955  O   TYR B 235      22.841 -23.337 -36.579  1.00 54.95           O  
ANISOU 3955  O   TYR B 235     6746   7052   7079  -3066  -2801   1095       O  
ATOM   3956  CB  TYR B 235      23.903 -20.620 -35.366  1.00 44.34           C  
ANISOU 3956  CB  TYR B 235     4886   5886   6076  -2406  -2409   1021       C  
ATOM   3957  CG  TYR B 235      23.287 -19.469 -34.602  1.00 43.73           C  
ANISOU 3957  CG  TYR B 235     4483   5936   6195  -2249  -2322   1157       C  
ATOM   3958  CD1 TYR B 235      21.921 -19.223 -34.668  1.00 46.66           C  
ANISOU 3958  CD1 TYR B 235     4652   6420   6657  -2369  -2437   1381       C  
ATOM   3959  CD2 TYR B 235      24.062 -18.642 -33.802  1.00 40.54           C  
ANISOU 3959  CD2 TYR B 235     3988   5532   5883  -1990  -2127   1072       C  
ATOM   3960  CE1 TYR B 235      21.348 -18.179 -33.972  1.00 46.36           C  
ANISOU 3960  CE1 TYR B 235     4336   6481   6796  -2217  -2340   1512       C  
ATOM   3961  CE2 TYR B 235      23.498 -17.596 -33.101  1.00 40.62           C  
ANISOU 3961  CE2 TYR B 235     3753   5630   6051  -1854  -2038   1191       C  
ATOM   3962  CZ  TYR B 235      22.140 -17.369 -33.190  1.00 49.24           C  
ANISOU 3962  CZ  TYR B 235     4654   6823   7233  -1960  -2135   1409       C  
ATOM   3963  OH  TYR B 235      21.570 -16.329 -32.495  1.00 63.18           O  
ANISOU 3963  OH  TYR B 235     6185   8662   9157  -1816  -2030   1536       O  
ATOM   3964  N   PHE B 236      24.873 -23.805 -35.734  1.00 46.98           N  
ANISOU 3964  N   PHE B 236     5981   5845   6025  -2812  -2543    813       N  
ATOM   3965  CA  PHE B 236      25.014 -24.961 -36.611  1.00 49.77           C  
ANISOU 3965  CA  PHE B 236     6758   6030   6124  -3070  -2680    776       C  
ATOM   3966  C   PHE B 236      24.071 -26.081 -36.193  1.00 53.31           C  
ANISOU 3966  C   PHE B 236     7267   6442   6547  -3310  -2769    844       C  
ATOM   3967  O   PHE B 236      23.473 -26.748 -37.045  1.00 60.40           O  
ANISOU 3967  O   PHE B 236     8397   7284   7268  -3594  -2954    909       O  
ATOM   3968  CB  PHE B 236      26.459 -25.457 -36.615  1.00 59.30           C  
ANISOU 3968  CB  PHE B 236     8286   7044   7201  -2975  -2563    598       C  
ATOM   3969  CG  PHE B 236      26.688 -26.637 -37.515  1.00 76.45           C  
ANISOU 3969  CG  PHE B 236    10981   8995   9072  -3215  -2657    542       C  
ATOM   3970  CD1 PHE B 236      26.718 -26.483 -38.892  1.00 86.42           C  
ANISOU 3970  CD1 PHE B 236    12498  10208  10129  -3346  -2782    562       C  
ATOM   3971  CD2 PHE B 236      26.864 -27.904 -36.985  1.00 80.81           C  
ANISOU 3971  CD2 PHE B 236    11809   9370   9526  -3310  -2606    470       C  
ATOM   3972  CE1 PHE B 236      26.923 -27.571 -39.721  1.00 92.09           C  
ANISOU 3972  CE1 PHE B 236    13762  10695  10534  -3564  -2844    506       C  
ATOM   3973  CE2 PHE B 236      27.070 -28.993 -37.806  1.00 91.43           C  
ANISOU 3973  CE2 PHE B 236    13692  10482  10564  -3517  -2657    412       C  
ATOM   3974  CZ  PHE B 236      27.100 -28.828 -39.176  1.00 95.62           C  
ANISOU 3974  CZ  PHE B 236    14497  10957  10876  -3644  -2771    428       C  
ATOM   3975  N   GLN B 237      23.928 -26.305 -34.885  1.00 55.43           N  
ANISOU 3975  N   GLN B 237     7346   6734   6980  -3216  -2645    833       N  
ATOM   3976  CA  GLN B 237      22.945 -27.274 -34.418  1.00 63.05           C  
ANISOU 3976  CA  GLN B 237     8319   7685   7953  -3443  -2724    914       C  
ATOM   3977  C   GLN B 237      21.530 -26.787 -34.690  1.00 65.33           C  
ANISOU 3977  C   GLN B 237     8317   8159   8346  -3577  -2875   1118       C  
ATOM   3978  O   GLN B 237      20.643 -27.584 -35.023  1.00 70.99           O  
ANISOU 3978  O   GLN B 237     9131   8862   8982  -3873  -3047   1219       O  
ATOM   3979  CB  GLN B 237      23.144 -27.551 -32.928  1.00 65.46           C  
ANISOU 3979  CB  GLN B 237     8485   7970   8416  -3302  -2546    861       C  
ATOM   3980  CG  GLN B 237      24.332 -28.450 -32.623  1.00 71.11           C  
ANISOU 3980  CG  GLN B 237     9549   8467   9004  -3263  -2438    692       C  
ATOM   3981  CD  GLN B 237      24.190 -29.175 -31.297  1.00 84.30           C  
ANISOU 3981  CD  GLN B 237    11176  10079  10775  -3263  -2331    678       C  
ATOM   3982  OE1 GLN B 237      23.533 -28.687 -30.376  1.00 86.47           O  
ANISOU 3982  OE1 GLN B 237    11103  10494  11256  -3185  -2272    764       O  
ATOM   3983  NE2 GLN B 237      24.816 -30.342 -31.189  1.00 92.09           N  
ANISOU 3983  NE2 GLN B 237    12547  10840  11604  -3346  -2289    572       N  
ATOM   3984  N   ILE B 238      21.299 -25.479 -34.551  1.00 66.14           N  
ANISOU 3984  N   ILE B 238     8075   8430   8626  -3369  -2814   1191       N  
ATOM   3985  CA  ILE B 238      19.991 -24.926 -34.886  1.00 69.50           C  
ANISOU 3985  CA  ILE B 238     8229   9026   9151  -3477  -2954   1404       C  
ATOM   3986  C   ILE B 238      19.716 -25.087 -36.373  1.00 73.86           C  
ANISOU 3986  C   ILE B 238     8994   9563   9507  -3726  -3195   1477       C  
ATOM   3987  O   ILE B 238      18.581 -25.353 -36.786  1.00 78.83           O  
ANISOU 3987  O   ILE B 238     9553  10272  10129  -3980  -3396   1658       O  
ATOM   3988  CB  ILE B 238      19.910 -23.451 -34.455  1.00 65.07           C  
ANISOU 3988  CB  ILE B 238     7322   8612   8789  -3200  -2829   1481       C  
ATOM   3989  CG1 ILE B 238      19.740 -23.349 -32.937  1.00 63.33           C  
ANISOU 3989  CG1 ILE B 238     6874   8425   8762  -3037  -2641   1486       C  
ATOM   3990  CG2 ILE B 238      18.770 -22.755 -35.177  1.00 69.44           C  
ANISOU 3990  CG2 ILE B 238     7664   9321   9398  -3323  -3011   1733       C  
ATOM   3991  CD1 ILE B 238      20.231 -22.038 -32.361  1.00 63.77           C  
ANISOU 3991  CD1 ILE B 238     6741   8540   8949  -2719  -2454   1464       C  
ATOM   3992  N   PHE B 239      20.752 -24.924 -37.199  1.00 73.30           N  
ANISOU 3992  N   PHE B 239     9192   9390   9268  -3667  -3185   1349       N  
ATOM   3993  CA  PHE B 239      20.600 -25.089 -38.641  1.00 76.97           C  
ANISOU 3993  CA  PHE B 239     9923   9812   9511  -3906  -3405   1404       C  
ATOM   3994  C   PHE B 239      20.251 -26.526 -39.005  1.00 75.51           C  
ANISOU 3994  C   PHE B 239    10100   9483   9106  -4260  -3571   1411       C  
ATOM   3995  O   PHE B 239      19.382 -26.766 -39.853  1.00 80.01           O  
ANISOU 3995  O   PHE B 239    10748  10088   9565  -4553  -3813   1560       O  
ATOM   3996  CB  PHE B 239      21.889 -24.652 -39.340  1.00 85.08           C  
ANISOU 3996  CB  PHE B 239    11187  10735  10403  -3751  -3323   1251       C  
ATOM   3997  CG  PHE B 239      22.026 -25.162 -40.745  1.00 88.32           C  
ANISOU 3997  CG  PHE B 239    12031  11015  10513  -4011  -3512   1249       C  
ATOM   3998  CD1 PHE B 239      21.365 -24.541 -41.790  1.00 87.02           C  
ANISOU 3998  CD1 PHE B 239    11814  10948  10301  -4147  -3707   1401       C  
ATOM   3999  CD2 PHE B 239      22.836 -26.252 -41.021  1.00 87.86           C  
ANISOU 3999  CD2 PHE B 239    12463  10717  10203  -4117  -3484   1098       C  
ATOM   4000  CE1 PHE B 239      21.499 -25.005 -43.084  1.00 88.54           C  
ANISOU 4000  CE1 PHE B 239    12443  11004  10194  -4398  -3883   1398       C  
ATOM   4001  CE2 PHE B 239      22.975 -26.720 -42.313  1.00 87.78           C  
ANISOU 4001  CE2 PHE B 239    12914  10555   9883  -4354  -3634   1090       C  
ATOM   4002  CZ  PHE B 239      22.305 -26.095 -43.346  1.00 88.28           C  
ANISOU 4002  CZ  PHE B 239    12928  10719   9896  -4502  -3840   1239       C  
ATOM   4003  N   ARG B 240      20.921 -27.495 -38.378  1.00 74.30           N  
ANISOU 4003  N   ARG B 240    10191   9161   8877  -4247  -3446   1256       N  
ATOM   4004  CA  ARG B 240      20.643 -28.894 -38.674  1.00 76.11           C  
ANISOU 4004  CA  ARG B 240    10816   9225   8879  -4577  -3574   1245       C  
ATOM   4005  C   ARG B 240      19.243 -29.288 -38.224  1.00 81.15           C  
ANISOU 4005  C   ARG B 240    11210   9986   9637  -4807  -3718   1428       C  
ATOM   4006  O   ARG B 240      18.563 -30.067 -38.903  1.00 85.65           O  
ANISOU 4006  O   ARG B 240    12015  10502  10025  -5162  -3939   1518       O  
ATOM   4007  CB  ARG B 240      21.693 -29.785 -38.009  1.00 75.19           C  
ANISOU 4007  CB  ARG B 240    11002   8893   8673  -4477  -3376   1043       C  
ATOM   4008  CG  ARG B 240      23.077 -29.666 -38.626  1.00 82.76           C  
ANISOU 4008  CG  ARG B 240    12309   9685   9452  -4319  -3260    874       C  
ATOM   4009  CD  ARG B 240      23.138 -30.315 -40.001  1.00 98.77           C  
ANISOU 4009  CD  ARG B 240    14872  11531  11123  -4594  -3413    864       C  
ATOM   4010  NE  ARG B 240      23.148 -31.774 -39.933  1.00109.43           N  
ANISOU 4010  NE  ARG B 240    16684  12650  12245  -4815  -3411    797       N  
ATOM   4011  CZ  ARG B 240      24.247 -32.504 -39.777  1.00110.57           C  
ANISOU 4011  CZ  ARG B 240    17244  12544  12222  -4709  -3216    621       C  
ATOM   4012  NH1 ARG B 240      25.428 -31.911 -39.670  1.00110.27           N  
ANISOU 4012  NH1 ARG B 240    17195  12469  12235  -4396  -3024    501       N  
ATOM   4013  NH2 ARG B 240      24.167 -33.827 -39.732  1.00109.37           N  
ANISOU 4013  NH2 ARG B 240    17529  12174  11854  -4913  -3205    573       N  
ATOM   4014  N   LYS B 241      18.795 -28.757 -37.084  1.00 83.90           N  
ANISOU 4014  N   LYS B 241    11102  10493  10283  -4621  -3596   1493       N  
ATOM   4015  CA  LYS B 241      17.476 -29.110 -36.571  1.00 83.66           C  
ANISOU 4015  CA  LYS B 241    10814  10581  10392  -4823  -3709   1677       C  
ATOM   4016  C   LYS B 241      16.357 -28.483 -37.391  1.00 77.31           C  
ANISOU 4016  C   LYS B 241     9782   9962   9631  -4993  -3947   1919       C  
ATOM   4017  O   LYS B 241      15.245 -29.021 -37.434  1.00111.05           O  
ANISOU 4017  O   LYS B 241    13970  14302  13922  -5288  -4135   2095       O  
ATOM   4018  CB  LYS B 241      17.356 -28.669 -35.111  1.00 77.54           C  
ANISOU 4018  CB  LYS B 241     9645   9905   9912  -4558  -3485   1680       C  
ATOM   4019  CG  LYS B 241      16.182 -29.271 -34.351  1.00 73.79           C  
ANISOU 4019  CG  LYS B 241     8955   9502   9578  -4753  -3541   1833       C  
ATOM   4020  CD  LYS B 241      16.510 -30.672 -33.850  1.00 74.53           C  
ANISOU 4020  CD  LYS B 241     9377   9394   9547  -4913  -3495   1703       C  
ATOM   4021  CE  LYS B 241      15.498 -31.147 -32.812  1.00 96.33           C  
ANISOU 4021  CE  LYS B 241    11874  12224  12503  -5033  -3475   1831       C  
ATOM   4022  NZ  LYS B 241      16.148 -31.636 -31.559  1.00 93.89           N  
ANISOU 4022  NZ  LYS B 241    11620  11788  12266  -4870  -3226   1677       N  
ATOM   4023  N   LEU B 242      16.618 -27.337 -38.024  1.00 88.77           N  
ANISOU 4023  N   LEU B 242    11118  11500  11109  -4817  -3944   1944       N  
ATOM   4024  CA  LEU B 242      15.589 -26.648 -38.796  1.00 89.07           C  
ANISOU 4024  CA  LEU B 242    10925  11717  11201  -4956  -4163   2188       C  
ATOM   4025  C   LEU B 242      15.595 -26.999 -40.283  1.00 93.27           C  
ANISOU 4025  C   LEU B 242    11833  12167  11439  -5257  -4424   2219       C  
ATOM   4026  O   LEU B 242      14.525 -27.106 -40.890  1.00100.81           O  
ANISOU 4026  O   LEU B 242    12711  13224  12368  -5553  -4691   2442       O  
ATOM   4027  CB  LEU B 242      15.737 -25.134 -38.623  1.00 76.09           C  
ANISOU 4027  CB  LEU B 242     8936  10218   9755  -4625  -4031   2251       C  
ATOM   4028  CG  LEU B 242      15.290 -24.592 -37.263  1.00 74.34           C  
ANISOU 4028  CG  LEU B 242     8291  10122   9833  -4400  -3844   2341       C  
ATOM   4029  CD1 LEU B 242      15.596 -23.107 -37.141  1.00100.76           C  
ANISOU 4029  CD1 LEU B 242    11388  13565  13329  -4067  -3691   2369       C  
ATOM   4030  CD2 LEU B 242      13.807 -24.858 -37.039  1.00 79.09           C  
ANISOU 4030  CD2 LEU B 242     8607  10874  10570  -4642  -4019   2629       C  
ATOM   4031  N   TRP B 243      16.767 -27.192 -40.890  1.00 89.94           N  
ANISOU 4031  N   TRP B 243    11829  11558  10787  -5202  -4360   2016       N  
ATOM   4032  CA  TRP B 243      16.851 -27.506 -42.314  1.00 96.48           C  
ANISOU 4032  CA  TRP B 243    13074  12277  11307  -5480  -4586   2033       C  
ATOM   4033  C   TRP B 243      17.278 -28.940 -42.602  1.00104.79           C  
ANISOU 4033  C   TRP B 243    14701  13069  12044  -5739  -4630   1897       C  
ATOM   4034  O   TRP B 243      17.594 -29.260 -43.753  1.00105.33           O  
ANISOU 4034  O   TRP B 243    15225  12986  11811  -5936  -4762   1863       O  
ATOM   4035  CB  TRP B 243      17.794 -26.535 -43.025  1.00 94.32           C  
ANISOU 4035  CB  TRP B 243    12884  11977  10977  -5248  -4497   1935       C  
ATOM   4036  CG  TRP B 243      17.223 -25.171 -43.222  1.00 97.61           C  
ANISOU 4036  CG  TRP B 243    12858  12622  11606  -5106  -4539   2107       C  
ATOM   4037  CD1 TRP B 243      16.457 -24.752 -44.269  1.00101.03           C  
ANISOU 4037  CD1 TRP B 243    13256  13155  11976  -5321  -4801   2306       C  
ATOM   4038  CD2 TRP B 243      17.394 -24.034 -42.368  1.00 97.83           C  
ANISOU 4038  CD2 TRP B 243    12451  12794  11928  -4722  -4310   2097       C  
ATOM   4039  NE1 TRP B 243      16.127 -23.429 -44.115  1.00101.53           N  
ANISOU 4039  NE1 TRP B 243    12875  13417  12285  -5083  -4741   2426       N  
ATOM   4040  CE2 TRP B 243      16.692 -22.963 -42.956  1.00 96.95           C  
ANISOU 4040  CE2 TRP B 243    12060  12858  11917  -4717  -4436   2300       C  
ATOM   4041  CE3 TRP B 243      18.067 -23.818 -41.162  1.00 97.41           C  
ANISOU 4041  CE3 TRP B 243    12236  12727  12048  -4394  -4015   1945       C  
ATOM   4042  CZ2 TRP B 243      16.643 -21.697 -42.380  1.00 92.80           C  
ANISOU 4042  CZ2 TRP B 243    11137  12479  11645  -4410  -4276   2374       C  
ATOM   4043  CZ3 TRP B 243      18.018 -22.558 -40.592  1.00 88.78           C  
ANISOU 4043  CZ3 TRP B 243    10753  11780  11199  -4096  -3863   2006       C  
ATOM   4044  CH2 TRP B 243      17.311 -21.515 -41.201  1.00 86.67           C  
ANISOU 4044  CH2 TRP B 243    10245  11671  11016  -4107  -3988   2221       C  
ATOM   4045  N   GLY B 244      17.289 -29.810 -41.600  1.00113.27           N  
ANISOU 4045  N   GLY B 244    15798  14071  13168  -5746  -4515   1821       N  
ATOM   4046  CA  GLY B 244      17.608 -31.202 -41.837  1.00122.49           C  
ANISOU 4046  CA  GLY B 244    17526  14981  14032  -6001  -4548   1704       C  
ATOM   4047  C   GLY B 244      16.374 -31.982 -42.239  1.00139.44           C  
ANISOU 4047  C   GLY B 244    19760  17152  16067  -6458  -4849   1892       C  
ATOM   4048  O   GLY B 244      15.503 -31.453 -42.937  1.00146.15           O  
ANISOU 4048  O   GLY B 244    20423  18162  16944  -6638  -5094   2101       O  
ATOM   4049  N   ARG B 245      16.293 -33.240 -41.820  1.00147.11           N  
ANISOU 4049  N   ARG B 245    21024  17962  16910  -6662  -4840   1826       N  
ATOM   4050  CA  ARG B 245      15.128 -34.057 -42.119  1.00157.84           C  
ANISOU 4050  CA  ARG B 245    22473  19335  18163  -7121  -5126   2001       C  
ATOM   4051  C   ARG B 245      13.914 -33.533 -41.365  1.00159.22           C  
ANISOU 4051  C   ARG B 245    21983  19808  18705  -7128  -5212   2233       C  
ATOM   4052  O   ARG B 245      14.026 -32.954 -40.281  1.00156.25           O  
ANISOU 4052  O   ARG B 245    21174  19556  18639  -6794  -4989   2208       O  
ATOM   4053  CB  ARG B 245      15.396 -35.520 -41.766  1.00163.03           C  
ANISOU 4053  CB  ARG B 245    23614  19732  18600  -7312  -5058   1860       C  
ATOM   4054  CG  ARG B 245      16.486 -36.160 -42.614  1.00168.17           C  
ANISOU 4054  CG  ARG B 245    25000  20057  18841  -7350  -4978   1660       C  
ATOM   4055  CD  ARG B 245      16.003 -36.354 -44.043  1.00177.43           C  
ANISOU 4055  CD  ARG B 245    26558  21162  19694  -7747  -5289   1780       C  
ATOM   4056  NE  ARG B 245      17.043 -36.861 -44.933  1.00180.82           N  
ANISOU 4056  NE  ARG B 245    27714  21268  19720  -7764  -5193   1601       N  
ATOM   4057  CZ  ARG B 245      17.862 -36.091 -45.643  1.00182.60           C  
ANISOU 4057  CZ  ARG B 245    28057  21452  19872  -7544  -5106   1527       C  
ATOM   4058  NH1 ARG B 245      17.762 -34.770 -45.578  1.00182.30           N  
ANISOU 4058  NH1 ARG B 245    27459  21677  20129  -7298  -5115   1611       N  
ATOM   4059  NH2 ARG B 245      18.777 -36.643 -46.428  1.00183.75           N  
ANISOU 4059  NH2 ARG B 245    28899  21279  19640  -7568  -4997   1373       N  
ATOM   4060  N   GLN B 246      12.739 -33.746 -41.947  1.00162.24           N  
ANISOU 4060  N   GLN B 246    22301  20298  19043  -7522  -5538   2473       N  
ATOM   4061  CA  GLN B 246      11.499 -33.224 -41.388  1.00160.29           C  
ANISOU 4061  CA  GLN B 246    21428  20342  19134  -7558  -5645   2739       C  
ATOM   4062  C   GLN B 246      10.708 -34.343 -40.718  1.00158.09           C  
ANISOU 4062  C   GLN B 246    21141  20041  18886  -7863  -5726   2813       C  
ATOM   4063  O   GLN B 246      10.645 -35.467 -41.220  1.00164.31           O  
ANISOU 4063  O   GLN B 246    22419  20640  19372  -8238  -5885   2775       O  
ATOM   4064  CB  GLN B 246      10.659 -32.537 -42.471  1.00167.55           C  
ANISOU 4064  CB  GLN B 246    22184  21441  20037  -7770  -5964   3004       C  
ATOM   4065  CG  GLN B 246      11.240 -31.195 -42.944  1.00165.12           C  
ANISOU 4065  CG  GLN B 246    21720  21216  19801  -7425  -5865   2977       C  
ATOM   4066  CD  GLN B 246      10.429 -30.534 -44.045  1.00169.94           C  
ANISOU 4066  CD  GLN B 246    22193  21992  20386  -7642  -6182   3242       C  
ATOM   4067  OE1 GLN B 246       9.316 -30.956 -44.347  1.00179.77           O  
ANISOU 4067  OE1 GLN B 246    23352  23338  21616  -8031  -6484   3486       O  
ATOM   4068  NE2 GLN B 246      10.966 -29.460 -44.616  1.00161.86           N  
ANISOU 4068  NE2 GLN B 246    21120  21006  19372  -7392  -6118   3208       N  
ATOM   4069  N   ILE B 247      10.094 -34.010 -39.588  1.00149.38           N  
ANISOU 4069  N   ILE B 247    19492  19122  18143  -7707  -5608   2924       N  
ATOM   4070  CA  ILE B 247       9.473 -34.994 -38.697  1.00143.43           C  
ANISOU 4070  CA  ILE B 247    18674  18344  17481  -7913  -5600   2965       C  
ATOM   4071  C   ILE B 247       8.384 -35.759 -39.438  1.00147.59           C  
ANISOU 4071  C   ILE B 247    19328  18898  17851  -8470  -5985   3186       C  
ATOM   4072  O   ILE B 247       7.591 -35.146 -40.176  1.00149.95           O  
ANISOU 4072  O   ILE B 247    19387  19393  18196  -8628  -6249   3442       O  
ATOM   4073  CB  ILE B 247       8.905 -34.297 -37.449  1.00133.04           C  
ANISOU 4073  CB  ILE B 247    16703  17248  16597  -7637  -5412   3091       C  
ATOM   4074  CG1 ILE B 247       9.971 -33.429 -36.797  1.00121.77           C  
ANISOU 4074  CG1 ILE B 247    15162  15801  15305  -7105  -5060   2888       C  
ATOM   4075  CG2 ILE B 247       8.349 -35.317 -36.473  1.00133.99           C  
ANISOU 4075  CG2 ILE B 247    16765  17323  16822  -7831  -5367   3115       C  
ATOM   4076  CD1 ILE B 247       9.990 -32.000 -37.297  1.00117.16           C  
ANISOU 4076  CD1 ILE B 247    14283  15397  14836  -6847  -5066   2989       C  
ATOM   4077  N   PRO B 248       8.310 -37.088 -39.303  1.00146.75           N  
ANISOU 4077  N   PRO B 248    19613  18597  17550  -8796  -6041   3107       N  
ATOM   4078  CA  PRO B 248       7.273 -37.834 -40.031  1.00154.88           C  
ANISOU 4078  CA  PRO B 248    20793  19645  18411  -9363  -6428   3322       C  
ATOM   4079  C   PRO B 248       5.972 -37.136 -39.668  1.00158.03           C  
ANISOU 4079  C   PRO B 248    20523  20364  19156  -9500  -6607   3678       C  
ATOM   4080  O   PRO B 248       5.285 -36.601 -40.553  1.00163.11           O  
ANISOU 4080  O   PRO B 248    21123  21129  19721  -9884  -6974   3937       O  
ATOM   4081  CB  PRO B 248       7.522 -39.283 -39.602  1.00156.58           C  
ANISOU 4081  CB  PRO B 248    21484  19586  18421  -9595  -6356   3145       C  
ATOM   4082  CG  PRO B 248       8.203 -39.161 -38.266  1.00148.73           C  
ANISOU 4082  CG  PRO B 248    20290  18550  17673  -9149  -5944   2950       C  
ATOM   4083  CD  PRO B 248       9.085 -37.957 -38.406  1.00142.38           C  
ANISOU 4083  CD  PRO B 248    19346  17806  16944  -8672  -5755   2844       C  
ATOM   4084  N   GLY B 249       5.591 -37.195 -38.391  1.00152.64           N  
ANISOU 4084  N   GLY B 249    19342  19808  18848  -9211  -6352   3706       N  
ATOM   4085  CA  GLY B 249       4.348 -36.638 -37.864  1.00154.19           C  
ANISOU 4085  CA  GLY B 249    18881  20294  19410  -9285  -6444   4041       C  
ATOM   4086  C   GLY B 249       4.182 -35.170 -37.494  1.00152.00           C  
ANISOU 4086  C   GLY B 249    18013  20267  19473  -8850  -6288   4182       C  
ATOM   4087  O   GLY B 249       3.986 -34.850 -36.310  1.00150.36           O  
ANISOU 4087  O   GLY B 249    17395  20150  19584  -8580  -6027   4215       O  
ATOM   4088  N   THR B 250       4.231 -34.273 -38.480  1.00151.47           N  
ANISOU 4088  N   THR B 250    17917  20304  19331  -8797  -6447   4291       N  
ATOM   4089  CA  THR B 250       4.183 -32.833 -38.243  1.00143.52           C  
ANISOU 4089  CA  THR B 250    16429  19504  18597  -8385  -6301   4423       C  
ATOM   4090  C   THR B 250       2.780 -32.255 -38.422  1.00144.99           C  
ANISOU 4090  C   THR B 250    16060  19998  19033  -8558  -6546   4882       C  
ATOM   4091  O   THR B 250       2.134 -32.471 -39.455  1.00143.69           O  
ANISOU 4091  O   THR B 250    15971  19905  18721  -8961  -6927   5097       O  
ATOM   4092  CB  THR B 250       5.147 -32.101 -39.179  1.00139.63           C  
ANISOU 4092  CB  THR B 250    16223  18934  17897  -8179  -6286   4261       C  
ATOM   4093  OG1 THR B 250       6.277 -32.939 -39.449  1.00135.93           O  
ANISOU 4093  OG1 THR B 250    16381  18165  17101  -8205  -6196   3898       O  
ATOM   4094  CG2 THR B 250       5.633 -30.799 -38.537  1.00135.65           C  
ANISOU 4094  CG2 THR B 250    15372  18524  17644  -7631  -5964   4216       C  
ATOM   4095  N   THR B 251       2.316 -31.536 -37.401  1.00139.69           N  
ANISOU 4095  N   THR B 251    14840  19500  18734  -8254  -6322   5040       N  
ATOM   4096  CA  THR B 251       1.034 -30.847 -37.418  1.00141.80           C  
ANISOU 4096  CA  THR B 251    14518  20067  19292  -8320  -6479   5493       C  
ATOM   4097  C   THR B 251       1.108 -29.607 -38.309  1.00143.18           C  
ANISOU 4097  C   THR B 251    14577  20367  19459  -8147  -6570   5630       C  
ATOM   4098  O   THR B 251       2.185 -29.063 -38.577  1.00140.64           O  
ANISOU 4098  O   THR B 251    14519  19918  18998  -7851  -6404   5363       O  
ATOM   4099  CB  THR B 251       0.619 -30.446 -35.998  1.00139.42           C  
ANISOU 4099  CB  THR B 251    13716  19876  19379  -8001  -6150   5597       C  
ATOM   4100  OG1 THR B 251       0.442 -31.624 -35.203  1.00140.66           O  
ANISOU 4100  OG1 THR B 251    13958  19927  19558  -8203  -6083   5500       O  
ATOM   4101  CG2 THR B 251      -0.679 -29.641 -36.000  1.00144.47           C  
ANISOU 4101  CG2 THR B 251    13728  20826  20339  -8014  -6270   6090       C  
ATOM   4102  N   SER B 252      -0.063 -29.142 -38.758  1.00148.84           N  
ANISOU 4102  N   SER B 252    14871  21338  20342  -8334  -6832   6067       N  
ATOM   4103  CA  SER B 252      -0.098 -27.908 -39.536  1.00147.85           C  
ANISOU 4103  CA  SER B 252    14579  21347  20250  -8160  -6904   6236       C  
ATOM   4104  C   SER B 252       0.443 -26.727 -38.741  1.00146.81           C  
ANISOU 4104  C   SER B 252    14209  21231  20340  -7570  -6485   6140       C  
ATOM   4105  O   SER B 252       1.043 -25.815 -39.320  1.00143.52           O  
ANISOU 4105  O   SER B 252    13886  20798  19849  -7338  -6433   6060       O  
ATOM   4106  CB  SER B 252      -1.526 -27.615 -39.999  1.00154.36           C  
ANISOU 4106  CB  SER B 252    14925  22461  21264  -8442  -7233   6762       C  
ATOM   4107  OG  SER B 252      -1.560 -26.474 -40.840  1.00154.68           O  
ANISOU 4107  OG  SER B 252    14834  22621  21315  -8307  -7324   6928       O  
ATOM   4108  N   ALA B 285       0.237 -26.715 -37.423  1.00149.42           N  
ANISOU 4108  N   ALA B 285    14246  21588  20939  -7331  -6184   6150       N  
ATOM   4109  CA  ALA B 285       0.850 -25.682 -36.598  1.00143.32           C  
ANISOU 4109  CA  ALA B 285    13329  20788  20336  -6785  -5773   6016       C  
ATOM   4110  C   ALA B 285       2.332 -25.950 -36.376  1.00137.03           C  
ANISOU 4110  C   ALA B 285    13033  19724  19309  -6575  -5540   5515       C  
ATOM   4111  O   ALA B 285       3.115 -25.006 -36.210  1.00119.80           O  
ANISOU 4111  O   ALA B 285    10882  17492  17146  -6179  -5294   5356       O  
ATOM   4112  CB  ALA B 285       0.116 -25.564 -35.261  1.00132.93           C  
ANISOU 4112  CB  ALA B 285    11551  19581  19375  -6604  -5521   6207       C  
ATOM   4113  N   GLU B 286       2.738 -27.221 -36.366  1.00139.03           N  
ANISOU 4113  N   GLU B 286    13678  19800  19346  -6835  -5610   5273       N  
ATOM   4114  CA  GLU B 286       4.156 -27.523 -36.222  1.00118.72           C  
ANISOU 4114  CA  GLU B 286    11583  16975  16551  -6648  -5402   4821       C  
ATOM   4115  C   GLU B 286       4.938 -27.053 -37.437  1.00118.04           C  
ANISOU 4115  C   GLU B 286    11826  16814  16208  -6622  -5519   4688       C  
ATOM   4116  O   GLU B 286       6.117 -26.702 -37.321  1.00116.74           O  
ANISOU 4116  O   GLU B 286    11905  16504  15947  -6317  -5287   4384       O  
ATOM   4117  CB  GLU B 286       4.350 -29.028 -36.032  1.00119.84           C  
ANISOU 4117  CB  GLU B 286    12087  16936  16509  -6958  -5464   4624       C  
ATOM   4118  CG  GLU B 286       3.433 -29.634 -34.985  1.00136.17           C  
ANISOU 4118  CG  GLU B 286    13839  19081  18818  -7081  -5407   4788       C  
ATOM   4119  CD  GLU B 286       3.761 -29.204 -33.575  1.00130.93           C  
ANISOU 4119  CD  GLU B 286    12955  18398  18396  -6659  -4990   4675       C  
ATOM   4120  OE1 GLU B 286       4.952 -28.972 -33.285  1.00127.37           O  
ANISOU 4120  OE1 GLU B 286    12765  17786  17845  -6352  -4747   4351       O  
ATOM   4121  OE2 GLU B 286       2.825 -29.115 -32.751  1.00133.20           O  
ANISOU 4121  OE2 GLU B 286    12811  18826  18971  -6643  -4906   4920       O  
ATOM   4122  N   VAL B 287       4.304 -27.054 -38.608  1.00124.15           N  
ANISOU 4122  N   VAL B 287    12615  17687  16870  -6953  -5879   4918       N  
ATOM   4123  CA  VAL B 287       4.973 -26.592 -39.817  1.00121.14           C  
ANISOU 4123  CA  VAL B 287    12541  17238  16247  -6951  -5999   4814       C  
ATOM   4124  C   VAL B 287       4.988 -25.074 -39.877  1.00131.89           C  
ANISOU 4124  C   VAL B 287    13571  18741  17799  -6586  -5863   4942       C  
ATOM   4125  O   VAL B 287       5.985 -24.465 -40.282  1.00129.54           O  
ANISOU 4125  O   VAL B 287    13497  18341  17380  -6348  -5736   4722       O  
ATOM   4126  CB  VAL B 287       4.309 -27.199 -41.062  1.00127.85           C  
ANISOU 4126  CB  VAL B 287    13577  18123  16879  -7467  -6445   5003       C  
