HEADER    MEMBRANE PROTEIN/ANTAGONIST             13-APR-18   6D27              
TITLE     CRYSTAL STRUCTURE OF THE PROSTAGLANDIN D2 RECEPTOR CRTH2 WITH CAY10471
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN D2 RECEPTOR 2, ENDOLYSIN CHIMERA;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CRTH2 (UNP RESIDUES 1-236), T4 LIGASE (UNP RESIDUES 2-12,  
COMPND   5 61-161), CRTH2 (UNP RESIDUES 238-339);                               
COMPND   6 SYNONYM: CHEMOATTRACTANT RECEPTOR-HOMOLOGOUS MOLECULE EXPRESSED ON   
COMPND   7 TH2 CELLS,G-PROTEIN COUPLED RECEPTOR 44,LYSIS PROTEIN,LYSOZYME,      
COMPND   8 MURAMIDASE;                                                          
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: PTGDR2, CRTH2, DL1R, GPR44, E, T4TP126;                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9                                     
KEYWDS    GPCR, MEMBRANE PROTEIN-ANTAGONIST COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.WANG,D.YAO,K.DEEPAK,H.LIU,W.GONG,H.FAN,Z.WEI,C.ZHANG                
REVDAT   3   08-JAN-20 6D27    1       REMARK                                   
REVDAT   2   17-APR-19 6D27    1       JRNL                                     
REVDAT   1   03-OCT-18 6D27    0                                                
JRNL        AUTH   L.WANG,D.YAO,R.N.V.K.DEEPAK,H.LIU,Q.XIAO,H.FAN,W.GONG,Z.WEI, 
JRNL        AUTH 2 C.ZHANG                                                      
JRNL        TITL   STRUCTURES OF THE HUMAN PGD2RECEPTOR CRTH2 REVEAL NOVEL      
JRNL        TITL 2 MECHANISMS FOR LIGAND RECOGNITION.                           
JRNL        REF    MOL. CELL                     V.  72    48 2018              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   30220562                                                     
JRNL        DOI    10.1016/J.MOLCEL.2018.08.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 22256                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1115                            
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 30.0431 -  5.4659    0.93     2884   153  0.2100 0.2199        
REMARK   3     2  5.4659 -  4.3426    0.95     2791   146  0.2197 0.2521        
REMARK   3     3  4.3426 -  3.7949    0.97     2840   150  0.2284 0.2986        
REMARK   3     4  3.7949 -  3.4485    0.97     2793   147  0.2659 0.3616        
REMARK   3     5  3.4485 -  3.2016    0.97     2778   146  0.2964 0.3279        
REMARK   3     6  3.2016 -  3.0130    0.94     2674   142  0.3132 0.3394        
REMARK   3     7  3.0130 -  2.8623    0.87     2500   132  0.3141 0.3350        
REMARK   3     8  2.8623 -  2.7378    0.67     1881    99  0.3383 0.4232        
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 95.20                          
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      :  0.002           3677                                  
REMARK   3   ANGLE     :  0.609           4976                                  
REMARK   3   CHIRALITY :  0.020            564                                  
REMARK   3   PLANARITY :  0.003            610                                  
REMARK   3   DIHEDRAL  : 12.031           1335                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 215 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  49.1293 -50.1752 296.8546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5435 T22:   0.7213                                     
REMARK   3      T33:   0.4353 T12:  -0.0181                                     
REMARK   3      T13:  -0.0049 T23:   0.0986                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0982 L22:   1.5271                                     
REMARK   3      L33:   5.0114 L12:  -0.4550                                     
REMARK   3      L13:   0.5274 L23:  -0.4313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0300 S12:   0.7749 S13:   0.2321                       
REMARK   3      S21:  -0.3103 S22:  -0.0359 S23:   0.0714                       
REMARK   3      S31:   0.1063 S32:  -0.0253 S33:   0.0087                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 1261 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  62.1237 -65.3919 328.8454              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1329 T22:   0.7121                                     
REMARK   3      T33:   0.6075 T12:   0.0444                                     
REMARK   3      T13:  -0.1115 T23:   0.1090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0785 L22:   4.2147                                     
REMARK   3      L33:   2.5762 L12:   0.7128                                     
REMARK   3      L13:   0.7555 L23:  -2.3680                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9628 S12:  -0.3685 S13:  -0.4742                       
REMARK   3      S21:   1.2084 S22:  -0.3802 S23:  -0.3238                       
REMARK   3      S31:   0.7474 S32:   1.8192 S33:  -0.2759                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1262 THROUGH 2244 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  61.7959 -44.5557 340.0589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8750 T22:   0.8578                                     
REMARK   3      T33:   0.4772 T12:   0.0655                                     
REMARK   3      T13:  -0.0630 T23:  -0.0820                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9663 L22:   5.0120                                     
REMARK   3      L33:   4.0817 L12:  -0.8323                                     
REMARK   3      L13:  -2.0076 L23:   2.3456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0887 S12:  -0.1890 S13:   0.0434                       
REMARK   3      S21:   0.1907 S22:   0.1576 S23:  -0.2852                       
REMARK   3      S31:   0.4130 S32:   0.9380 S33:  -0.1133                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2245 THROUGH 2327 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  42.1516 -58.8052 303.0287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4063 T22:   0.5669                                     
REMARK   3      T33:   0.3679 T12:  -0.1195                                     
REMARK   3      T13:  -0.0642 T23:   0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5882 L22:   4.0865                                     
REMARK   3      L33:   2.8311 L12:  -1.2525                                     
REMARK   3      L13:   1.1704 L23:  -0.2641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1886 S12:   0.6298 S13:  -0.2494                       
REMARK   3      S21:  -0.1855 S22:   0.2008 S23:  -0.0153                       
REMARK   3      S31:   0.6279 S32:  -0.1914 S33:   0.0809                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6D27 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000233864.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL CRYO-COOLED         
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22351                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.16600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62800                            
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: PDB ENTRY 6D26                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG300, 100 MM MES, PH 6.5, 100 MM   
REMARK 280  AMMONIUM SULFATE, 2% P400, LIPIDIC CUBIC PHASE, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       26.08750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      136.10750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.31800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      136.10750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.08750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.31800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
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 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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     GLN A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     VAL A  2328                                                      
REMARK 465     ASP A  2329                                                      
REMARK 465     ASP A  2330                                                      
REMARK 465     SER A  2331                                                      
REMARK 465     GLU A  2332                                                      
REMARK 465     LEU A  2333                                                      
REMARK 465     GLY A  2334                                                      
REMARK 465     GLY A  2335                                                      
REMARK 465     ALA A  2336                                                      
REMARK 465     GLY A  2337                                                      
REMARK 465     SER A  2338                                                      
REMARK 465     SER A  2339                                                      
REMARK 465     LEU A  2340                                                      
REMARK 465     GLU A  2341                                                      
REMARK 465     VAL A  2342                                                      
REMARK 465     LEU A  2343                                                      
REMARK 465     PHE A  2344                                                      
REMARK 465     GLN A  2345                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 176    CG   CD1  CD2                                       
REMARK 470     LEU A 189    CG   CD1  CD2                                       
REMARK 470     ASN A 190    CG   OD1  ND2                                       
REMARK 470     ARG A1245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A1247    CG1  CG2  CD1                                       
REMARK 470     ARG A1281    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1338    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A2327    CG   CD1  CD2                                       