ATOM   4127  CG1 VAL B 287       5.002 -26.696 -42.319  1.00126.84           C  
ANISOU 4127  CG1 VAL B 287    13779  17916  16500  -7462  -6556   4895       C  
ATOM   4128  CG2 VAL B 287       4.366 -28.709 -40.986  1.00129.99           C  
ANISOU 4128  CG2 VAL B 287    14234  18221  16936  -7826  -6556   4851       C  
ATOM   4129  N   LYS B 288       3.886 -24.439 -39.481  1.00134.41           N  
ANISOU 4129  N   LYS B 288    13356  19292  18421  -6536  -5880   5307       N  
ATOM   4130  CA  LYS B 288       3.842 -22.982 -39.458  1.00132.72           C  
ANISOU 4130  CA  LYS B 288    12822  19203  18402  -6176  -5723   5448       C  
ATOM   4131  C   LYS B 288       4.890 -22.410 -38.513  1.00126.14           C  
ANISOU 4131  C   LYS B 288    12049  18241  17637  -5700  -5299   5146       C  
ATOM   4132  O   LYS B 288       5.362 -21.285 -38.714  1.00109.97           O  
ANISOU 4132  O   LYS B 288     9957  16204  15625  -5402  -5156   5109       O  
ATOM   4133  CB  LYS B 288       2.444 -22.537 -39.034  1.00125.29           C  
ANISOU 4133  CB  LYS B 288    11296  18517  17791  -6197  -5776   5906       C  
ATOM   4134  CG  LYS B 288       1.449 -22.425 -40.171  1.00138.27           C  
ANISOU 4134  CG  LYS B 288    12769  20349  19419  -6548  -6181   6283       C  
ATOM   4135  CD  LYS B 288       0.050 -22.744 -39.669  1.00144.60           C  
ANISOU 4135  CD  LYS B 288    13094  21360  20485  -6747  -6305   6697       C  
ATOM   4136  CE  LYS B 288      -0.908 -23.039 -40.813  1.00147.76           C  
ANISOU 4136  CE  LYS B 288    13407  21924  20812  -7222  -6781   7045       C  
ATOM   4137  NZ  LYS B 288      -2.237 -23.537 -40.348  1.00152.76           N  
ANISOU 4137  NZ  LYS B 288    13602  22754  21686  -7477  -6933   7441       N  
ATOM   4138  N   GLN B 289       5.255 -23.166 -37.475  1.00123.86           N  
ANISOU 4138  N   GLN B 289    11862  17831  17366  -5637  -5100   4934       N  
ATOM   4139  CA  GLN B 289       6.306 -22.746 -36.556  1.00115.89           C  
ANISOU 4139  CA  GLN B 289    10950  16689  16396  -5225  -4721   4634       C  
ATOM   4140  C   GLN B 289       7.699 -22.957 -37.137  1.00109.79           C  
ANISOU 4140  C   GLN B 289    10675  15707  15331  -5172  -4685   4254       C  
ATOM   4141  O   GLN B 289       8.556 -22.071 -37.032  1.00110.75           O  
ANISOU 4141  O   GLN B 289    10848  15774  15458  -4838  -4469   4090       O  
ATOM   4142  CB  GLN B 289       6.149 -23.489 -35.229  1.00114.32           C  
ANISOU 4142  CB  GLN B 289    10664  16442  16328  -5191  -4531   4566       C  
ATOM   4143  CG  GLN B 289       7.334 -23.384 -34.290  1.00 96.28           C  
ANISOU 4143  CG  GLN B 289     8570  13986  14025  -4847  -4182   4214       C  
ATOM   4144  CD  GLN B 289       7.080 -24.099 -32.976  1.00 96.00           C  
ANISOU 4144  CD  GLN B 289     8428  13915  14132  -4831  -4002   4176       C  
ATOM   4145  OE1 GLN B 289       7.070 -25.329 -32.912  1.00 97.42           O  
ANISOU 4145  OE1 GLN B 289     8809  14005  14200  -5101  -4100   4075       O  
ATOM   4146  NE2 GLN B 289       6.852 -23.326 -31.921  1.00 94.42           N  
ANISOU 4146  NE2 GLN B 289     7924  13776  14176  -4521  -3729   4263       N  
ATOM   4147  N   MET B 290       7.946 -24.114 -37.753  1.00103.88           N  
ANISOU 4147  N   MET B 290    10305  14836  14328  -5499  -4885   4118       N  
ATOM   4148  CA  MET B 290       9.274 -24.371 -38.299  1.00102.49           C  
ANISOU 4148  CA  MET B 290    10610  14452  13878  -5442  -4831   3771       C  
ATOM   4149  C   MET B 290       9.574 -23.438 -39.466  1.00107.90           C  
ANISOU 4149  C   MET B 290    11365  15170  14461  -5389  -4935   3805       C  
ATOM   4150  O   MET B 290      10.693 -22.925 -39.580  1.00111.99           O  
ANISOU 4150  O   MET B 290    12072  15579  14899  -5126  -4752   3565       O  
ATOM   4151  CB  MET B 290       9.414 -25.838 -38.713  1.00108.19           C  
ANISOU 4151  CB  MET B 290    11751  15018  14339  -5811  -5012   3638       C  
ATOM   4152  CG  MET B 290      10.837 -26.219 -39.127  1.00112.46           C  
ANISOU 4152  CG  MET B 290    12801  15320  14608  -5724  -4904   3275       C  
ATOM   4153  SD  MET B 290      10.971 -27.796 -39.995  1.00125.19           S  
ANISOU 4153  SD  MET B 290    14986  16729  15851  -6185  -5153   3156       S  
ATOM   4154  CE  MET B 290      11.940 -28.744 -38.820  1.00126.66           C  
ANISOU 4154  CE  MET B 290    15410  16701  16014  -6015  -4842   2825       C  
ATOM   4155  N   ARG B 291       8.596 -23.207 -40.349  1.00112.80           N  
ANISOU 4155  N   ARG B 291    11830  15943  15086  -5644  -5232   4108       N  
ATOM   4156  CA  ARG B 291       8.832 -22.297 -41.469  1.00113.04           C  
ANISOU 4156  CA  ARG B 291    11915  16009  15027  -5603  -5335   4153       C  
ATOM   4157  C   ARG B 291       9.108 -20.876 -40.994  1.00 98.44           C  
ANISOU 4157  C   ARG B 291     9771  14237  13394  -5167  -5066   4170       C  
ATOM   4158  O   ARG B 291       9.833 -20.131 -41.663  1.00 96.05           O  
ANISOU 4158  O   ARG B 291     9609  13889  12998  -5015  -5021   4055       O  
ATOM   4159  CB  ARG B 291       7.639 -22.308 -42.430  1.00126.78           C  
ANISOU 4159  CB  ARG B 291    13504  17916  16752  -5970  -5718   4509       C  
ATOM   4160  CG  ARG B 291       7.378 -23.636 -43.143  1.00135.43           C  
ANISOU 4160  CG  ARG B 291    14956  18921  17579  -6453  -6035   4503       C  
ATOM   4161  CD  ARG B 291       8.226 -23.763 -44.404  1.00133.84           C  
ANISOU 4161  CD  ARG B 291    15260  18554  17040  -6572  -6159   4303       C  
ATOM   4162  NE  ARG B 291       8.090 -25.070 -45.041  1.00136.92           N  
ANISOU 4162  NE  ARG B 291    16076  18811  17137  -7022  -6427   4262       N  
ATOM   4163  CZ  ARG B 291       7.190 -25.342 -45.982  1.00140.07           C  
ANISOU 4163  CZ  ARG B 291    16505  19295  17420  -7443  -6815   4519       C  
ATOM   4164  NH1 ARG B 291       6.351 -24.401 -46.391  1.00138.82           N  
ANISOU 4164  NH1 ARG B 291    15947  19368  17431  -7458  -6979   4845       N  
ATOM   4165  NH2 ARG B 291       7.129 -26.555 -46.518  1.00127.74           N  
ANISOU 4165  NH2 ARG B 291    15385  17583  15567  -7857  -7041   4460       N  
ATOM   4166  N   ALA B 292       8.559 -20.493 -39.838  1.00 97.93           N  
ANISOU 4166  N   ALA B 292     9322  14276  13610  -4966  -4875   4308       N  
ATOM   4167  CA  ALA B 292       8.786 -19.181 -39.247  1.00 94.51           C  
ANISOU 4167  CA  ALA B 292     8635  13895  13380  -4554  -4593   4326       C  
ATOM   4168  C   ALA B 292      10.076 -19.105 -38.447  1.00104.39           C  
ANISOU 4168  C   ALA B 292    10100  14971  14592  -4241  -4269   3962       C  
ATOM   4169  O   ALA B 292      10.817 -18.121 -38.564  1.00 99.70           O  
ANISOU 4169  O   ALA B 292     9542  14340  13998  -3969  -4105   3845       O  
ATOM   4170  CB  ALA B 292       7.614 -18.810 -38.330  1.00 97.19           C  
ANISOU 4170  CB  ALA B 292     8490  14406  14030  -4474  -4515   4647       C  
ATOM   4171  N   ARG B 293      10.360 -20.127 -37.640  1.00103.55           N  
ANISOU 4171  N   ARG B 293    10133  14757  14453  -4285  -4181   3788       N  
ATOM   4172  CA  ARG B 293      11.605 -20.121 -36.892  1.00 88.22           C  
ANISOU 4172  CA  ARG B 293     8396  12654  12468  -4009  -3895   3455       C  
ATOM   4173  C   ARG B 293      12.808 -20.179 -37.815  1.00 84.40           C  
ANISOU 4173  C   ARG B 293     8307  12027  11733  -4002  -3922   3192       C  
ATOM   4174  O   ARG B 293      13.885 -19.711 -37.436  1.00 85.25           O  
ANISOU 4174  O   ARG B 293     8525  12038  11828  -3722  -3692   2964       O  
ATOM   4175  CB  ARG B 293      11.643 -21.253 -35.853  1.00 80.22           C  
ANISOU 4175  CB  ARG B 293     7451  11557  11472  -4072  -3803   3333       C  
ATOM   4176  CG  ARG B 293      10.828 -20.906 -34.607  1.00 80.83           C  
ANISOU 4176  CG  ARG B 293     7140  11741  11830  -3923  -3634   3515       C  
ATOM   4177  CD  ARG B 293      11.216 -21.737 -33.385  1.00 78.45           C  
ANISOU 4177  CD  ARG B 293     6924  11327  11555  -3864  -3442   3322       C  
ATOM   4178  NE  ARG B 293      10.850 -23.145 -33.466  1.00 81.35           N  
ANISOU 4178  NE  ARG B 293     7434  11649  11826  -4203  -3612   3311       N  
ATOM   4179  CZ  ARG B 293      10.719 -23.938 -32.406  1.00 83.83           C  
ANISOU 4179  CZ  ARG B 293     7724  11911  12216  -4229  -3490   3249       C  
ATOM   4180  NH1 ARG B 293      10.388 -25.210 -32.573  1.00 84.05           N  
ANISOU 4180  NH1 ARG B 293     7906  11885  12142  -4559  -3655   3239       N  
ATOM   4181  NH2 ARG B 293      10.906 -23.461 -31.179  1.00 84.67           N  
ANISOU 4181  NH2 ARG B 293     7667  12010  12492  -3938  -3204   3201       N  
ATOM   4182  N   ARG B 294      12.648 -20.743 -39.011  1.00 81.45           N  
ANISOU 4182  N   ARG B 294     8155  11634  11158  -4311  -4200   3228       N  
ATOM   4183  CA  ARG B 294      13.734 -20.739 -39.983  1.00 79.46           C  
ANISOU 4183  CA  ARG B 294     8278  11246  10665  -4305  -4225   3005       C  
ATOM   4184  C   ARG B 294      14.060 -19.323 -40.433  1.00 77.59           C  
ANISOU 4184  C   ARG B 294     7916  11073  10492  -4062  -4144   3035       C  
ATOM   4185  O   ARG B 294      15.230 -18.987 -40.660  1.00 73.80           O  
ANISOU 4185  O   ARG B 294     7648  10480   9911  -3876  -4003   2800       O  
ATOM   4186  CB  ARG B 294      13.346 -21.592 -41.189  1.00 84.05           C  
ANISOU 4186  CB  ARG B 294     9130  11794  11011  -4711  -4553   3072       C  
ATOM   4187  CG  ARG B 294      13.412 -23.098 -40.989  1.00 86.67           C  
ANISOU 4187  CG  ARG B 294     9759  11988  11184  -4964  -4622   2950       C  
ATOM   4188  CD  ARG B 294      12.711 -23.804 -42.149  1.00103.67           C  
ANISOU 4188  CD  ARG B 294    12122  14140  13128  -5407  -4983   3098       C  
ATOM   4189  NE  ARG B 294      12.778 -25.258 -42.038  1.00117.75           N  
ANISOU 4189  NE  ARG B 294    14242  15767  14728  -5673  -5054   2979       N  
ATOM   4190  CZ  ARG B 294      12.599 -26.100 -43.051  1.00129.41           C  
ANISOU 4190  CZ  ARG B 294    16096  17146  15930  -6050  -5316   2993       C  
ATOM   4191  NH1 ARG B 294      12.347 -25.636 -44.267  1.00136.25           N  
ANISOU 4191  NH1 ARG B 294    17043  18056  16668  -6210  -5546   3119       N  
ATOM   4192  NH2 ARG B 294      12.671 -27.408 -42.845  1.00131.74           N  
ANISOU 4192  NH2 ARG B 294    16708  17284  16064  -6274  -5349   2880       N  
ATOM   4193  N   LYS B 295      13.039 -18.478 -40.596  1.00 80.48           N  
ANISOU 4193  N   LYS B 295     7933  11619  11025  -4065  -4232   3333       N  
ATOM   4194  CA  LYS B 295      13.330 -17.108 -41.014  1.00 78.87           C  
ANISOU 4194  CA  LYS B 295     7615  11469  10882  -3832  -4146   3366       C  
ATOM   4195  C   LYS B 295      13.970 -16.293 -39.903  1.00 74.76           C  
ANISOU 4195  C   LYS B 295     6968  10915  10522  -3444  -3802   3235       C  
ATOM   4196  O   LYS B 295      14.706 -15.343 -40.188  1.00 76.16           O  
ANISOU 4196  O   LYS B 295     7189  11062  10685  -3231  -3679   3132       O  
ATOM   4197  CB  LYS B 295      12.079 -16.405 -41.558  1.00 86.88           C  
ANISOU 4197  CB  LYS B 295     8300  12683  12026  -3939  -4336   3735       C  
ATOM   4198  CG  LYS B 295      11.704 -16.800 -42.991  1.00 93.82           C  
ANISOU 4198  CG  LYS B 295     9349  13592  12706  -4289  -4690   3845       C  
ATOM   4199  CD  LYS B 295      10.375 -16.139 -43.387  1.00103.82           C  
ANISOU 4199  CD  LYS B 295    10231  15080  14135  -4396  -4883   4250       C  
ATOM   4200  CE  LYS B 295       9.839 -16.666 -44.707  1.00110.96           C  
ANISOU 4200  CE  LYS B 295    11287  16027  14845  -4799  -5276   4396       C  
ATOM   4201  NZ  LYS B 295       8.493 -16.096 -45.014  1.00113.39           N  
ANISOU 4201  NZ  LYS B 295    11180  16570  15331  -4917  -5477   4822       N  
ATOM   4202  N   THR B 296      13.705 -16.634 -38.645  1.00 74.42           N  
ANISOU 4202  N   THR B 296     6781  10872  10624  -3358  -3648   3239       N  
ATOM   4203  CA  THR B 296      14.377 -15.927 -37.564  1.00 79.53           C  
ANISOU 4203  CA  THR B 296     7362  11465  11391  -3012  -3331   3097       C  
ATOM   4204  C   THR B 296      15.814 -16.396 -37.412  1.00 64.43           C  
ANISOU 4204  C   THR B 296     5787   9376   9317  -2918  -3202   2744       C  
ATOM   4205  O   THR B 296      16.715 -15.580 -37.179  1.00 60.79           O  
ANISOU 4205  O   THR B 296     5369   8859   8869  -2663  -3008   2594       O  
ATOM   4206  CB  THR B 296      13.612 -16.098 -36.258  1.00 82.71           C  
ANISOU 4206  CB  THR B 296     7506  11922  11998  -2948  -3204   3226       C  
ATOM   4207  OG1 THR B 296      12.204 -16.017 -36.520  1.00 90.33           O  
ANISOU 4207  OG1 THR B 296     8172  13055  13094  -3113  -3376   3578       O  
ATOM   4208  CG2 THR B 296      14.014 -15.009 -35.274  1.00 66.18           C  
ANISOU 4208  CG2 THR B 296     5289   9806  10051  -2595  -2901   3172       C  
ATOM   4209  N   ALA B 297      16.042 -17.703 -37.543  1.00 64.99           N  
ANISOU 4209  N   ALA B 297     6098   9357   9238  -3126  -3306   2620       N  
ATOM   4210  CA  ALA B 297      17.402 -18.220 -37.498  1.00 61.34           C  
ANISOU 4210  CA  ALA B 297     5959   8729   8619  -3048  -3194   2308       C  
ATOM   4211  C   ALA B 297      18.227 -17.678 -38.656  1.00 60.22           C  
ANISOU 4211  C   ALA B 297     6013   8541   8328  -3010  -3235   2204       C  
ATOM   4212  O   ALA B 297      19.426 -17.421 -38.506  1.00 56.48           O  
ANISOU 4212  O   ALA B 297     5682   7971   7806  -2813  -3066   1985       O  
ATOM   4213  CB  ALA B 297      17.379 -19.751 -37.518  1.00 62.87           C  
ANISOU 4213  CB  ALA B 297     6387   8829   8670  -3302  -3310   2224       C  
ATOM   4214  N   LYS B 298      17.599 -17.498 -39.821  1.00 65.88           N  
ANISOU 4214  N   LYS B 298     6732   9329   8972  -3204  -3466   2367       N  
ATOM   4215  CA  LYS B 298      18.297 -16.906 -40.958  1.00 68.60           C  
ANISOU 4215  CA  LYS B 298     7248   9638   9179  -3172  -3511   2288       C  
ATOM   4216  C   LYS B 298      18.739 -15.482 -40.647  1.00 68.94           C  
ANISOU 4216  C   LYS B 298     7106   9726   9363  -2856  -3308   2273       C  
ATOM   4217  O   LYS B 298      19.876 -15.092 -40.938  1.00 69.12           O  
ANISOU 4217  O   LYS B 298     7291   9666   9304  -2705  -3195   2081       O  
ATOM   4218  CB  LYS B 298      17.388 -16.933 -42.188  1.00 80.90           C  
ANISOU 4218  CB  LYS B 298     8814  11280  10645  -3452  -3812   2499       C  
ATOM   4219  CG  LYS B 298      18.038 -16.481 -43.484  1.00 90.90           C  
ANISOU 4219  CG  LYS B 298    10305  12500  11733  -3469  -3895   2420       C  
ATOM   4220  CD  LYS B 298      16.989 -16.392 -44.586  1.00102.88           C  
ANISOU 4220  CD  LYS B 298    11779  14124  13186  -3745  -4204   2670       C  
ATOM   4221  CE  LYS B 298      17.595 -16.006 -45.926  1.00106.76           C  
ANISOU 4221  CE  LYS B 298    12528  14562  13475  -3786  -4307   2591       C  
ATOM   4222  NZ  LYS B 298      16.563 -15.880 -46.998  1.00112.15           N  
ANISOU 4222  NZ  LYS B 298    13169  15354  14089  -4061  -4624   2845       N  
ATOM   4223  N   MET B 299      17.846 -14.687 -40.054  1.00 64.76           N  
ANISOU 4223  N   MET B 299     6241   9323   9043  -2758  -3255   2484       N  
ATOM   4224  CA  MET B 299      18.188 -13.312 -39.710  1.00 62.86           C  
ANISOU 4224  CA  MET B 299     5842   9110   8930  -2470  -3056   2482       C  
ATOM   4225  C   MET B 299      19.271 -13.259 -38.639  1.00 69.43           C  
ANISOU 4225  C   MET B 299     6756   9832   9792  -2235  -2792   2243       C  
ATOM   4226  O   MET B 299      20.239 -12.500 -38.758  1.00 77.13           O  
ANISOU 4226  O   MET B 299     7808  10755  10741  -2053  -2661   2101       O  
ATOM   4227  CB  MET B 299      16.940 -12.568 -39.240  1.00 61.09           C  
ANISOU 4227  CB  MET B 299     5258   9031   8922  -2420  -3044   2775       C  
ATOM   4228  CG  MET B 299      17.144 -11.081 -39.051  1.00 61.51           C  
ANISOU 4228  CG  MET B 299     5164   9113   9094  -2152  -2862   2811       C  
ATOM   4229  SD  MET B 299      15.852 -10.333 -38.044  1.00 69.79           S  
ANISOU 4229  SD  MET B 299     5816  10285  10415  -2025  -2744   3115       S  
ATOM   4230  CE  MET B 299      16.397 -10.789 -36.401  1.00 65.52           C  
ANISOU 4230  CE  MET B 299     5331   9630   9934  -1867  -2490   2918       C  
ATOM   4231  N   LEU B 300      19.125 -14.063 -37.583  1.00 66.37           N  
ANISOU 4231  N   LEU B 300     6350   9410   9456  -2246  -2720   2202       N  
ATOM   4232  CA  LEU B 300      20.078 -13.999 -36.480  1.00 49.65           C  
ANISOU 4232  CA  LEU B 300     4291   7200   7374  -2032  -2481   1999       C  
ATOM   4233  C   LEU B 300      21.464 -14.475 -36.893  1.00 47.01           C  
ANISOU 4233  C   LEU B 300     4249   6743   6871  -2011  -2451   1737       C  
ATOM   4234  O   LEU B 300      22.468 -13.971 -36.376  1.00 43.78           O  
ANISOU 4234  O   LEU B 300     3883   6274   6478  -1807  -2270   1582       O  
ATOM   4235  CB  LEU B 300      19.561 -14.815 -35.295  1.00 50.05           C  
ANISOU 4235  CB  LEU B 300     4259   7245   7511  -2065  -2427   2024       C  
ATOM   4236  CG  LEU B 300      18.307 -14.256 -34.625  1.00 58.75           C  
ANISOU 4236  CG  LEU B 300     5048   8461   8813  -2026  -2391   2276       C  
ATOM   4237  CD1 LEU B 300      17.657 -15.310 -33.743  1.00 67.03           C  
ANISOU 4237  CD1 LEU B 300     6031   9516   9922  -2138  -2401   2325       C  
ATOM   4238  CD2 LEU B 300      18.647 -13.011 -33.817  1.00 55.48           C  
ANISOU 4238  CD2 LEU B 300     4528   8033   8516  -1744  -2155   2255       C  
ATOM   4239  N   MET B 301      21.546 -15.443 -37.809  1.00 48.58           N  
ANISOU 4239  N   MET B 301     4656   6899   6904  -2225  -2626   1694       N  
ATOM   4240  CA  MET B 301      22.856 -15.898 -38.263  1.00 46.41           C  
ANISOU 4240  CA  MET B 301     4661   6503   6468  -2199  -2588   1462       C  
ATOM   4241  C   MET B 301      23.565 -14.819 -39.069  1.00 48.02           C  
ANISOU 4241  C   MET B 301     4896   6715   6636  -2072  -2552   1416       C  
ATOM   4242  O   MET B 301      24.791 -14.672 -38.982  1.00 50.08           O  
ANISOU 4242  O   MET B 301     5272   6901   6854  -1925  -2419   1233       O  
ATOM   4243  CB  MET B 301      22.715 -17.182 -39.080  1.00 53.32           C  
ANISOU 4243  CB  MET B 301     5791   7311   7156  -2471  -2780   1434       C  
ATOM   4244  CG  MET B 301      22.407 -18.411 -38.233  1.00 55.18           C  
ANISOU 4244  CG  MET B 301     6072   7496   7397  -2581  -2778   1407       C  
ATOM   4245  SD  MET B 301      21.837 -19.825 -39.196  1.00 65.59           S  
ANISOU 4245  SD  MET B 301     7675   8745   8502  -2958  -3038   1443       S  
ATOM   4246  CE  MET B 301      21.021 -20.805 -37.935  1.00 67.30           C  
ANISOU 4246  CE  MET B 301     7770   8972   8827  -3058  -3023   1506       C  
ATOM   4247  N   VAL B 302      22.812 -14.058 -39.864  1.00 60.73           N  
ANISOU 4247  N   VAL B 302     6393   8419   8265  -2131  -2675   1590       N  
ATOM   4248  CA  VAL B 302      23.413 -12.951 -40.594  1.00 58.15           C  
ANISOU 4248  CA  VAL B 302     6075   8105   7914  -2005  -2637   1560       C  
ATOM   4249  C   VAL B 302      23.878 -11.865 -39.640  1.00 56.57           C  
ANISOU 4249  C   VAL B 302     5714   7912   7866  -1737  -2405   1520       C  
ATOM   4250  O   VAL B 302      24.875 -11.180 -39.902  1.00 55.74           O  
ANISOU 4250  O   VAL B 302     5674   7773   7732  -1596  -2305   1403       O  
ATOM   4251  CB  VAL B 302      22.419 -12.404 -41.632  1.00 54.89           C  
ANISOU 4251  CB  VAL B 302     5568   7798   7491  -2137  -2832   1775       C  
ATOM   4252  CG1 VAL B 302      23.039 -11.237 -42.379  1.00 55.66           C  
ANISOU 4252  CG1 VAL B 302     5676   7909   7562  -2000  -2790   1744       C  
ATOM   4253  CG2 VAL B 302      22.015 -13.511 -42.583  1.00 56.42           C  
ANISOU 4253  CG2 VAL B 302     5968   7966   7503  -2432  -3078   1806       C  
ATOM   4254  N   VAL B 303      23.168 -11.681 -38.528  1.00 55.04           N  
ANISOU 4254  N   VAL B 303     5322   7760   7829  -1673  -2318   1622       N  
ATOM   4255  CA  VAL B 303      23.581 -10.685 -37.548  1.00 45.45           C  
ANISOU 4255  CA  VAL B 303     3998   6532   6739  -1438  -2100   1580       C  
ATOM   4256  C   VAL B 303      24.896 -11.090 -36.900  1.00 51.14           C  
ANISOU 4256  C   VAL B 303     4874   7148   7410  -1333  -1957   1344       C  
ATOM   4257  O   VAL B 303      25.828 -10.286 -36.789  1.00 46.29           O  
ANISOU 4257  O   VAL B 303     4288   6498   6800  -1178  -1830   1242       O  
ATOM   4258  CB  VAL B 303      22.479 -10.481 -36.497  1.00 42.27           C  
ANISOU 4258  CB  VAL B 303     3372   6187   6501  -1404  -2041   1748       C  
ATOM   4259  CG1 VAL B 303      23.017  -9.659 -35.340  1.00 39.69           C  
ANISOU 4259  CG1 VAL B 303     3001   5812   6268  -1182  -1812   1668       C  
ATOM   4260  CG2 VAL B 303      21.282  -9.809 -37.132  1.00 45.46           C  
ANISOU 4260  CG2 VAL B 303     3582   6710   6983  -1463  -2153   2006       C  
ATOM   4261  N   VAL B 304      24.988 -12.343 -36.454  1.00 59.22           N  
ANISOU 4261  N   VAL B 304     5991   8122   8386  -1422  -1980   1267       N  
ATOM   4262  CA  VAL B 304      26.224 -12.810 -35.842  1.00 47.74           C  
ANISOU 4262  CA  VAL B 304     4669   6579   6889  -1327  -1856   1063       C  
ATOM   4263  C   VAL B 304      27.363 -12.795 -36.847  1.00 46.50           C  
ANISOU 4263  C   VAL B 304     4683   6378   6607  -1315  -1873    930       C  
ATOM   4264  O   VAL B 304      28.519 -12.539 -36.486  1.00 48.37           O  
ANISOU 4264  O   VAL B 304     4966   6570   6842  -1178  -1743    795       O  
ATOM   4265  CB  VAL B 304      26.022 -14.215 -35.248  1.00 42.19           C  
ANISOU 4265  CB  VAL B 304     4038   5835   6158  -1438  -1890   1021       C  
ATOM   4266  CG1 VAL B 304      27.305 -14.695 -34.608  1.00 32.85           C  
ANISOU 4266  CG1 VAL B 304     2976   4568   4938  -1335  -1765    828       C  
ATOM   4267  CG2 VAL B 304      24.881 -14.198 -34.246  1.00 43.08           C  
ANISOU 4267  CG2 VAL B 304     3965   6000   6403  -1448  -1867   1161       C  
ATOM   4268  N   LEU B 305      27.065 -13.080 -38.116  1.00 50.61           N  
ANISOU 4268  N   LEU B 305     5302   6912   7017  -1467  -2040    974       N  
ATOM   4269  CA  LEU B 305      28.111 -13.100 -39.131  1.00 51.31           C  
ANISOU 4269  CA  LEU B 305     5571   6954   6970  -1463  -2060    851       C  
ATOM   4270  C   LEU B 305      28.671 -11.705 -39.381  1.00 56.13           C  
ANISOU 4270  C   LEU B 305     6096   7600   7633  -1300  -1967    848       C  
ATOM   4271  O   LEU B 305      29.891 -11.530 -39.479  1.00 60.68           O  
ANISOU 4271  O   LEU B 305     6747   8137   8173  -1197  -1874    715       O  
ATOM   4272  CB  LEU B 305      27.566 -13.705 -40.424  1.00 59.43           C  
ANISOU 4272  CB  LEU B 305     6763   7973   7844  -1693  -2282    921       C  
ATOM   4273  CG  LEU B 305      28.563 -13.977 -41.552  1.00 68.53           C  
ANISOU 4273  CG  LEU B 305     8195   9031   8811  -1779  -2374    858       C  
ATOM   4274  CD1 LEU B 305      29.650 -14.933 -41.089  1.00 64.29           C  
ANISOU 4274  CD1 LEU B 305     7843   8371   8215  -1766  -2302    708       C  
ATOM   4275  CD2 LEU B 305      27.848 -14.523 -42.779  1.00 79.76           C  
ANISOU 4275  CD2 LEU B 305     9825  10430  10052  -2047  -2618    960       C  
ATOM   4276  N   VAL B 306      27.801 -10.698 -39.487  1.00 53.07           N  
ANISOU 4276  N   VAL B 306     5545   7288   7332  -1279  -1991   1005       N  
ATOM   4277  CA  VAL B 306      28.286  -9.337 -39.694  1.00 53.62           C  
ANISOU 4277  CA  VAL B 306     5542   7380   7450  -1129  -1899   1008       C  
ATOM   4278  C   VAL B 306      29.034  -8.839 -38.465  1.00 50.61           C  
ANISOU 4278  C   VAL B 306     5102   6958   7167   -955  -1696    918       C  
ATOM   4279  O   VAL B 306      30.057  -8.154 -38.579  1.00 53.91           O  
ANISOU 4279  O   VAL B 306     5548   7355   7580   -846  -1602    832       O  
ATOM   4280  CB  VAL B 306      27.124  -8.402 -40.067  1.00 54.09           C  
ANISOU 4280  CB  VAL B 306     5441   7528   7584  -1146  -1970   1211       C  
ATOM   4281  CG1 VAL B 306      26.496  -8.854 -41.365  1.00 45.46           C  
ANISOU 4281  CG1 VAL B 306     4425   6478   6371  -1334  -2194   1302       C  
ATOM   4282  CG2 VAL B 306      26.102  -8.373 -38.948  1.00 65.33           C  
ANISOU 4282  CG2 VAL B 306     6691   8982   9148  -1130  -1922   1333       C  
ATOM   4283  N   PHE B 307      28.542  -9.173 -37.270  1.00 46.66           N  
ANISOU 4283  N   PHE B 307     4528   6449   6753   -939  -1634    942       N  
ATOM   4284  CA  PHE B 307      29.243  -8.777 -36.054  1.00 39.17           C  
ANISOU 4284  CA  PHE B 307     3557   5455   5872   -797  -1463    854       C  
ATOM   4285  C   PHE B 307      30.645  -9.372 -36.015  1.00 40.98           C  
ANISOU 4285  C   PHE B 307     3916   5628   6027   -763  -1410    682       C  
ATOM   4286  O   PHE B 307      31.614  -8.685 -35.674  1.00 38.01           O  
ANISOU 4286  O   PHE B 307     3544   5228   5671   -653  -1298    609       O  
ATOM   4287  CB  PHE B 307      28.440  -9.205 -34.823  1.00 40.48           C  
ANISOU 4287  CB  PHE B 307     3642   5619   6119   -802  -1425    908       C  
ATOM   4288  CG  PHE B 307      29.066  -8.804 -33.516  1.00 47.58           C  
ANISOU 4288  CG  PHE B 307     4536   6470   7073   -675  -1269    827       C  
ATOM   4289  CD1 PHE B 307      30.070  -9.572 -32.947  1.00 55.10           C  
ANISOU 4289  CD1 PHE B 307     5588   7371   7977   -654  -1220    686       C  
ATOM   4290  CD2 PHE B 307      28.643  -7.665 -32.850  1.00 53.70           C  
ANISOU 4290  CD2 PHE B 307     5209   7252   7943   -583  -1178    901       C  
ATOM   4291  CE1 PHE B 307      30.643  -9.209 -31.742  1.00 57.41           C  
ANISOU 4291  CE1 PHE B 307     5882   7625   8308   -557  -1102    624       C  
ATOM   4292  CE2 PHE B 307      29.212  -7.298 -31.640  1.00 53.97           C  
ANISOU 4292  CE2 PHE B 307     5260   7236   8009   -489  -1054    824       C  
ATOM   4293  CZ  PHE B 307      30.214  -8.071 -31.087  1.00 56.13           C  
ANISOU 4293  CZ  PHE B 307     5637   7465   8226   -483  -1025    687       C  
ATOM   4294  N   ALA B 308      30.771 -10.655 -36.365  1.00 31.55           N  
ANISOU 4294  N   ALA B 308     2829   4413   4747   -866  -1492    625       N  
ATOM   4295  CA  ALA B 308      32.086 -11.285 -36.405  1.00 27.28           C  
ANISOU 4295  CA  ALA B 308     2400   3826   4140   -833  -1445    477       C  
ATOM   4296  C   ALA B 308      33.007 -10.567 -37.384  1.00 40.34           C  
ANISOU 4296  C   ALA B 308     4087   5493   5749   -782  -1431    432       C  
ATOM   4297  O   ALA B 308      34.175 -10.300 -37.074  1.00 43.04           O  
ANISOU 4297  O   ALA B 308     4425   5821   6107   -683  -1326    351       O  
ATOM   4298  CB  ALA B 308      31.952 -12.763 -36.775  1.00 30.59           C  
ANISOU 4298  CB  ALA B 308     2954   4208   4462   -972  -1549    430       C  
ATOM   4299  N   LEU B 309      32.502 -10.255 -38.580  1.00 51.27           N  
ANISOU 4299  N   LEU B 309     5502   6903   7076   -862  -1553    508       N  
ATOM   4300  CA  LEU B 309      33.330  -9.579 -39.575  1.00 51.03           C  
ANISOU 4300  CA  LEU B 309     5513   6862   7012   -849  -1588    526       C  
ATOM   4301  C   LEU B 309      33.659  -8.151 -39.158  1.00 53.29           C  
ANISOU 4301  C   LEU B 309     5669   7187   7392   -691  -1437    519       C  
ATOM   4302  O   LEU B 309      34.776  -7.676 -39.387  1.00 56.49           O  
ANISOU 4302  O   LEU B 309     6077   7573   7816   -632  -1386    489       O  
ATOM   4303  CB  LEU B 309      32.627  -9.587 -40.932  1.00 46.50           C  
ANISOU 4303  CB  LEU B 309     5033   6302   6332  -1001  -1787    639       C  
ATOM   4304  CG  LEU B 309      32.525 -10.939 -41.639  1.00 47.85           C  
ANISOU 4304  CG  LEU B 309     5443   6401   6339  -1205  -1969    638       C  
ATOM   4305  CD1 LEU B 309      31.311 -10.981 -42.561  1.00 54.45           C  
ANISOU 4305  CD1 LEU B 309     6335   7273   7079  -1370  -2150    764       C  
ATOM   4306  CD2 LEU B 309      33.799 -11.226 -42.412  1.00 45.46           C  
ANISOU 4306  CD2 LEU B 309     5360   6005   5906  -1252  -2033    584       C  
ATOM   4307  N   CYS B 310      32.701  -7.450 -38.545  1.00 51.58           N  
ANISOU 4307  N   CYS B 310     5345   6998   7256   -655  -1397    596       N  
ATOM   4308  CA  CYS B 310      32.923  -6.047 -38.210  1.00 50.97           C  
ANISOU 4308  CA  CYS B 310     5183   6921   7262   -546  -1292    629       C  
ATOM   4309  C   CYS B 310      33.991  -5.889 -37.136  1.00 48.37           C  
ANISOU 4309  C   CYS B 310     4857   6544   6976   -460  -1152    531       C  
ATOM   4310  O   CYS B 310      34.844  -4.998 -37.226  1.00 52.71           O  
ANISOU 4310  O   CYS B 310     5396   7083   7547   -395  -1078    503       O  
ATOM   4311  CB  CYS B 310      31.617  -5.403 -37.753  1.00 56.79           C  
ANISOU 4311  CB  CYS B 310     5809   7681   8086   -541  -1299    767       C  
ATOM   4312  SG  CYS B 310      30.471  -5.033 -39.094  1.00 69.66           S  
ANISOU 4312  SG  CYS B 310     7390   9389   9689   -619  -1456    930       S  
ATOM   4313  N   TYR B 311      33.961  -6.734 -36.113  1.00 40.53           N  
ANISOU 4313  N   TYR B 311     3880   5523   5996   -467  -1125    489       N  
ATOM   4314  CA  TYR B 311      34.898  -6.621 -35.007  1.00 38.30           C  
ANISOU 4314  CA  TYR B 311     3606   5201   5746   -399  -1016    415       C  
ATOM   4315  C   TYR B 311      36.171  -7.430 -35.209  1.00 39.54           C  
ANISOU 4315  C   TYR B 311     3818   5353   5852   -393  -1000    320       C  
ATOM   4316  O   TYR B 311      37.079  -7.345 -34.375  1.00 32.09           O  
ANISOU 4316  O   TYR B 311     2873   4386   4934   -342   -924    275       O  
ATOM   4317  CB  TYR B 311      34.217  -7.037 -33.703  1.00 23.71           C  
ANISOU 4317  CB  TYR B 311     1739   3330   3940   -400   -994    431       C  
ATOM   4318  CG  TYR B 311      33.158  -6.063 -33.242  1.00 25.57           C  
ANISOU 4318  CG  TYR B 311     1894   3570   4251   -376   -971    527       C  
ATOM   4319  CD1 TYR B 311      31.884  -6.065 -33.795  1.00 34.96           C  
ANISOU 4319  CD1 TYR B 311     3020   4803   5462   -425  -1046    642       C  
ATOM   4320  CD2 TYR B 311      33.447  -5.114 -32.277  1.00 27.61           C  
ANISOU 4320  CD2 TYR B 311     2133   3795   4562   -309   -881    515       C  
ATOM   4321  CE1 TYR B 311      30.921  -5.166 -33.368  1.00 39.83           C  
ANISOU 4321  CE1 TYR B 311     3538   5432   6163   -388  -1013    752       C  
ATOM   4322  CE2 TYR B 311      32.497  -4.219 -31.841  1.00 31.48           C  
ANISOU 4322  CE2 TYR B 311     2546   4288   5127   -276   -848    605       C  
ATOM   4323  CZ  TYR B 311      31.237  -4.244 -32.389  1.00 44.40           C  
ANISOU 4323  CZ  TYR B 311     4103   5971   6797   -305   -904    729       C  
ATOM   4324  OH  TYR B 311      30.295  -3.340 -31.955  1.00 65.17           O  
ANISOU 4324  OH  TYR B 311     6633   8610   9518   -254   -854    842       O  
ATOM   4325  N   LEU B 312      36.261  -8.215 -36.281  1.00 35.37           N  
ANISOU 4325  N   LEU B 312     3340   4849   5251   -449  -1078    297       N  
ATOM   4326  CA  LEU B 312      37.490  -8.964 -36.529  1.00 39.68           C  
ANISOU 4326  CA  LEU B 312     3919   5381   5777   -440  -1072    235       C  
ATOM   4327  C   LEU B 312      38.705  -8.060 -36.681  1.00 47.05           C  
ANISOU 4327  C   LEU B 312     4796   6317   6763   -365   -992    234       C  
ATOM   4328  O   LEU B 312      39.733  -8.330 -36.035  1.00 54.15           O  
ANISOU 4328  O   LEU B 312     5670   7210   7695   -312   -922    199       O  
ATOM   4329  CB  LEU B 312      37.314  -9.858 -37.758  1.00 39.69           C  
ANISOU 4329  CB  LEU B 312     4012   5332   5737   -565  -1259    288       C  
ATOM   4330  CG  LEU B 312      38.537 -10.693 -38.151  1.00 30.03           C  
ANISOU 4330  CG  LEU B 312     2836   4029   4544   -586  -1334    284       C  
ATOM   4331  CD1 LEU B 312      38.736 -11.859 -37.193  1.00 30.85           C  
ANISOU 4331  CD1 LEU B 312     2966   4087   4669   -580  -1323    232       C  
ATOM   4332  CD2 LEU B 312      38.419 -11.182 -39.587  1.00 36.72           C  
ANISOU 4332  CD2 LEU B 312     3872   4805   5273   -748  -1561    334       C  
ATOM   4333  N   PRO B 313      38.676  -7.001 -37.497  1.00 41.91           N  
ANISOU 4333  N   PRO B 313     4116   5677   6132   -360  -1002    285       N  
ATOM   4334  CA  PRO B 313      39.900  -6.195 -37.672  1.00 35.54           C  
ANISOU 4334  CA  PRO B 313     3245   4864   5395   -303   -923    293       C  
ATOM   4335  C   PRO B 313      40.388  -5.542 -36.389  1.00 45.33           C  
ANISOU 4335  C   PRO B 313     4468   6119   6635   -247   -795    234       C  
ATOM   4336  O   PRO B 313      41.581  -5.625 -36.067  1.00 49.36           O  
ANISOU 4336  O   PRO B 313     4943   6635   7177   -214   -736    213       O  
ATOM   4337  CB  PRO B 313      39.484  -5.160 -38.731  1.00 21.38           C  
ANISOU 4337  CB  PRO B 313     1432   3074   3617   -324   -974    377       C  
ATOM   4338  CG  PRO B 313      38.270  -5.740 -39.396  1.00 27.20           C  
ANISOU 4338  CG  PRO B 313     2234   3819   4280   -409  -1124    428       C  
ATOM   4339  CD  PRO B 313      37.567  -6.525 -38.341  1.00 37.48           C  
ANISOU 4339  CD  PRO B 313     3567   5131   5540   -413  -1095    358       C  
ATOM   4340  N   ILE B 314      39.494  -4.894 -35.638  1.00 48.75           N  
ANISOU 4340  N   ILE B 314     4908   6517   7097   -254   -798    266       N  
ATOM   4341  CA  ILE B 314      39.923  -4.208 -34.424  1.00 46.34           C  
ANISOU 4341  CA  ILE B 314     4590   6171   6845   -235   -742    259       C  
ATOM   4342  C   ILE B 314      40.401  -5.201 -33.372  1.00 48.03           C  
ANISOU 4342  C   ILE B 314     4823   6373   7053   -230   -737    218       C  
ATOM   4343  O   ILE B 314      41.318  -4.901 -32.597  1.00 55.69           O  
ANISOU 4343  O   ILE B 314     5775   7331   8054   -220   -706    203       O  
ATOM   4344  CB  ILE B 314      38.784  -3.322 -33.883  1.00 46.95           C  
ANISOU 4344  CB  ILE B 314     4663   6219   6957   -235   -744    304       C  
ATOM   4345  CG1 ILE B 314      39.317  -2.373 -32.810  1.00 41.73           C  
ANISOU 4345  CG1 ILE B 314     3992   5517   6346   -227   -696    290       C  
ATOM   4346  CG2 ILE B 314      37.650  -4.177 -33.344  1.00 55.59           C  
ANISOU 4346  CG2 ILE B 314     5774   7311   8037   -251   -784    319       C  
ATOM   4347  CD1 ILE B 314      40.455  -1.501 -33.293  1.00 46.73           C  
ANISOU 4347  CD1 ILE B 314     4596   6152   7007   -232   -661    285       C  
ATOM   4348  N   SER B 315      39.801  -6.393 -33.324  1.00 45.67           N  
ANISOU 4348  N   SER B 315     4557   6082   6715   -244   -778    207       N  
ATOM   4349  CA  SER B 315      40.190  -7.375 -32.319  1.00 36.88           C  
ANISOU 4349  CA  SER B 315     3459   4955   5598   -234   -775    176       C  
ATOM   4350  C   SER B 315      41.576  -7.935 -32.606  1.00 39.10           C  
ANISOU 4350  C   SER B 315     3708   5267   5881   -200   -752    156       C  
ATOM   4351  O   SER B 315      42.425  -8.009 -31.710  1.00 52.44           O  
ANISOU 4351  O   SER B 315     5372   6953   7599   -177   -731    151       O  
ATOM   4352  CB  SER B 315      39.157  -8.501 -32.253  1.00 37.18           C  
ANISOU 4352  CB  SER B 315     3536   4990   5600   -268   -827    175       C  
ATOM   4353  OG  SER B 315      37.892  -8.000 -31.860  1.00 42.84           O  
ANISOU 4353  OG  SER B 315     4250   5691   6337   -290   -841    214       O  
ATOM   4354  N   VAL B 316      41.824  -8.336 -33.853  1.00 35.20           N  
ANISOU 4354  N   VAL B 316     3201   4813   5361   -195   -760    153       N  
ATOM   4355  CA  VAL B 316      43.135  -8.872 -34.203  1.00 32.63           C  
ANISOU 4355  CA  VAL B 316     2806   4502   5089   -139   -733    167       C  
ATOM   4356  C   VAL B 316      44.204  -7.790 -34.113  1.00 42.35           C  
ANISOU 4356  C   VAL B 316     3970   5770   6350   -110   -657    176       C  
ATOM   4357  O   VAL B 316      45.321  -8.041 -33.645  1.00 50.08           O  
ANISOU 4357  O   VAL B 316     4882   6772   7375    -64   -621    192       O  
ATOM   4358  CB  VAL B 316      43.090  -9.514 -35.599  1.00 27.90           C  
ANISOU 4358  CB  VAL B 316     2175   3836   4590   -149   -821    228       C  
ATOM   4359  CG1 VAL B 316      44.463 -10.053 -35.970  1.00 30.74           C  
ANISOU 4359  CG1 VAL B 316     2405   4163   5112    -43   -771    298       C  
ATOM   4360  CG2 VAL B 316      42.048 -10.615 -35.626  1.00 25.81           C  
ANISOU 4360  CG2 VAL B 316     2001   3521   4284   -224   -947    213       C  
ATOM   4361  N   LEU B 317      43.885  -6.573 -34.562  1.00 42.06           N  
ANISOU 4361  N   LEU B 317     3936   5721   6323   -143   -650    190       N  
ATOM   4362  CA  LEU B 317      44.850  -5.481 -34.478  1.00 39.22           C  
ANISOU 4362  CA  LEU B 317     3510   5365   6028   -145   -601    215       C  
ATOM   4363  C   LEU B 317      45.200  -5.166 -33.030  1.00 43.81           C  
ANISOU 4363  C   LEU B 317     4087   5919   6638   -170   -618    212       C  
ATOM   4364  O   LEU B 317      46.350  -4.830 -32.720  1.00 44.66           O  
ANISOU 4364  O   LEU B 317     4117   6051   6802   -174   -599    233       O  
ATOM   4365  CB  LEU B 317      44.306  -4.234 -35.176  1.00 33.69           C  
ANISOU 4365  CB  LEU B 317     2821   4647   5332   -176   -596    232       C  
ATOM   4366  CG  LEU B 317      44.405  -4.154 -36.700  1.00 31.98           C  
ANISOU 4366  CG  LEU B 317     2556   4429   5167   -164   -590    286       C  
ATOM   4367  CD1 LEU B 317      43.872  -2.819 -37.198  1.00 41.83           C  
ANISOU 4367  CD1 LEU B 317     3811   5656   6428   -194   -590    318       C  
ATOM   4368  CD2 LEU B 317      45.841  -4.358 -37.147  1.00 37.95           C  
ANISOU 4368  CD2 LEU B 317     3190   5185   6043   -120   -516    350       C  
ATOM   4369  N   ASN B 318      44.223  -5.270 -32.126  1.00 39.39           N  
ANISOU 4369  N   ASN B 318     3600   5319   6048   -191   -659    191       N  
ATOM   4370  CA  ASN B 318      44.497  -4.989 -30.721  1.00 39.05           C  
ANISOU 4370  CA  ASN B 318     3557   5257   6023   -216   -683    183       C  
ATOM   4371  C   ASN B 318      45.424  -6.038 -30.120  1.00 32.29           C  
ANISOU 4371  C   ASN B 318     2656   4438   5175   -189   -697    186       C  
ATOM   4372  O   ASN B 318      46.296  -5.714 -29.305  1.00 31.56           O  
ANISOU 4372  O   ASN B 318     2510   4367   5116   -213   -721    197       O  
ATOM   4373  CB  ASN B 318      43.190  -4.921 -29.934  1.00 47.96           C  
ANISOU 4373  CB  ASN B 318     4761   6338   7124   -230   -706    167       C  
ATOM   4374  CG  ASN B 318      43.322  -4.120 -28.652  1.00 57.97           C  
ANISOU 4374  CG  ASN B 318     6031   7584   8411   -267   -727    156       C  
ATOM   4375  OD1 ASN B 318      43.865  -3.016 -28.651  1.00 59.98           O  
ANISOU 4375  OD1 ASN B 318     6253   7838   8698   -304   -724    161       O  
ATOM   4376  ND2 ASN B 318      42.825  -4.675 -27.552  1.00 56.03           N  
ANISOU 4376  ND2 ASN B 318     5823   7323   8143   -266   -751    138       N  
ATOM   4377  N   VAL B 319      45.248  -7.301 -30.509  1.00 30.00           N  
ANISOU 4377  N   VAL B 319     2379   4162   4856   -142   -692    180       N  
ATOM   4378  CA  VAL B 319      46.103  -8.358 -29.984  1.00 26.95           C  
ANISOU 4378  CA  VAL B 319     1940   3814   4485    -94   -699    194       C  
ATOM   4379  C   VAL B 319      47.500  -8.264 -30.583  1.00 35.89           C  
ANISOU 4379  C   VAL B 319     2949   5007   5682    -48   -656    239       C  
ATOM   4380  O   VAL B 319      48.504  -8.457 -29.886  1.00 38.45           O  
ANISOU 4380  O   VAL B 319     3186   5372   6052    -29   -672    274       O  
ATOM   4381  CB  VAL B 319      45.468  -9.733 -30.244  1.00 22.21           C  
ANISOU 4381  CB  VAL B 319     1391   3208   3841    -54   -705    176       C  
ATOM   4382  CG1 VAL B 319      46.537 -10.815 -30.229  1.00 28.15           C  
ANISOU 4382  CG1 VAL B 319     2062   4011   4622     43   -683    207       C  
ATOM   4383  CG2 VAL B 319      44.389 -10.014 -29.213  1.00 23.00           C  
ANISOU 4383  CG2 VAL B 319     1578   3257   3905    -96   -748    150       C  
ATOM   4384  N   LEU B 320      47.591  -7.975 -31.883  1.00 39.18           N  
ANISOU 4384  N   LEU B 320     3341   5436   6110    -25   -600    248       N  
ATOM   4385  CA  LEU B 320      48.900  -7.817 -32.508  1.00 38.45           C  
ANISOU 4385  CA  LEU B 320     3118   5395   6097     29   -533    304       C  
ATOM   4386  C   LEU B 320      49.639  -6.606 -31.957  1.00 41.80           C  
ANISOU 4386  C   LEU B 320     3471   5829   6583    -50   -555    336       C  
ATOM   4387  O   LEU B 320      50.873  -6.609 -31.896  1.00 46.42           O  
ANISOU 4387  O   LEU B 320     3921   6464   7253    -26   -530    402       O  
ATOM   4388  CB  LEU B 320      48.749  -7.701 -34.025  1.00 38.86           C  
ANISOU 4388  CB  LEU B 320     3150   5419   6197     66   -468    338       C  
ATOM   4389  CG  LEU B 320      48.088  -8.882 -34.737  1.00 30.98           C  
ANISOU 4389  CG  LEU B 320     2174   4348   5247    132   -475    371       C  
ATOM   4390  CD1 LEU B 320      47.829  -8.543 -36.198  1.00 27.01           C  
ANISOU 4390  CD1 LEU B 320     1638   3791   4833    145   -435    436       C  
ATOM   4391  CD2 LEU B 320      48.952 -10.127 -34.617  1.00 31.08           C  
ANISOU 4391  CD2 LEU B 320     2098   4347   5366    274   -409    454       C  
ATOM   4392  N   LYS B 321      48.906  -5.567 -31.555  1.00 44.36           N  
ANISOU 4392  N   LYS B 321     3873   6107   6876   -141   -601    301       N  
ATOM   4393  CA  LYS B 321      49.533  -4.376 -30.994  1.00 40.33           C  
ANISOU 4393  CA  LYS B 321     3306   5602   6416   -227   -634    322       C  
ATOM   4394  C   LYS B 321      49.958  -4.598 -29.546  1.00 49.04           C  
ANISOU 4394  C   LYS B 321     4383   6727   7525   -265   -718    325       C  
ATOM   4395  O   LYS B 321      51.124  -4.400 -29.191  1.00 60.25           O  
ANISOU 4395  O   LYS B 321     5676   8201   9015   -297   -749    380       O  
ATOM   4396  CB  LYS B 321      48.572  -3.188 -31.096  1.00 36.46           C  
ANISOU 4396  CB  LYS B 321     2908   5050   5893   -290   -641    284       C  
ATOM   4397  CG  LYS B 321      49.066  -1.916 -30.426  1.00 40.43           C  
ANISOU 4397  CG  LYS B 321     3375   5550   6437   -393   -681    290       C  
ATOM   4398  CD  LYS B 321      47.992  -0.836 -30.457  1.00 45.63           C  
ANISOU 4398  CD  LYS B 321     4130   6142   7065   -433   -677    254       C  
ATOM   4399  CE  LYS B 321      48.437   0.417 -29.717  1.00 57.45           C  
ANISOU 4399  CE  LYS B 321     5605   7628   8595   -552   -719    245       C  
ATOM   4400  NZ  LYS B 321      47.568   1.587 -30.026  1.00 72.77           N  
ANISOU 4400  NZ  LYS B 321     7613   9506  10531   -584   -687    225       N  
ATOM   4401  N   ARG B 322      49.016  -5.005 -28.697  1.00 45.45           N  
ANISOU 4401  N   ARG B 322     4036   6232   6999   -266   -762    276       N  
ATOM   4402  CA  ARG B 322      49.288  -5.130 -27.269  1.00 44.72           C  
ANISOU 4402  CA  ARG B 322     3936   6156   6897   -310   -848    273       C  
ATOM   4403  C   ARG B 322      50.109  -6.378 -26.958  1.00 52.54           C  
ANISOU 4403  C   ARG B 322     4839   7210   7915   -241   -866    319       C  
ATOM   4404  O   ARG B 322      51.206  -6.289 -26.396  1.00 75.02           O  
ANISOU 4404  O   ARG B 322     7567  10118  10818   -271   -926    374       O  
ATOM   4405  CB  ARG B 322      47.971  -5.144 -26.490  1.00 47.78           C  
ANISOU 4405  CB  ARG B 322     4463   6481   7211   -324   -869    214       C  
ATOM   4406  CG  ARG B 322      47.067  -3.962 -26.798  1.00 48.41           C  
ANISOU 4406  CG  ARG B 322     4617   6500   7277   -366   -841    183       C  
ATOM   4407  CD  ARG B 322      47.444  -2.738 -25.974  1.00 52.23           C  
ANISOU 4407  CD  ARG B 322     5089   6982   7774   -472   -898    170       C  
ATOM   4408  NE  ARG B 322      46.809  -1.521 -26.475  1.00 69.34           N  
ANISOU 4408  NE  ARG B 322     7299   9099   9949   -506   -858    153       N  
ATOM   4409  CZ  ARG B 322      46.999  -0.307 -25.965  1.00 78.43           C  
ANISOU 4409  CZ  ARG B 322     8456  10232  11111   -612   -891    130       C  
ATOM   4410  NH1 ARG B 322      47.809  -0.135 -24.928  1.00 80.82           N  
ANISOU 4410  NH1 ARG B 322     8733  10566  11410   -710   -979    119       N  
ATOM   4411  NH2 ARG B 322      46.379   0.739 -26.494  1.00 75.99           N  
ANISOU 4411  NH2 ARG B 322     8183   9874  10817   -633   -842    120       N  
ATOM   4412  N   VAL B 323      49.592  -7.554 -27.318  1.00 43.99           N  
ANISOU 4412  N   VAL B 323     3804   6113   6796   -150   -823    305       N  
ATOM   4413  CA  VAL B 323      50.239  -8.797 -26.911  1.00 44.07           C  
ANISOU 4413  CA  VAL B 323     3744   6175   6826    -67   -838    347       C  
ATOM   4414  C   VAL B 323      51.518  -9.035 -27.705  1.00 51.35           C  
ANISOU 4414  C   VAL B 323     4505   7160   7845      9   -783    431       C  
ATOM   4415  O   VAL B 323      52.542  -9.447 -27.146  1.00 53.85           O  
ANISOU 4415  O   VAL B 323     4695   7540   8225     45   -820    507       O  
ATOM   4416  CB  VAL B 323      49.261  -9.974 -27.057  1.00 37.89           C  
ANISOU 4416  CB  VAL B 323     3065   5352   5977      2   -808    306       C  
ATOM   4417  CG1 VAL B 323      49.839 -11.217 -26.410  1.00 35.66           C  
ANISOU 4417  CG1 VAL B 323     2727   5114   5709     93   -833    346       C  
ATOM   4418  CG2 VAL B 323      47.922  -9.619 -26.438  1.00 43.05           C  
ANISOU 4418  CG2 VAL B 323     3861   5935   6560    -73   -839    242       C  
ATOM   4419  N   PHE B 324      51.485  -8.792 -29.014  1.00 49.87           N  
ANISOU 4419  N   PHE B 324     4311   6959   7677     43   -690    432       N  
ATOM   4420  CA  PHE B 324      52.618  -9.097 -29.878  1.00 46.64           C  
ANISOU 4420  CA  PHE B 324     3755   6598   7367    142   -599    521       C  
ATOM   4421  C   PHE B 324      53.519  -7.900 -30.161  1.00 56.60           C  
ANISOU 4421  C   PHE B 324     4892   7893   8718     64   -590    586       C  
ATOM   4422  O   PHE B 324      54.508  -8.052 -30.883  1.00 63.63           O  
ANISOU 4422  O   PHE B 324     5645   8823   9709    142   -496    683       O  
ATOM   4423  CB  PHE B 324      52.126  -9.707 -31.192  1.00 43.37           C  
ANISOU 4423  CB  PHE B 324     3404   6152   6923    250   -486    492       C  
ATOM   4424  CG  PHE B 324      51.588 -11.098 -31.042  1.00 46.93           C  
ANISOU 4424  CG  PHE B 324     3921   6562   7350    353   -484    487       C  
ATOM   4425  CD1 PHE B 324      50.313 -11.317 -30.551  1.00 40.57           C  
ANISOU 4425  CD1 PHE B 324     3267   5724   6424    288   -558    388       C  
ATOM   4426  CD2 PHE B 324      52.369 -12.190 -31.380  1.00 46.66           C  
ANISOU 4426  CD2 PHE B 324     3789   6502   7437    526   -388    615       C  
ATOM   4427  CE1 PHE B 324      49.825 -12.602 -30.410  1.00 30.99           C  
ANISOU 4427  CE1 PHE B 324     2099   4451   5225    368   -569    408       C  
ATOM   4428  CE2 PHE B 324      51.887 -13.474 -31.241  1.00 43.47           C  
ANISOU 4428  CE2 PHE B 324     3449   6028   7038    638   -376    635       C  
ATOM   4429  CZ  PHE B 324      50.613 -13.682 -30.756  1.00 30.42           C  
ANISOU 4429  CZ  PHE B 324     1938   4341   5281    547   -484    527       C  
ATOM   4430  N   GLY B 325      53.199  -6.722 -29.631  1.00 59.04           N  
ANISOU 4430  N   GLY B 325     5248   8183   9002    -79   -671    545       N  
ATOM   4431  CA  GLY B 325      54.087  -5.575 -29.743  1.00 59.18           C  
ANISOU 4431  CA  GLY B 325     5144   8234   9107   -173   -683    607       C  
ATOM   4432  C   GLY B 325      54.363  -5.090 -31.150  1.00 58.32           C  
ANISOU 4432  C   GLY B 325     4986   8120   9053   -143   -558    642       C  
ATOM   4433  O   GLY B 325      55.466  -4.607 -31.427  1.00 71.22           O  
ANISOU 4433  O   GLY B 325     6457   9804  10798   -170   -527    743       O  
ATOM   4434  N   MET B 326      53.392  -5.209 -32.051  1.00 47.07           N  
ANISOU 4434  N   MET B 326     3689   6640   7554    -94   -487    572       N  
ATOM   4435  CA  MET B 326      53.542  -4.766 -33.429  1.00 42.25           C  
ANISOU 4435  CA  MET B 326     3051   6022   6980    -63   -366    599       C  
ATOM   4436  C   MET B 326      53.178  -3.290 -33.583  1.00 42.96           C  
ANISOU 4436  C   MET B 326     3186   6078   7060   -190   -393    566       C  
ATOM   4437  O   MET B 326      52.754  -2.614 -32.642  1.00 52.56           O  
ANISOU 4437  O   MET B 326     4465   7268   8238   -293   -496    518       O  
ATOM   4438  CB  MET B 326      52.695  -5.628 -34.368  1.00 45.36           C  
ANISOU 4438  CB  MET B 326     3545   6373   7319     47   -292    565       C  
ATOM   4439  CG  MET B 326      53.081  -7.099 -34.393  1.00 52.73           C  
ANISOU 4439  CG  MET B 326     4424   7303   8309    194   -234    638       C  
ATOM   4440  SD  MET B 326      52.326  -7.973 -35.781  1.00 65.52           S  
ANISOU 4440  SD  MET B 326     6100   8822   9973    329   -106    695       S  
ATOM   4441  CE  MET B 326      52.706  -9.683 -35.394  1.00 76.68           C  
ANISOU 4441  CE  MET B 326     7488  10216  11430    510    -44    766       C  
ATOM   4442  N   PHE B 327      53.361  -2.792 -34.805  1.00 41.50           N  
ANISOU 4442  N   PHE B 327     2968   5888   6911   -172   -282    598       N  
ATOM   4443  CA  PHE B 327      52.995  -1.428 -35.181  1.00 49.90           C  
ANISOU 4443  CA  PHE B 327     4075   6915   7970   -273   -280    575       C  
ATOM   4444  C   PHE B 327      53.711  -0.390 -34.321  1.00 58.34           C  
ANISOU 4444  C   PHE B 327     5062   7999   9105   -413   -355    604       C  
ATOM   4445  O   PHE B 327      53.151   0.653 -33.976  1.00 58.40           O  
ANISOU 4445  O   PHE B 327     5151   7961   9079   -516   -409    551       O  
ATOM   4446  CB  PHE B 327      51.478  -1.226 -35.118  1.00 48.26           C  
ANISOU 4446  CB  PHE B 327     4048   6643   7647   -286   -338    480       C  
ATOM   4447  CG  PHE B 327      50.684  -2.440 -35.518  1.00 47.92           C  
ANISOU 4447  CG  PHE B 327     4082   6586   7539   -183   -329    452       C  
ATOM   4448  CD1 PHE B 327      50.791  -2.974 -36.793  1.00 47.08           C  
ANISOU 4448  CD1 PHE B 327     3918   6446   7522    -95   -229    545       C  
ATOM   4449  CD2 PHE B 327      49.823  -3.044 -34.618  1.00 45.87           C  
ANISOU 4449  CD2 PHE B 327     3930   6312   7188   -181   -416    382       C  
ATOM   4450  CE1 PHE B 327      50.055  -4.092 -37.159  1.00 44.36           C  
ANISOU 4450  CE1 PHE B 327     3631   6073   7152    -16   -236    539       C  
ATOM   4451  CE2 PHE B 327      49.084  -4.158 -34.977  1.00 51.50           C  
ANISOU 4451  CE2 PHE B 327     4712   7023   7833   -108   -415    348       C  
ATOM   4452  CZ  PHE B 327      49.200  -4.683 -36.249  1.00 48.27           C  
ANISOU 4452  CZ  PHE B 327     4241   6575   7523    -34   -345    435       C  
ATOM   4453  N   ARG B 328      54.965  -0.664 -33.974  1.00 66.72           N  
ANISOU 4453  N   ARG B 328     5954   9128  10267   -422   -359    697       N  
ATOM   4454  CA  ARG B 328      55.763   0.326 -33.272  1.00 68.26           C  
ANISOU 4454  CA  ARG B 328     6045   9354  10538   -578   -439    737       C  
ATOM   4455  C   ARG B 328      56.862   0.935 -34.129  1.00 80.38           C  
ANISOU 4455  C   ARG B 328     7410  10929  12201   -616   -334    851       C  
ATOM   4456  O   ARG B 328      57.440   1.948 -33.724  1.00 77.29           O  
ANISOU 4456  O   ARG B 328     6941  10554  11871   -778   -394    878       O  
ATOM   4457  CB  ARG B 328      56.371  -0.258 -31.993  1.00 67.16           C  
ANISOU 4457  CB  ARG B 328     5822   9274  10423   -606   -566    774       C  
ATOM   4458  CG  ARG B 328      55.360  -0.389 -30.874  1.00 79.37           C  
ANISOU 4458  CG  ARG B 328     7536  10773  11848   -636   -685    661       C  
ATOM   4459  CD  ARG B 328      55.924  -1.218 -29.750  1.00 95.09           C  
ANISOU 4459  CD  ARG B 328     9450  12825  13855   -630   -792    705       C  
ATOM   4460  NE  ARG B 328      56.898  -0.441 -28.994  1.00112.43           N  
ANISOU 4460  NE  ARG B 328    11518  15076  16126   -795   -908    769       N  
ATOM   4461  CZ  ARG B 328      57.655  -0.921 -28.015  1.00123.39           C  
ANISOU 4461  CZ  ARG B 328    12793  16537  17553   -830  -1029    844       C  
ATOM   4462  NH1 ARG B 328      58.512  -0.123 -27.393  1.00129.23           N  
ANISOU 4462  NH1 ARG B 328    13419  17327  18357  -1008  -1152    907       N  
ATOM   4463  NH2 ARG B 328      57.567  -2.195 -27.660  1.00123.34           N  
ANISOU 4463  NH2 ARG B 328    12786  16555  17522   -697  -1033    862       N  
ATOM   4464  N   GLN B 329      57.164   0.365 -35.297  1.00 97.51           N  
ANISOU 4464  N   GLN B 329     9523  13109  14419   -480   -171    924       N  
ATOM   4465  CA  GLN B 329      58.125   0.997 -36.193  1.00107.02           C  
ANISOU 4465  CA  GLN B 329    10564  14325  15776   -507    -42   1077       C  
ATOM   4466  C   GLN B 329      57.377   2.080 -36.958  1.00102.06           C  
ANISOU 4466  C   GLN B 329    10048  13606  15124   -574     11   1039       C  
ATOM   4467  O   GLN B 329      56.526   1.781 -37.799  1.00 98.02           O  
ANISOU 4467  O   GLN B 329     9649  13025  14569   -468     95   1024       O  
ATOM   4468  CB  GLN B 329      58.756  -0.026 -37.138  1.00115.11           C  
ANISOU 4468  CB  GLN B 329    11473  15360  16902   -316    147   1236       C  
ATOM   4469  CG  GLN B 329      60.127  -0.527 -36.692  1.00122.03           C  
ANISOU 4469  CG  GLN B 329    12120  16339  17908   -287    156   1386       C  
ATOM   4470  CD  GLN B 329      61.267   0.309 -37.236  1.00127.63           C  
ANISOU 4470  CD  GLN B 329    12624  17089  18782   -359    258   1554       C  
ATOM   4471  OE1 GLN B 329      61.858  -0.027 -38.261  1.00128.92           O  