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    THR A  64     -164.57   -121.71                                   
REMARK 500    HIS A  95       73.23     57.21                                   
REMARK 500    PHE A 215      -64.07   -150.84                                   
REMARK 500    ASP A1254       40.60    -80.20                                   
REMARK 500    ASP A1262       44.18   -102.97                                   
REMARK 500    ASP A1271       94.61    -68.02                                   
REMARK 500    LYS A1336       53.96   -103.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2402                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2403                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2404                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2405                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2406                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2407                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FT4 A 2408                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 2409                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2411                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 2412                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 2413                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 2414                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 2416                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 2417                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 2418                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6D26   RELATED DB: PDB                                   
DBREF  6D27 A    1   236  UNP    Q9Y5Y4   PD2R2_HUMAN      1    236             
DBREF  6D27 A 1246  1256  UNP    D9IEF7   D9IEF7_BPT4      2     12             
DBREF  6D27 A 1262  1362  UNP    D9IEF7   D9IEF7_BPT4     61    161             
DBREF  6D27 A 2238  2339  UNP    Q9Y5Y4   PD2R2_HUMAN    238    339             
SEQADV 6D27 GLY A    0  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 ALA A   25  UNP  Q9Y5Y4    ASN    25 ENGINEERED MUTATION            
SEQADV 6D27 ALA A  204  UNP  Q9Y5Y4    VAL   204 VARIANT                        
SEQADV 6D27 ALA A 1238  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 ASP A 1239  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 LEU A 1240  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 GLY A 1241  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 LEU A 1242  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 GLN A 1243  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 HIS A 1244  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 ARG A 1245  UNP  Q9Y5Y4              INSERTION                      
SEQADV 6D27 GLY A 1257  UNP  D9IEF7              INSERTION                      
SEQADV 6D27 GLY A 1258  UNP  D9IEF7              INSERTION                      
SEQADV 6D27 SER A 1259  UNP  D9IEF7              INSERTION                      
SEQADV 6D27 GLY A 1260  UNP  D9IEF7              INSERTION                      
SEQADV 6D27 GLY A 1261  UNP  D9IEF7              INSERTION                      
SEQADV 6D27 ALA A 1298  UNP  D9IEF7    CYS    97 ENGINEERED MUTATION            
SEQADV 6D27 LEU A 2340  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 GLU A 2341  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 VAL A 2342  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 LEU A 2343  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 PHE A 2344  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQADV 6D27 GLN A 2345  UNP  Q9Y5Y4              EXPRESSION TAG                 
SEQRES   1 A  470  GLY MET SER ALA ASN ALA THR LEU LYS PRO LEU CYS PRO          
SEQRES   2 A  470  ILE LEU GLU GLN MET SER ARG LEU GLN SER HIS SER ALA          
SEQRES   3 A  470  THR SER ILE ARG TYR ILE ASP HIS ALA ALA VAL LEU LEU          
SEQRES   4 A  470  HIS GLY LEU ALA SER LEU LEU GLY LEU VAL GLU ASN GLY          
SEQRES   5 A  470  VAL ILE LEU PHE VAL VAL GLY CYS ARG MET ARG GLN THR          
SEQRES   6 A  470  VAL VAL THR THR TRP VAL LEU HIS LEU ALA LEU SER ASP          
SEQRES   7 A  470  LEU LEU ALA SER ALA SER LEU PRO PHE PHE THR TYR PHE          
SEQRES   8 A  470  LEU ALA VAL GLY HIS SER TRP GLU LEU GLY THR THR PHE          
SEQRES   9 A  470  CYS LYS LEU HIS SER SER ILE PHE PHE LEU ASN MET PHE          
SEQRES  10 A  470  ALA SER GLY PHE LEU LEU SER ALA ILE SER LEU ASP ARG          
SEQRES  11 A  470  CYS LEU GLN VAL VAL ARG PRO VAL TRP ALA GLN ASN HIS          
SEQRES  12 A  470  ARG THR VAL ALA ALA ALA HIS LYS VAL CYS LEU VAL LEU          
SEQRES  13 A  470  TRP ALA LEU ALA VAL LEU ASN THR VAL PRO TYR PHE VAL          
SEQRES  14 A  470  PHE ARG ASP THR ILE SER ARG LEU ASP GLY ARG ILE MET          
SEQRES  15 A  470  CYS TYR TYR ASN VAL LEU LEU LEU ASN PRO GLY PRO ASP          
SEQRES  16 A  470  ARG ASP ALA THR CYS ASN SER ARG GLN ALA ALA LEU ALA          
SEQRES  17 A  470  VAL SER LYS PHE LEU LEU ALA PHE LEU VAL PRO LEU ALA          
SEQRES  18 A  470  ILE ILE ALA SER SER HIS ALA ALA VAL SER LEU ARG LEU          
SEQRES  19 A  470  GLN HIS ARG ALA ASP LEU GLY LEU GLN HIS ARG ASN ILE          
SEQRES  20 A  470  PHE GLU MET LEU ARG ILE ASP GLU GLY GLY GLY SER GLY          
SEQRES  21 A  470  GLY ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  22 A  470  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  23 A  470  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  24 A  470  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  25 A  470  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  26 A  470  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  27 A  470  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  28 A  470  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR ARG ARG          
SEQRES  29 A  470  ARG PRO GLY ARG PHE VAL ARG LEU VAL ALA ALA VAL VAL          
SEQRES  30 A  470  ALA ALA PHE ALA LEU CYS TRP GLY PRO TYR HIS VAL PHE          
SEQRES  31 A  470  SER LEU LEU GLU ALA ARG ALA HIS ALA ASN PRO GLY LEU          
SEQRES  32 A  470  ARG PRO LEU VAL TRP ARG GLY LEU PRO PHE VAL THR SER          
SEQRES  33 A  470  LEU ALA PHE PHE ASN SER VAL ALA ASN PRO VAL LEU TYR          
SEQRES  34 A  470  VAL LEU THR YCM PRO ASP MET LEU ARG LYS LEU ARG ARG          
SEQRES  35 A  470  SER LEU ARG THR VAL LEU GLU SER VAL LEU VAL ASP ASP          
SEQRES  36 A  470  SER GLU LEU GLY GLY ALA GLY SER SER LEU GLU VAL LEU          
SEQRES  37 A  470  PHE GLN                                                      
MODRES 6D27 YCM A 2308  CYS  MODIFIED RESIDUE                                   
HET    YCM  A2308      10                                                       
HET    SO4  A2401       5                                                       
HET    SO4  A2402       5                                                       
HET    SO4  A2403       5                                                       
HET    SO4  A2404       5                                                       
HET    SO4  A2405       5                                                       
HET    SO4  A2406       5                                                       
HET    SO4  A2407       5                                                       
HET    FT4  A2408      29                                                       
HET    MES  A2409      12                                                       
HET    OLA  A2410      20                                                       
HET    OLA  A2411      20                                                       
HET    PGE  A2412      10                                                       
HET    PGE  A2413      10                                                       
HET    PGO  A2414       5                                                       
HET    PGO  A2415       5                                                       
HET    PGO  A2416       5                                                       
HET    PGO  A2417       5                                                       
HET    PEG  A2418       7                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FT4 [(3R)-3-{[(4-FLUOROPHENYL)SULFONYL](METHYL)AMINO}-1,2,           
HETNAM   2 FT4  3,4-TETRAHYDRO-9H-CARBAZOL-9-YL]ACETIC ACID                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     OLA OLEIC ACID                                                       
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     PGO S-1,2-PROPANEDIOL                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     FT4 CAY10471                                                         
FORMUL   1  YCM    C5 H10 N2 O3 S                                               
FORMUL   2  SO4    7(O4 S 2-)                                                   
FORMUL   9  FT4    C21 H21 F N2 O4 S                                            
FORMUL  10  MES    C6 H13 N O4 S                                                
FORMUL  11  OLA    2(C18 H34 O2)                                                
FORMUL  13  PGE    2(C6 H14 O4)                                                 
FORMUL  15  PGO    4(C3 H8 O2)                                                  
FORMUL  19  PEG    C4 H10 O3                                                    
FORMUL  20  HOH   *8(H2 O)                                                      
HELIX    1 AA1 CYS A   11  SER A   18  1                                   8    
HELIX    2 AA2 ASP A   32  ARG A   60  1                                  29    
HELIX    3 AA3 VAL A   65  VAL A   93  1                                  29    
HELIX    4 AA4 THR A  101  ARG A  135  1                                  35    
HELIX    5 AA5 ARG A  135  ARG A  143  1                                   9    
HELIX    6 AA6 THR A  144  THR A  163  1                                  20    