ANISOU 4471  OE1 GLN B 329    12687  17240  19055   -217    482   1723       O  
ATOM   4472  NE2 GLN B 329      61.588   1.399 -36.549  1.00128.05           N  
ANISOU 4472  NE2 GLN B 329    12619  17182  18854   -578    112   1518       N  
ATOM   4473  N   ALA B 330      57.719   3.340 -36.681  1.00108.93           N  
ANISOU 4473  N   ALA B 330    10880  14474  16036   -755    -37   1038       N  
ATOM   4474  CA  ALA B 330      56.999   4.515 -37.157  1.00115.63           C  
ANISOU 4474  CA  ALA B 330    11844  15227  16863   -847    -10    999       C  
ATOM   4475  C   ALA B 330      57.366   4.921 -38.577  1.00120.72           C  
ANISOU 4475  C   ALA B 330    12418  15830  17620   -806    191   1138       C  
ATOM   4476  O   ALA B 330      57.085   6.065 -38.960  1.00121.09           O  
ANISOU 4476  O   ALA B 330    12519  15802  17686   -913    227   1140       O  
ATOM   4477  CB  ALA B 330      57.236   5.695 -36.212  1.00119.50           C  
ANISOU 4477  CB  ALA B 330    12338  15713  17355  -1075   -132    944       C  
ATOM   4478  N   SER B 331      57.996   4.060 -39.378  1.00123.03           N  
ANISOU 4478  N   SER B 331    12600  16155  17992   -650    348   1266       N  
ATOM   4479  CA  SER B 331      58.398   4.478 -40.717  1.00122.63           C  
ANISOU 4479  CA  SER B 331    12494  16056  18044   -602    580   1413       C  
ATOM   4480  C   SER B 331      57.188   4.745 -41.609  1.00108.25           C  
ANISOU 4480  C   SER B 331    10853  14123  16156   -543    660   1378       C  
ATOM   4481  O   SER B 331      57.120   5.780 -42.283  1.00107.86           O  
ANISOU 4481  O   SER B 331    10831  14004  16147   -614    761   1429       O  
ATOM   4482  CB  SER B 331      59.301   3.407 -41.326  1.00130.77           C  
ANISOU 4482  CB  SER B 331    13389  17131  19165   -416    766   1569       C  
ATOM   4483  OG  SER B 331      58.548   2.250 -41.655  1.00128.44           O  
ANISOU 4483  OG  SER B 331    13215  16799  18789   -232    819   1535       O  
ATOM   4484  N   ASP B 332      56.223   3.831 -41.627  1.00100.47           N  
ANISOU 4484  N   ASP B 332     9986  13117  15072   -421    618   1304       N  
ATOM   4485  CA  ASP B 332      54.970   4.076 -42.329  1.00 94.16           C  
ANISOU 4485  CA  ASP B 332     9340  12228  14210   -385    649   1274       C  
ATOM   4486  C   ASP B 332      53.869   4.368 -41.319  1.00 83.43           C  
ANISOU 4486  C   ASP B 332     8103  10856  12742   -473    410   1111       C  
ATOM   4487  O   ASP B 332      52.883   3.632 -41.238  1.00 79.65           O  
ANISOU 4487  O   ASP B 332     7720  10370  12175   -396    332   1041       O  
ATOM   4488  CB  ASP B 332      54.581   2.910 -43.239  1.00 98.74           C  
ANISOU 4488  CB  ASP B 332     9967  12788  14764   -193    802   1333       C  
ATOM   4489  CG  ASP B 332      53.576   3.322 -44.297  1.00 96.33           C  
ANISOU 4489  CG  ASP B 332     9776  12398  14426   -162    909   1378       C  
ATOM   4490  OD1 ASP B 332      53.087   4.468 -44.220  1.00 92.41           O  
ANISOU 4490  OD1 ASP B 332     9324  11855  13931   -283    834   1353       O  
ATOM   4491  OD2 ASP B 332      53.284   2.514 -45.205  1.00 97.19           O  
ANISOU 4491  OD2 ASP B 332     9942  12483  14503    -14   1092   1453       O  
ATOM   4492  N   ARG B 333      54.042   5.432 -40.536  1.00 80.08           N  
ANISOU 4492  N   ARG B 333     7680  10423  12324   -635    309   1059       N  
ATOM   4493  CA  ARG B 333      53.103   5.750 -39.465  1.00 68.95           C  
ANISOU 4493  CA  ARG B 333     6395   8992  10813   -704    127    920       C  
ATOM   4494  C   ARG B 333      51.678   5.894 -39.989  1.00 63.84           C  
ANISOU 4494  C   ARG B 333     5875   8264  10119   -640    118    903       C  
ATOM   4495  O   ARG B 333      50.721   5.575 -39.271  1.00 64.84           O  
ANISOU 4495  O   ARG B 333     6101   8388  10145   -615    -10    802       O  
ATOM   4496  CB  ARG B 333      53.578   7.016 -38.756  1.00 77.98           C  
ANISOU 4496  CB  ARG B 333     7523  10111  11995   -897     78    902       C  
ATOM   4497  CG  ARG B 333      53.139   7.198 -37.319  1.00 84.32           C  
ANISOU 4497  CG  ARG B 333     8415  10915  12706   -985    -89    773       C  
ATOM   4498  CD  ARG B 333      53.076   8.680 -36.971  1.00 94.86           C  
ANISOU 4498  CD  ARG B 333     9807  12151  14083  -1175   -100    766       C  
ATOM   4499  NE  ARG B 333      53.613   8.942 -35.637  1.00104.84           N  
ANISOU 4499  NE  ARG B 333    11069  13450  15315  -1336   -221    692       N  
ATOM   4500  CZ  ARG B 333      54.910   9.037 -35.359  1.00114.04           C  
ANISOU 4500  CZ  ARG B 333    12097  14694  16541  -1457   -239    730       C  
ATOM   4501  NH1 ARG B 333      55.811   8.889 -36.322  1.00115.92           N  
ANISOU 4501  NH1 ARG B 333    12181  14985  16880  -1424   -126    848       N  
ATOM   4502  NH2 ARG B 333      55.311   9.277 -34.117  1.00119.98           N  
ANISOU 4502  NH2 ARG B 333    12855  15466  17264  -1613   -365    663       N  
ATOM   4503  N   GLU B 334      51.510   6.381 -41.222  1.00 61.08           N  
ANISOU 4503  N   GLU B 334     5518   7849   9841   -612    263   1018       N  
ATOM   4504  CA  GLU B 334      50.168   6.597 -41.762  1.00 55.88           C  
ANISOU 4504  CA  GLU B 334     4951   7125   9156   -560    247   1038       C  
ATOM   4505  C   GLU B 334      49.442   5.280 -42.024  1.00 58.78           C  
ANISOU 4505  C   GLU B 334     5346   7545   9444   -435    188   1014       C  
ATOM   4506  O   GLU B 334      48.244   5.164 -41.740  1.00 67.57           O  
ANISOU 4506  O   GLU B 334     6538   8651  10486   -412     54    962       O  
ATOM   4507  CB  GLU B 334      50.234   7.423 -43.047  1.00 54.80           C  
ANISOU 4507  CB  GLU B 334     4806   6909   9106   -564    444   1196       C  
ATOM   4508  CG  GLU B 334      50.446   8.911 -42.821  1.00 61.37           C  
ANISOU 4508  CG  GLU B 334     5671   7643  10006   -703    485   1218       C  
ATOM   4509  CD  GLU B 334      49.405   9.501 -41.893  1.00 57.92           C  
ANISOU 4509  CD  GLU B 334     5320   7144   9544   -750    334   1137       C  
ATOM   4510  OE1 GLU B 334      49.669  10.569 -41.297  1.00 55.98           O  
ANISOU 4510  OE1 GLU B 334     5115   6815   9342   -886    337   1116       O  
ATOM   4511  OE2 GLU B 334      48.322   8.893 -41.760  1.00 62.79           O  
ANISOU 4511  OE2 GLU B 334     5967   7790  10100   -654    224   1105       O  
ATOM   4512  N   ALA B 335      50.137   4.276 -42.569  1.00 55.56           N  
ANISOU 4512  N   ALA B 335     4872   7185   9052   -352    296   1065       N  
ATOM   4513  CA  ALA B 335      49.451   3.028 -42.891  1.00 56.49           C  
ANISOU 4513  CA  ALA B 335     5018   7338   9110   -250    254   1058       C  
ATOM   4514  C   ALA B 335      48.900   2.358 -41.641  1.00 51.93           C  
ANISOU 4514  C   ALA B 335     4518   6797   8415   -261     44    894       C  
ATOM   4515  O   ALA B 335      47.857   1.695 -41.699  1.00 47.16           O  
ANISOU 4515  O   ALA B 335     3980   6202   7735   -226    -67    860       O  
ATOM   4516  CB  ALA B 335      50.394   2.076 -43.630  1.00 59.33           C  
ANISOU 4516  CB  ALA B 335     5300   7720   9523   -136    470   1158       C  
ATOM   4517  N   VAL B 336      49.589   2.502 -40.509  1.00 44.98           N  
ANISOU 4517  N   VAL B 336     3632   5946   7512   -317     -5    808       N  
ATOM   4518  CA  VAL B 336      49.043   1.990 -39.258  1.00 36.90           C  
ANISOU 4518  CA  VAL B 336     2703   4955   6364   -327   -154    669       C  
ATOM   4519  C   VAL B 336      47.863   2.843 -38.809  1.00 39.10           C  
ANISOU 4519  C   VAL B 336     3085   5185   6586   -371   -244    618       C  
ATOM   4520  O   VAL B 336      46.859   2.322 -38.307  1.00 46.63           O  
ANISOU 4520  O   VAL B 336     4134   6148   7436   -340   -331    545       O  
ATOM   4521  CB  VAL B 336      50.142   1.909 -38.187  1.00 42.73           C  
ANISOU 4521  CB  VAL B 336     3387   5749   7100   -376   -172    626       C  
ATOM   4522  CG1 VAL B 336      49.524   1.807 -36.803  1.00 51.19           C  
ANISOU 4522  CG1 VAL B 336     4565   6837   8048   -409   -294    502       C  
ATOM   4523  CG2 VAL B 336      51.034   0.711 -38.465  1.00 46.35           C  
ANISOU 4523  CG2 VAL B 336     3751   6259   7601   -288   -100    679       C  
ATOM   4524  N   TYR B 337      47.960   4.165 -38.987  1.00 38.79           N  
ANISOU 4524  N   TYR B 337     3022   5087   6631   -440   -203    672       N  
ATOM   4525  CA  TYR B 337      46.840   5.033 -38.637  1.00 37.84           C  
ANISOU 4525  CA  TYR B 337     2974   4900   6503   -460   -259    662       C  
ATOM   4526  C   TYR B 337      45.630   4.761 -39.516  1.00 44.53           C  
ANISOU 4526  C   TYR B 337     3849   5741   7328   -380   -293    723       C  
ATOM   4527  O   TYR B 337      44.490   4.774 -39.036  1.00 54.20           O  
ANISOU 4527  O   TYR B 337     5141   6957   8494   -351   -372    693       O  
ATOM   4528  CB  TYR B 337      47.226   6.509 -38.775  1.00 38.17           C  
ANISOU 4528  CB  TYR B 337     2976   4857   6671   -555   -188    733       C  
ATOM   4529  CG  TYR B 337      48.136   7.102 -37.721  1.00 52.39           C  
ANISOU 4529  CG  TYR B 337     4765   6649   8491   -684   -200    678       C  
ATOM   4530  CD1 TYR B 337      48.220   6.561 -36.444  1.00 67.13           C  
ANISOU 4530  CD1 TYR B 337     6673   8570  10264   -703   -293    571       C  
ATOM   4531  CD2 TYR B 337      48.859   8.256 -37.991  1.00 55.85           C  
ANISOU 4531  CD2 TYR B 337     5161   7020   9039   -806   -119    742       C  
ATOM   4532  CE1 TYR B 337      49.032   7.138 -35.476  1.00 72.46           C  
ANISOU 4532  CE1 TYR B 337     7333   9243  10955   -846   -325    534       C  
ATOM   4533  CE2 TYR B 337      49.667   8.834 -37.041  1.00 63.54           C  
ANISOU 4533  CE2 TYR B 337     6131   7990  10023   -963   -154    696       C  
ATOM   4534  CZ  TYR B 337      49.752   8.274 -35.784  1.00 73.25           C  
ANISOU 4534  CZ  TYR B 337     7389   9283  11159   -985   -266    593       C  
ATOM   4535  OH  TYR B 337      50.563   8.856 -34.835  1.00 82.79           O  
ANISOU 4535  OH  TYR B 337     8592  10490  12374  -1163   -316    555       O  
ATOM   4536  N   ALA B 338      45.854   4.501 -40.806  1.00 37.16           N  
ANISOU 4536  N   ALA B 338     2851   4821   6446   -347   -232    830       N  
ATOM   4537  CA  ALA B 338      44.729   4.227 -41.694  1.00 27.56           C  
ANISOU 4537  CA  ALA B 338     1646   3623   5201   -293   -305    917       C  
ATOM   4538  C   ALA B 338      44.058   2.901 -41.369  1.00 39.72           C  
ANISOU 4538  C   ALA B 338     3261   5223   6607   -259   -431    827       C  
ATOM   4539  O   ALA B 338      42.835   2.778 -41.507  1.00 52.04           O  
ANISOU 4539  O   ALA B 338     4875   6802   8094   -241   -548    850       O  
ATOM   4540  CB  ALA B 338      45.193   4.246 -43.152  1.00 36.78           C  
ANISOU 4540  CB  ALA B 338     2813   4783   6379   -261   -185   1047       C  
ATOM   4541  N   ALA B 339      44.833   1.903 -40.939  1.00 40.93           N  
ANISOU 4541  N   ALA B 339     3414   5405   6731   -251   -402    742       N  
ATOM   4542  CA  ALA B 339      44.247   0.617 -40.583  1.00 35.55           C  
ANISOU 4542  CA  ALA B 339     2805   4764   5939   -230   -500    662       C  
ATOM   4543  C   ALA B 339      43.384   0.732 -39.335  1.00 37.57           C  
ANISOU 4543  C   ALA B 339     3163   5022   6089   -239   -554    551       C  
ATOM   4544  O   ALA B 339      42.214   0.330 -39.334  1.00 30.11           O  
ANISOU 4544  O   ALA B 339     2281   4095   5066   -231   -639    543       O  
ATOM   4545  CB  ALA B 339      45.351  -0.421 -40.380  1.00 27.99           C  
ANISOU 4545  CB  ALA B 339     1798   3828   5008   -201   -433    630       C  
ATOM   4546  N   PHE B 340      43.947   1.285 -38.260  1.00 41.19           N  
ANISOU 4546  N   PHE B 340     3629   5469   6553   -261   -503    486       N  
ATOM   4547  CA  PHE B 340      43.193   1.410 -37.020  1.00 36.17           C  
ANISOU 4547  CA  PHE B 340     3069   4832   5843   -264   -532    413       C  
ATOM   4548  C   PHE B 340      41.987   2.322 -37.195  1.00 38.38           C  
ANISOU 4548  C   PHE B 340     3357   5069   6156   -251   -558    480       C  
ATOM   4549  O   PHE B 340      40.928   2.082 -36.603  1.00 40.69           O  
ANISOU 4549  O   PHE B 340     3697   5371   6391   -228   -590    459       O  
ATOM   4550  CB  PHE B 340      44.106   1.914 -35.904  1.00 32.54           C  
ANISOU 4550  CB  PHE B 340     2597   4363   5403   -311   -499    364       C  
ATOM   4551  CG  PHE B 340      44.963   0.842 -35.301  1.00 46.05           C  
ANISOU 4551  CG  PHE B 340     4299   6122   7076   -309   -503    314       C  
ATOM   4552  CD1 PHE B 340      44.425  -0.068 -34.409  1.00 59.91           C  
ANISOU 4552  CD1 PHE B 340     6107   7870   8787   -289   -552    283       C  
ATOM   4553  CD2 PHE B 340      46.303   0.735 -35.634  1.00 44.20           C  
ANISOU 4553  CD2 PHE B 340     3981   5926   6886   -323   -458    330       C  
ATOM   4554  CE1 PHE B 340      45.207  -1.064 -33.851  1.00 59.49           C  
ANISOU 4554  CE1 PHE B 340     6029   7845   8728   -281   -563    264       C  
ATOM   4555  CE2 PHE B 340      47.093  -0.259 -35.079  1.00 53.79           C  
ANISOU 4555  CE2 PHE B 340     5157   7176   8106   -307   -469    321       C  
ATOM   4556  CZ  PHE B 340      46.543  -1.160 -34.186  1.00 59.68           C  
ANISOU 4556  CZ  PHE B 340     5962   7912   8800   -284   -525    286       C  
ATOM   4557  N   THR B 341      42.117   3.364 -38.019  1.00 45.69           N  
ANISOU 4557  N   THR B 341     4221   5949   7192   -259   -535    586       N  
ATOM   4558  CA  THR B 341      40.980   4.246 -38.266  1.00 37.42           C  
ANISOU 4558  CA  THR B 341     3156   4863   6199   -227   -557    691       C  
ATOM   4559  C   THR B 341      39.822   3.480 -38.887  1.00 38.00           C  
ANISOU 4559  C   THR B 341     3256   5000   6181   -190   -646    731       C  
ATOM   4560  O   THR B 341      38.679   3.575 -38.425  1.00 38.11           O  
ANISOU 4560  O   THR B 341     3284   5021   6174   -159   -672    753       O  
ATOM   4561  CB  THR B 341      41.395   5.409 -39.165  1.00 32.96           C  
ANISOU 4561  CB  THR B 341     2508   4242   5775   -236   -505    826       C  
ATOM   4562  OG1 THR B 341      42.327   6.240 -38.463  1.00 48.87           O  
ANISOU 4562  OG1 THR B 341     4498   6182   7888   -303   -426    791       O  
ATOM   4563  CG2 THR B 341      40.177   6.234 -39.546  1.00 24.57           C  
ANISOU 4563  CG2 THR B 341     1408   3156   4771   -171   -528    977       C  
ATOM   4564  N   PHE B 342      40.100   2.713 -39.943  1.00 35.54           N  
ANISOU 4564  N   PHE B 342     2940   4735   5830   -203   -699    758       N  
ATOM   4565  CA  PHE B 342      39.055   1.909 -40.567  1.00 33.68           C  
ANISOU 4565  CA  PHE B 342     2738   4559   5500   -207   -821    800       C  
ATOM   4566  C   PHE B 342      38.514   0.858 -39.604  1.00 49.08           C  
ANISOU 4566  C   PHE B 342     4755   6535   7357   -214   -833    675       C  
ATOM   4567  O   PHE B 342      37.320   0.539 -39.629  1.00 58.02           O  
ANISOU 4567  O   PHE B 342     5903   7702   8438   -218   -903    708       O  
ATOM   4568  CB  PHE B 342      39.605   1.254 -41.834  1.00 31.47           C  
ANISOU 4568  CB  PHE B 342     2445   4309   5202   -241   -900    870       C  
ATOM   4569  CG  PHE B 342      38.713   0.199 -42.416  1.00 37.40           C  
ANISOU 4569  CG  PHE B 342     3267   5115   5827   -291  -1068    898       C  
ATOM   4570  CD1 PHE B 342      37.602   0.551 -43.161  1.00 42.44           C  
ANISOU 4570  CD1 PHE B 342     3926   5797   6403   -308  -1197   1029       C  
ATOM   4571  CD2 PHE B 342      38.998  -1.144 -42.234  1.00 34.36           C  
ANISOU 4571  CD2 PHE B 342     2936   4735   5382   -332  -1108    807       C  
ATOM   4572  CE1 PHE B 342      36.783  -0.416 -43.707  1.00 41.42           C  
ANISOU 4572  CE1 PHE B 342     3888   5715   6135   -391  -1370   1053       C  
ATOM   4573  CE2 PHE B 342      38.182  -2.117 -42.778  1.00 39.69           C  
ANISOU 4573  CE2 PHE B 342     3708   5444   5931   -414  -1282    835       C  
ATOM   4574  CZ  PHE B 342      37.072  -1.752 -43.516  1.00 39.41           C  
ANISOU 4574  CZ  PHE B 342     3711   5451   5814   -456  -1416    951       C  
ATOM   4575  N   SER B 343      39.379   0.309 -38.747  1.00 42.74           N  
ANISOU 4575  N   SER B 343     3979   5724   6536   -217   -764    552       N  
ATOM   4576  CA  SER B 343      38.919  -0.669 -37.766  1.00 30.14           C  
ANISOU 4576  CA  SER B 343     2440   4155   4858   -217   -764    454       C  
ATOM   4577  C   SER B 343      37.981  -0.035 -36.748  1.00 43.73           C  
ANISOU 4577  C   SER B 343     4155   5847   6614   -198   -742    480       C  
ATOM   4578  O   SER B 343      37.016  -0.669 -36.305  1.00 52.79           O  
ANISOU 4578  O   SER B 343     5309   6999   7748   -207   -783    500       O  
ATOM   4579  CB  SER B 343      40.113  -1.313 -37.064  1.00 35.16           C  
ANISOU 4579  CB  SER B 343     3090   4789   5481   -219   -707    363       C  
ATOM   4580  OG  SER B 343      40.980  -1.919 -38.007  1.00 44.55           O  
ANISOU 4580  OG  SER B 343     4248   5984   6694   -228   -725    383       O  
ATOM   4581  N   HIS B 344      38.242   1.219 -36.366  1.00 50.97           N  
ANISOU 4581  N   HIS B 344     5044   6725   7596   -177   -680    498       N  
ATOM   4582  CA  HIS B 344      37.339   1.893 -35.438  1.00 48.69           C  
ANISOU 4582  CA  HIS B 344     4735   6401   7365   -149   -656    542       C  
ATOM   4583  C   HIS B 344      35.992   2.168 -36.091  1.00 47.33           C  
ANISOU 4583  C   HIS B 344     4515   6259   7210   -113   -697    660       C  
ATOM   4584  O   HIS B 344      34.943   2.024 -35.452  1.00 46.17           O  
ANISOU 4584  O   HIS B 344     4342   6116   7086    -93   -699    705       O  
ATOM   4585  CB  HIS B 344      37.958   3.201 -34.937  1.00 48.37           C  
ANISOU 4585  CB  HIS B 344     4662   6280   7436   -149   -596    566       C  
ATOM   4586  CG  HIS B 344      39.323   3.046 -34.344  1.00 50.49           C  
ANISOU 4586  CG  HIS B 344     4961   6536   7686   -202   -572    464       C  
ATOM   4587  ND1 HIS B 344      40.288   4.022 -34.457  1.00 47.79           N  
ANISOU 4587  ND1 HIS B 344     4579   6131   7447   -245   -543    487       N  
ATOM   4588  CD2 HIS B 344      39.887   2.042 -33.633  1.00 54.22           C  
ANISOU 4588  CD2 HIS B 344     5475   7033   8091   -227   -585    379       C  
ATOM   4589  CE1 HIS B 344      41.391   3.628 -33.847  1.00 51.22           C  
ANISOU 4589  CE1 HIS B 344     5037   6589   7835   -297   -539    398       C  
ATOM   4590  NE2 HIS B 344      41.173   2.429 -33.337  1.00 50.24           N  
ANISOU 4590  NE2 HIS B 344     4961   6519   7610   -277   -563    339       N  
ATOM   4591  N   TRP B 345      36.005   2.558 -37.367  1.00 45.12           N  
ANISOU 4591  N   TRP B 345     4201   5990   6951   -113   -743    757       N  
ATOM   4592  CA  TRP B 345      34.761   2.839 -38.075  1.00 42.70           C  
ANISOU 4592  CA  TRP B 345     3837   5725   6661    -87   -806    907       C  
ATOM   4593  C   TRP B 345      33.910   1.586 -38.244  1.00 42.71           C  
ANISOU 4593  C   TRP B 345     3859   5800   6568   -132   -896    883       C  
ATOM   4594  O   TRP B 345      32.681   1.650 -38.138  1.00 44.69           O  
ANISOU 4594  O   TRP B 345     4050   6087   6843   -116   -924    980       O  
ATOM   4595  CB  TRP B 345      35.071   3.458 -39.432  1.00 38.38           C  
ANISOU 4595  CB  TRP B 345     3259   5186   6139    -85   -855   1029       C  
ATOM   4596  CG  TRP B 345      33.869   3.659 -40.281  1.00 32.34           C  
ANISOU 4596  CG  TRP B 345     2441   4486   5362    -68   -948   1197       C  
ATOM   4597  CD1 TRP B 345      33.021   4.725 -40.260  1.00 37.24           C  
ANISOU 4597  CD1 TRP B 345     2977   5104   6069     14   -909   1360       C  
ATOM   4598  CD2 TRP B 345      33.381   2.773 -41.292  1.00 40.93           C  
ANISOU 4598  CD2 TRP B 345     3553   5654   6344   -139  -1103   1238       C  
ATOM   4599  NE1 TRP B 345      32.031   4.558 -41.200  1.00 46.61           N  
ANISOU 4599  NE1 TRP B 345     4123   6380   7205      0  -1033   1499       N  
ATOM   4600  CE2 TRP B 345      32.230   3.367 -41.847  1.00 49.00           C  
ANISOU 4600  CE2 TRP B 345     4499   6734   7386   -107  -1166   1424       C  
ATOM   4601  CE3 TRP B 345      33.806   1.536 -41.782  1.00 53.17           C  
ANISOU 4601  CE3 TRP B 345     5185   7230   7787   -230  -1200   1151       C  
ATOM   4602  CZ2 TRP B 345      31.499   2.764 -42.868  1.00 50.67           C  
ANISOU 4602  CZ2 TRP B 345     4719   7032   7501   -186  -1343   1516       C  
ATOM   4603  CZ3 TRP B 345      33.081   0.939 -42.794  1.00 52.99           C  
ANISOU 4603  CZ3 TRP B 345     5189   7277   7668   -312  -1374   1244       C  
ATOM   4604  CH2 TRP B 345      31.940   1.553 -43.327  1.00 47.04           C  
ANISOU 4604  CH2 TRP B 345     4365   6585   6924   -299  -1453   1420       C  
ATOM   4605  N   LEU B 346      34.541   0.438 -38.509  1.00 41.70           N  
ANISOU 4605  N   LEU B 346     3801   5690   6353   -189   -939    775       N  
ATOM   4606  CA  LEU B 346      33.779  -0.796 -38.661  1.00 49.04           C  
ANISOU 4606  CA  LEU B 346     4750   6662   7223   -255  -1037    780       C  
ATOM   4607  C   LEU B 346      33.001  -1.131 -37.397  1.00 58.90           C  
ANISOU 4607  C   LEU B 346     5963   7889   8529   -255  -1004    800       C  
ATOM   4608  O   LEU B 346      31.896  -1.685 -37.476  1.00 64.54           O  
ANISOU 4608  O   LEU B 346     6637   8643   9245   -302  -1081    884       O  
ATOM   4609  CB  LEU B 346      34.706  -1.951 -39.040  1.00 44.93           C  
ANISOU 4609  CB  LEU B 346     4311   6144   6615   -304  -1069    666       C  
ATOM   4610  CG  LEU B 346      34.778  -2.292 -40.529  1.00 35.26           C  
ANISOU 4610  CG  LEU B 346     3119   4941   5336   -382  -1221    755       C  
ATOM   4611  CD1 LEU B 346      35.645  -3.518 -40.765  1.00 32.70           C  
ANISOU 4611  CD1 LEU B 346     2875   4595   4952   -441  -1267    676       C  
ATOM   4612  CD2 LEU B 346      33.379  -2.503 -41.098  1.00 26.68           C  
ANISOU 4612  CD2 LEU B 346     2019   3909   4209   -449  -1359    872       C  
ATOM   4613  N   VAL B 347      33.549  -0.808 -36.224  1.00 56.33           N  
ANISOU 4613  N   VAL B 347     5648   7505   8248   -213   -899    734       N  
ATOM   4614  CA  VAL B 347      32.824  -1.068 -34.985  1.00 45.75           C  
ANISOU 4614  CA  VAL B 347     4277   6146   6959   -204   -865    754       C  
ATOM   4615  C   VAL B 347      31.504  -0.313 -34.976  1.00 51.68           C  
ANISOU 4615  C   VAL B 347     4921   6924   7790   -163   -859    908       C  
ATOM   4616  O   VAL B 347      30.458  -0.858 -34.600  1.00 63.00           O  
ANISOU 4616  O   VAL B 347     6295   8387   9255   -186   -888    987       O  
ATOM   4617  CB  VAL B 347      33.695  -0.698 -33.772  1.00 41.92           C  
ANISOU 4617  CB  VAL B 347     3830   5597   6499   -169   -769    661       C  
ATOM   4618  CG1 VAL B 347      32.881  -0.778 -32.491  1.00 42.36           C  
ANISOU 4618  CG1 VAL B 347     3848   5635   6612   -145   -727    691       C  
ATOM   4619  CG2 VAL B 347      34.907  -1.609 -33.707  1.00 39.88           C  
ANISOU 4619  CG2 VAL B 347     3652   5327   6173   -205   -779    541       C  
ATOM   4620  N   TYR B 348      31.532   0.953 -35.386  1.00 53.27           N  
ANISOU 4620  N   TYR B 348     5085   7120   8034    -98   -815    969       N  
ATOM   4621  CA  TYR B 348      30.311   1.739 -35.467  1.00 50.47           C  
ANISOU 4621  CA  TYR B 348     4616   6797   7764    -35   -796   1140       C  
ATOM   4622  C   TYR B 348      29.470   1.366 -36.680  1.00 49.75           C  
ANISOU 4622  C   TYR B 348     4465   6794   7643    -89   -927   1266       C  
ATOM   4623  O   TYR B 348      28.242   1.489 -36.631  1.00 54.59           O  
ANISOU 4623  O   TYR B 348     4961   7458   8324    -73   -943   1430       O  
ATOM   4624  CB  TYR B 348      30.660   3.225 -35.488  1.00 43.12           C  
ANISOU 4624  CB  TYR B 348     3670   5819   6894     65   -696   1175       C  
ATOM   4625  CG  TYR B 348      31.433   3.653 -34.265  1.00 35.09           C  
ANISOU 4625  CG  TYR B 348     2697   4705   5931     94   -587   1088       C  
ATOM   4626  CD1 TYR B 348      30.807   3.762 -33.033  1.00 35.30           C  
ANISOU 4626  CD1 TYR B 348     2682   4695   6037    147   -500   1129       C  
ATOM   4627  CD2 TYR B 348      32.791   3.934 -34.337  1.00 33.21           C  
ANISOU 4627  CD2 TYR B 348     2529   4411   5680     62   -576    983       C  
ATOM   4628  CE1 TYR B 348      31.504   4.147 -31.908  1.00 36.06           C  
ANISOU 4628  CE1 TYR B 348     2812   4692   6197    163   -416   1066       C  
ATOM   4629  CE2 TYR B 348      33.499   4.321 -33.215  1.00 39.13           C  
ANISOU 4629  CE2 TYR B 348     3303   5069   6494     63   -503    918       C  
ATOM   4630  CZ  TYR B 348      32.849   4.426 -32.003  1.00 41.59           C  
ANISOU 4630  CZ  TYR B 348     3578   5337   6886    112   -430    958       C  
ATOM   4631  OH  TYR B 348      33.539   4.811 -30.877  1.00 51.78           O  
ANISOU 4631  OH  TYR B 348     4884   6523   8268    105   -371    906       O  
ATOM   4632  N   ALA B 349      30.101   0.924 -37.773  1.00 47.68           N  
ANISOU 4632  N   ALA B 349     4277   6557   7283   -153  -1024   1204       N  
ATOM   4633  CA  ALA B 349      29.333   0.478 -38.930  1.00 46.25           C  
ANISOU 4633  CA  ALA B 349     4061   6461   7053   -228  -1178   1314       C  
ATOM   4634  C   ALA B 349      28.423  -0.687 -38.574  1.00 56.16           C  
ANISOU 4634  C   ALA B 349     5277   7752   8310   -324  -1259   1362       C  
ATOM   4635  O   ALA B 349      27.340  -0.832 -39.154  1.00 66.15           O  
ANISOU 4635  O   ALA B 349     6451   9096   9586   -383  -1373   1521       O  
ATOM   4636  CB  ALA B 349      30.270   0.093 -40.076  1.00 46.55           C  
ANISOU 4636  CB  ALA B 349     4212   6507   6968   -280  -1263   1217       C  
ATOM   4637  N   ASN B 350      28.842  -1.527 -37.627  1.00 57.50           N  
ANISOU 4637  N   ASN B 350     5508   7870   8469   -348  -1210   1240       N  
ATOM   4638  CA  ASN B 350      27.987  -2.620 -37.182  1.00 55.81           C  
ANISOU 4638  CA  ASN B 350     5256   7683   8266   -434  -1274   1288       C  
ATOM   4639  C   ASN B 350      26.709  -2.097 -36.537  1.00 64.80           C  
ANISOU 4639  C   ASN B 350     6229   8860   9532   -388  -1230   1470       C  
ATOM   4640  O   ASN B 350      25.643  -2.705 -36.672  1.00 66.77           O  
ANISOU 4640  O   ASN B 350     6386   9174   9808   -472  -1327   1604       O  
ATOM   4641  CB  ASN B 350      28.754  -3.514 -36.207  1.00 46.20           C  
ANISOU 4641  CB  ASN B 350     4136   6399   7019   -441  -1211   1124       C  
ATOM   4642  CG  ASN B 350      27.948  -4.711 -35.754  1.00 57.73           C  
ANISOU 4642  CG  ASN B 350     5570   7880   8485   -532  -1277   1164       C  
ATOM   4643  OD1 ASN B 350      27.812  -5.697 -36.481  1.00 69.38           O  
ANISOU 4643  OD1 ASN B 350     7098   9381   9884   -650  -1406   1159       O  
ATOM   4644  ND2 ASN B 350      27.407  -4.634 -34.545  1.00 55.16           N  
ANISOU 4644  ND2 ASN B 350     5169   7541   8249   -484  -1190   1207       N  
ATOM   4645  N   SER B 351      26.797  -0.966 -35.828  1.00 68.73           N  
ANISOU 4645  N   SER B 351     6684   9318  10114   -257  -1082   1489       N  
ATOM   4646  CA  SER B 351      25.606  -0.402 -35.201  1.00 59.19           C  
ANISOU 4646  CA  SER B 351     5314   8141   9035   -185  -1009   1676       C  
ATOM   4647  C   SER B 351      24.568   0.013 -36.233  1.00 56.29           C  
ANISOU 4647  C   SER B 351     4804   7875   8708   -201  -1104   1899       C  
ATOM   4648  O   SER B 351      23.363  -0.074 -35.971  1.00 48.13           O  
ANISOU 4648  O   SER B 351     3609   6908   7771   -204  -1111   2094       O  
ATOM   4649  CB  SER B 351      25.991   0.794 -34.332  1.00 63.09           C  
ANISOU 4649  CB  SER B 351     5815   8558   9597    -34   -825   1646       C  
ATOM   4650  OG  SER B 351      26.946   0.420 -33.356  1.00 78.24           O  
ANISOU 4650  OG  SER B 351     7857  10395  11475    -35   -759   1452       O  
ATOM   4651  N   ALA B 352      25.010   0.472 -37.406  1.00 59.46           N  
ANISOU 4651  N   ALA B 352     5251   8298   9041   -209  -1180   1888       N  
ATOM   4652  CA  ALA B 352      24.073   0.836 -38.463  1.00 56.07           C  
ANISOU 4652  CA  ALA B 352     4694   7975   8634   -233  -1296   2102       C  
ATOM   4653  C   ALA B 352      23.634  -0.370 -39.278  1.00 54.57           C  
ANISOU 4653  C   ALA B 352     4512   7862   8360   -423  -1516   2137       C  
ATOM   4654  O   ALA B 352      22.539  -0.361 -39.850  1.00 61.38           O  
ANISOU 4654  O   ALA B 352     5228   8831   9264   -483  -1636   2354       O  
ATOM   4655  CB  ALA B 352      24.694   1.891 -39.378  1.00 52.09           C  
ANISOU 4655  CB  ALA B 352     4241   7463   8088   -154  -1289   2087       C  
ATOM   4656  N   ALA B 353      24.475  -1.401 -39.348  1.00 48.88           N  
ANISOU 4656  N   ALA B 353     3960   7089   7523   -521  -1571   1938       N  
ATOM   4657  CA  ALA B 353      24.154  -2.563 -40.169  1.00 49.07           C  
ANISOU 4657  CA  ALA B 353     4034   7164   7446   -710  -1779   1954       C  
ATOM   4658  C   ALA B 353      22.959  -3.328 -39.613  1.00 63.27           C  
ANISOU 4658  C   ALA B 353     5699   9019   9321   -807  -1841   2104       C  
ATOM   4659  O   ALA B 353      22.066  -3.729 -40.365  1.00 73.40           O  
ANISOU 4659  O   ALA B 353     6907  10394  10587   -950  -2026   2266       O  
ATOM   4660  CB  ALA B 353      25.373  -3.479 -40.282  1.00 38.39           C  
ANISOU 4660  CB  ALA B 353     2899   5729   5958   -765  -1789   1711       C  
ATOM   4661  N   ASN B 354      22.925  -3.547 -38.299  1.00 62.46           N  
ANISOU 4661  N   ASN B 354     5566   8866   9301   -742  -1698   2060       N  
ATOM   4662  CA  ASN B 354      21.885  -4.392 -37.708  1.00 64.40           C  
ANISOU 4662  CA  ASN B 354     5695   9159   9617   -836  -1750   2187       C  
ATOM   4663  C   ASN B 354      20.473  -3.945 -38.046  1.00 72.49           C  
ANISOU 4663  C   ASN B 354     6477  10310  10756   -864  -1828   2492       C  
ATOM   4664  O   ASN B 354      19.671  -4.791 -38.480  1.00 82.75           O  
ANISOU 4664  O   ASN B 354     7713  11687  12041  -1043  -2011   2619       O  
ATOM   4665  CB  ASN B 354      22.087  -4.452 -36.187  1.00 64.37           C  
ANISOU 4665  CB  ASN B 354     5687   9079   9690   -724  -1558   2102       C  
ATOM   4666  CG  ASN B 354      23.349  -5.180 -35.804  1.00 65.44           C  
ANISOU 4666  CG  ASN B 354     6037   9112   9717   -731  -1516   1832       C  
ATOM   4667  OD1 ASN B 354      23.758  -6.122 -36.482  1.00 64.94           O  
ANISOU 4667  OD1 ASN B 354     6101   9039   9535   -858  -1643   1738       O  
ATOM   4668  ND2 ASN B 354      23.972  -4.759 -34.710  1.00 67.07           N  
ANISOU 4668  ND2 ASN B 354     6284   9240   9960   -598  -1339   1717       N  
ATOM   4669  N   PRO B 355      20.094  -2.675 -37.880  1.00 67.57           N  
ANISOU 4669  N   PRO B 355     5710   9716  10249   -702  -1704   2636       N  
ATOM   4670  CA  PRO B 355      18.739  -2.276 -38.300  1.00 66.84           C  
ANISOU 4670  CA  PRO B 355     5365   9760  10271   -725  -1786   2958       C  
ATOM   4671  C   PRO B 355      18.483  -2.524 -39.771  1.00 66.76           C  
ANISOU 4671  C   PRO B 355     5360   9843  10161   -895  -2044   3044       C  
ATOM   4672  O   PRO B 355      17.345  -2.844 -40.155  1.00 64.80           O  
ANISOU 4672  O   PRO B 355     4932   9718   9970  -1023  -2203   3291       O  
ATOM   4673  CB  PRO B 355      18.699  -0.775 -37.969  1.00 70.83           C  
ANISOU 4673  CB  PRO B 355     5775  10249  10887   -490  -1579   3049       C  
ATOM   4674  CG  PRO B 355      19.799  -0.558 -36.983  1.00 71.78           C  
ANISOU 4674  CG  PRO B 355     6071  10222  10981   -366  -1379   2794       C  
ATOM   4675  CD  PRO B 355      20.855  -1.567 -37.295  1.00 72.13           C  
ANISOU 4675  CD  PRO B 355     6344  10203  10860   -498  -1487   2528       C  
ATOM   4676  N   ILE B 356      19.507  -2.401 -40.609  1.00 69.08           N  
ANISOU 4676  N   ILE B 356     5858  10084  10307   -908  -2098   2856       N  
ATOM   4677  CA  ILE B 356      19.342  -2.711 -42.024  1.00 67.11           C  
ANISOU 4677  CA  ILE B 356     5659   9908   9932  -1080  -2352   2914       C  
ATOM   4678  C   ILE B 356      19.087  -4.197 -42.218  1.00 71.12           C  
ANISOU 4678  C   ILE B 356     6255  10423  10344  -1328  -2545   2883       C  
ATOM   4679  O   ILE B 356      18.299  -4.598 -43.086  1.00 80.68           O  
ANISOU 4679  O   ILE B 356     7411  11733  11511  -1519  -2784   3052       O  
ATOM   4680  CB  ILE B 356      20.568  -2.239 -42.821  1.00 57.62           C  
ANISOU 4680  CB  ILE B 356     4670   8637   8588  -1018  -2342   2713       C  
ATOM   4681  CG1 ILE B 356      20.756  -0.735 -42.642  1.00 51.17           C  
ANISOU 4681  CG1 ILE B 356     3764   7810   7867   -784  -2159   2763       C  
ATOM   4682  CG2 ILE B 356      20.412  -2.601 -44.288  1.00 54.29           C  
ANISOU 4682  CG2 ILE B 356     4336   8280   8012  -1200  -2611   2764       C  
ATOM   4683  CD1 ILE B 356      22.110  -0.236 -43.067  1.00 48.19           C  
ANISOU 4683  CD1 ILE B 356     3589   7341   7378   -691  -2088   2543       C  
ATOM   4684  N   ILE B 357      19.756  -5.039 -41.428  1.00 71.10           N  
ANISOU 4684  N   ILE B 357     6400  10314  10301  -1335  -2453   2672       N  
ATOM   4685  CA  ILE B 357      19.542  -6.479 -41.538  1.00 75.11           C  
ANISOU 4685  CA  ILE B 357     7010  10812  10716  -1562  -2617   2635       C  
ATOM   4686  C   ILE B 357      18.107  -6.840 -41.180  1.00 79.17           C  
ANISOU 4686  C   ILE B 357     7283  11439  11359  -1677  -2714   2907       C  
ATOM   4687  O   ILE B 357      17.492  -7.704 -41.818  1.00 86.61           O  
ANISOU 4687  O   ILE B 357     8242  12437  12229  -1921  -2950   3007       O  
ATOM   4688  CB  ILE B 357      20.553  -7.243 -40.662  1.00 65.60           C  
ANISOU 4688  CB  ILE B 357     5991   9475   9460  -1513  -2474   2368       C  
ATOM   4689  CG1 ILE B 357      21.973  -7.043 -41.190  1.00 53.78           C  
ANISOU 4689  CG1 ILE B 357     4727   7882   7825  -1437  -2416   2125       C  
ATOM   4690  CG2 ILE B 357      20.193  -8.716 -40.621  1.00 67.90           C  
ANISOU 4690  CG2 ILE B 357     6366   9755   9678  -1734  -2622   2357       C  
ATOM   4691  CD1 ILE B 357      23.052  -7.374 -40.190  1.00 47.31           C  
ANISOU 4691  CD1 ILE B 357     4028   6947   7001  -1319  -2225   1892       C  
ATOM   4692  N   TYR B 358      17.553  -6.196 -40.150  1.00 72.93           N  
ANISOU 4692  N   TYR B 358     6271  10681  10759  -1512  -2535   3038       N  
ATOM   4693  CA  TYR B 358      16.170  -6.472 -39.776  1.00 74.46           C  
ANISOU 4693  CA  TYR B 358     6201  10992  11097  -1600  -2607   3325       C  
ATOM   4694  C   TYR B 358      15.209  -6.083 -40.892  1.00 76.54           C  
ANISOU 4694  C   TYR B 358     6289  11409  11384  -1722  -2825   3611       C  
ATOM   4695  O   TYR B 358      14.192  -6.749 -41.109  1.00 81.04           O  
ANISOU 4695  O   TYR B 358     6718  12084  11989  -1927  -3019   3826       O  
ATOM   4696  CB  TYR B 358      15.800  -5.727 -38.493  1.00 77.62           C  
ANISOU 4696  CB  TYR B 358     6407  11388  11695  -1368  -2345   3422       C  
ATOM   4697  CG  TYR B 358      16.761  -5.898 -37.336  1.00 70.13           C  
ANISOU 4697  CG  TYR B 358     5624  10293  10730  -1226  -2122   3152       C  
ATOM   4698  CD1 TYR B 358      17.373  -7.117 -37.080  1.00 62.72           C  
ANISOU 4698  CD1 TYR B 358     4884   9272   9674  -1345  -2171   2935       C  
ATOM   4699  CD2 TYR B 358      17.040  -4.835 -36.487  1.00 71.02           C  
ANISOU 4699  CD2 TYR B 358     5694  10348  10941   -979  -1866   3128       C  
ATOM   4700  CE1 TYR B 358      18.244  -7.270 -36.012  1.00 63.22           C  
ANISOU 4700  CE1 TYR B 358     5083   9214   9726  -1216  -1979   2707       C  
ATOM   4701  CE2 TYR B 358      17.907  -4.977 -35.420  1.00 69.24           C  
ANISOU 4701  CE2 TYR B 358     5620   9994  10694   -868  -1685   2893       C  
ATOM   4702  CZ  TYR B 358      18.507  -6.194 -35.186  1.00 66.68           C  
ANISOU 4702  CZ  TYR B 358     5473   9604  10258   -986  -1747   2687       C  
ATOM   4703  OH  TYR B 358      19.373  -6.339 -34.123  1.00 69.34           O  
ANISOU 4703  OH  TYR B 358     5946   9825  10574   -879  -1579   2468       O  
ATOM   4704  N   ASN B 359      15.525  -5.010 -41.618  1.00 77.48           N  
ANISOU 4704  N   ASN B 359     6412  11546  11480  -1607  -2807   3625       N  
ATOM   4705  CA  ASN B 359      14.624  -4.521 -42.656  1.00 80.97           C  
ANISOU 4705  CA  ASN B 359     6673  12142  11951  -1697  -3008   3910       C  
ATOM   4706  C   ASN B 359      14.471  -5.527 -43.791  1.00 83.01           C  
ANISOU 4706  C   ASN B 359     7074  12437  12028  -2015  -3340   3913       C  
ATOM   4707  O   ASN B 359      13.388  -5.652 -44.375  1.00100.36           O  
ANISOU 4707  O   ASN B 359     9086  14781  14265  -2191  -3567   4199       O  
ATOM   4708  CB  ASN B 359      15.131  -3.184 -43.192  1.00 68.73           C  
ANISOU 4708  CB  ASN B 359     5136  10586  10393  -1494  -2910   3889       C  
ATOM   4709  CG  ASN B 359      14.289  -2.660 -44.332  1.00 83.75           C  
ANISOU 4709  CG  ASN B 359     6868  12646  12306  -1576  -3127   4171       C  
ATOM   4710  OD1 ASN B 359      13.165  -2.205 -44.126  1.00 96.44           O  
ANISOU 4710  OD1 ASN B 359     8163  14386  14093  -1534  -3124   4494       O  
ATOM   4711  ND2 ASN B 359      14.828  -2.720 -45.544  1.00 79.01           N  
ANISOU 4711  ND2 ASN B 359     6472  12036  11513  -1686  -3315   4064       N  
ATOM   4712  N   PHE B 360      15.538  -6.251 -44.121  1.00 71.75           N  
ANISOU 4712  N   PHE B 360     5983  10879  10399  -2099  -3377   3611       N  
ATOM   4713  CA  PHE B 360      15.506  -7.184 -45.243  1.00 79.71           C  
ANISOU 4713  CA  PHE B 360     7196  11890  11202  -2398  -3677   3588       C  
ATOM   4714  C   PHE B 360      15.203  -8.621 -44.843  1.00 83.90           C  
ANISOU 4714  C   PHE B 360     7811  12383  11682  -2629  -3784   3558       C  
ATOM   4715  O   PHE B 360      14.582  -9.350 -45.623  1.00 88.75           O  
ANISOU 4715  O   PHE B 360     8477  13053  12192  -2924  -4070   3682       O  
ATOM   4716  CB  PHE B 360      16.840  -7.141 -46.000  1.00 85.63           C  
ANISOU 4716  CB  PHE B 360     8286  12512  11737  -2361  -3662   3297       C  
ATOM   4717  CG  PHE B 360      17.123  -5.813 -46.652  1.00 92.24           C  
ANISOU 4717  CG  PHE B 360     9075  13391  12581  -2182  -3618   3333       C  
ATOM   4718  CD1 PHE B 360      18.064  -4.947 -46.117  1.00 87.94           C  
ANISOU 4718  CD1 PHE B 360     8557  12765  12091  -1900  -3343   3163       C  
ATOM   4719  CD2 PHE B 360      16.443  -5.431 -47.795  1.00 99.18           C  
ANISOU 4719  CD2 PHE B 360     9886  14391  13407  -2305  -3861   3544       C  
ATOM   4720  CE1 PHE B 360      18.325  -3.728 -46.719  1.00 86.77           C  
ANISOU 4720  CE1 PHE B 360     8374  12650  11943  -1738  -3303   3200       C  
ATOM   4721  CE2 PHE B 360      16.699  -4.216 -48.400  1.00 94.37           C  
ANISOU 4721  CE2 PHE B 360     9239  13821  12798  -2130  -3821   3581       C  
ATOM   4722  CZ  PHE B 360      17.640  -3.363 -47.862  1.00 87.14           C  
ANISOU 4722  CZ  PHE B 360     8355  12817  11937  -1843  -3537   3408       C  
ATOM   4723  N   LEU B 361      15.626  -9.052 -43.656  1.00 82.14           N  
ANISOU 4723  N   LEU B 361     7619  12068  11524  -2515  -3571   3400       N  
ATOM   4724  CA  LEU B 361      15.431 -10.423 -43.211  1.00 70.45           C  
ANISOU 4724  CA  LEU B 361     6237  10540   9992  -2711  -3650   3349       C  
ATOM   4725  C   LEU B 361      14.303 -10.560 -42.198  1.00 72.62           C  
ANISOU 4725  C   LEU B 361     6196  10915  10481  -2712  -3608   3583       C  
ATOM   4726  O   LEU B 361      14.117 -11.645 -41.635  1.00 72.99           O  
ANISOU 4726  O   LEU B 361     6293  10925  10514  -2845  -3639   3544       O  
ATOM   4727  CB  LEU B 361      16.733 -10.978 -42.633  1.00 65.74           C  
ANISOU 4727  CB  LEU B 361     5916   9767   9294  -2603  -3463   3002       C  
ATOM   4728  CG  LEU B 361      17.812 -11.266 -43.679  1.00 64.32           C  
ANISOU 4728  CG  LEU B 361     6088   9477   8873  -2670  -3539   2775       C  
ATOM   4729  CD1 LEU B 361      19.202 -11.320 -43.052  1.00 95.73           C  
ANISOU 4729  CD1 LEU B 361    10252  13310  12812  -2461  -3291   2468       C  
ATOM   4730  CD2 LEU B 361      17.508 -12.560 -44.419  1.00 67.39           C  
ANISOU 4730  CD2 LEU B 361     6702   9833   9072  -3008  -3804   2781       C  
ATOM   4731  N   SER B 362      13.550  -9.491 -41.948  1.00 74.21           N  
ANISOU 4731  N   SER B 362     6077  11239  10882  -2560  -3529   3832       N  
ATOM   4732  CA  SER B 362      12.394  -9.546 -41.058  1.00 76.90           C  
ANISOU 4732  CA  SER B 362     6090  11688  11440  -2551  -3487   4100       C  
ATOM   4733  C   SER B 362      11.277  -8.724 -41.684  1.00105.04           C  
ANISOU 4733  C   SER B 362     9338  15438  15134  -2578  -3618   4474       C  
ATOM   4734  O   SER B 362      11.380  -7.496 -41.766  1.00108.80           O  
ANISOU 4734  O   SER B 362     9705  15942  15694  -2350  -3475   4535       O  
ATOM   4735  CB  SER B 362      12.739  -9.027 -39.662  1.00 73.40           C  
ANISOU 4735  CB  SER B 362     5572  11171  11145  -2246  -3141   4004       C  
ATOM   4736  OG  SER B 362      11.569  -8.652 -38.954  1.00 76.40           O  
ANISOU 4736  OG  SER B 362     5597  11671  11760  -2172  -3065   4318       O  
ATOM   4737  N   GLY B 363      10.214  -9.398 -42.128  1.00105.89           N  
ANISOU 4737  N   GLY B 363     9298  15676  15260  -2863  -3892   4735       N  
ATOM   4738  CA  GLY B 363       9.090  -8.687 -42.708  1.00106.52           C  
ANISOU 4738  CA  GLY B 363     9045  15953  15477  -2905  -4038   5127       C  
ATOM   4739  C   GLY B 363       8.298  -7.880 -41.703  1.00103.95           C  
ANISOU 4739  C   GLY B 363     8337  15720  15440  -2655  -3799   5394       C  
ATOM   4740  O   GLY B 363       7.639  -6.908 -42.084  1.00107.66           O  
ANISOU 4740  O   GLY B 363     8539  16325  16040  -2560  -3808   5682       O  
ATOM   4741  N   LYS B 364       8.348  -8.259 -40.425  1.00 98.23           N  
ANISOU 4741  N   LYS B 364     7588  14921  14816  -2538  -3578   5310       N  
ATOM   4742  CA  LYS B 364       7.640  -7.488 -39.410  1.00 91.79           C  
ANISOU 4742  CA  LYS B 364     6443  14169  14266  -2281  -3318   5554       C  
ATOM   4743  C   LYS B 364       8.348  -6.171 -39.127  1.00 88.22           C  
ANISOU 4743  C   LYS B 364     6046  13627  13846  -1931  -3019   5431       C  
ATOM   4744  O   LYS B 364       7.697  -5.127 -38.994  1.00126.44           O  
ANISOU 4744  O   LYS B 364    10613  18558  18868  -1737  -2884   5710       O  
ATOM   4745  CB  LYS B 364       7.498  -8.319 -38.138  1.00 90.77           C  
ANISOU 4745  CB  LYS B 364     6294  13977  14217  -2271  -3178   5491       C  
ATOM   4746  CG  LYS B 364       6.409  -9.382 -38.223  1.00 95.74           C  
ANISOU 4746  CG  LYS B 364     6729  14740  14908  -2577  -3430   5747       C  
ATOM   4747  CD  LYS B 364       6.727 -10.564 -37.331  1.00 93.56           C  
ANISOU 4747  CD  LYS B 364     6615  14351  14580  -2661  -3379   5524       C  
ATOM   4748  CE  LYS B 364       5.657 -11.638 -37.430  1.00123.07           C  
ANISOU 4748  CE  LYS B 364    10169  18218  18374  -2987  -3638   5773       C  
ATOM   4749  NZ  LYS B 364       5.596 -12.254 -38.787  1.00101.39           N  
ANISOU 4749  NZ  LYS B 364     7572  15523  15429  -3348  -4026   5787       N  
ATOM   4750  N   PHE B 365       9.680  -6.203 -39.019  1.00 94.89           N  
ANISOU 4750  N   PHE B 365     7241  14294  14520  -1847  -2908   5028       N  
ATOM   4751  CA  PHE B 365      10.453  -4.969 -38.905  1.00 97.42           C  
ANISOU 4751  CA  PHE B 365     7649  14527  14840  -1558  -2666   4892       C  
ATOM   4752  C   PHE B 365      10.383  -4.156 -40.190  1.00 95.32           C  
ANISOU 4752  C   PHE B 365     7342  14350  14525  -1573  -2813   5012       C  
ATOM   4753  O   PHE B 365      10.300  -2.924 -40.151  1.00 94.00           O  
ANISOU 4753  O   PHE B 365     7053  14203  14461  -1337  -2639   5128       O  
ATOM   4754  CB  PHE B 365      11.916  -5.291 -38.589  1.00 93.07           C  
ANISOU 4754  CB  PHE B 365     7473  13780  14111  -1505  -2556   4448       C  
ATOM   4755  CG  PHE B 365      12.214  -5.450 -37.129  1.00 85.07           C  
ANISOU 4755  CG  PHE B 365     6497  12653  13172  -1342  -2291   4311       C  
ATOM   4756  CD1 PHE B 365      12.209  -4.361 -36.275  1.00 80.69           C  
ANISOU 4756  CD1 PHE B 365     5850  12055  12755  -1056  -1996   4363       C  
ATOM   4757  CD2 PHE B 365      12.538  -6.695 -36.617  1.00 77.21           C  
ANISOU 4757  CD2 PHE B 365     5655  11585  12096  -1478  -2336   4122       C  
ATOM   4758  CE1 PHE B 365      12.510  -4.515 -34.929  1.00 72.17           C  
ANISOU 4758  CE1 PHE B 365     4832  10864  11727   -918  -1763   4229       C  
ATOM   4759  CE2 PHE B 365      12.837  -6.858 -35.276  1.00 66.99           C  
ANISOU 4759  CE2 PHE B 365     4404  10189  10862  -1332  -2104   3991       C  
ATOM   4760  CZ  PHE B 365      12.823  -5.768 -34.429  1.00 66.06           C  
ANISOU 4760  CZ  PHE B 365     4194  10029  10874  -1058  -1824   4043       C  
ATOM   4761  N   ARG B 366      10.405  -4.840 -41.335  1.00 89.47           N  
ANISOU 4761  N   ARG B 366     6715  13658  13621  -1852  -3133   4989       N  
ATOM   4762  CA  ARG B 366      10.390  -4.166 -42.629  1.00 84.97           C  
ANISOU 4762  CA  ARG B 366     6140  13170  12975  -1891  -3306   5083       C  
ATOM   4763  C   ARG B 366       9.183  -3.248 -42.767  1.00 89.78           C  
ANISOU 4763  C   ARG B 366     6352  13963  13797  -1796  -3305   5516       C  
ATOM   4764  O   ARG B 366       9.327  -2.058 -43.069  1.00 94.35           O  
ANISOU 4764  O   ARG B 366     6873  14558  14418  -1583  -3187   5574       O  
ATOM   4765  CB  ARG B 366      10.382  -5.220 -43.734  1.00 86.98           C  
ANISOU 4765  CB  ARG B 366     6568  13454  13027  -2248  -3674   5039       C  
ATOM   4766  CG  ARG B 366      10.550  -4.724 -45.154  1.00 88.56           C  
ANISOU 4766  CG  ARG B 366     6854  13710  13087  -2328  -3888   5068       C  
ATOM   4767  CD  ARG B 366      10.190  -5.868 -46.092  1.00 93.93           C  
ANISOU 4767  CD  ARG B 366     7657  14437  13594  -2722  -4270   5113       C  
ATOM   4768  NE  ARG B 366      11.188  -6.936 -46.040  1.00102.24           N  
ANISOU 4768  NE  ARG B 366     9100  15311  14437  -2846  -4280   4749       N  
ATOM   4769  CZ  ARG B 366      10.979  -8.189 -46.438  1.00116.56           C  
ANISOU 4769  CZ  ARG B 366    11077  17109  16103  -3178  -4536   4728       C  
ATOM   4770  NH1 ARG B 366       9.801  -8.557 -46.926  1.00127.20           N  
ANISOU 4770  NH1 ARG B 366    12231  18614  17486  -3448  -4828   5050       N  
ATOM   4771  NH2 ARG B 366      11.953  -9.084 -46.339  1.00116.00           N  
ANISOU 4771  NH2 ARG B 366    11367  16861  15847  -3245  -4499   4396       N  
ATOM   4772  N   GLU B 367       7.972  -3.774 -42.539  1.00 94.41           N  
ANISOU 4772  N   GLU B 367     6649  14694  14529  -1943  -3428   5841       N  
ATOM   4773  CA  GLU B 367       6.794  -2.917 -42.676  1.00 99.49           C  
ANISOU 4773  CA  GLU B 367     6884  15526  15392  -1845  -3422   6291       C  
ATOM   4774  C   GLU B 367       6.769  -1.828 -41.605  1.00 97.94           C  
ANISOU 4774  C   GLU B 367     6548  15275  15390  -1457  -3008   6358       C  
ATOM   4775  O   GLU B 367       6.245  -0.738 -41.844  1.00100.61           O  
ANISOU 4775  O   GLU B 367     6655  15711  15863  -1272  -2918   6631       O  
ATOM   4776  CB  GLU B 367       5.513  -3.757 -42.651  1.00105.12           C  
ANISOU 4776  CB  GLU B 367     7302  16411  16226  -2100  -3649   6643       C  
ATOM   4777  CG  GLU B 367       4.273  -2.938 -42.993  1.00145.06           C  
ANISOU 4777  CG  GLU B 367    11918  21693  21504  -2034  -3697   7148       C  
ATOM   4778  CD  GLU B 367       3.008  -3.764 -42.993  1.00151.05           C  
ANISOU 4778  CD  GLU B 367    12362  22637  22393  -2303  -3940   7522       C  
ATOM   4779  OE1 GLU B 367       3.088  -4.973 -42.682  1.00149.50           O  
ANISOU 4779  OE1 GLU B 367    12303  22385  22115  -2537  -4060   7375       O  
ATOM   4780  OE2 GLU B 367       1.940  -3.208 -43.319  1.00122.82           O  
ANISOU 4780  OE2 GLU B 367     8397  19265  19003  -2284  -4016   7971       O  
ATOM   4781  N   GLN B 368       7.302  -2.119 -40.410  1.00 93.98           N  
ANISOU 4781  N   GLN B 368     6190  14615  14902  -1332  -2754   6124       N  
ATOM   4782  CA  GLN B 368       7.400  -1.095 -39.382  1.00 94.89           C  
ANISOU 4782  CA  GLN B 368     6244  14645  15165   -975  -2358   6146       C  
ATOM   4783  C   GLN B 368       8.379  -0.023 -39.799  1.00 93.25           C  
ANISOU 4783  C   GLN B 368     6244  14335  14852   -782  -2230   5934       C  
ATOM   4784  O   GLN B 368       8.188   1.155 -39.466  1.00 93.49           O  
ANISOU 4784  O   GLN B 368     6154  14356  15010   -502  -1972   6082       O  
ATOM   4785  CB  GLN B 368       7.800  -1.702 -38.047  1.00 94.25           C  
ANISOU 4785  CB  GLN B 368     6300  14415  15097   -912  -2149   5926       C  
ATOM   4786  CG  GLN B 368       6.649  -2.357 -37.317  1.00 97.71           C  
ANISOU 4786  CG  GLN B 368     6451  14951  15722   -977  -2145   6220       C  
ATOM   4787  CD  GLN B 368       5.665  -1.341 -36.817  1.00101.38           C  
ANISOU 4787  CD  GLN B 368     6576  15499  16443   -716  -1898   6620       C  
ATOM   4788  OE1 GLN B 368       6.042  -0.441 -36.079  1.00104.19           O  
ANISOU 4788  OE1 GLN B 368     7007  15732  16849   -420  -1563   6548       O  
ATOM   4789  NE2 GLN B 368       4.396  -1.476 -37.200  1.00107.61           N  
ANISOU 4789  NE2 GLN B 368     6995  16497  17397   -824  -2054   7057       N  
ATOM   4790  N   PHE B 369       9.439  -0.409 -40.503  1.00 91.55           N  
ANISOU 4790  N   PHE B 369     6346  14034  14405   -919  -2389   5594       N  
ATOM   4791  CA  PHE B 369      10.290   0.601 -41.106  1.00 92.04           C  
ANISOU 4791  CA  PHE B 369     6574  14028  14368   -766  -2318   5435       C  
ATOM   4792  C   PHE B 369       9.605   1.257 -42.295  1.00 93.56           C  
ANISOU 4792  C   PHE B 369     6566  14392  14591   -792  -2503   5732       C  
ATOM   4793  O   PHE B 369       9.858   2.433 -42.579  1.00 90.46           O  
ANISOU 4793  O   PHE B 369     6172  13983  14216   -575  -2366   5760       O  
ATOM   4794  CB  PHE B 369      11.633  -0.009 -41.524  1.00 88.77           C  
ANISOU 4794  CB  PHE B 369     6547  13475  13706   -893  -2422   5006       C  
ATOM   4795  CG  PHE B 369      12.402  -0.624 -40.384  1.00 82.10           C  
ANISOU 4795  CG  PHE B 369     5906  12465  12824   -857  -2246   4707       C  
ATOM   4796  CD1 PHE B 369      12.299  -0.109 -39.098  1.00 87.13           C  
ANISOU 4796  CD1 PHE B 369     6469  13030  13608   -626  -1934   4734       C  
ATOM   4797  CD2 PHE B 369      13.230  -1.713 -40.596  1.00 78.25           C  
ANISOU 4797  CD2 PHE B 369     5693  11891  12149  -1047  -2387   4407       C  
ATOM   4798  CE1 PHE B 369      13.003  -0.672 -38.053  1.00 87.77           C  
ANISOU 4798  CE1 PHE B 369     6737  12965  13646   -599  -1791   4465       C  
ATOM   4799  CE2 PHE B 369      13.937  -2.281 -39.553  1.00 83.32           C  
ANISOU 4799  CE2 PHE B 369     6508  12391  12759  -1007  -2231   4147       C  
ATOM   4800  CZ  PHE B 369      13.823  -1.760 -38.281  1.00 87.10           C  
ANISOU 4800  CZ  PHE B 369     6903  12809  13383   -788  -1944   4175       C  
ATOM   4801  N   LYS B 370       8.716   0.531 -42.976  1.00 99.18           N  
ANISOU 4801  N   LYS B 370     7104  15269  15310  -1056  -2817   5970       N  
ATOM   4802  CA  LYS B 370       7.944   1.133 -44.058  1.00100.88           C  
ANISOU 4802  CA  LYS B 370     7091  15669  15570  -1089  -3014   6299       C  
ATOM   4803  C   LYS B 370       6.966   2.168 -43.522  1.00100.43           C  
ANISOU 4803  C   LYS B 370     6666  15714  15778   -822  -2777   6693       C  
ATOM   4804  O   LYS B 370       6.888   3.287 -44.037  1.00119.28           O  
ANISOU 4804  O   LYS B 370     8967  18149  18204   -633  -2711   6833       O  
ATOM   4805  CB  LYS B 370       7.205   0.053 -44.853  1.00102.52           C  
ANISOU 4805  CB  LYS B 370     7205  16030  15720  -1466  -3424   6471       C  
ATOM   4806  CG  LYS B 370       7.921  -0.377 -46.123  1.00102.19           C  
ANISOU 4806  CG  LYS B 370     7468  15958  15403  -1696  -3730   6240       C  
ATOM   4807  CD  LYS B 370       7.027  -1.235 -47.017  1.00110.24           C  
ANISOU 4807  CD  LYS B 370     8371  17146  16369  -2068  -4153   6483       C  
ATOM   4808  CE  LYS B 370       6.803  -2.635 -46.461  1.00113.02           C  
ANISOU 4808  CE  LYS B 370     8776  17465  16699  -2328  -4256   6423       C  
ATOM   4809  NZ  LYS B 370       5.951  -3.460 -47.369  1.00111.48           N  
ANISOU 4809  NZ  LYS B 370     8495  17426  16437  -2720  -4686   6661       N  
ATOM   4810  N   ALA B 371       6.209   1.811 -42.480  1.00102.12           N  
ANISOU 4810  N   ALA B 371     6666  15956  16178   -788  -2634   6885       N  
ATOM   4811  CA  ALA B 371       5.250   2.759 -41.925  1.00105.86           C  
ANISOU 4811  CA  ALA B 371     6792  16518  16912   -518  -2377   7284       C  
ATOM   4812  C   ALA B 371       5.963   3.958 -41.320  1.00120.87           C  
ANISOU 4812  C   ALA B 371     8846  18248  18830   -153  -1981   7126       C  
ATOM   4813  O   ALA B 371       5.470   5.090 -41.404  1.00131.20           O  
ANISOU 4813  O   ALA B 371     9960  19614  20274     95  -1802   7404       O  
ATOM   4814  CB  ALA B 371       4.369   2.074 -40.881  1.00130.23           C  
ANISOU 4814  CB  ALA B 371     9646  19649  20185   -550  -2287   7502       C  
ATOM   4815  N   ALA B 372       7.124   3.725 -40.706  1.00111.22           N  
ANISOU 4815  N   ALA B 372     7977  16815  17469   -119  -1840   6690       N  