HELIX    7 AA7 THR A  163  PHE A  169  1                                   7    
HELIX    8 AA8 ASP A  194  ALA A  214  1                                  21    
HELIX    9 AA9 PHE A  215  LEU A 1242  1                                  27    
HELIX   10 AB1 ASP A 1271  ASN A 1282  1                                  12    
HELIX   11 AB2 LEU A 1285  LEU A 1292  1                                   8    
HELIX   12 AB3 ASP A 1293  ALA A 1313  1                                  21    
HELIX   13 AB4 PHE A 1315  GLN A 1324  1                                  10    
HELIX   14 AB5 ARG A 1326  LYS A 1336  1                                  11    
HELIX   15 AB6 SER A 1337  THR A 1343  1                                   7    
HELIX   16 AB7 THR A 1343  GLY A 1357  1                                  15    
HELIX   17 AB8 ALA A 1361  ARG A 2240  5                                   5    
HELIX   18 AB9 PHE A 2244  TRP A 2259  1                                  16    
HELIX   19 AC1 TRP A 2259  ALA A 2272  1                                  14    
HELIX   20 AC2 HIS A 2273  ALA A 2274  5                                   2    
HELIX   21 AC3 ASN A 2275  GLY A 2277  5                                   3    
HELIX   22 AC4 LEU A 2278  PHE A 2295  1                                  18    
HELIX   23 AC5 PHE A 2295  THR A 2307  1                                  13    
HELIX   24 AC6 YCM A 2308  LEU A 2327  1                                  20    
SHEET    1 AA1 2 ARG A 170  SER A 174  0                                        
SHEET    2 AA1 2 ILE A 180  TYR A 184 -1  O  MET A 181   N  ILE A 173           
SSBOND   1 CYS A   11    CYS A  199                          1555   1555  2.03  
SSBOND   2 CYS A  104    CYS A  182                          1555   1555  2.03  
LINK         C   THR A2307                 N   YCM A2308     1555   1555  1.33  
LINK         C   YCM A2308                 N   PRO A2309     1555   1555  1.34  
SITE     1 AC1  9 ARG A1320  GLN A1324  ARG A1326  GLY A2242                    
SITE     2 AC1  9 ARG A2243  PHE A2244  VAL A2245  ARG A2246                    
SITE     3 AC1  9 YCM A2308                                                     
SITE     1 AC2  7 GLN A 140  LEU A1251  ARG A1349  TRP A1359                    
SITE     2 AC2  7 ALA A1361  TYR A1362  ARG A2238                               
SITE     1 AC3  6 THR A 144  VAL A 145  THR A1343  PRO A1344                    
SITE     2 AC3  6 ASN A1345  ARG A1346                                          
SITE     1 AC4  6 THR A  64  VAL A  65  VAL A  66  ARG A 143                    
SITE     2 AC4  6 ARG A2243  HOH A2502                                          
SITE     1 AC5  3 ARG A  62  ASP A2310  LYS A2314                               
SITE     1 AC6  3 GLY A1256  GLY A1257  LYS A1266                               
SITE     1 AC7  2 ARG A1277  HOH A2504                                          
SITE     1 AC8 10 MET A  17  PHE A 111  ARG A 170  TYR A 183                    
SITE     2 AC8 10 TYR A 184  TYR A2262  TRP A2283  LEU A2286                    
SITE     3 AC8 10 THR A2290  PGO A2416                                          
SITE     1 AC9  6 PHE A1315  THR A1316  ASN A1317  SER A1318                    
SITE     2 AC9  6 ASN A1333  ARG A2239                                          
SITE     1 AD1  3 LEU A  71  HIS A  72  HIS A 149                               
SITE     1 AD2  2 ASP A 128  ARG A 143                                          
SITE     1 AD3  2 GLU A1249  MET A1250                                          
SITE     1 AD4  5 ARG A2246  YCM A2308  PRO A2309  ASP A2310                    
SITE     2 AD4  5 ARG A2313                                                     
SITE     1 AD5  3 ARG A 175  ARG A 179  FT4 A2408                               
SITE     1 AD6  4 GLY A  40  LEU A  44  PRO A  85  THR A  88                    
SITE     1 AD7  3 SER A 109  THR A 163  PHE A 167                               
CRYST1   52.175   62.636  272.215  90.00  90.00  90.00 P 21 21 21    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      0.019166  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015965  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003674        0.00000                         
ATOM      1  N   ALA A   5      50.796 -37.332 265.589  1.00113.03           N  
ANISOU    1  N   ALA A   5    14347  20817   7783    598    177   5567       N  
ATOM      2  CA  ALA A   5      50.697 -38.544 266.393  1.00119.48           C  
ANISOU    2  CA  ALA A   5    15045  21662   8690    636    151   5203       C  
ATOM      3  C   ALA A   5      52.062 -38.955 266.931  1.00122.31           C  
ANISOU    3  C   ALA A   5    15280  22061   9131    496    349   5131       C  
ATOM      4  O   ALA A   5      53.096 -38.553 266.398  1.00110.49           O  
ANISOU    4  O   ALA A   5    13747  20694   7543    395    510   5310       O  
ATOM      5  CB  ALA A   5      50.085 -39.675 265.578  1.00109.87           C  
ANISOU    5  CB  ALA A   5    13792  20754   7201    809     54   4910       C  
ATOM      6  N   THR A   6      52.061 -39.755 267.991  1.00104.18           N  
ANISOU    6  N   THR A   6    12912  19668   7002    491    334   4873       N  
ATOM      7  CA  THR A   6      53.304 -40.220 268.594  1.00123.50           C  
ANISOU    7  CA  THR A   6    15232  22159   9535    386    507   4778       C  
ATOM      8  C   THR A   6      53.417 -41.739 268.527  1.00124.09           C  
ANISOU    8  C   THR A   6    15230  22458   9459    524    515   4386       C  
ATOM      9  O   THR A   6      52.563 -42.409 267.946  1.00125.15           O  
ANISOU    9  O   THR A   6    15422  22716   9415    673    388   4192       O  
ATOM     10  CB  THR A   6      53.424 -39.772 270.063  1.00117.93           C  
ANISOU   10  CB  THR A   6    14527  21100   9183    239    505   4835       C  
ATOM     11  OG1 THR A   6      52.366 -40.356 270.836  1.00 99.83           O  
ANISOU   11  OG1 THR A   6    12268  18659   7005    336    347   4611       O  
ATOM     12  CG2 THR A   6      53.351 -38.255 270.164  1.00119.68           C  
ANISOU   12  CG2 THR A   6    14873  21046   9556    101    491   5211       C  
ATOM     13  N   LEU A   7      54.478 -42.273 269.124  1.00119.49           N  
ANISOU   13  N   LEU A   7    14532  21920   8948    475    658   4267       N  
ATOM     14  CA  LEU A   7      54.708 -43.713 269.150  1.00123.43           C  
ANISOU   14  CA  LEU A   7    14990  22590   9316    620    678   3891       C  
ATOM     15  C   LEU A   7      55.693 -44.088 270.252  1.00126.30           C  
ANISOU   15  C   LEU A   7    15239  22882   9866    553    801   3796       C  
ATOM     16  O   LEU A   7      56.814 -43.583 270.291  1.00130.33           O  
ANISOU   16  O   LEU A   7    15625  23473  10422    441    958   3976       O  
ATOM     17  CB  LEU A   7      55.227 -44.202 267.795  1.00125.58           C  
ANISOU   17  CB  LEU A   7    15238  23230   9248    754    765   3827       C  
ATOM     18  CG  LEU A   7      55.526 -45.699 267.691  1.00127.66           C  
ANISOU   18  CG  LEU A   7    15503  23660   9343    936    788   3431       C  
ATOM     19  CD1 LEU A   7      54.291 -46.516 268.040  1.00134.13           C  
ANISOU   19  CD1 LEU A   7    16466  24325  10172   1013    584   3140       C  
ATOM     20  CD2 LEU A   7      56.032 -46.052 266.301  1.00126.91           C  
ANISOU   20  CD2 LEU A   7    15397  23922   8903   1079    875   3396       C  
ATOM     21  N   LYS A   8      55.270 -44.976 271.146  1.00121.97           N  
ANISOU   21  N   LYS A   8    14729  22194   9418    612    722   3514       N  
ATOM     22  CA  LYS A   8      56.130 -45.422 272.235  1.00115.10           C  
ANISOU   22  CA  LYS A   8    13764  21253   8714    574    823   3398       C  
ATOM     23  C   LYS A   8      56.511 -46.894 272.074  1.00117.19           C  
ANISOU   23  C   LYS A   8    14039  21692   8795    776    860   3027       C  
ATOM     24  O   LYS A   8      55.675 -47.723 271.716  1.00121.30           O  
ANISOU   24  O   LYS A   8    14699  22220   9171    905    734   2779       O  
ATOM     25  CB  LYS A   8      55.447 -45.194 273.590  1.00 99.64           C  
ANISOU   25  CB  LYS A   8    11857  18952   7052    471    716   3394       C  
ATOM     26  CG  LYS A   8      54.119 -45.922 273.762  1.00105.80           C  
ANISOU   26  CG  LYS A   8    12771  19628   7802    569    525   3152       C  
ATOM     27  CD  LYS A   8      53.513 -45.682 275.139  1.00102.67           C  
ANISOU   27  CD  LYS A   8    12399  18918   7694    472    434   3161       C  
ATOM     28  CE  LYS A   8      53.045 -44.244 275.300  1.00100.75           C  
ANISOU   28  CE  LYS A   8    12175  18476   7630    346    382   3507       C  
ATOM     29  NZ  LYS A   8      52.323 -44.036 276.587  1.00 79.83           N  
ANISOU   29  NZ  LYS A   8     9562  15528   5242    288    278   3503       N  
ATOM     30  N   PRO A   9      57.790 -47.216 272.314  1.00109.98           N  
ANISOU   30  N   PRO A   9    12985  20920   7882    808   1027   2987       N  
ATOM     31  CA  PRO A   9      58.253 -48.608 272.332  1.00106.15           C  
ANISOU   31  CA  PRO A   9    12525  20553   7252   1028   1069   2632       C  
ATOM     32  C   PRO A   9      57.798 -49.333 273.596  1.00105.01           C  
ANISOU   32  C   PRO A   9    12478  20137   7284   1043    980   2391       C  
ATOM     33  O   PRO A   9      57.862 -48.767 274.689  1.00 99.53           O  
ANISOU   33  O   PRO A   9    11717  19246   6853    884    985   2521       O  
ATOM     34  CB  PRO A   9      59.777 -48.472 272.288  1.00102.14           C  
ANISOU   34  CB  PRO A   9    11796  20285   6729   1040   1272   2737       C  
ATOM     35  CG  PRO A   9      60.047 -47.131 272.874  1.00101.96           C  
ANISOU   35  CG  PRO A   9    11645  20142   6954    761   1309   3091       C  
ATOM     36  CD  PRO A   9      58.901 -46.260 272.459  1.00102.24           C  
ANISOU   36  CD  PRO A   9    11814  20018   7013    643   1179   3284       C  
ATOM     37  N   LEU A  10      57.340 -50.572 273.444  1.00102.18           N  
ANISOU   37  N   LEU A  10    12292  19755   6775   1221    894   2041       N  
ATOM     38  CA  LEU A  10      56.782 -51.322 274.564  1.00 99.55           C  
ANISOU   38  CA  LEU A  10    12087  19156   6582   1226    789   1799       C  
ATOM     39  C   LEU A  10      57.433 -52.694 274.721  1.00102.04           C  
ANISOU   39  C   LEU A  10    12494  19497   6781   1454    841   1452       C  
ATOM     40  O   LEU A  10      57.991 -53.240 273.769  1.00111.46           O  
ANISOU   40  O   LEU A  10    13709  20904   7737   1639    910   1339       O  
ATOM     41  CB  LEU A  10      55.270 -51.485 274.388  1.00102.96           C  
ANISOU   41  CB  LEU A  10    12697  19443   6981   1173    570   1700       C  
ATOM     42  CG  LEU A  10      54.451 -50.201 274.241  1.00102.00           C  
ANISOU   42  CG  LEU A  10    12516  19270   6971    996    487   2019       C  
ATOM     43  CD1 LEU A  10      52.977 -50.523 274.045  1.00 92.57           C  
ANISOU   43  CD1 LEU A  10    11466  17985   5722    975    260   1883       C  
ATOM     44  CD2 LEU A  10      54.653 -49.298 275.447  1.00111.45           C  
ANISOU   44  CD2 LEU A  10    13597  20269   8478    828    532   2250       C  
ATOM     45  N   CYS A  11      57.353 -53.243 275.930  1.00 98.55           N  
ANISOU   45  N   CYS A  11    12117  18824   6502   1453    805   1287       N  
ATOM     46  CA  CYS A  11      57.863 -54.582 276.209  1.00 96.67           C  
ANISOU   46  CA  CYS A  11    12017  18536   6177   1680    831    946       C  
ATOM     47  C   CYS A  11      56.977 -55.642 275.564  1.00101.20           C  
ANISOU   47  C   CYS A  11    12887  19019   6544   1779    671    630       C  
ATOM     48  O   CYS A  11      55.773 -55.435 275.413  1.00112.30           O  
ANISOU   48  O   CYS A  11    14388  20327   7956   1629    504    639       O  
ATOM     49  CB  CYS A  11      57.955 -54.820 277.720  1.00 87.47           C  
ANISOU   49  CB  CYS A  11    10859  17128   5249   1637    825    874       C  
ATOM     50  SG  CYS A  11      59.247 -53.871 278.554  1.00123.42           S  
ANISOU   50  SG  CYS A  11    15082  21791  10021   1551   1016   1167       S  
ATOM     51  N   PRO A  12      57.575 -56.781 275.175  1.00 98.06           N  
ANISOU   51  N   PRO A  12    12637  18655   5965   2032    712    350       N  
ATOM     52  CA  PRO A  12      56.832 -57.890 274.565  1.00106.33           C  
ANISOU   52  CA  PRO A  12    14009  19582   6809   2120    556     21       C  
ATOM     53  C   PRO A  12      55.654 -58.370 275.415  1.00120.37           C  
ANISOU   53  C   PRO A  12    16001  21025   8711   1960    354   -157       C  
ATOM     54  O   PRO A  12      54.659 -58.841 274.864  1.00129.62           O  
ANISOU   54  O   PRO A  12    17380  22120   9750   1890    175   -324       O  
ATOM     55  CB  PRO A  12      57.890 -58.988 274.440  1.00 97.11           C  
ANISOU   55  CB  PRO A  12    12953  18434   5511   2429    661   -225       C  
ATOM     56  CG  PRO A  12      59.170 -58.246 274.306  1.00 93.90           C  
ANISOU   56  CG  PRO A  12    12211  18338   5129   2515    880     34       C  
ATOM     57  CD  PRO A  12      59.027 -57.035 275.185  1.00 90.34           C  
ANISOU   57  CD  PRO A  12    11518  17858   4950   2252    905    347       C  
ATOM     58  N   ILE A  13      55.772 -58.253 276.735  1.00113.62           N  
ANISOU   58  N   ILE A  13    15085  19988   8097   1892    377   -121       N  
ATOM     59  CA  ILE A  13      54.687 -58.627 277.634  1.00107.36           C  
ANISOU   59  CA  ILE A  13    14458  18900   7435   1724    195   -262       C  
ATOM     60  C   ILE A  13      53.463 -57.747 277.387  1.00101.61           C  
ANISOU   60  C   ILE A  13    13630  18201   6774   1464     51    -71       C  
ATOM     61  O   ILE A  13      52.326 -58.217 277.428  1.00102.88           O  
ANISOU   61  O   ILE A  13    13951  18168   6972   1314   -149   -232       O  
ATOM     62  CB  ILE A  13      55.111 -58.512 279.114  1.00112.18           C  
ANISOU   62  CB  ILE A  13    14975  19253   8396   1671    262   -211       C  
ATOM     63  CG1 ILE A  13      56.420 -59.264 279.359  1.00118.93           C  
ANISOU   63  CG1 ILE A  13    15881  20170   9137   1974    417   -358       C  
ATOM     64  CG2 ILE A  13      54.013 -59.033 280.030  1.00109.78           C  
ANISOU   64  CG2 ILE A  13    14843  18509   8357   1464     75   -372       C  
ATOM     65  CD1 ILE A  13      56.909 -59.186 280.793  1.00111.35           C  
ANISOU   65  CD1 ILE A  13    14823  18957   8529   1932    477   -310       C  
ATOM     66  N   LEU A  14      53.711 -56.470 277.116  1.00 98.12           N  
ANISOU   66  N   LEU A  14    12922  17981   6376   1401    150    280       N  
ATOM     67  CA  LEU A  14      52.644 -55.502 276.889  1.00 93.91           C  
ANISOU   67  CA  LEU A  14    12280  17462   5938   1191     29    503       C  
ATOM     68  C   LEU A  14      52.049 -55.586 275.491  1.00 94.08           C  
ANISOU   68  C   LEU A  14    12381  17683   5683   1216    -75    467       C  
ATOM     69  O   LEU A  14      50.834 -55.486 275.321  1.00106.76           O  
ANISOU   69  O   LEU A  14    14022  19261   7282   1076   -266    457       O  
ATOM     70  CB  LEU A  14      53.161 -54.085 277.127  1.00 91.09           C  
ANISOU   70  CB  LEU A  14    11656  17197   5758   1112    167    899       C  
ATOM     71  CG  LEU A  14      53.284 -53.632 278.577  1.00 93.46           C  
ANISOU   71  CG  LEU A  14    11851  17168   6492    974    199    990       C  
ATOM     72  CD1 LEU A  14      54.085 -52.347 278.643  1.00108.78           C  
ANISOU   72  CD1 LEU A  14    13565  19239   8526    917    355   1353       C  
ATOM     73  CD2 LEU A  14      51.904 -53.440 279.186  1.00 86.26           C  
ANISOU   73  CD2 LEU A  14    10971  15973   5833    787     11    975       C  
ATOM     74  N   GLU A  15      52.910 -55.757 274.493  1.00 87.00           N  
ANISOU   74  N   GLU A  15    11491  16982   4582   1390     50    450       N  
ATOM     75  CA  GLU A  15      52.489 -55.706 273.098  1.00 91.76           C  
ANISOU   75  CA  GLU A  15    12146  17780   4937   1421    -21    453       C  
ATOM     76  C   GLU A  15      51.453 -56.776 272.764  1.00102.84           C  
ANISOU   76  C   GLU A  15    13816  19069   6188   1384   -247    122       C  
ATOM     77  O   GLU A  15      50.542 -56.537 271.970  1.00109.64           O  
ANISOU   77  O   GLU A  15    14693  20034   6933   1299   -394    159       O  
ATOM     78  CB  GLU A  15      53.698 -55.841 272.171  1.00 94.18           C  
ANISOU   78  CB  GLU A  15    12420  18321   5043   1633    166    461       C  
ATOM     79  CG  GLU A  15      53.381 -55.567 270.712  1.00111.86           C  
ANISOU   79  CG  GLU A  15    14674  20802   7027   1665    125    530       C  
ATOM     80  CD  GLU A  15      54.415 -54.680 270.053  1.00122.25           C  
ANISOU   80  CD  GLU A  15    15769  22397   8284   1738    334    823       C  
ATOM     81  OE1 GLU A  15      55.359 -54.251 270.750  1.00123.59           O  
ANISOU   81  OE1 GLU A  15    15761  22574   8624   1740    501    978       O  
ATOM     82  OE2 GLU A  15      54.282 -54.410 268.840  1.00129.79           O  
ANISOU   82  OE2 GLU A  15    16725  23570   9018   1779    325    902       O  
ATOM     83  N   GLN A  16      51.588 -57.950 273.372  1.00107.59           N  
ANISOU   83  N   GLN A  16    14636  19450   6794   1437   -284   -196       N  
ATOM     84  CA  GLN A  16      50.615 -59.016 273.167  1.00114.91           C  
ANISOU   84  CA  GLN A  16    15845  20217   7596   1352   -512   -520       C  
ATOM     85  C   GLN A  16      49.293 -58.674 273.847  1.00119.20           C  
ANISOU   85  C   GLN A  16    16319  20657   8314   1080   -712   -463       C  
ATOM     86  O   GLN A  16      48.222 -59.006 273.340  1.00127.69           O  
ANISOU   86  O   GLN A  16    17494  21740   9281    939   -925   -585       O  
ATOM     87  CB  GLN A  16      51.150 -60.353 273.686  1.00114.76           C  
ANISOU   87  CB  GLN A  16    16111  19940   7551   1477   -496   -863       C  
ATOM     88  CG  GLN A  16      52.302 -60.913 272.870  1.00111.74           C  
ANISOU   88  CG  GLN A  16    15834  19665   6956   1766   -338   -980       C  
ATOM     89  CD  GLN A  16      52.586 -62.370 273.182  1.00113.56           C  
ANISOU   89  CD  GLN A  16    16420  19602   7125   1890   -377  -1357       C  
ATOM     90  OE1 GLN A  16      51.889 -62.994 273.981  1.00109.26           O  
ANISOU   90  OE1 GLN A  16    16069  18754   6690   1734   -532  -1538       O  
ATOM     91  NE2 GLN A  16      53.614 -62.919 272.547  1.00122.51           N  
ANISOU   91  NE2 GLN A  16    17642  20821   8085   2174   -239  -1469       N  
ATOM     92  N   MET A  17      49.374 -58.006 274.994  1.00112.52           N  
ANISOU   92  N   MET A  17    15285  19731   7736   1003   -644   -273       N  
ATOM     93  CA  MET A  17      48.180 -57.556 275.702  1.00111.82           C  
ANISOU   93  CA  MET A  17    15077  19506   7904    750   -801   -176       C  
ATOM     94  C   MET A  17      47.482 -56.438 274.937  1.00117.31           C  
ANISOU   94  C   MET A  17    15571  20487   8514    694   -872    107       C  
ATOM     95  O   MET A  17      46.273 -56.251 275.060  1.00129.79           O  
ANISOU   95  O   MET A  17    17084  22036  10195    514  -1056    132       O  
ATOM     96  CB  MET A  17      48.532 -57.084 277.114  1.00100.80           C  
ANISOU   96  CB  MET A  17    13539  17826   6936    685   -682    -34       C  
ATOM     97  CG  MET A  17      48.756 -58.208 278.109  1.00 94.17           C  
ANISOU   97  CG  MET A  17    12898  16631   6251    666   -685   -311       C  
ATOM     98  SD  MET A  17      49.279 -57.594 279.720  1.00139.84           S  
ANISOU   98  SD  MET A  17    18506  22131  12496    617   -536   -133       S  