ATOM   4816  CA  ALA B 372       7.886   4.799 -40.083  1.00107.00           C  
ANISOU 4816  CA  ALA B 372     7624  16102  16930    191  -1482   6512       C  
ATOM   4817  C   ALA B 372       8.414   5.810 -41.091  1.00108.56           C  
ANISOU 4817  C   ALA B 372     7921  16297  17031    295  -1515   6459       C  
ATOM   4818  O   ALA B 372       8.617   6.973 -40.727  1.00110.95           O  
ANISOU 4818  O   ALA B 372     8256  16507  17392    587  -1213   6483       O  
ATOM   4819  CB  ALA B 372       9.053   4.219 -39.280  1.00101.25           C  
ANISOU 4819  CB  ALA B 372     7245  15164  16060    158  -1383   6058       C  
ATOM   4820  N   PHE B 373       8.638   5.408 -42.346  1.00108.70           N  
ANISOU 4820  N   PHE B 373     8004  16401  16896     69  -1866   6391       N  
ATOM   4821  CA  PHE B 373       9.204   6.357 -43.293  1.00106.47           C  
ANISOU 4821  CA  PHE B 373     7840  16104  16511    179  -1895   6322       C  
ATOM   4822  C   PHE B 373       8.176   7.369 -43.784  1.00103.94           C  
ANISOU 4822  C   PHE B 373     7198  15944  16351    352  -1861   6763       C  
ATOM   4823  O   PHE B 373       8.555   8.474 -44.183  1.00 97.32           O  
ANISOU 4823  O   PHE B 373     6434  15058  15487    565  -1739   6752       O  
ATOM   4824  CB  PHE B 373       9.786   5.613 -44.500  1.00111.74           C  
ANISOU 4824  CB  PHE B 373     8705  16802  16948   -105  -2274   6112       C  
ATOM   4825  CG  PHE B 373      11.149   5.019 -44.262  1.00113.43           C  
ANISOU 4825  CG  PHE B 373     9304  16826  16968   -187  -2256   5637       C  
ATOM   4826  CD1 PHE B 373      12.214   5.811 -43.877  1.00110.72           C  
ANISOU 4826  CD1 PHE B 373     9189  16306  16572     30  -2001   5377       C  
ATOM   4827  CD2 PHE B 373      11.372   3.667 -44.487  1.00116.19           C  
ANISOU 4827  CD2 PHE B 373     9789  17174  17183   -488  -2504   5465       C  
ATOM   4828  CE1 PHE B 373      13.466   5.260 -43.667  1.00104.80           C  
ANISOU 4828  CE1 PHE B 373     8765  15397  15658    -48  -1991   4970       C  
ATOM   4829  CE2 PHE B 373      12.619   3.109 -44.285  1.00110.33           C  
ANISOU 4829  CE2 PHE B 373     9386  16263  16271   -548  -2476   5054       C  
ATOM   4830  CZ  PHE B 373      13.669   3.906 -43.877  1.00104.43           C  
ANISOU 4830  CZ  PHE B 373     8835  15357  15488   -327  -2223   4812       C  
ATOM   4831  N   SER B 374       6.891   7.016 -43.777  1.00114.60           N  
ANISOU 4831  N   SER B 374     8189  17484  17870    267  -1969   7162       N  
ATOM   4832  CA  SER B 374       5.831   7.974 -44.072  1.00126.33           C  
ANISOU 4832  CA  SER B 374     9325  19130  19546    462  -1891   7631       C  
ATOM   4833  C   SER B 374       5.311   8.659 -42.814  1.00132.13           C  
ANISOU 4833  C   SER B 374     9902  19800  20503    778  -1445   7842       C  
ATOM   4834  O   SER B 374       5.059   9.870 -42.814  1.00135.16           O  
ANISOU 4834  O   SER B 374    10189  20177  20988   1079  -1194   8050       O  
ATOM   4835  CB  SER B 374       4.675   7.282 -44.794  1.00128.74           C  
ANISOU 4835  CB  SER B 374     9295  19694  19927    200  -2257   8001       C  
ATOM   4836  OG  SER B 374       5.027   6.946 -46.122  1.00127.74           O  
ANISOU 4836  OG  SER B 374     9301  19638  19595    -43  -2656   7883       O  
ATOM   4837  N   TRP B 375       5.157   7.872 -41.748  1.00135.76           N  
ANISOU 4837  N   TRP B 375    10355  20200  21029    713  -1339   7788       N  
ATOM   4838  CA  TRP B 375       4.587   8.337 -40.490  1.00144.65           C  
ANISOU 4838  CA  TRP B 375    11339  21260  22360    985   -928   8000       C  
ATOM   4839  C   TRP B 375       5.394   9.473 -39.873  1.00145.83           C  
ANISOU 4839  C   TRP B 375    11755  21183  22472   1311   -525   7795       C  
ATOM   4840  O   TRP B 375       4.812  10.374 -39.256  1.00141.47           O  
ANISOU 4840  O   TRP B 375    11065  20600  22088   1616   -165   8075       O  
ATOM   4841  CB  TRP B 375       4.476   7.119 -39.563  1.00150.72           C  
ANISOU 4841  CB  TRP B 375    12124  21990  23151    810   -952   7895       C  
ATOM   4842  CG  TRP B 375       4.069   7.288 -38.116  1.00154.33           C  
ANISOU 4842  CG  TRP B 375    12518  22340  23778   1041   -551   8017       C  
ATOM   4843  CD1 TRP B 375       4.907   7.329 -37.038  1.00149.18           C  
ANISOU 4843  CD1 TRP B 375    12176  21451  23054   1163   -278   7680       C  
ATOM   4844  CD2 TRP B 375       2.733   7.322 -37.583  1.00159.30           C  
ANISOU 4844  CD2 TRP B 375    12760  23097  24670   1153   -401   8508       C  
ATOM   4845  NE1 TRP B 375       4.182   7.432 -35.875  1.00149.52           N  
ANISOU 4845  NE1 TRP B 375    12072  21453  23286   1355     44   7920       N  
ATOM   4846  CE2 TRP B 375       2.847   7.430 -36.180  1.00155.87           C  
ANISOU 4846  CE2 TRP B 375    12447  22476  24302   1361    -13   8432       C  
ATOM   4847  CE3 TRP B 375       1.456   7.299 -38.155  1.00164.68           C  
ANISOU 4847  CE3 TRP B 375    12998  24033  25540   1102   -554   9020       C  
ATOM   4848  CZ2 TRP B 375       1.733   7.514 -35.342  1.00158.18           C  
ANISOU 4848  CZ2 TRP B 375    12446  22815  24841   1535    247   8847       C  
ATOM   4849  CZ3 TRP B 375       0.348   7.382 -37.317  1.00169.60           C  
ANISOU 4849  CZ3 TRP B 375    13302  24716  26422   1271   -301   9446       C  
ATOM   4850  CH2 TRP B 375       0.497   7.488 -35.928  1.00165.74           C  
ANISOU 4850  CH2 TRP B 375    12957  24024  25991   1493    105   9355       C  
ATOM   4851  N   TRP B 376       6.720   9.460 -40.023  1.00152.21           N  
ANISOU 4851  N   TRP B 376    12946  21824  23062   1256   -567   7328       N  
ATOM   4852  CA  TRP B 376       7.540  10.510 -39.424  1.00153.91           C  
ANISOU 4852  CA  TRP B 376    13424  21818  23237   1534   -203   7136       C  
ATOM   4853  C   TRP B 376       8.300  11.333 -40.456  1.00150.33           C  
ANISOU 4853  C   TRP B 376    13133  21336  22651   1590   -278   7013       C  
ATOM   4854  O   TRP B 376       8.373  12.559 -40.334  1.00154.85           O  
ANISOU 4854  O   TRP B 376    13740  21821  23275   1877     22   7130       O  
ATOM   4855  CB  TRP B 376       8.522   9.878 -38.418  1.00156.22           C  
ANISOU 4855  CB  TRP B 376    14033  21908  23415   1461   -111   6710       C  
ATOM   4856  CG  TRP B 376       9.399  10.847 -37.664  1.00164.79           C  
ANISOU 4856  CG  TRP B 376    15397  22756  24460   1708    255   6519       C  
ATOM   4857  CD1 TRP B 376       9.009  11.645 -36.629  1.00170.45           C  
ANISOU 4857  CD1 TRP B 376    16095  23359  25311   1997    683   6710       C  
ATOM   4858  CD2 TRP B 376      10.802  11.094 -37.852  1.00167.04           C  
ANISOU 4858  CD2 TRP B 376    16029  22881  24557   1681    236   6117       C  
ATOM   4859  NE1 TRP B 376      10.071  12.383 -36.170  1.00171.00           N  
ANISOU 4859  NE1 TRP B 376    16489  23203  25279   2140    922   6444       N  
ATOM   4860  CE2 TRP B 376      11.183  12.066 -36.904  1.00167.58           C  
ANISOU 4860  CE2 TRP B 376    16268  22746  24658   1947    647   6086       C  
ATOM   4861  CE3 TRP B 376      11.768  10.599 -38.732  1.00164.44           C  
ANISOU 4861  CE3 TRP B 376    15886  22556  24037   1462    -74   5799       C  
ATOM   4862  CZ2 TRP B 376      12.487  12.552 -36.811  1.00162.63           C  
ANISOU 4862  CZ2 TRP B 376    15970  21932  23890   1985    732   5752       C  
ATOM   4863  CZ3 TRP B 376      13.066  11.085 -38.639  1.00158.79           C  
ANISOU 4863  CZ3 TRP B 376    15483  21658  23190   1516     24   5479       C  
ATOM   4864  CH2 TRP B 376      13.411  12.051 -37.685  1.00158.36           C  
ANISOU 4864  CH2 TRP B 376    15571  21414  23183   1767    412   5461       C  
ATOM   4865  N   LEU B 377       8.872  10.681 -41.477  1.00146.75           N  
ANISOU 4865  N   LEU B 377    12796  20941  22021   1327   -659   6786       N  
ATOM   4866  CA  LEU B 377       9.671  11.292 -42.538  1.00145.94           C  
ANISOU 4866  CA  LEU B 377    12870  20812  21769   1344   -778   6643       C  
ATOM   4867  C   LEU B 377       8.837  11.613 -43.779  1.00144.68           C  
ANISOU 4867  C   LEU B 377    12451  20870  21650   1324  -1016   6991       C  
ATOM   4868  O   LEU B 377       7.617  11.406 -43.773  1.00148.47           O  
ANISOU 4868  O   LEU B 377    12591  21529  22292   1302  -1076   7362       O  
ATOM   4869  CB  LEU B 377      10.850  10.379 -42.877  1.00145.69           C  
ANISOU 4869  CB  LEU B 377    13148  20696  21510   1086  -1025   6192       C  
ATOM   4870  CG  LEU B 377      11.998  10.526 -41.873  1.00137.36           C  
ANISOU 4870  CG  LEU B 377    12401  19400  20388   1176   -763   5834       C  
ATOM   4871  CD1 LEU B 377      12.810   9.243 -41.746  1.00131.57           C  
ANISOU 4871  CD1 LEU B 377    11884  18609  19496    907   -967   5454       C  
ATOM   4872  CD2 LEU B 377      12.894  11.712 -42.220  1.00131.65           C  
ANISOU 4872  CD2 LEU B 377    11879  18546  19595   1371   -604   5729       C  
ATOM   4873  N   PRO B 378       9.452  12.131 -44.863  1.00139.81           N  
ANISOU 4873  N   PRO B 378    11977  20250  20894   1332  -1162   6902       N  
ATOM   4874  CA  PRO B 378       8.692  12.474 -46.071  1.00143.42           C  
ANISOU 4874  CA  PRO B 378    12206  20913  21374   1320  -1406   7233       C  
ATOM   4875  C   PRO B 378       7.869  11.312 -46.614  1.00140.33           C  
ANISOU 4875  C   PRO B 378    11600  20735  20983    998  -1805   7382       C  
ATOM   4876  O   PRO B 378       7.005  11.556 -47.456  1.00139.21           O  
ANISOU 4876  O   PRO B 378    11199  20792  20901    982  -2002   7732       O  
ATOM   4877  CB  PRO B 378       9.785  12.874 -47.076  1.00141.76           C  
ANISOU 4877  CB  PRO B 378    12292  20621  20949   1310  -1544   6984       C  
ATOM   4878  CG  PRO B 378      11.040  12.264 -46.552  1.00132.46           C  
ANISOU 4878  CG  PRO B 378    11459  19248  19621   1191  -1503   6511       C  
ATOM   4879  CD  PRO B 378      10.899  12.327 -45.063  1.00130.80           C  
ANISOU 4879  CD  PRO B 378    11218  18922  19558   1330  -1143   6493       C  
TER    4880      PRO B 378                                                      
HETATM 4881  C1  NVK A 401      36.362 -25.647 -18.023  1.00 82.45           C  
HETATM 4882  C10 NVK A 401      36.779 -36.448 -17.167  1.00 68.31           C  
HETATM 4883  C11 NVK A 401      36.432 -37.367 -16.130  1.00 66.43           C  
HETATM 4884  C12 NVK A 401      36.701 -38.739 -16.313  1.00 66.79           C  
HETATM 4885  C13 NVK A 401      37.592 -38.321 -18.391  1.00 69.06           C  
HETATM 4886  C14 NVK A 401      37.365 -36.941 -18.302  1.00 73.27           C  
HETATM 4887  C15 NVK A 401      36.362 -39.651 -15.296  1.00 68.73           C  
HETATM 4888  C16 NVK A 401      35.783 -39.183 -14.165  1.00 65.14           C  
HETATM 4889  C17 NVK A 401      35.542 -37.802 -14.047  1.00 62.86           C  
HETATM 4890  C2  NVK A 401      36.518 -27.106 -18.194  1.00 74.84           C  
HETATM 4891  C3  NVK A 401      36.943 -29.081 -18.932  1.00 75.70           C  
HETATM 4892  C4  NVK A 401      36.418 -29.222 -17.666  1.00 72.55           C  
HETATM 4893  C5  NVK A 401      36.241 -30.448 -17.076  1.00 63.18           C  
HETATM 4894  C6  NVK A 401      36.611 -31.568 -17.805  1.00 61.41           C  
HETATM 4895  C7  NVK A 401      37.146 -31.441 -19.090  1.00 68.11           C  
HETATM 4896  C8  NVK A 401      37.314 -30.202 -19.660  1.00 73.11           C  
HETATM 4897  C9  NVK A 401      36.760 -34.049 -17.771  1.00 58.52           C  
HETATM 4898  N1  NVK A 401      36.991 -27.709 -19.235  1.00 73.91           N  
HETATM 4899  N2  NVK A 401      36.440 -32.835 -17.218  1.00 57.66           N  
HETATM 4900  N3  NVK A 401      36.494 -35.100 -16.942  1.00 56.21           N  
HETATM 4901  N4  NVK A 401      37.289 -39.208 -17.465  1.00 70.21           N  
HETATM 4902  N5  NVK A 401      35.845 -36.918 -14.975  1.00 64.51           N  
HETATM 4903  O1  NVK A 401      36.142 -27.952 -17.185  1.00 70.27           O  
HETATM 4904  O2  NVK A 401      37.241 -34.187 -18.888  1.00 62.99           O  
HETATM 4905  H3  NVK A 401      37.040 -25.185 -18.532  1.00100.87           H  
HETATM 4906  H1  NVK A 401      36.454 -25.418 -17.090  1.00100.87           H  
HETATM 4907  H2  NVK A 401      35.490 -25.375 -18.333  1.00100.87           H  
HETATM 4908  H9  NVK A 401      38.000 -38.640 -19.188  1.00 84.79           H  
HETATM 4909  H10 NVK A 401      37.609 -36.356 -19.010  1.00 89.84           H  
HETATM 4910  H11 NVK A 401      36.538 -40.573 -15.409  1.00 84.40           H  
HETATM 4911  H12 NVK A 401      35.544 -39.770 -13.468  1.00 80.10           H  
HETATM 4912  H13 NVK A 401      35.140 -37.487 -13.255  1.00 77.35           H  
HETATM 4913  H4  NVK A 401      35.879 -30.530 -16.204  1.00 77.74           H  
HETATM 4914  H5  NVK A 401      37.394 -32.213 -19.573  1.00 83.65           H  
HETATM 4915  H6  NVK A 401      37.674 -30.117 -20.527  1.00 89.66           H  
HETATM 4916  H7  NVK A 401      36.090 -32.848 -16.411  1.00 71.12           H  
HETATM 4917  H8  NVK A 401      36.106 -34.934 -16.190  1.00 69.38           H  
HETATM 4918  C1  NVK A 402      38.324 -38.362 -12.064  1.00 84.35           C  
HETATM 4919  C10 NVK A 402      39.684 -28.244 -15.679  1.00 79.44           C  
HETATM 4920  C11 NVK A 402      39.372 -26.942 -15.179  1.00 79.31           C  
HETATM 4921  C12 NVK A 402      39.601 -25.818 -16.001  1.00 85.32           C  
HETATM 4922  C13 NVK A 402      40.381 -27.169 -17.687  1.00 95.29           C  
HETATM 4923  C14 NVK A 402      40.189 -28.345 -16.946  1.00 86.77           C  
HETATM 4924  C15 NVK A 402      39.296 -24.533 -15.515  1.00 90.07           C  
HETATM 4925  C16 NVK A 402      38.790 -24.409 -14.266  1.00 91.59           C  
HETATM 4926  C17 NVK A 402      38.589 -25.570 -13.498  1.00 87.96           C  
HETATM 4927  C2  NVK A 402      38.646 -37.102 -12.761  1.00 84.02           C  
HETATM 4928  C3  NVK A 402      39.320 -35.621 -14.160  1.00 80.65           C  
HETATM 4929  C4  NVK A 402      38.760 -34.949 -13.094  1.00 81.17           C  
HETATM 4930  C5  NVK A 402      38.697 -33.579 -13.044  1.00 84.76           C  
HETATM 4931  C6  NVK A 402      39.221 -32.884 -14.124  1.00 88.15           C  
HETATM 4932  C7  NVK A 402      39.792 -33.548 -15.209  1.00 89.61           C  
HETATM 4933  C8  NVK A 402      39.846 -34.918 -15.235  1.00 86.01           C  
HETATM 4934  C9  NVK A 402      39.629 -30.652 -15.115  1.00 85.61           C  
HETATM 4935  N1  NVK A 402      39.230 -36.999 -13.907  1.00 80.90           N  
HETATM 4936  N2  NVK A 402      39.179 -31.482 -14.121  1.00 89.14           N  
HETATM 4937  N3  NVK A 402      39.435 -29.330 -14.836  1.00 82.58           N  
HETATM 4938  N4  NVK A 402      40.114 -25.948 -17.270  1.00 91.29           N  
HETATM 4939  N5  NVK A 402      38.859 -26.790 -13.917  1.00 83.16           N  
HETATM 4940  O1  NVK A 402      38.325 -35.902 -12.185  1.00 82.64           O  
HETATM 4941  O2  NVK A 402      40.150 -31.042 -16.152  1.00 84.06           O  
HETATM 4942  H3  NVK A 402      38.148 -39.056 -12.711  1.00103.14           H  
HETATM 4943  H1  NVK A 402      37.544 -38.237 -11.510  1.00103.14           H  
HETATM 4944  H2  NVK A 402      39.069 -38.625 -11.509  1.00103.14           H  
HETATM 4945  H9  NVK A 402      40.734 -27.266 -18.563  1.00116.28           H  
HETATM 4946  H10 NVK A 402      40.403 -29.196 -17.311  1.00106.05           H  
HETATM 4947  H11 NVK A 402      39.446 -23.773 -16.059  1.00110.01           H  
HETATM 4948  H12 NVK A 402      38.575 -23.562 -13.915  1.00111.83           H  
HETATM 4949  H13 NVK A 402      38.239 -25.473 -12.628  1.00107.48           H  
HETATM 4950  H4  NVK A 402      38.314 -33.124 -12.305  1.00103.64           H  
HETATM 4951  H5  NVK A 402      40.144 -33.054 -15.932  1.00109.46           H  
HETATM 4952  H6  NVK A 402      40.232 -35.371 -15.966  1.00105.14           H  
HETATM 4953  H7  NVK A 402      38.829 -31.101 -13.411  1.00108.89           H  
HETATM 4954  H8  NVK A 402      39.124 -29.121 -14.060  1.00101.03           H  
HETATM 4955  S   SO4 A 403      24.192  -6.737   2.653  1.00110.86           S  
HETATM 4956  O1  SO4 A 403      23.518  -5.555   2.125  1.00108.54           O  
HETATM 4957  O2  SO4 A 403      25.441  -6.955   1.929  1.00111.54           O  
HETATM 4958  O3  SO4 A 403      23.329  -7.904   2.490  1.00113.22           O  
HETATM 4959  O4  SO4 A 403      24.478  -6.535   4.070  1.00107.98           O  
HETATM 4960  C1  SOG A 404      36.152 -61.118 -19.207  1.00 64.38           C  
HETATM 4961  C2  SOG A 404      36.340 -59.670 -19.623  1.00 63.87           C  
HETATM 4962  C3  SOG A 404      35.053 -58.914 -19.309  1.00 68.54           C  
HETATM 4963  C4  SOG A 404      33.830 -59.608 -19.891  1.00 69.88           C  
HETATM 4964  C5  SOG A 404      33.840 -61.126 -19.659  1.00 69.02           C  
HETATM 4965  C6  SOG A 404      32.792 -61.845 -20.491  1.00 71.61           C  
HETATM 4966  C1' SOG A 404      38.347 -61.727 -20.884  1.00 44.29           C  
HETATM 4967  C2' SOG A 404      39.568 -62.599 -21.068  1.00 27.80           C  
HETATM 4968  C3' SOG A 404      40.270 -62.392 -22.389  1.00 26.30           C  
HETATM 4969  C4' SOG A 404      41.140 -61.157 -22.442  1.00 33.37           C  
HETATM 4970  C5' SOG A 404      42.071 -61.131 -23.634  1.00 35.62           C  
HETATM 4971  C6' SOG A 404      42.998 -59.940 -23.705  1.00 45.29           C  
HETATM 4972  C7' SOG A 404      43.956 -59.981 -24.872  1.00 50.57           C  
HETATM 4973  C8' SOG A 404      44.965 -61.104 -24.808  1.00 55.10           C  
HETATM 4974  S1  SOG A 404      37.654 -62.133 -19.249  1.00 59.61           S  
HETATM 4975  O2  SOG A 404      37.410 -59.073 -18.899  1.00 61.01           O  
HETATM 4976  O3  SOG A 404      35.130 -57.566 -19.771  1.00 73.30           O  
HETATM 4977  O4  SOG A 404      32.640 -59.065 -19.319  1.00 70.80           O  
HETATM 4978  O5  SOG A 404      35.119 -61.690 -19.995  1.00 66.64           O  
HETATM 4979  O6  SOG A 404      32.940 -63.262 -20.433  1.00 74.84           O  
HETATM 4980  C1  SOG A 405      35.703 -32.563 -34.367  1.00126.20           C  
HETATM 4981  C2  SOG A 405      37.145 -32.266 -34.746  1.00119.30           C  
HETATM 4982  C3  SOG A 405      37.256 -30.844 -35.287  1.00117.59           C  
HETATM 4983  C4  SOG A 405      36.251 -30.609 -36.395  1.00120.88           C  
HETATM 4984  C5  SOG A 405      34.853 -30.996 -35.934  1.00124.82           C  
HETATM 4985  C6  SOG A 405      33.825 -30.886 -37.045  1.00123.17           C  
HETATM 4986  C1' SOG A 405      37.199 -34.966 -33.925  1.00132.56           C  
HETATM 4987  C2' SOG A 405      37.022 -36.373 -33.405  1.00131.16           C  
HETATM 4988  C3' SOG A 405      35.938 -36.452 -32.362  1.00127.42           C  
HETATM 4989  C4' SOG A 405      35.344 -37.825 -32.225  1.00127.05           C  
HETATM 4990  C5' SOG A 405      33.949 -37.834 -31.654  1.00128.49           C  
HETATM 4991  C6' SOG A 405      33.058 -36.769 -32.239  1.00127.34           C  
HETATM 4992  C7' SOG A 405      31.580 -37.054 -32.220  1.00125.83           C  
HETATM 4993  C8' SOG A 405      31.156 -38.088 -33.234  1.00124.06           C  
HETATM 4994  S1  SOG A 405      35.540 -34.265 -33.782  1.00130.73           S  
HETATM 4995  O2  SOG A 405      37.997 -32.414 -33.619  1.00116.92           O  
HETATM 4996  O3  SOG A 405      38.575 -30.594 -35.763  1.00114.96           O  
HETATM 4997  O4  SOG A 405      36.249 -29.242 -36.790  1.00118.59           O  
HETATM 4998  O5  SOG A 405      34.855 -32.361 -35.488  1.00128.23           O  
HETATM 4999  O6  SOG A 405      32.521 -31.237 -36.597  1.00122.35           O  
HETATM 5000  C1  SOG A 406      51.441 -24.251 -33.604  1.00123.41           C  
HETATM 5001  C2  SOG A 406      52.768 -24.970 -33.717  1.00127.64           C  
HETATM 5002  C3  SOG A 406      52.910 -25.502 -35.140  1.00128.35           C  
HETATM 5003  C4  SOG A 406      51.691 -26.306 -35.578  1.00130.14           C  
HETATM 5004  C5  SOG A 406      50.362 -25.643 -35.183  1.00127.06           C  
HETATM 5005  C6  SOG A 406      49.186 -26.597 -35.287  1.00123.36           C  
HETATM 5006  C1' SOG A 406      49.535 -22.705 -32.346  1.00 97.94           C  
HETATM 5007  C2' SOG A 406      48.979 -21.805 -31.272  1.00 87.97           C  
HETATM 5008  C3' SOG A 406      48.468 -22.561 -30.070  1.00 74.94           C  
HETATM 5009  C4' SOG A 406      47.807 -21.671 -29.045  1.00 59.30           C  
HETATM 5010  C5' SOG A 406      46.508 -21.045 -29.498  1.00 43.96           C  
HETATM 5011  C6' SOG A 406      45.842 -20.184 -28.452  1.00 37.04           C  
HETATM 5012  C7' SOG A 406      44.511 -19.615 -28.869  1.00 37.39           C  
HETATM 5013  C8' SOG A 406      43.899 -18.705 -27.832  1.00 40.50           C  
HETATM 5014  S1  SOG A 406      51.172 -23.437 -32.013  1.00110.75           S  
HETATM 5015  O2  SOG A 406      53.836 -24.068 -33.450  1.00128.54           O  
HETATM 5016  O3  SOG A 406      54.097 -26.284 -35.270  1.00127.05           O  
HETATM 5017  O4  SOG A 406      51.709 -26.488 -36.994  1.00134.01           O  
HETATM 5018  O5  SOG A 406      50.398 -25.186 -33.822  1.00127.44           O  
HETATM 5019  O6  SOG A 406      49.392 -27.735 -34.450  1.00119.05           O  
HETATM 5020  C1  SOG A 407      54.282 -24.437 -28.803  1.00124.83           C  
HETATM 5021  C2  SOG A 407      52.823 -24.872 -28.643  1.00116.32           C  
HETATM 5022  C3  SOG A 407      51.864 -23.693 -28.781  1.00118.93           C  
HETATM 5023  C4  SOG A 407      52.315 -22.521 -27.941  1.00120.14           C  
HETATM 5024  C5  SOG A 407      53.736 -22.176 -28.320  1.00127.61           C  
HETATM 5025  C6  SOG A 407      54.270 -20.979 -27.556  1.00130.14           C  
HETATM 5026  C1' SOG A 407      56.880 -25.032 -27.893  1.00128.90           C  
HETATM 5027  C2' SOG A 407      57.660 -25.840 -26.878  1.00128.96           C  
HETATM 5028  C3' SOG A 407      59.092 -25.378 -26.737  1.00127.79           C  
HETATM 5029  C4' SOG A 407      59.933 -25.711 -27.946  1.00126.05           C  
HETATM 5030  C5' SOG A 407      61.232 -24.941 -28.047  1.00126.05           C  
HETATM 5031  C6' SOG A 407      62.319 -25.331 -27.065  1.00126.23           C  
HETATM 5032  C7' SOG A 407      63.558 -24.486 -27.280  1.00124.48           C  
HETATM 5033  C8' SOG A 407      64.768 -24.893 -26.473  1.00122.67           C  
HETATM 5034  S1  SOG A 407      55.293 -25.843 -28.278  1.00130.41           S  
HETATM 5035  O2  SOG A 407      52.490 -25.867 -29.606  1.00111.03           O  
HETATM 5036  O3  SOG A 407      50.544 -24.089 -28.415  1.00125.99           O  
HETATM 5037  O4  SOG A 407      51.483 -21.384 -28.164  1.00117.59           O  
HETATM 5038  O5  SOG A 407      54.578 -23.297 -28.007  1.00129.33           O  
HETATM 5039  O6  SOG A 407      55.536 -20.573 -28.065  1.00128.87           O  
HETATM 5040  C1  SOG A 408      45.096 -15.374  -5.411  1.00 89.96           C  
HETATM 5041  C1' SOG A 408      42.354 -15.800  -5.507  1.00 92.10           C  
HETATM 5042  C2' SOG A 408      42.016 -14.489  -4.844  1.00 84.61           C  
HETATM 5043  C3' SOG A 408      41.170 -14.662  -3.603  1.00 85.83           C  
HETATM 5044  C4' SOG A 408      40.536 -13.377  -3.128  1.00 84.56           C  
HETATM 5045  C5' SOG A 408      41.504 -12.233  -2.937  1.00 79.95           C  
HETATM 5046  S1  SOG A 408      43.787 -15.650  -6.622  1.00 94.33           S  
HETATM 5047  C1' SOG A 409      42.160  -8.058   8.256  1.00 68.67           C  
HETATM 5048  C2' SOG A 409      41.963  -9.288   7.404  1.00 72.93           C  
HETATM 5049  C3' SOG A 409      41.368  -8.970   6.051  1.00 73.54           C  
HETATM 5050  C4' SOG A 409      41.167 -10.191   5.187  1.00 69.04           C  
HETATM 5051  C1' SOG A 410      45.082  -8.125   1.632  1.00 60.87           C  
HETATM 5052  C2' SOG A 410      44.148  -9.068   0.913  1.00 55.54           C  
HETATM 5053  C3' SOG A 410      43.402  -8.400  -0.218  1.00 53.20           C  
HETATM 5054  C4' SOG A 410      42.466  -9.333  -0.946  1.00 49.62           C  
HETATM 5055  CAD PGW A 411      38.318   4.168 -10.628  1.00101.57           C  
HETATM 5056  OAE PGW A 411      39.298   5.050 -11.170  1.00103.51           O  
HETATM 5057  OAF PGW A 411      37.820   1.865 -10.118  1.00 91.81           O  
HETATM 5058  P   PGW A 411      41.712   1.093  -8.241  1.00115.24           P  
HETATM 5059  C01 PGW A 411      41.826  -1.073 -11.419  1.00 83.79           C  
HETATM 5060  C1  PGW A 411      38.960  -2.714 -10.483  1.00 85.19           C  
HETATM 5061  O01 PGW A 411      40.300  -2.703 -10.502  1.00 86.87           O  
HETATM 5062  C02 PGW A 411      40.951  -1.431 -10.241  1.00 88.44           C  
HETATM 5063  C2  PGW A 411      38.348  -4.021 -10.909  1.00 74.75           C  
HETATM 5064  O02 PGW A 411      38.341  -1.735 -10.160  1.00 91.62           O  
HETATM 5065  C03 PGW A 411      41.711  -1.471  -8.936  1.00100.31           C  
HETATM 5066  C3  PGW A 411      37.140  -4.414 -10.115  1.00 70.40           C  
HETATM 5067  O03 PGW A 411      42.915  -2.015 -11.513  1.00 85.87           O  
HETATM 5068  C04 PGW A 411      39.903   2.707  -9.295  1.00101.42           C  
HETATM 5069  C4  PGW A 411      36.050  -5.008 -10.987  1.00 67.39           C  
HETATM 5070  O04 PGW A 411      44.432  -0.391 -11.616  1.00 81.45           O  
HETATM 5071  C05 PGW A 411      38.879   2.778 -10.407  1.00 96.97           C  
HETATM 5072  C5  PGW A 411      35.402  -6.249 -10.417  1.00 61.59           C  
HETATM 5073  C06 PGW A 411      32.477 -11.478 -13.654  1.00 65.54           C  
HETATM 5074  C6  PGW A 411      34.364  -6.885 -11.314  1.00 59.48           C  
HETATM 5075  C07 PGW A 411      31.612 -12.665 -13.922  1.00 77.11           C  
HETATM 5076  C7  PGW A 411      33.936  -8.270 -10.848  1.00 60.03           C  
HETATM 5077  C08 PGW A 411      30.608 -12.483 -15.044  1.00 80.63           C  
HETATM 5078  C8  PGW A 411      33.344  -9.145 -11.906  1.00 56.32           C  
HETATM 5079  C09 PGW A 411      30.882 -13.327 -16.263  1.00 86.82           C  
HETATM 5080  C9  PGW A 411      33.519 -10.596 -11.582  1.00 48.82           C  
HETATM 5081  C10 PGW A 411      33.200 -11.598 -12.350  1.00 52.81           C  
HETATM 5082  C11 PGW A 411      32.021 -12.834 -17.120  1.00 88.92           C  
HETATM 5083  O11 PGW A 411      42.446  -0.220  -8.807  1.00109.74           O  
HETATM 5084  C12 PGW A 411      32.454 -13.806 -18.188  1.00 84.45           C  
HETATM 5085  O12 PGW A 411      40.534   1.392  -9.291  1.00110.78           O  
HETATM 5086  C13 PGW A 411      33.221 -14.986 -17.652  1.00 76.85           C  
HETATM 5087  O13 PGW A 411      42.693   2.229  -8.339  1.00113.19           O  
HETATM 5088  C14 PGW A 411      34.543 -14.598 -17.033  1.00 73.56           C  
HETATM 5089  O14 PGW A 411      41.122   0.725  -6.908  1.00117.66           O  
HETATM 5090  C15 PGW A 411      44.704 -10.506 -14.942  1.00 56.69           C  
HETATM 5091  C16 PGW A 411      43.493 -11.199 -15.516  1.00 44.94           C  
HETATM 5092  C17 PGW A 411      42.536 -10.231 -16.169  1.00 37.22           C  
HETATM 5093  C18 PGW A 411      41.297 -10.833 -16.787  1.00 34.41           C  
HETATM 5094  C19 PGW A 411      44.070  -1.498 -11.919  1.00 81.83           C  
HETATM 5095  C20 PGW A 411      44.760  -2.416 -12.877  1.00 72.66           C  