ATOM     99  CE  MET A  17      48.063 -56.309 280.001  1.00 91.46           C  
ANISOU   99  CE  MET A  17    12120  16020   6611    402   -638    157       C  
ATOM    100  N   SER A  18      48.253 -55.700 274.145  1.00115.06           N  
ANISOU  100  N   SER A  18    15185  20395   8137    839   -713    326       N  
ATOM    101  CA  SER A  18      47.712 -54.603 273.351  1.00133.76           C  
ANISOU  101  CA  SER A  18    17392  22958  10473    810   -756    612       C  
ATOM    102  C   SER A  18      47.126 -55.107 272.035  1.00147.26           C  
ANISOU  102  C   SER A  18    19230  24826  11896    832   -900    457       C  
ATOM    103  O   SER A  18      46.631 -54.323 271.224  1.00142.68           O  
ANISOU  103  O   SER A  18    18546  24424  11243    830   -954    660       O  
ATOM    104  CB  SER A  18      48.795 -53.556 273.079  1.00138.24           C  
ANISOU  104  CB  SER A  18    17805  23645  11074    918   -526    929       C  
ATOM    105  OG  SER A  18      48.283 -52.471 272.326  1.00145.64           O  
ANISOU  105  OG  SER A  18    18620  24734  11981    895   -567   1215       O  
ATOM    106  N   ARG A  19      47.187 -56.419 271.830  1.00154.56           N  
ANISOU  106  N   ARG A  19    20404  25667  12657    857   -969     95       N  
ATOM    107  CA  ARG A  19      46.689 -57.035 270.604  1.00160.99           C  
ANISOU  107  CA  ARG A  19    21386  26602  13182    869  -1115    -93       C  
ATOM    108  C   ARG A  19      45.875 -58.294 270.893  1.00171.37           C  
ANISOU  108  C   ARG A  19    22939  27723  14452    713  -1338   -459       C  
ATOM    109  O   ARG A  19      46.291 -59.402 270.551  1.00177.92           O  
ANISOU  109  O   ARG A  19    24051  28449  15100    789  -1346   -759       O  
ATOM    110  CB  ARG A  19      47.851 -57.376 269.668  1.00151.57           C  
ANISOU  110  CB  ARG A  19    20312  25531  11748   1100   -942   -161       C  
ATOM    111  CG  ARG A  19      48.590 -56.169 269.117  1.00143.26           C  
ANISOU  111  CG  ARG A  19    19033  24713  10686   1218   -744    198       C  
ATOM    112  CD  ARG A  19      49.887 -56.585 268.445  1.00146.94           C  
ANISOU  112  CD  ARG A  19    19576  25301  10955   1445   -543    121       C  
ATOM    113  NE  ARG A  19      50.514 -55.475 267.733  1.00154.03           N  
ANISOU  113  NE  ARG A  19    20266  26457  11802   1523   -375    459       N  
ATOM    114  CZ  ARG A  19      50.352 -55.235 266.436  1.00147.83           C  
ANISOU  114  CZ  ARG A  19    19495  25910  10765   1583   -401    525       C  
ATOM    115  NH1 ARG A  19      49.583 -56.030 265.704  1.00143.20           N  
ANISOU  115  NH1 ARG A  19    19116  25342   9952   1575   -593    269       N  
ATOM    116  NH2 ARG A  19      50.960 -54.202 265.870  1.00141.83           N  
ANISOU  116  NH2 ARG A  19    18550  25367   9974   1634   -242    847       N  
ATOM    117  N   LEU A  20      44.716 -58.121 271.520  1.00170.69           N  
ANISOU  117  N   LEU A  20    22740  27581  14532    487  -1521   -430       N  
ATOM    118  CA  LEU A  20      43.845 -59.248 271.839  1.00169.37           C  
ANISOU  118  CA  LEU A  20    22768  27236  14347    272  -1749   -750       C  
ATOM    119  C   LEU A  20      42.441 -59.040 271.280  1.00165.89           C  
ANISOU  119  C   LEU A  20    22215  26956  13858     79  -1999   -717       C  
ATOM    120  O   LEU A  20      41.696 -58.181 271.751  1.00162.36           O  
ANISOU  120  O   LEU A  20    21486  26595  13606    -24  -2050   -486       O  
ATOM    121  CB  LEU A  20      43.781 -59.467 273.352  1.00166.46           C  
ANISOU  121  CB  LEU A  20    22365  26626  14254    135  -1736   -794       C  
ATOM    122  CG  LEU A  20      45.078 -59.909 274.032  1.00164.44           C  
ANISOU  122  CG  LEU A  20    22254  26175  14049    313  -1524   -890       C  
ATOM    123  CD1 LEU A  20      44.869 -60.091 275.529  1.00157.33           C  
ANISOU  123  CD1 LEU A  20    21317  24943  13518    147  -1516   -909       C  
ATOM    124  CD2 LEU A  20      45.605 -61.188 273.400  1.00167.38           C  
ANISOU  124  CD2 LEU A  20    23008  26413  14175    428  -1539  -1234       C  
ATOM    125  N   ALA A  25      38.618 -56.408 266.704  1.00140.20           N  
ANISOU  125  N   ALA A  25    18336  24932  10002     75  -2631    -90       N  
ATOM    126  CA  ALA A  25      38.125 -55.930 265.418  1.00122.86           C  
ANISOU  126  CA  ALA A  25    16084  23022   7577    160  -2732     24       C  
ATOM    127  C   ALA A  25      36.825 -55.147 265.578  1.00122.15           C  
ANISOU  127  C   ALA A  25    15683  23101   7629     82  -2892    226       C  
ATOM    128  O   ALA A  25      36.121 -54.896 264.602  1.00139.67           O  
ANISOU  128  O   ALA A  25    17839  25562   9667    107  -3039    279       O  
ATOM    129  CB  ALA A  25      37.927 -57.096 264.461  1.00116.09           C  
ANISOU  129  CB  ALA A  25    15506  22197   6405     83  -2906   -313       C  
ATOM    130  N   THR A  26      36.508 -54.769 266.814  1.00124.44           N  
ANISOU  130  N   THR A  26    15777  23270   8233      2  -2862    337       N  
ATOM    131  CA  THR A  26      35.303 -53.994 267.101  1.00127.81           C  
ANISOU  131  CA  THR A  26    15893  23851   8820    -39  -2989    537       C  
ATOM    132  C   THR A  26      35.513 -53.115 268.334  1.00113.72           C  
ANISOU  132  C   THR A  26    13926  21921   7360     23  -2831    781       C  
ATOM    133  O   THR A  26      36.270 -53.471 269.236  1.00108.90           O  
ANISOU  133  O   THR A  26    13412  21073   6891    -21  -2698    700       O  
ATOM    134  CB  THR A  26      34.075 -54.907 267.325  1.00139.36           C  
ANISOU  134  CB  THR A  26    17291  25360  10300   -324  -3250    290       C  
ATOM    135  OG1 THR A  26      34.079 -55.969 266.364  1.00153.63           O  
ANISOU  135  OG1 THR A  26    19356  27200  11816   -419  -3391     -5       O  
ATOM    136  CG2 THR A  26      32.780 -54.116 267.188  1.00134.04           C  
ANISOU  136  CG2 THR A  26    16287  24950   9691   -316  -3397    492       C  
ATOM    137  N   SER A  27      34.846 -51.965 268.365  1.00113.40           N  
ANISOU  137  N   SER A  27    13641  22016   7429    141  -2851   1076       N  
ATOM    138  CA  SER A  27      34.969 -51.031 269.481  1.00112.98           C  
ANISOU  138  CA  SER A  27    13433  21819   7674    225  -2718   1322       C  
ATOM    139  C   SER A  27      34.040 -51.397 270.637  1.00120.01           C  
ANISOU  139  C   SER A  27    14140  22664   8796     36  -2828   1223       C  
ATOM    140  O   SER A  27      34.210 -50.916 271.759  1.00117.03           O  
ANISOU  140  O   SER A  27    13673  22124   8671     64  -2720   1348       O  
ATOM    141  CB  SER A  27      34.674 -49.604 269.014  1.00113.07           C  
ANISOU  141  CB  SER A  27    13305  21958   7697    463  -2690   1683       C  
ATOM    142  OG  SER A  27      35.528 -49.228 267.949  1.00124.49           O  
ANISOU  142  OG  SER A  27    14914  23453   8933    616  -2581   1798       O  
ATOM    143  N   ILE A  28      33.060 -52.248 270.354  1.00103.57           N  
ANISOU  143  N   ILE A  28    12000  20730   6621   -169  -3041   1001       N  
ATOM    144  CA  ILE A  28      32.070 -52.652 271.346  1.00106.98           C  
ANISOU  144  CA  ILE A  28    12231  21164   7252   -386  -3154    906       C  
ATOM    145  C   ILE A  28      32.703 -53.477 272.466  1.00107.85           C  
ANISOU  145  C   ILE A  28    12481  20981   7515   -569  -3068    716       C  
ATOM    146  O   ILE A  28      33.454 -54.419 272.211  1.00110.64           O  
ANISOU  146  O   ILE A  28    13117  21187   7735   -661  -3047    480       O  
ATOM    147  CB  ILE A  28      30.932 -53.458 270.692  1.00112.65           C  
ANISOU  147  CB  ILE A  28    12876  22108   7817   -605  -3406    703       C  
ATOM    148  CG1 ILE A  28      30.333 -52.670 269.525  1.00122.34           C  
ANISOU  148  CG1 ILE A  28    13976  23642   8865   -411  -3498    884       C  
ATOM    149  CG2 ILE A  28      29.861 -53.806 271.713  1.00113.71           C  
ANISOU  149  CG2 ILE A  28    12761  22279   8164   -844  -3506    640       C  
ATOM    150  CD1 ILE A  28      29.214 -53.390 268.806  1.00134.46           C  
ANISOU  150  CD1 ILE A  28    15426  25431  10232   -616  -3753    702       C  
ATOM    151  N   ARG A  29      32.395 -53.112 273.707  1.00103.18           N  
ANISOU  151  N   ARG A  29    11702  20305   7196   -602  -3015    820       N  
ATOM    152  CA  ARG A  29      32.970 -53.774 274.873  1.00101.39           C  
ANISOU  152  CA  ARG A  29    11590  19802   7132   -762  -2926    675       C  
ATOM    153  C   ARG A  29      31.927 -54.591 275.631  1.00102.85           C  
ANISOU  153  C   ARG A  29    11634  20003   7442  -1085  -3069    503       C  
ATOM    154  O   ARG A  29      30.767 -54.191 275.733  1.00 96.37           O  
ANISOU  154  O   ARG A  29    10515  19405   6698  -1111  -3170    609       O  
ATOM    155  CB  ARG A  29      33.599 -52.742 275.811  1.00 90.60           C  
ANISOU  155  CB  ARG A  29    10153  18286   5984   -558  -2731    930       C  
ATOM    156  CG  ARG A  29      34.448 -51.698 275.106  1.00 90.65           C  
ANISOU  156  CG  ARG A  29    10241  18294   5907   -253  -2589   1176       C  
ATOM    157  CD  ARG A  29      34.826 -50.565 276.047  1.00 90.66           C  
ANISOU  157  CD  ARG A  29    10151  18147   6147    -71  -2432   1454       C  
ATOM    158  NE  ARG A  29      35.492 -49.469 275.348  1.00 88.04           N  
ANISOU  158  NE  ARG A  29     9889  17811   5752    189  -2311   1722       N  
ATOM    159  CZ  ARG A  29      35.789 -48.299 275.904  1.00 86.50           C  
ANISOU  159  CZ  ARG A  29     9650  17481   5736    372  -2190   2004       C  
ATOM    160  NH1 ARG A  29      35.479 -48.066 277.170  1.00 87.65           N  
ANISOU  160  NH1 ARG A  29     9675  17500   6126    356  -2173   2049       N  
ATOM    161  NH2 ARG A  29      36.396 -47.359 275.193  1.00 95.97           N  
ANISOU  161  NH2 ARG A  29    10939  18659   6865    563  -2088   2242       N  
ATOM    162  N   TYR A  30      32.345 -55.734 276.164  1.00102.12           N  
ANISOU  162  N   TYR A  30    11761  19672   7369  -1327  -3068    242       N  
ATOM    163  CA  TYR A  30      31.467 -56.561 276.985  1.00112.54           C  
ANISOU  163  CA  TYR A  30    12983  20950   8827  -1673  -3179     87       C  
ATOM    164  C   TYR A  30      31.662 -56.229 278.461  1.00103.79           C  
ANISOU  164  C   TYR A  30    11762  19681   7993  -1680  -3044    195       C  
ATOM    165  O   TYR A  30      32.791 -56.179 278.948  1.00 96.00           O  
ANISOU  165  O   TYR A  30    10972  18436   7068  -1569  -2879    195       O  
ATOM    166  CB  TYR A  30      31.729 -58.046 276.733  1.00123.25           C  
ANISOU  166  CB  TYR A  30    14684  22095  10051  -1954  -3272   -262       C  
ATOM    167  N   ILE A  31      30.559 -56.003 279.168  1.00109.00           N  
ANISOU  167  N   ILE A  31    12101  20486   8826  -1796  -3098    286       N  
ATOM    168  CA  ILE A  31      30.622 -55.596 280.568  1.00111.22           C  
ANISOU  168  CA  ILE A  31    12241  20653   9364  -1777  -2976    406       C  
ATOM    169  C   ILE A  31      30.220 -56.720 281.516  1.00109.77           C  
ANISOU  169  C   ILE A  31    12092  20300   9314  -2167  -3011    208       C  
ATOM    170  O   ILE A  31      29.085 -57.196 281.484  1.00116.58           O  
ANISOU  170  O   ILE A  31    12771  21347  10177  -2424  -3147    149       O  
ATOM    171  CB  ILE A  31      29.720 -54.379 280.836  1.00107.82           C  
ANISOU  171  CB  ILE A  31    11417  20487   9061  -1554  -2963    684       C  
ATOM    172  CG1 ILE A  31      30.012 -53.267 279.827  1.00108.68           C  
ANISOU  172  CG1 ILE A  31    11523  20724   9047  -1179  -2933    891       C  
ATOM    173  CG2 ILE A  31      29.905 -53.881 282.261  1.00102.42           C  
ANISOU  173  CG2 ILE A  31    10646  19582   8686  -1460  -2783    801       C  
ATOM    174  CD1 ILE A  31      29.106 -52.064 279.965  1.00111.95           C  
ANISOU  174  CD1 ILE A  31    11604  21372   9561   -921  -2930   1154       C  
ATOM    175  N   ASP A  32      31.159 -57.138 282.359  1.00106.91           N  
ANISOU  175  N   ASP A  32    11997  19479   9146  -2177  -2826    119       N  
ATOM    176  CA  ASP A  32      30.882 -58.143 283.378  1.00115.74           C  
ANISOU  176  CA  ASP A  32    13186  20372  10419  -2518  -2824    -36       C  
ATOM    177  C   ASP A  32      30.218 -57.490 284.585  1.00118.63           C  
ANISOU  177  C   ASP A  32    13219  20806  11051  -2487  -2728    152       C  
ATOM    178  O   ASP A  32      30.896 -57.032 285.504  1.00121.08           O  
ANISOU  178  O   ASP A  32    13587  20825  11592  -2296  -2517    238       O  
ATOM    179  CB  ASP A  32      32.170 -58.858 283.797  1.00120.62           C  
ANISOU  179  CB  ASP A  32    14231  20482  11118  -2504  -2668   -201       C  
ATOM    180  CG  ASP A  32      31.922 -59.967 284.802  1.00129.24           C  
ANISOU  180  CG  ASP A  32    15453  21307  12345  -2859  -2676   -358       C  
ATOM    181  OD1 ASP A  32      30.819 -60.554 284.784  1.00140.61           O  
ANISOU  181  OD1 ASP A  32    16753  22953  13717  -3216  -2859   -424       O  
ATOM    182  OD2 ASP A  32      32.830 -60.256 285.609  1.00124.47           O  
ANISOU  182  OD2 ASP A  32    15088  20298  11907  -2790  -2503   -407       O  
ATOM    183  N   HIS A  33      28.888 -57.452 284.572  1.00122.59           N  
ANISOU  183  N   HIS A  33    13362  21716  11502  -2670  -2888    210       N  
ATOM    184  CA  HIS A  33      28.117 -56.778 285.613  1.00127.68           C  
ANISOU  184  CA  HIS A  33    13639  22521  12352  -2604  -2808    396       C  
ATOM    185  C   HIS A  33      28.310 -57.407 286.992  1.00117.57           C  
ANISOU  185  C   HIS A  33    12465  20898  11309  -2805  -2665    326       C  
ATOM    186  O   HIS A  33      28.169 -56.734 288.013  1.00107.28           O  
ANISOU  186  O   HIS A  33    10979  19570  10213  -2638  -2514    474       O  
ATOM    187  CB  HIS A  33      26.631 -56.778 285.250  1.00143.15           C  
ANISOU  187  CB  HIS A  33    15206  24972  14211  -2767  -2983    449       C  
ATOM    188  CG  HIS A  33      26.045 -58.149 285.113  1.00164.56           C  
ANISOU  188  CG  HIS A  33    18018  27639  16867  -3250  -3104    238       C  
ATOM    189  ND1 HIS A  33      26.120 -58.877 283.946  1.00171.72           N  
ANISOU  189  ND1 HIS A  33    19163  28510  17571  -3402  -3252     60       N  
ATOM    190  CD2 HIS A  33      25.375 -58.924 285.998  1.00173.32           C  
ANISOU  190  CD2 HIS A  33    19043  28717  18094  -3615  -3097    186       C  
ATOM    191  CE1 HIS A  33      25.522 -60.043 284.117  1.00176.25           C  
ANISOU  191  CE1 HIS A  33    19807  29011  18147  -3842  -3341    -97       C  
ATOM    192  NE2 HIS A  33      25.060 -60.096 285.354  1.00178.00           N  
ANISOU  192  NE2 HIS A  33    19836  29235  18562  -3988  -3245    -14       N  
ATOM    193  N   ALA A  34      28.626 -58.699 287.013  1.00113.27           N  
ANISOU  193  N   ALA A  34    12237  20084  10717  -3150  -2719     99       N  
ATOM    194  CA  ALA A  34      28.859 -59.413 288.262  1.00100.90           C  
ANISOU  194  CA  ALA A  34    10826  18164   9348  -3356  -2596     28       C  
ATOM    195  C   ALA A  34      30.054 -58.829 289.010  1.00 98.90           C  
ANISOU  195  C   ALA A  34    10759  17516   9302  -3005  -2343     95       C  
ATOM    196  O   ALA A  34      30.003 -58.635 290.225  1.00 92.34           O  
ANISOU  196  O   ALA A  34     9841  16563   8682  -2983  -2198    176       O  
ATOM    197  CB  ALA A  34      29.072 -60.893 287.992  1.00 94.64           C  
ANISOU  197  CB  ALA A  34    10411  17110   8436  -3752  -2716   -231       C  
ATOM    198  N   ALA A  35      31.125 -58.547 288.276  1.00 96.91           N  
ANISOU  198  N   ALA A  35    10754  17093   8975  -2740  -2294     64       N  
ATOM    199  CA  ALA A  35      32.329 -57.972 288.867  1.00 94.36           C  
ANISOU  199  CA  ALA A  35    10599  16429   8825  -2423  -2071    129       C  
ATOM    200  C   ALA A  35      32.095 -56.525 289.284  1.00 85.62           C  
ANISOU  200  C   ALA A  35     9189  15482   7859  -2102  -1966    378       C  
ATOM    201  O   ALA A  35      32.713 -56.034 290.229  1.00 84.91           O  
ANISOU  201  O   ALA A  35     9147  15142   7973  -1923  -1786    451       O  
ATOM    202  CB  ALA A  35      33.493 -58.060 287.892  1.00 95.39           C  
ANISOU  202  CB  ALA A  35    11035  16399   8808  -2244  -2052     41       C  
ATOM    203  N   VAL A  36      31.202 -55.848 288.571  1.00 87.08           N  
ANISOU  203  N   VAL A  36     9079  16082   7924  -2020  -2088    502       N  
ATOM    204  CA  VAL A  36      30.878 -54.458 288.864  1.00 87.25           C  
ANISOU  204  CA  VAL A  36     8833  16267   8050  -1688  -2013    739       C  
ATOM    205  C   VAL A  36      30.163 -54.348 290.204  1.00 85.33           C  
ANISOU  205  C   VAL A  36     8364  16057   8000  -1743  -1934    800       C  
ATOM    206  O   VAL A  36      30.469 -53.474 291.016  1.00 86.84           O  
ANISOU  206  O   VAL A  36     8525  16100   8370  -1479  -1778    922       O  
ATOM    207  CB  VAL A  36      29.998 -53.838 287.763  1.00 85.60           C  
ANISOU  207  CB  VAL A  36     8359  16524   7642  -1578  -2182    858       C  
ATOM    208  CG1 VAL A  36      29.691 -52.384 288.083  1.00 82.27           C  
ANISOU  208  CG1 VAL A  36     7708  16227   7324  -1192  -2104   1105       C  
ATOM    209  CG2 VAL A  36      30.683 -53.955 286.413  1.00 86.79           C  
ANISOU  209  CG2 VAL A  36     8733  16671   7571  -1523  -2259    802       C  
ATOM    210  N   LEU A  37      29.213 -55.249 290.428  1.00 84.28           N  
ANISOU  210  N   LEU A  37     8080  16125   7817  -2100  -2043    712       N  
ATOM    211  CA  LEU A  37      28.465 -55.280 291.678  1.00 95.28           C  
ANISOU  211  CA  LEU A  37     9238  17603   9360  -2199  -1969    767       C  
ATOM    212  C   LEU A  37      29.335 -55.776 292.829  1.00 88.11           C  
ANISOU  212  C   LEU A  37     8612  16225   8642  -2265  -1792    685       C  
ATOM    213  O   LEU A  37      29.241 -55.276 293.949  1.00 92.18           O  
ANISOU  213  O   LEU A  37     9017  16684   9325  -2128  -1648    776       O  
ATOM    214  CB  LEU A  37      27.226 -56.163 291.534  1.00105.95           C  
ANISOU  214  CB  LEU A  37    10345  19325  10587  -2618  -2143    707       C  
ATOM    215  CG  LEU A  37      26.364 -56.327 292.786  1.00115.92           C  
ANISOU  215  CG  LEU A  37    11332  20742  11970  -2780  -2069    770       C  
ATOM    216  CD1 LEU A  37      25.882 -54.973 293.285  1.00121.08           C  
ANISOU  216  CD1 LEU A  37    11651  21644  12709  -2359  -1966    976       C  
ATOM    217  CD2 LEU A  37      25.190 -57.251 292.507  1.00115.00           C  
ANISOU  217  CD2 LEU A  37    10978  21011  11707  -3253  -2259    714       C  
ATOM    218  N   LEU A  38      30.184 -56.759 292.541  1.00 84.97           N  
ANISOU  218  N   LEU A  38     8586  15499   8200  -2452  -1809    509       N  
ATOM    219  CA  LEU A  38      31.064 -57.342 293.547  1.00 84.88           C  
ANISOU  219  CA  LEU A  38     8869  15040   8340  -2512  -1662    421       C  
ATOM    220  C   LEU A  38      32.066 -56.322 294.081  1.00 86.24           C  
ANISOU  220  C   LEU A  38     9129  14964   8675  -2118  -1476    518       C  
ATOM    221  O   LEU A  38      32.352 -56.288 295.278  1.00 95.27           O  
ANISOU  221  O   LEU A  38    10318  15893   9986  -2083  -1334    536       O  
ATOM    222  CB  LEU A  38      31.806 -58.550 292.972  1.00 88.18           C  
ANISOU  222  CB  LEU A  38     9686  15171   8646  -2725  -1732    210       C  
ATOM    223  CG  LEU A  38      32.716 -59.315 293.935  1.00 93.30           C  