HETATM 5096  C21 PGW A 411      43.854  -2.842 -13.991  1.00 65.59           C  
HETATM 5097  C22 PGW A 411      43.892  -4.338 -14.249  1.00 59.47           C  
HETATM 5098  C23 PGW A 411      44.772  -4.739 -15.406  1.00 54.47           C  
HETATM 5099  C24 PGW A 411      45.649  -5.947 -15.160  1.00 45.74           C  
HETATM 5100  C25 PGW A 411      45.014  -7.302 -15.396  1.00 37.48           C  
HETATM 5101  C26 PGW A 411      46.041  -8.414 -15.511  1.00 40.05           C  
HETATM 5102  C27 PGW A 411      45.505  -9.750 -15.974  1.00 54.11           C  
HETATM 5103  C28 PGW A 411      40.339  -9.794 -17.332  1.00 40.50           C  
HETATM 5104  C29 PGW A 411      39.091 -11.182 -19.070  1.00 57.23           C  
HETATM 5105  C30 PGW A 411      39.010 -10.282 -17.859  1.00 48.89           C  
HETATM 5106  C1  NVK B 401      37.000  -6.559 -24.692  1.00102.49           C  
HETATM 5107  C10 NVK B 401      38.829   3.861 -27.069  1.00 82.55           C  
HETATM 5108  C11 NVK B 401      38.018   4.901 -27.618  1.00 80.07           C  
HETATM 5109  C12 NVK B 401      38.602   6.156 -27.887  1.00 74.94           C  
HETATM 5110  C13 NVK B 401      40.640   5.406 -27.130  1.00 84.98           C  
HETATM 5111  C14 NVK B 401      40.150   4.127 -26.829  1.00 87.26           C  
HETATM 5112  C15 NVK B 401      37.810   7.185 -28.427  1.00 73.97           C  
HETATM 5113  C16 NVK B 401      36.500   6.942 -28.674  1.00 66.45           C  
HETATM 5114  C17 NVK B 401      35.981   5.668 -28.382  1.00 66.81           C  
HETATM 5115  C2  NVK B 401      37.527  -5.193 -24.896  1.00 98.63           C  
HETATM 5116  C3  NVK B 401      38.752  -3.429 -24.998  1.00 99.05           C  
HETATM 5117  C4  NVK B 401      37.502  -3.086 -25.464  1.00 96.24           C  
HETATM 5118  C5  NVK B 401      37.200  -1.818 -25.892  1.00 90.88           C  
HETATM 5119  C6  NVK B 401      38.209  -0.868 -25.843  1.00 87.61           C  
HETATM 5120  C7  NVK B 401      39.482  -1.202 -25.372  1.00 91.41           C  
HETATM 5121  C8  NVK B 401      39.761  -2.478 -24.948  1.00 94.21           C  
HETATM 5122  C9  NVK B 401      38.784   1.501 -26.327  1.00 72.95           C  
HETATM 5123  N1  NVK B 401      38.728  -4.789 -24.643  1.00100.39           N  
HETATM 5124  N2  NVK B 401      37.920   0.438 -26.280  1.00 79.19           N  
HETATM 5125  N3  NVK B 401      38.208   2.636 -26.819  1.00 73.32           N  
HETATM 5126  N4  NVK B 401      39.933   6.397 -27.634  1.00 74.43           N  
HETATM 5127  N5  NVK B 401      36.690   4.679 -27.876  1.00 76.14           N  
HETATM 5128  O1  NVK B 401      36.707  -4.219 -25.401  1.00 93.95           O  
HETATM 5129  O2  NVK B 401      39.954   1.448 -25.972  1.00 77.45           O  
HETATM 5130  H3  NVK B 401      37.713  -7.201 -24.799  1.00124.91           H  
HETATM 5131  H1  NVK B 401      36.309  -6.741 -25.340  1.00124.91           H  
HETATM 5132  H2  NVK B 401      36.633  -6.636 -23.803  1.00124.91           H  
HETATM 5133  H9  NVK B 401      41.560   5.567 -26.955  1.00103.90           H  
HETATM 5134  H10 NVK B 401      40.718   3.456 -26.467  1.00106.64           H  
HETATM 5135  H11 NVK B 401      38.192   8.031 -28.611  1.00 90.69           H  
HETATM 5136  H12 NVK B 401      35.946   7.612 -29.035  1.00 81.67           H  
HETATM 5137  H13 NVK B 401      35.069   5.508 -28.559  1.00 82.09           H  
HETATM 5138  H4  NVK B 401      36.335  -1.596 -26.210  1.00110.98           H  
HETATM 5139  H5  NVK B 401      40.159  -0.544 -25.345  1.00111.62           H  
HETATM 5140  H6  NVK B 401      40.620  -2.702 -24.630  1.00114.98           H  
HETATM 5141  H7  NVK B 401      37.096   0.585 -26.551  1.00 96.96           H  
HETATM 5142  H8  NVK B 401      37.366   2.615 -27.001  1.00 89.91           H  
HETATM 5143  C1  NVK B 402      38.357   6.202 -31.664  1.00104.28           C  
HETATM 5144  C10 NVK B 402      38.060  -4.304 -28.991  1.00 95.13           C  
HETATM 5145  C11 NVK B 402      37.083  -5.344 -29.038  1.00 99.00           C  
HETATM 5146  C12 NVK B 402      37.394  -6.598 -28.470  1.00103.36           C  
HETATM 5147  C13 NVK B 402      39.476  -5.842 -27.853  1.00111.91           C  
HETATM 5148  C14 NVK B 402      39.261  -4.564 -28.388  1.00102.96           C  
HETATM 5149  C15 NVK B 402      36.439  -7.630 -28.509  1.00103.45           C  
HETATM 5150  C16 NVK B 402      35.242  -7.391 -29.094  1.00106.40           C  
HETATM 5151  C17 NVK B 402      34.999  -6.120 -29.645  1.00109.40           C  
HETATM 5152  C2  NVK B 402      38.582   4.806 -31.235  1.00 89.12           C  
HETATM 5153  C3  NVK B 402      39.415   2.969 -30.495  1.00 86.66           C  
HETATM 5154  C4  NVK B 402      38.115   2.705 -30.869  1.00 84.80           C  
HETATM 5155  C5  NVK B 402      37.555   1.457 -30.747  1.00 81.95           C  
HETATM 5156  C6  NVK B 402      38.352   0.448 -30.223  1.00 83.95           C  
HETATM 5157  C7  NVK B 402      39.670   0.703 -29.840  1.00 87.39           C  
HETATM 5158  C8  NVK B 402      40.209   1.959 -29.973  1.00 88.28           C  
HETATM 5159  C9  NVK B 402      38.484  -1.944 -29.571  1.00 96.30           C  
HETATM 5160  N1  NVK B 402      39.678   4.326 -30.749  1.00 81.19           N  
HETATM 5161  N2  NVK B 402      37.828  -0.850 -30.078  1.00 86.43           N  
HETATM 5162  N3  NVK B 402      37.716  -3.071 -29.549  1.00 95.38           N  
HETATM 5163  N4  NVK B 402      38.611  -6.836 -27.875  1.00109.66           N  
HETATM 5164  N5  NVK B 402      35.865  -5.128 -29.627  1.00106.13           N  
HETATM 5165  O1  NVK B 402      37.573   3.886 -31.350  1.00 82.08           O  
HETATM 5166  O2  NVK B 402      39.643  -1.927 -29.180  1.00104.38           O  
HETATM 5167  H3  NVK B 402      39.038   6.772 -31.287  1.00127.06           H  
HETATM 5168  H1  NVK B 402      37.490   6.499 -31.362  1.00127.06           H  
HETATM 5169  H2  NVK B 402      38.394   6.256 -32.627  1.00127.06           H  
HETATM 5170  H9  NVK B 402      40.318  -6.001 -27.442  1.00136.22           H  
HETATM 5171  H10 NVK B 402      39.929  -3.891 -28.336  1.00125.48           H  
HETATM 5172  H11 NVK B 402      36.638  -8.474 -28.130  1.00126.07           H  
HETATM 5173  H12 NVK B 402      34.582  -8.062 -29.133  1.00129.61           H  
HETATM 5174  H13 NVK B 402      34.164  -5.965 -30.054  1.00133.20           H  
HETATM 5175  H4  NVK B 402      36.660   1.288 -31.008  1.00100.26           H  
HETATM 5176  H5  NVK B 402      40.198   0.006 -29.486  1.00106.79           H  
HETATM 5177  H6  NVK B 402      41.100   2.130 -29.714  1.00107.86           H  
HETATM 5178  H7  NVK B 402      36.997  -0.970 -30.339  1.00105.64           H  
HETATM 5179  H8  NVK B 402      36.935  -3.040 -29.912  1.00116.38           H  
HETATM 5180  S   SO4 B 403       9.710 -19.941 -30.400  1.00106.09           S  
HETATM 5181  O1  SO4 B 403       8.840 -21.112 -30.453  1.00104.96           O  
HETATM 5182  O2  SO4 B 403       9.446 -19.089 -31.557  1.00106.36           O  
HETATM 5183  O3  SO4 B 403       9.443 -19.197 -29.172  1.00103.60           O  
HETATM 5184  O4  SO4 B 403      11.109 -20.359 -30.417  1.00109.55           O  
HETATM 5185  S   SO4 B 404       8.886 -12.116 -40.066  1.00145.67           S  
HETATM 5186  O1  SO4 B 404       9.903 -12.777 -40.879  1.00144.98           O  
HETATM 5187  O2  SO4 B 404       7.612 -12.123 -40.778  1.00145.37           O  
HETATM 5188  O3  SO4 B 404       8.737 -12.828 -38.800  1.00145.54           O  
HETATM 5189  O4  SO4 B 404       9.290 -10.737 -39.809  1.00147.69           O  
HETATM 5190  C1  SOG B 405      56.018 -12.630 -29.510  1.00 97.94           C  
HETATM 5191  C2  SOG B 405      56.654 -11.765 -28.401  1.00 95.31           C  
HETATM 5192  C3  SOG B 405      55.779 -11.473 -27.175  1.00 94.74           C  
HETATM 5193  C4  SOG B 405      54.547 -12.350 -26.988  1.00 99.68           C  
HETATM 5194  C5  SOG B 405      54.539 -13.529 -27.919  1.00102.14           C  
HETATM 5195  C6  SOG B 405      53.225 -14.290 -27.864  1.00101.82           C  
HETATM 5196  C1' SOG B 405      55.589 -12.987 -32.272  1.00101.52           C  
HETATM 5197  C2' SOG B 405      55.422 -12.399 -33.656  1.00106.55           C  
HETATM 5198  C3' SOG B 405      55.053 -13.435 -34.694  1.00111.01           C  
HETATM 5199  C4' SOG B 405      54.496 -12.850 -35.975  1.00110.94           C  
HETATM 5200  C5' SOG B 405      55.462 -12.003 -36.774  1.00108.61           C  
HETATM 5201  C6' SOG B 405      54.883 -11.453 -38.059  1.00106.15           C  
HETATM 5202  C7' SOG B 405      55.824 -10.604 -38.878  1.00103.18           C  
HETATM 5203  C8' SOG B 405      56.987 -11.353 -39.484  1.00 97.60           C  
HETATM 5204  S1  SOG B 405      56.122 -11.720 -31.074  1.00 96.34           S  
HETATM 5205  O2  SOG B 405      57.874 -12.360 -27.969  1.00100.45           O  
HETATM 5206  O3  SOG B 405      55.406 -10.095 -27.144  1.00 93.26           O  
HETATM 5207  O4  SOG B 405      54.447 -12.796 -25.635  1.00105.04           O  
HETATM 5208  O5  SOG B 405      54.677 -13.010 -29.246  1.00106.26           O  
HETATM 5209  O6  SOG B 405      53.358 -15.613 -28.385  1.00104.10           O  
HETATM 5210  C1  SOG B 406      47.957   0.090 -13.298  1.00152.60           C  
HETATM 5211  C2  SOG B 406      48.956  -0.655 -14.163  1.00149.34           C  
HETATM 5212  C3  SOG B 406      49.217  -2.027 -13.548  1.00148.99           C  
HETATM 5213  C4  SOG B 406      49.622  -1.904 -12.090  1.00152.78           C  
HETATM 5214  C5  SOG B 406      48.627  -1.038 -11.324  1.00157.03           C  
HETATM 5215  C6  SOG B 406      49.073  -0.747  -9.902  1.00158.04           C  
HETATM 5216  C1' SOG B 406      46.346   2.214 -12.646  1.00144.39           C  
HETATM 5217  C2' SOG B 406      45.762   3.600 -12.719  1.00136.31           C  
HETATM 5218  C3' SOG B 406      44.767   3.828 -11.608  1.00129.85           C  
HETATM 5219  C4' SOG B 406      44.171   5.210 -11.571  1.00127.87           C  
HETATM 5220  C5' SOG B 406      43.122   5.370 -10.500  1.00127.96           C  
HETATM 5221  C6' SOG B 406      42.533   6.751 -10.400  1.00125.67           C  
HETATM 5222  C7' SOG B 406      41.624   6.902  -9.210  1.00123.28           C  
HETATM 5223  C8' SOG B 406      41.170   8.322  -8.987  1.00119.09           C  
HETATM 5224  S1  SOG B 406      47.556   1.737 -13.919  1.00151.44           S  
HETATM 5225  O2  SOG B 406      48.441  -0.817 -15.479  1.00149.37           O  
HETATM 5226  O3  SOG B 406      50.216  -2.724 -14.288  1.00145.83           O  
HETATM 5227  O4  SOG B 406      49.693  -3.189 -11.473  1.00149.93           O  
HETATM 5228  O5  SOG B 406      48.472   0.229 -11.982  1.00157.33           O  
HETATM 5229  O6  SOG B 406      48.159   0.125  -9.242  1.00157.79           O  
HETATM 5230  C1  SOG B 407      37.110  18.105 -50.319  1.00149.35           C  
HETATM 5231  C2  SOG B 407      37.387  16.981 -51.312  1.00151.37           C  
HETATM 5232  C3  SOG B 407      36.661  17.231 -52.630  1.00154.23           C  
HETATM 5233  C4  SOG B 407      35.204  17.563 -52.392  1.00157.23           C  
HETATM 5234  C5  SOG B 407      35.109  18.724 -51.423  1.00156.85           C  
HETATM 5235  C6  SOG B 407      33.675  19.123 -51.130  1.00157.24           C  
HETATM 5236  C1' SOG B 407      36.750  18.504 -47.582  1.00136.00           C  
HETATM 5237  C2' SOG B 407      37.151  18.247 -46.152  1.00133.44           C  
HETATM 5238  C3' SOG B 407      36.284  18.999 -45.178  1.00135.22           C  
HETATM 5239  C4' SOG B 407      36.824  19.022 -43.773  1.00140.10           C  
HETATM 5240  C5' SOG B 407      36.747  20.386 -43.136  1.00143.61           C  
HETATM 5241  C6' SOG B 407      36.929  20.403 -41.641  1.00143.54           C  
HETATM 5242  C7' SOG B 407      36.679  21.772 -41.062  1.00139.64           C  
HETATM 5243  C8' SOG B 407      36.569  21.801 -39.558  1.00137.34           C  
HETATM 5244  S1  SOG B 407      37.834  17.615 -48.738  1.00141.44           S  
HETATM 5245  O2  SOG B 407      38.785  16.867 -51.552  1.00151.84           O  
HETATM 5246  O3  SOG B 407      36.780  16.092 -53.480  1.00153.67           O  
HETATM 5247  O4  SOG B 407      34.557  17.918 -53.612  1.00159.39           O  
HETATM 5248  O5  SOG B 407      35.715  18.339 -50.179  1.00154.26           O  
HETATM 5249  O6  SOG B 407      33.616  20.338 -50.388  1.00156.07           O  
HETATM 5250  C1  SOG B 408      38.311  21.824 -54.011  1.00133.27           C  
HETATM 5251  C2  SOG B 408      38.474  20.462 -54.653  1.00129.36           C  
HETATM 5252  C3  SOG B 408      39.689  20.492 -55.575  1.00128.49           C  
HETATM 5253  C4  SOG B 408      39.632  21.659 -56.551  1.00129.20           C  
HETATM 5254  C5  SOG B 408      39.219  22.972 -55.871  1.00130.81           C  
HETATM 5255  C6  SOG B 408      38.855  24.055 -56.871  1.00127.23           C  
HETATM 5256  C1' SOG B 408      37.404  23.384 -51.906  1.00130.68           C  
HETATM 5257  C2' SOG B 408      36.300  24.404 -51.786  1.00126.25           C  
HETATM 5258  C3' SOG B 408      35.338  24.102 -50.664  1.00121.26           C  
HETATM 5259  C4' SOG B 408      33.896  24.188 -51.089  1.00117.44           C  
HETATM 5260  C5' SOG B 408      32.912  24.055 -49.956  1.00111.98           C  
HETATM 5261  C6' SOG B 408      31.479  23.905 -50.398  1.00102.83           C  
HETATM 5262  C7' SOG B 408      30.501  23.808 -49.258  1.00 91.57           C  
HETATM 5263  C8' SOG B 408      29.088  23.536 -49.713  1.00 85.44           C  
HETATM 5264  S1  SOG B 408      36.955  21.864 -52.813  1.00132.98           S  
HETATM 5265  O2  SOG B 408      38.671  19.475 -53.647  1.00126.81           O  
HETATM 5266  O3  SOG B 408      39.804  19.261 -56.288  1.00126.73           O  
HETATM 5267  O4  SOG B 408      40.897  21.835 -57.192  1.00127.32           O  
HETATM 5268  O5  SOG B 408      38.068  22.780 -55.031  1.00135.89           O  
HETATM 5269  O6  SOG B 408      38.269  25.180 -56.220  1.00125.57           O  
HETATM 5270  CAD PGW B 409      26.495 -35.872 -29.006  1.00111.68           C  
HETATM 5271  OAE PGW B 409      27.561 -36.803 -28.843  1.00106.38           O  
HETATM 5272  OAF PGW B 409      26.274 -33.474 -29.185  1.00108.12           O  
HETATM 5273  P   PGW B 409      27.161 -32.991 -33.248  1.00146.02           P  
HETATM 5274  C01 PGW B 409      28.215 -30.267 -30.235  1.00104.99           C  
HETATM 5275  C1  PGW B 409      30.547 -29.573 -32.927  1.00108.26           C  
HETATM 5276  O01 PGW B 409      30.076 -29.859 -31.705  1.00110.02           O  
HETATM 5277  C02 PGW B 409      28.781 -30.504 -31.615  1.00114.01           C  
HETATM 5278  C2  PGW B 409      31.993 -29.942 -33.116  1.00107.51           C  
HETATM 5279  O02 PGW B 409      29.856 -29.045 -33.759  1.00106.06           O  
HETATM 5280  C03 PGW B 409      29.130 -31.958 -31.830  1.00128.04           C  
HETATM 5281  C3  PGW B 409      32.481 -30.957 -32.129  1.00102.19           C  
HETATM 5282  O03 PGW B 409      28.569 -28.946 -29.772  1.00 96.14           O  
HETATM 5283  C04 PGW B 409      26.765 -34.651 -31.218  1.00130.27           C  
HETATM 5284  C4  PGW B 409      33.823 -30.579 -31.535  1.00 98.34           C  
HETATM 5285  O04 PGW B 409      26.628 -28.068 -30.427  1.00 79.94           O  
HETATM 5286  C05 PGW B 409      26.952 -34.612 -29.716  1.00116.78           C  
HETATM 5287  C5  PGW B 409      33.785 -29.314 -30.710  1.00 95.90           C  
HETATM 5288  C06 PGW B 409      37.202 -23.950 -30.185  1.00 78.52           C  
HETATM 5289  C6  PGW B 409      35.128 -28.852 -30.200  1.00 90.85           C  
HETATM 5290  C07 PGW B 409      37.119 -22.567 -30.755  1.00 71.57           C  
HETATM 5291  C7  PGW B 409      35.988 -28.106 -31.212  1.00 82.87           C  
HETATM 5292  C08 PGW B 409      36.133 -21.651 -30.047  1.00 58.27           C  
HETATM 5293  C8  PGW B 409      36.221 -26.669 -30.850  1.00 73.84           C  
HETATM 5294  C09 PGW B 409      36.161 -21.755 -28.541  1.00 53.67           C  
HETATM 5295  C9  PGW B 409      37.476 -26.082 -31.419  1.00 69.48           C  
HETATM 5296  C10 PGW B 409      37.940 -24.911 -31.065  1.00 72.26           C  
HETATM 5297  C11 PGW B 409      34.984 -22.497 -27.952  1.00 60.91           C  
HETATM 5298  O11 PGW B 409      28.683 -32.502 -33.100  1.00139.28           O  
HETATM 5299  C12 PGW B 409      35.255 -23.138 -26.611  1.00 70.35           C  
HETATM 5300  O12 PGW B 409      26.742 -33.284 -31.725  1.00141.91           O  
HETATM 5301  C13 PGW B 409      35.623 -22.220 -25.472  1.00 75.05           C  
HETATM 5302  O13 PGW B 409      26.364 -31.816 -33.743  1.00143.32           O  
HETATM 5303  C14 PGW B 409      34.481 -21.380 -24.955  1.00 78.49           C  
HETATM 5304  O14 PGW B 409      27.164 -34.294 -33.999  1.00149.31           O  
HETATM 5305  C15 PGW B 409      26.694 -18.571 -25.329  1.00 63.41           C  
HETATM 5306  C16 PGW B 409      27.470 -18.856 -24.066  1.00 62.92           C  
HETATM 5307  C17 PGW B 409      27.429 -17.746 -23.045  1.00 63.06           C  
HETATM 5308  C18 PGW B 409      28.740 -17.018 -22.868  1.00 59.06           C  
HETATM 5309  C19 PGW B 409      27.580 -28.062 -29.689  1.00 79.53           C  
HETATM 5310  C20 PGW B 409      27.788 -27.131 -28.526  1.00 61.11           C  
HETATM 5311  C21 PGW B 409      26.602 -26.276 -28.202  1.00 43.13           C  
HETATM 5312  C22 PGW B 409      27.010 -24.871 -27.799  1.00 34.81           C  
HETATM 5313  C23 PGW B 409      25.884 -23.977 -27.340  1.00 32.41           C  
HETATM 5314  C24 PGW B 409      26.256 -22.515 -27.257  1.00 38.13           C  
HETATM 5315  C25 PGW B 409      25.169 -21.618 -26.716  1.00 45.62           C  
HETATM 5316  C26 PGW B 409      25.432 -20.137 -26.879  1.00 55.09           C  
HETATM 5317  C27 PGW B 409      26.771 -19.677 -26.352  1.00 59.02           C  
HETATM 5318  C28 PGW B 409      29.866 -17.892 -22.359  1.00 57.29           C  
HETATM 5319  C29 PGW B 409      31.221 -16.081 -21.186  1.00 57.34           C  
HETATM 5320  C30 PGW B 409      31.206 -17.218 -22.182  1.00 55.44           C  
HETATM 5321  O   HOH A 501      41.334 -37.306 -20.986  1.00 30.00           O  
HETATM 5322  O   HOH A 502      39.732 -34.094 -19.998  1.00 30.00           O  
HETATM 5323  O   HOH A 503      29.690 -50.834 -24.631  1.00 60.48           O  
HETATM 5324  O   HOH A 504      23.700  -1.785  -1.128  1.00 65.81           O  
HETATM 5325  O   HOH A 505      42.498 -25.694 -19.202  1.00 63.54           O  
HETATM 5326  O   HOH A 506      21.265 -28.042  10.323  1.00 45.06           O  
HETATM 5327  O   HOH A 507      49.708 -37.521 -20.469  1.00 27.92           O  
HETATM 5328  O   HOH A 508      37.431 -49.525 -29.453  1.00 39.46           O  
HETATM 5329  O   HOH A 509      28.619 -14.987  11.099  1.00 41.80           O  
HETATM 5330  O   HOH A 510      12.819 -16.679  -2.779  1.00 44.13           O  
HETATM 5331  O   HOH A 511      30.363   1.461 -11.908  1.00 30.83           O  
HETATM 5332  O   HOH B 501      47.903   2.875 -32.019  1.00 59.45           O  
HETATM 5333  O   HOH B 502      48.598   8.045 -21.895  1.00 45.78           O  
HETATM 5334  O   HOH B 503      44.614   9.975 -28.010  1.00 55.64           O  
HETATM 5335  O   HOH B 504      56.438  -3.681 -35.047  1.00 41.13           O  
HETATM 5336  O   HOH B 505      43.152  10.706 -16.908  1.00 30.79           O  
HETATM 5337  O   HOH B 506      42.984   1.288 -30.646  1.00 59.59           O  
HETATM 5338  O   HOH B 507       8.352   2.491 -36.234  1.00 47.23           O  
HETATM 5339  O   HOH B 508      56.467  -7.963 -36.900  1.00 62.87           O  
CONECT  581 1209                                                                
CONECT 1209  581                                                                
CONECT 3150 3695                                                                
CONECT 3695 3150                                                                
CONECT 4881 4890 4905 4906 4907                                                 
CONECT 4882 4883 4886 4900                                                      
CONECT 4883 4882 4884 4902                                                      
CONECT 4884 4883 4887 4901                                                      
CONECT 4885 4886 4901 4908                                                      
CONECT 4886 4882 4885 4909                                                      
CONECT 4887 4884 4888 4910                                                      
CONECT 4888 4887 4889 4911                                                      
CONECT 4889 4888 4902 4912                                                      
CONECT 4890 4881 4898 4903                                                      
CONECT 4891 4892 4896 4898                                                      
CONECT 4892 4891 4893 4903                                                      
CONECT 4893 4892 4894 4913                                                      
CONECT 4894 4893 4895 4899                                                      
CONECT 4895 4894 4896 4914                                                      
CONECT 4896 4891 4895 4915                                                      
CONECT 4897 4899 4900 4904                                                      
CONECT 4898 4890 4891                                                           
CONECT 4899 4894 4897 4916                                                      
CONECT 4900 4882 4897 4917                                                      
CONECT 4901 4884 4885                                                           
CONECT 4902 4883 4889                                                           
CONECT 4903 4890 4892                                                           
CONECT 4904 4897                                                                
CONECT 4905 4881                                                                
CONECT 4906 4881                                                                
CONECT 4907 4881                                                                
CONECT 4908 4885                                                                
CONECT 4909 4886                                                                
CONECT 4910 4887                                                                
CONECT 4911 4888                                                                
CONECT 4912 4889                                                                
CONECT 4913 4893                                                                
CONECT 4914 4895                                                                
CONECT 4915 4896                                                                
CONECT 4916 4899                                                                
CONECT 4917 4900                                                                
CONECT 4918 4927 4942 4943 4944                                                 
CONECT 4919 4920 4923 4937                                                      
CONECT 4920 4919 4921 4939                                                      
CONECT 4921 4920 4924 4938                                                      
CONECT 4922 4923 4938 4945                                                      
CONECT 4923 4919 4922 4946                                                      
CONECT 4924 4921 4925 4947                                                      
CONECT 4925 4924 4926 4948                                                      
CONECT 4926 4925 4939 4949                                                      
CONECT 4927 4918 4935 4940                                                      
CONECT 4928 4929 4933 4935                                                      
CONECT 4929 4928 4930 4940                                                      
CONECT 4930 4929 4931 4950                                                      
CONECT 4931 4930 4932 4936                                                      
CONECT 4932 4931 4933 4951                                                      
CONECT 4933 4928 4932 4952                                                      
CONECT 4934 4936 4937 4941                                                      
CONECT 4935 4927 4928                                                           
CONECT 4936 4931 4934 4953                                                      
CONECT 4937 4919 4934 4954                                                      
CONECT 4938 4921 4922                                                           
CONECT 4939 4920 4926                                                           
CONECT 4940 4927 4929                                                           
CONECT 4941 4934                                                                
CONECT 4942 4918                                                                
CONECT 4943 4918                                                                
CONECT 4944 4918                                                                
CONECT 4945 4922                                                                
CONECT 4946 4923                                                                
CONECT 4947 4924                                                                
CONECT 4948 4925                                                                
CONECT 4949 4926                                                                
CONECT 4950 4930                                                                
CONECT 4951 4932                                                                
CONECT 4952 4933                                                                
CONECT 4953 4936                                                                
CONECT 4954 4937                                                                
CONECT 4955 4956 4957 4958 4959                                                 
CONECT 4956 4955                                                                
CONECT 4957 4955                                                                
CONECT 4958 4955                                                                
CONECT 4959 4955                                                                
CONECT 4960 4961 4974 4978                                                      
CONECT 4961 4960 4962 4975                                                      
CONECT 4962 4961 4963 4976                                                      
CONECT 4963 4962 4964 4977                                                      
CONECT 4964 4963 4965 4978                                                      
CONECT 4965 4964 4979                                                           
CONECT 4966 4967 4974                                                           
CONECT 4967 4966 4968                                                           
CONECT 4968 4967 4969                                                           
CONECT 4969 4968 4970                                                           
CONECT 4970 4969 4971                                                           
CONECT 4971 4970 4972                                                           
CONECT 4972 4971 4973                                                           
CONECT 4973 4972                                                                
CONECT 4974 4960 4966                                                           
CONECT 4975 4961                                                                
CONECT 4976 4962                                                                
CONECT 4977 4963                                                                