ANISOU  223  CG  LEU A  38    10672  15358   9421  -2791  -1604    106       C  
ATOM    224  CD1 LEU A  38      31.905 -59.936 295.064  1.00 94.96           C  
ANISOU  224  CD1 LEU A  38    10782  15575   9722  -3098  -1587    117       C  
ATOM    225  CD2 LEU A  38      33.515 -60.377 293.194  1.00100.10           C  
ANISOU  225  CD2 LEU A  38    11944  15949  10141  -2902  -1677   -102       C  
ATOM    226  N   HIS A  39      32.599 -55.494 293.188  1.00 81.26           N  
ANISOU  226  N   HIS A  39     8528  14366   7982  -1841  -1482    586       N  
ATOM    227  CA  HIS A  39      33.543 -54.454 293.584  1.00 77.40           C  
ANISOU  227  CA  HIS A  39     8120  13655   7633  -1499  -1325    692       C  
ATOM    228  C   HIS A  39      32.808 -53.207 294.059  1.00 75.36           C  
ANISOU  228  C   HIS A  39     7567  13601   7466  -1256  -1284    882       C  
ATOM    229  O   HIS A  39      33.379 -52.361 294.747  1.00 65.35           O  
ANISOU  229  O   HIS A  39     6350  12131   6348  -1014  -1151    966       O  
ATOM    230  CB  HIS A  39      34.480 -54.105 292.426  1.00 72.72           C  
ANISOU  230  CB  HIS A  39     7702  13003   6925  -1328  -1340    700       C  
ATOM    231  CG  HIS A  39      35.431 -55.203 292.068  1.00 70.80           C  
ANISOU  231  CG  HIS A  39     7784  12517   6600  -1469  -1341    512       C  
ATOM    232  ND1 HIS A  39      35.026 -56.372 291.462  1.00 71.91           N  
ANISOU  232  ND1 HIS A  39     8016  12732   6573  -1748  -1482    346       N  
ATOM    233  CD2 HIS A  39      36.770 -55.311 292.236  1.00 69.84           C  
ANISOU  233  CD2 HIS A  39     7920  12086   6530  -1356  -1221    460       C  
ATOM    234  CE1 HIS A  39      36.074 -57.153 291.270  1.00 83.81           C  
ANISOU  234  CE1 HIS A  39     9849  13965   8029  -1770  -1446    193       C  
ATOM    235  NE2 HIS A  39      37.145 -56.532 291.731  1.00 80.31           N  
ANISOU  235  NE2 HIS A  39     9492  13309   7715  -1527  -1284    264       N  
ATOM    236  N   GLY A  40      31.536 -53.103 293.687  1.00 83.98           N  
ANISOU  236  N   GLY A  40     8353  15100   8456  -1315  -1407    942       N  
ATOM    237  CA  GLY A  40      30.710 -51.981 294.091  1.00 91.61           C  
ANISOU  237  CA  GLY A  40     9021  16309   9478  -1055  -1381   1115       C  
ATOM    238  C   GLY A  40      30.336 -52.050 295.558  1.00 95.75           C  
ANISOU  238  C   GLY A  40     9441  16781  10160  -1087  -1259   1119       C  
ATOM    239  O   GLY A  40      30.460 -51.066 296.288  1.00102.23           O  
ANISOU  239  O   GLY A  40    10231  17507  11105   -791  -1144   1218       O  
ATOM    240  N   LEU A  41      29.873 -53.218 295.991  1.00 89.58           N  
ANISOU  240  N   LEU A  41     8621  16056   9360  -1453  -1288   1010       N  
ATOM    241  CA  LEU A  41      29.525 -53.422 297.389  1.00 91.13           C  
ANISOU  241  CA  LEU A  41     8728  16216   9682  -1525  -1167   1014       C  
ATOM    242  C   LEU A  41      30.774 -53.369 298.257  1.00 91.74           C  
ANISOU  242  C   LEU A  41     9128  15808   9920  -1417  -1006    964       C  
ATOM    243  O   LEU A  41      30.730 -52.907 299.396  1.00100.64           O  
ANISOU  243  O   LEU A  41    10204  16865  11169  -1272   -876   1013       O  
ATOM    244  CB  LEU A  41      28.805 -54.757 297.581  1.00101.14           C  
ANISOU  244  CB  LEU A  41     9918  17630  10880  -1993  -1242    922       C  
ATOM    245  CG  LEU A  41      27.528 -54.952 296.762  1.00130.52           C  
ANISOU  245  CG  LEU A  41    13295  21869  14430  -2179  -1422    959       C  
ATOM    246  CD1 LEU A  41      26.853 -56.266 297.123  1.00142.12           C  
ANISOU  246  CD1 LEU A  41    14707  23444  15848  -2690  -1485    877       C  
ATOM    247  CD2 LEU A  41      26.576 -53.781 296.958  1.00136.71           C  
ANISOU  247  CD2 LEU A  41    13667  23068  15209  -1855  -1400   1133       C  
ATOM    248  N   ALA A  42      31.888 -53.840 297.706  1.00 84.34           N  
ANISOU  248  N   ALA A  42     8517  14563   8967  -1476  -1019    862       N  
ATOM    249  CA  ALA A  42      33.154 -53.859 298.428  1.00 79.22           C  
ANISOU  249  CA  ALA A  42     8167  13483   8451  -1383   -884    809       C  
ATOM    250  C   ALA A  42      33.656 -52.447 298.717  1.00 73.64           C  
ANISOU  250  C   ALA A  42     7457  12671   7854  -1000   -788    928       C  
ATOM    251  O   ALA A  42      34.400 -52.226 299.673  1.00 74.91           O  
ANISOU  251  O   ALA A  42     7765  12550   8146   -901   -665    914       O  
ATOM    252  CB  ALA A  42      34.194 -54.640 297.643  1.00 80.44           C  
ANISOU  252  CB  ALA A  42     8633  13398   8533  -1494   -927    680       C  
ATOM    253  N   SER A  43      33.248 -51.493 297.888  1.00 78.83           N  
ANISOU  253  N   SER A  43     7961  13544   8445   -792   -854   1046       N  
ATOM    254  CA  SER A  43      33.663 -50.108 298.065  1.00 82.27           C  
ANISOU  254  CA  SER A  43     8427  13861   8971   -439   -783   1171       C  
ATOM    255  C   SER A  43      32.939 -49.469 299.244  1.00 83.60           C  
ANISOU  255  C   SER A  43     8421  14104   9237   -270   -701   1235       C  
ATOM    256  O   SER A  43      33.557 -48.796 300.068  1.00 73.58           O  
ANISOU  256  O   SER A  43     7287  12573   8096    -86   -595   1253       O  
ATOM    257  CB  SER A  43      33.415 -49.301 296.788  1.00 75.77           C  
ANISOU  257  CB  SER A  43     7521  13236   8031   -260   -885   1293       C  
ATOM    258  OG  SER A  43      34.260 -49.735 295.737  1.00 76.48           O  
ANISOU  258  OG  SER A  43     7802  13231   8025   -363   -935   1242       O  
ATOM    259  N   LEU A  44      31.629 -49.685 299.322  1.00 90.47           N  
ANISOU  259  N   LEU A  44     8987  15355  10033   -334   -754   1265       N  
ATOM    260  CA  LEU A  44      30.831 -49.137 300.414  1.00 98.19           C  
ANISOU  260  CA  LEU A  44     9760  16478  11069   -158   -670   1324       C  
ATOM    261  C   LEU A  44      31.172 -49.798 301.745  1.00 96.14           C  
ANISOU  261  C   LEU A  44     9610  16007  10913   -314   -544   1230       C  
ATOM    262  O   LEU A  44      31.399 -49.115 302.744  1.00 96.55           O  
ANISOU  262  O   LEU A  44     9720  15900  11065    -91   -431   1248       O  
ATOM    263  CB  LEU A  44      29.339 -49.293 300.120  1.00111.87           C  
ANISOU  263  CB  LEU A  44    11096  18737  12674   -211   -758   1386       C  
ATOM    264  CG  LEU A  44      28.787 -48.360 299.040  1.00131.19           C  
ANISOU  264  CG  LEU A  44    13378  21456  15014     59   -871   1514       C  
ATOM    265  CD1 LEU A  44      27.284 -48.537 298.889  1.00138.81           C  
ANISOU  265  CD1 LEU A  44    13904  22990  15848     13   -955   1575       C  
ATOM    266  CD2 LEU A  44      29.133 -46.913 299.362  1.00133.17           C  
ANISOU  266  CD2 LEU A  44    13743  21504  15350    517   -796   1617       C  
ATOM    267  N   LEU A  45      31.204 -51.128 301.751  1.00 91.07           N  
ANISOU  267  N   LEU A  45     9017  15351  10234   -694   -572   1128       N  
ATOM    268  CA  LEU A  45      31.549 -51.883 302.950  1.00 83.05           C  
ANISOU  268  CA  LEU A  45     8134  14125   9297   -867   -463   1049       C  
ATOM    269  C   LEU A  45      32.933 -51.498 303.466  1.00 86.52           C  
ANISOU  269  C   LEU A  45     8897  14117   9861   -703   -370   1004       C  
ATOM    270  O   LEU A  45      33.117 -51.278 304.660  1.00 92.31           O  
ANISOU  270  O   LEU A  45     9677  14716  10679   -608   -255    997       O  
ATOM    271  CB  LEU A  45      31.488 -53.387 302.674  1.00 78.28           C  
ANISOU  271  CB  LEU A  45     7609  13511   8622  -1302   -533    948       C  
ATOM    272  CG  LEU A  45      30.103 -53.978 302.401  1.00 84.53           C  
ANISOU  272  CG  LEU A  45     8082  14741   9294  -1572   -624    980       C  
ATOM    273  CD1 LEU A  45      30.204 -55.459 302.070  1.00 81.04           C  
ANISOU  273  CD1 LEU A  45     7812  14194   8784  -2019   -710    866       C  
ATOM    274  CD2 LEU A  45      29.179 -53.756 303.588  1.00 94.04           C  
ANISOU  274  CD2 LEU A  45     9013  16196  10522  -1534   -517   1061       C  
ATOM    275  N   GLY A  46      33.898 -51.404 302.557  1.00 83.46           N  
ANISOU  275  N   GLY A  46     8714  13529   9469   -672   -421    977       N  
ATOM    276  CA  GLY A  46      35.262 -51.060 302.918  1.00 86.16           C  
ANISOU  276  CA  GLY A  46     9333  13489   9913   -546   -347    942       C  
ATOM    277  C   GLY A  46      35.414 -49.683 303.540  1.00 95.79           C  
ANISOU  277  C   GLY A  46    10551  14616  11230   -220   -276   1023       C  
ATOM    278  O   GLY A  46      36.273 -49.476 304.397  1.00 99.36           O  
ANISOU  278  O   GLY A  46    11183  14789  11781   -151   -193    984       O  
ATOM    279  N   LEU A  47      34.580 -48.740 303.112  1.00100.65           N  
ANISOU  279  N   LEU A  47    10977  15459  11807     -9   -318   1133       N  
ATOM    280  CA  LEU A  47      34.643 -47.373 303.623  1.00101.91           C  
ANISOU  280  CA  LEU A  47    11169  15510  12043    327   -267   1210       C  
ATOM    281  C   LEU A  47      33.916 -47.225 304.957  1.00104.84           C  
ANISOU  281  C   LEU A  47    11416  15972  12446    433   -174   1195       C  
ATOM    282  O   LEU A  47      34.390 -46.533 305.857  1.00111.52           O  
ANISOU  282  O   LEU A  47    12408  16586  13379    617    -99   1179       O  
ATOM    283  CB  LEU A  47      34.057 -46.389 302.607  1.00105.84           C  
ANISOU  283  CB  LEU A  47    11548  16194  12472    556   -353   1342       C  
ATOM    284  CG  LEU A  47      34.877 -46.096 301.348  1.00100.93           C  
ANISOU  284  CG  LEU A  47    11083  15449  11818    550   -425   1396       C  
ATOM    285  CD1 LEU A  47      34.148 -45.097 300.464  1.00 97.68           C  