CONECT 4978 4960 4964                                                           
CONECT 4979 4965                                                                
CONECT 4980 4981 4994 4998                                                      
CONECT 4981 4980 4982 4995                                                      
CONECT 4982 4981 4983 4996                                                      
CONECT 4983 4982 4984 4997                                                      
CONECT 4984 4983 4985 4998                                                      
CONECT 4985 4984 4999                                                           
CONECT 4986 4987 4994                                                           
CONECT 4987 4986 4988                                                           
CONECT 4988 4987 4989                                                           
CONECT 4989 4988 4990                                                           
CONECT 4990 4989 4991                                                           
CONECT 4991 4990 4992                                                           
CONECT 4992 4991 4993                                                           
CONECT 4993 4992                                                                
CONECT 4994 4980 4986                                                           
CONECT 4995 4981                                                                
CONECT 4996 4982                                                                
CONECT 4997 4983                                                                
CONECT 4998 4980 4984                                                           
CONECT 4999 4985                                                                
CONECT 5000 5001 5014 5018                                                      
CONECT 5001 5000 5002 5015                                                      
CONECT 5002 5001 5003 5016                                                      
CONECT 5003 5002 5004 5017                                                      
CONECT 5004 5003 5005 5018                                                      
CONECT 5005 5004 5019                                                           
CONECT 5006 5007 5014                                                           
CONECT 5007 5006 5008                                                           
CONECT 5008 5007 5009                                                           
CONECT 5009 5008 5010                                                           
CONECT 5010 5009 5011                                                           
CONECT 5011 5010 5012                                                           
CONECT 5012 5011 5013                                                           
CONECT 5013 5012                                                                
CONECT 5014 5000 5006                                                           
CONECT 5015 5001                                                                
CONECT 5016 5002                                                                
CONECT 5017 5003                                                                
CONECT 5018 5000 5004                                                           
CONECT 5019 5005                                                                
CONECT 5020 5021 5034 5038                                                      
CONECT 5021 5020 5022 5035                                                      
CONECT 5022 5021 5023 5036                                                      
CONECT 5023 5022 5024 5037                                                      
CONECT 5024 5023 5025 5038                                                      
CONECT 5025 5024 5039                                                           
CONECT 5026 5027 5034                                                           
CONECT 5027 5026 5028                                                           
CONECT 5028 5027 5029                                                           
CONECT 5029 5028 5030                                                           
CONECT 5030 5029 5031                                                           
CONECT 5031 5030 5032                                                           
CONECT 5032 5031 5033                                                           
CONECT 5033 5032                                                                
CONECT 5034 5020 5026                                                           
CONECT 5035 5021                                                                
CONECT 5036 5022                                                                
CONECT 5037 5023                                                                
CONECT 5038 5020 5024                                                           
CONECT 5039 5025                                                                
CONECT 5040 5046                                                                
CONECT 5041 5042 5046                                                           
CONECT 5042 5041 5043                                                           
CONECT 5043 5042 5044                                                           
CONECT 5044 5043 5045                                                           
CONECT 5045 5044                                                                
CONECT 5046 5040 5041                                                           
CONECT 5047 5048                                                                
CONECT 5048 5047 5049                                                           
CONECT 5049 5048 5050                                                           
CONECT 5050 5049                                                                
CONECT 5051 5052                                                                
CONECT 5052 5051 5053                                                           
CONECT 5053 5052 5054                                                           
CONECT 5054 5053                                                                
CONECT 5055 5056 5071                                                           
CONECT 5056 5055                                                                
CONECT 5057 5071                                                                
CONECT 5058 5083 5085 5087 5089                                                 
CONECT 5059 5062 5067                                                           
CONECT 5060 5061 5063 5064                                                      
CONECT 5061 5060 5062                                                           
CONECT 5062 5059 5061 5065                                                      
CONECT 5063 5060 5066                                                           
CONECT 5064 5060                                                                
CONECT 5065 5062 5083                                                           
CONECT 5066 5063 5069                                                           
CONECT 5067 5059 5094                                                           
CONECT 5068 5071 5085                                                           
CONECT 5069 5066 5072                                                           
CONECT 5070 5094                                                                
CONECT 5071 5055 5057 5068                                                      
CONECT 5072 5069 5074                                                           
CONECT 5073 5075 5081                                                           
CONECT 5074 5072 5076                                                           
CONECT 5075 5073 5077                                                           
CONECT 5076 5074 5078                                                           
CONECT 5077 5075 5079                                                           
CONECT 5078 5076 5080                                                           
CONECT 5079 5077 5082                                                           
CONECT 5080 5078 5081                                                           
CONECT 5081 5073 5080                                                           
CONECT 5082 5079 5084                                                           
CONECT 5083 5058 5065                                                           
CONECT 5084 5082 5086                                                           
CONECT 5085 5058 5068                                                           
CONECT 5086 5084 5088                                                           
CONECT 5087 5058                                                                
CONECT 5088 5086                                                                
CONECT 5089 5058                                                                
CONECT 5090 5091 5102                                                           
CONECT 5091 5090 5092                                                           
CONECT 5092 5091 5093                                                           
CONECT 5093 5092 5103                                                           
CONECT 5094 5067 5070 5095                                                      
CONECT 5095 5094 5096                                                           
CONECT 5096 5095 5097                                                           
CONECT 5097 5096 5098                                                           
CONECT 5098 5097 5099                                                           
CONECT 5099 5098 5100                                                           
CONECT 5100 5099 5101                                                           
CONECT 5101 5100 5102                                                           
CONECT 5102 5090 5101                                                           
CONECT 5103 5093 5105                                                           
CONECT 5104 5105                                                                
CONECT 5105 5103 5104                                                           
CONECT 5106 5115 5130 5131 5132                                                 
CONECT 5107 5108 5111 5125                                                      
CONECT 5108 5107 5109 5127                                                      
CONECT 5109 5108 5112 5126                                                      
CONECT 5110 5111 5126 5133                                                      
CONECT 5111 5107 5110 5134                                                      
CONECT 5112 5109 5113 5135                                                      
CONECT 5113 5112 5114 5136                                                      
CONECT 5114 5113 5127 5137                                                      
CONECT 5115 5106 5123 5128                                                      
CONECT 5116 5117 5121 5123                                                      
CONECT 5117 5116 5118 5128                                                      
CONECT 5118 5117 5119 5138                                                      
CONECT 5119 5118 5120 5124                                                      
CONECT 5120 5119 5121 5139                                                      
CONECT 5121 5116 5120 5140                                                      
CONECT 5122 5124 5125 5129                                                      
CONECT 5123 5115 5116                                                           
CONECT 5124 5119 5122 5141                                                      
CONECT 5125 5107 5122 5142                                                      
CONECT 5126 5109 5110                                                           
CONECT 5127 5108 5114                                                           
CONECT 5128 5115 5117                                                           
CONECT 5129 5122                                                                
CONECT 5130 5106                                                                
CONECT 5131 5106                                                                
CONECT 5132 5106                                                                
CONECT 5133 5110                                                                
CONECT 5134 5111                                                                
CONECT 5135 5112                                                                
CONECT 5136 5113                                                                
CONECT 5137 5114                                                                
CONECT 5138 5118                                                                
CONECT 5139 5120                                                                
CONECT 5140 5121                                                                
CONECT 5141 5124                                                                
CONECT 5142 5125                                                                
CONECT 5143 5152 5167 5168 5169                                                 
CONECT 5144 5145 5148 5162                                                      
CONECT 5145 5144 5146 5164                                                      
CONECT 5146 5145 5149 5163                                                      
CONECT 5147 5148 5163 5170                                                      
CONECT 5148 5144 5147 5171                                                      
CONECT 5149 5146 5150 5172                                                      
CONECT 5150 5149 5151 5173                                                      
CONECT 5151 5150 5164 5174                                                      
CONECT 5152 5143 5160 5165                                                      
CONECT 5153 5154 5158 5160                                                      
CONECT 5154 5153 5155 5165                                                      
CONECT 5155 5154 5156 5175                                                      
CONECT 5156 5155 5157 5161                                                      
CONECT 5157 5156 5158 5176                                                      
CONECT 5158 5153 5157 5177                                                      
CONECT 5159 5161 5162 5166                                                      
CONECT 5160 5152 5153                                                           
CONECT 5161 5156 5159 5178                                                      
CONECT 5162 5144 5159 5179                                                      
CONECT 5163 5146 5147                                                           
CONECT 5164 5145 5151                                                           
CONECT 5165 5152 5154                                                           
CONECT 5166 5159                                                                
CONECT 5167 5143                                                                
CONECT 5168 5143                                                                
CONECT 5169 5143                                                                
CONECT 5170 5147                                                                
CONECT 5171 5148                                                                
CONECT 5172 5149                                                                
CONECT 5173 5150                                                                
CONECT 5174 5151                                                                
CONECT 5175 5155                                                                
CONECT 5176 5157                                                                
CONECT 5177 5158                                                                
CONECT 5178 5161                                                                
CONECT 5179 5162                                                                
CONECT 5180 5181 5182 5183 5184                                                 
CONECT 5181 5180                                                                
CONECT 5182 5180                                                                
CONECT 5183 5180                                                                
CONECT 5184 5180                                                                
CONECT 5185 5186 5187 5188 5189                                                 
CONECT 5186 5185                                                                
CONECT 5187 5185                                                                
CONECT 5188 5185                                                                
CONECT 5189 5185                                                                
CONECT 5190 5191 5204 5208                                                      
CONECT 5191 5190 5192 5205                                                      
CONECT 5192 5191 5193 5206                                                      
CONECT 5193 5192 5194 5207                                                      
CONECT 5194 5193 5195 5208                                                      
CONECT 5195 5194 5209                                                           
CONECT 5196 5197 5204                                                           
CONECT 5197 5196 5198                                                           
CONECT 5198 5197 5199                                                           
CONECT 5199 5198 5200                                                           
CONECT 5200 5199 5201                                                           
CONECT 5201 5200 5202                                                           
CONECT 5202 5201 5203                                                           
CONECT 5203 5202                                                                
CONECT 5204 5190 5196                                                           
CONECT 5205 5191                                                                
CONECT 5206 5192                                                                
CONECT 5207 5193                                                                
CONECT 5208 5190 5194                                                           
CONECT 5209 5195                                                                
CONECT 5210 5211 5224 5228                                                      
CONECT 5211 5210 5212 5225                                                      
CONECT 5212 5211 5213 5226                                                      
CONECT 5213 5212 5214 5227                                                      
CONECT 5214 5213 5215 5228                                                      
CONECT 5215 5214 5229                                                           
CONECT 5216 5217 5224                                                           
CONECT 5217 5216 5218                                                           
CONECT 5218 5217 5219                                                           
CONECT 5219 5218 5220                                                           
CONECT 5220 5219 5221                                                           
CONECT 5221 5220 5222                                                           
CONECT 5222 5221 5223                                                           
CONECT 5223 5222                                                                
CONECT 5224 5210 5216                                                           
CONECT 5225 5211                                                                
CONECT 5226 5212                                                                
CONECT 5227 5213                                                                
CONECT 5228 5210 5214                                                           
CONECT 5229 5215                                                                
CONECT 5230 5231 5244 5248                                                      
CONECT 5231 5230 5232 5245                                                      
CONECT 5232 5231 5233 5246                                                      
CONECT 5233 5232 5234 5247                                                      
CONECT 5234 5233 5235 5248                                                      
CONECT 5235 5234 5249                                                           
CONECT 5236 5237 5244                                                           
CONECT 5237 5236 5238                                                           
CONECT 5238 5237 5239                                                           
CONECT 5239 5238 5240                                                           
CONECT 5240 5239 5241                                                           
CONECT 5241 5240 5242                                                           
CONECT 5242 5241 5243                                                           
CONECT 5243 5242                                                                
CONECT 5244 5230 5236                                                           
CONECT 5245 5231                                                                
CONECT 5246 5232                                                                
CONECT 5247 5233                                                                
CONECT 5248 5230 5234                                                           
CONECT 5249 5235                                                                
CONECT 5250 5251 5264 5268                                                      
CONECT 5251 5250 5252 5265                                                      
CONECT 5252 5251 5253 5266                                                      
CONECT 5253 5252 5254 5267                                                      
CONECT 5254 5253 5255 5268                                                      
CONECT 5255 5254 5269                                                           
CONECT 5256 5257 5264                                                           
CONECT 5257 5256 5258                                                           
CONECT 5258 5257 5259                                                           
CONECT 5259 5258 5260                                                           
CONECT 5260 5259 5261                                                           
CONECT 5261 5260 5262                                                           
CONECT 5262 5261 5263                                                           
CONECT 5263 5262                                                                
CONECT 5264 5250 5256                                                           
CONECT 5265 5251                                                                
CONECT 5266 5252                                                                
CONECT 5267 5253                                                                
CONECT 5268 5250 5254                                                           
CONECT 5269 5255                                                                
CONECT 5270 5271 5286                                                           
CONECT 5271 5270                                                                
CONECT 5272 5286                                                                
CONECT 5273 5298 5300 5302 5304                                                 
CONECT 5274 5277 5282                                                           
CONECT 5275 5276 5278 5279                                                      
CONECT 5276 5275 5277                                                           
CONECT 5277 5274 5276 5280                                                      
CONECT 5278 5275 5281                                                           
CONECT 5279 5275                                                                
CONECT 5280 5277 5298                                                           
CONECT 5281 5278 5284                                                           
CONECT 5282 5274 5309                                                           
CONECT 5283 5286 5300                                                           
CONECT 5284 5281 5287                                                           
CONECT 5285 5309                                                                
CONECT 5286 5270 5272 5283                                                      
CONECT 5287 5284 5289                                                           
CONECT 5288 5290 5296                                                           
CONECT 5289 5287 5291                                                           
CONECT 5290 5288 5292                                                           
CONECT 5291 5289 5293                                                           
CONECT 5292 5290 5294                                                           
CONECT 5293 5291 5295                                                           
CONECT 5294 5292 5297                                                           
CONECT 5295 5293 5296                                                           
CONECT 5296 5288 5295                                                           
CONECT 5297 5294 5299                                                           
CONECT 5298 5273 5280                                                           
CONECT 5299 5297 5301                                                           
CONECT 5300 5273 5283                                                           
CONECT 5301 5299 5303                                                           
CONECT 5302 5273                                                                
CONECT 5303 5301                                                                
CONECT 5304 5273                                                                
CONECT 5305 5306 5317                                                           
CONECT 5306 5305 5307                                                           
CONECT 5307 5306 5308                                                           
CONECT 5308 5307 5318                                                           
CONECT 5309 5282 5285 5310                                                      
CONECT 5310 5309 5311                                                           
CONECT 5311 5310 5312                                                           
CONECT 5312 5311 5313                                                           
CONECT 5313 5312 5314                                                           
CONECT 5314 5313 5315                                                           
CONECT 5315 5314 5316                                                           
CONECT 5316 5315 5317                                                           
CONECT 5317 5305 5316                                                           
CONECT 5318 5308 5320                                                           
CONECT 5319 5320                                                                
CONECT 5320 5318 5319                                                           
MASTER      440    0   20   25    4    0    0    6 5285    2  444   58          
END