ANISOU  285  CD1 LEU A  47    10547  15241  11324    802   -509   1547       C  
ATOM    286  CD2 LEU A  47      36.261 -45.581 301.710  1.00105.91           C  
ANISOU  286  CD2 LEU A  47    12007  15670  12565    598   -363   1383       C  
ATOM    287  N   VAL A  48      32.762 -47.875 305.076  1.00 94.54           N  
ANISOU  287  N   VAL A  48     9840  15023  11058    307   -182   1201       N  
ATOM    288  CA  VAL A  48      31.957 -47.783 306.289  1.00 88.66           C  
ANISOU  288  CA  VAL A  48     8928  14446  10312    402    -84   1203       C  
ATOM    289  C   VAL A  48      32.586 -48.562 307.442  1.00 92.14           C  
ANISOU  289  C   VAL A  48     9538  14656  10815    218     16   1104       C  
ATOM    290  O   VAL A  48      32.641 -48.072 308.572  1.00101.60           O  
ANISOU  290  O   VAL A  48    10785  15764  12057    401    116   1087       O  
ATOM    291  CB  VAL A  48      30.525 -48.298 306.051  1.00 90.85           C  
ANISOU  291  CB  VAL A  48     8825  15227  10467    279   -122   1256       C  
ATOM    292  CG1 VAL A  48      29.745 -48.339 307.357  1.00 91.61           C  
ANISOU  292  CG1 VAL A  48     8735  15529  10545    341      1   1262       C  
ATOM    293  CG2 VAL A  48      29.814 -47.423 305.032  1.00 98.04           C  
ANISOU  293  CG2 VAL A  48     9541  16410  11301    527   -220   1365       C  
ATOM    294  N   GLU A  49      33.062 -49.770 307.152  1.00 84.15           N  
ANISOU  294  N   GLU A  49     8635  13543   9794   -125    -17   1037       N  
ATOM    295  CA  GLU A  49      33.667 -50.622 308.172  1.00 74.63           C  
ANISOU  295  CA  GLU A  49     7608  12115   8631   -306     64    954       C  
ATOM    296  C   GLU A  49      34.895 -49.969 308.800  1.00 73.63           C  
ANISOU  296  C   GLU A  49     7755  11610   8610   -112    121    907       C  
ATOM    297  O   GLU A  49      34.941 -49.767 310.011  1.00 79.32           O  
ANISOU  297  O   GLU A  49     8517  12259   9361    -12    217    884       O  
ATOM    298  CB  GLU A  49      34.041 -51.986 307.586  1.00 74.50           C  
ANISOU  298  CB  GLU A  49     7714  12014   8577   -668     -1    887       C  
ATOM    299  CG  GLU A  49      32.847 -52.898 307.330  1.00 77.85           C  
ANISOU  299  CG  GLU A  49     7906  12775   8897   -962    -49    912       C  
ATOM    300  CD  GLU A  49      33.230 -54.185 306.620  1.00 76.18           C  
ANISOU  300  CD  GLU A  49     7871  12438   8638  -1306   -138    831       C  
ATOM    301  OE1 GLU A  49      34.434 -54.395 306.368  1.00 65.02           O  
ANISOU  301  OE1 GLU A  49     6746  10692   7265  -1284   -148    756       O  
ATOM    302  OE2 GLU A  49      32.325 -54.988 306.310  1.00 80.33           O  
ANISOU  302  OE2 GLU A  49     8246  13203   9074  -1598   -203    841       O  
ATOM    303  N   ASN A  50      35.884 -49.635 307.978  1.00 66.35           N  
ANISOU  303  N   ASN A  50     7011  10468   7730    -68     61    896       N  
ATOM    304  CA  ASN A  50      37.087 -48.977 308.479  1.00 67.59           C  
ANISOU  304  CA  ASN A  50     7408  10292   7983     81     97    861       C  
ATOM    305  C   ASN A  50      36.786 -47.588 309.029  1.00 68.95           C  
ANISOU  305  C   ASN A  50     7557  10447   8195    402    132    908       C  
ATOM    306  O   ASN A  50      37.521 -47.069 309.870  1.00 73.13           O  
ANISOU  306  O   ASN A  50     8262  10731   8793    516    176    864       O  
ATOM    307  CB  ASN A  50      38.147 -48.882 307.381  1.00 69.49           C  
ANISOU  307  CB  ASN A  50     7801  10361   8241     44     28    863       C  
ATOM    308  CG  ASN A  50      38.773 -50.223 307.061  1.00 75.83           C  
ANISOU  308  CG  ASN A  50     8716  11087   9008   -216      9    781       C  
ATOM    309  OD1 ASN A  50      39.595 -50.734 307.823  1.00 84.24           O  
ANISOU  309  OD1 ASN A  50     9943  11950  10112   -274     57    708       O  
ATOM    310  ND2 ASN A  50      38.395 -50.798 305.925  1.00 78.20           N  
ANISOU  310  ND2 ASN A  50     8945  11547   9222   -356    -68    789       N  
ATOM    311  N   GLY A  51      35.701 -46.991 308.548  1.00 68.45           N  
ANISOU  311  N   GLY A  51     7285  10646   8077    558    102    992       N  
ATOM    312  CA  GLY A  51      35.275 -45.689 309.022  1.00 76.16           C  
ANISOU  312  CA  GLY A  51     8249  11621   9069    905    129   1035       C  
ATOM    313  C   GLY A  51      34.883 -45.712 310.487  1.00 78.00           C  
ANISOU  313  C   GLY A  51     8451  11891   9295    999    239    978       C  
ATOM    314  O   GLY A  51      35.367 -44.902 311.278  1.00 83.01           O  
ANISOU  314  O   GLY A  51     9269  12292   9981   1200    276    935       O  
ATOM    315  N   VAL A  52      34.009 -46.645 310.853  1.00 71.24           N  
ANISOU  315  N   VAL A  52     7371  11334   8362    837    288    978       N  
ATOM    316  CA  VAL A  52      33.541 -46.742 312.230  1.00 75.91           C  
ANISOU  316  CA  VAL A  52     7902  12023   8918    912    406    941       C  
ATOM    317  C   VAL A  52      34.617 -47.330 313.142  1.00 80.44           C  
ANISOU  317  C   VAL A  52     8728  12289   9545    758    457    846       C  
ATOM    318  O   VAL A  52      34.625 -47.068 314.343  1.00 87.23           O  
ANISOU  318  O   VAL A  52     9649  13103  10392    895    545    800       O  
ATOM    319  CB  VAL A  52      32.252 -47.590 312.343  1.00 73.61           C  
ANISOU  319  CB  VAL A  52     7272  12181   8517    745    448    995       C  
ATOM    320  CG1 VAL A  52      31.105 -46.914 311.605  1.00 62.49           C  
ANISOU  320  CG1 VAL A  52     5570  11139   7035    955    403   1091       C  
ATOM    321  CG2 VAL A  52      32.475 -49.000 311.819  1.00 73.32           C  
ANISOU  321  CG2 VAL A  52     7244  12143   8472    308    399    983       C  
ATOM    322  N   ILE A  53      35.526 -48.116 312.569  1.00 78.71           N  
ANISOU  322  N   ILE A  53     8659  11876   9372    498    398    816       N  
ATOM    323  CA  ILE A  53      36.639 -48.675 313.331  1.00 73.16           C  
ANISOU  323  CA  ILE A  53     8198  10886   8715    377    430    732       C  
ATOM    324  C   ILE A  53      37.542 -47.566 313.863  1.00 80.61           C  
ANISOU  324  C   ILE A  53     9356  11541   9731    613    430    682       C  
ATOM    325  O   ILE A  53      37.879 -47.542 315.048  1.00 89.26           O  
ANISOU  325  O   ILE A  53    10566  12524  10826    670    493    619       O  
ATOM    326  CB  ILE A  53      37.481 -49.653 312.482  1.00 63.26           C  
ANISOU  326  CB  ILE A  53     7066   9487   7482    109    360    707       C  
ATOM    327  CG1 ILE A  53      36.730 -50.969 312.277  1.00 62.47           C  
ANISOU  327  CG1 ILE A  53     6838   9593   7304   -181    361    724       C  
ATOM    328  CG2 ILE A  53      38.817 -49.928 313.151  1.00 58.90           C  
ANISOU  328  CG2 ILE A  53     6773   8622   6983     75    376    626       C  
ATOM    329  CD1 ILE A  53      36.414 -51.701 313.560  1.00 67.83           C  
ANISOU  329  CD1 ILE A  53     7520  10312   7938   -287    458    710       C  
ATOM    330  N   LEU A  54      37.919 -46.644 312.981  1.00 83.10           N  
ANISOU  330  N   LEU A  54     9735  11739  10101    735    354    716       N  
ATOM    331  CA  LEU A  54      38.782 -45.525 313.351  1.00 78.68           C  
ANISOU  331  CA  LEU A  54     9396  10887   9613    917    332    680       C  
ATOM    332  C   LEU A  54      38.173 -44.672 314.460  1.00 71.42           C  
ANISOU  332  C   LEU A  54     8488   9986   8662   1197    394    646       C  
ATOM    333  O   LEU A  54      38.892 -44.137 315.303  1.00 73.41           O  
ANISOU  333  O   LEU A  54     8947   9997   8948   1286    399    568       O  
ATOM    334  CB  LEU A  54      39.077 -44.650 312.129  1.00 81.19           C  
ANISOU  334  CB  LEU A  54     9762  11111   9976    990    241    758       C  
ATOM    335  CG  LEU A  54      40.014 -45.222 311.064  1.00 82.58           C  
ANISOU  335  CG  LEU A  54     9991  11205  10180    761    180    780       C  
ATOM    336  CD1 LEU A  54      40.102 -44.279 309.874  1.00 80.66           C  
ANISOU  336  CD1 LEU A  54     9772  10921   9954    853    104    883       C  
ATOM    337  CD2 LEU A  54      41.396 -45.483 311.644  1.00 76.16           C  
ANISOU  337  CD2 LEU A  54     9374  10139   9423    645    184    700       C  
ATOM    338  N   PHE A  55      36.850 -44.547 314.455  1.00 68.10           N  
ANISOU  338  N   PHE A  55     7840   9872   8162   1341    437    698       N  
ATOM    339  CA  PHE A  55      36.155 -43.751 315.461  1.00 81.48           C  
ANISOU  339  CA  PHE A  55     9522  11639   9799   1654    508    664       C  
ATOM    340  C   PHE A  55      36.098 -44.472 316.805  1.00 85.47           C  
ANISOU  340  C   PHE A  55    10019  12213  10241   1584    615    590       C  
ATOM    341  O   PHE A  55      36.329 -43.870 317.853  1.00 88.91           O  
ANISOU  341  O   PHE A  55    10615  12511  10657   1777    655    506       O  
ATOM    342  CB  PHE A  55      34.739 -43.409 314.992  1.00 84.45           C  
ANISOU  342  CB  PHE A  55     9616  12382  10091   1856    524    754       C  
ATOM    343  CG  PHE A  55      33.944 -42.617 315.992  1.00 93.67           C  
ANISOU  343  CG  PHE A  55    10746  13673  11171   2224    609    718       C  
ATOM    344  CD1 PHE A  55      34.107 -41.245 316.094  1.00105.06           C  
ANISOU  344  CD1 PHE A  55    12407  14878  12635   2575    569    688       C  
ATOM    345  CD2 PHE A  55      33.034 -43.243 316.828  1.00 91.06           C  
ANISOU  345  CD2 PHE A  55    10175  13697  10725   2222    730    718       C  
ATOM    346  CE1 PHE A  55      33.378 -40.513 317.013  1.00101.18           C  
ANISOU  346  CE1 PHE A  55    11908  14492  12045   2954    647    637       C  
ATOM    347  CE2 PHE A  55      32.303 -42.517 317.748  1.00 87.40           C  
ANISOU  347  CE2 PHE A  55     9666  13383  10158   2592    821    682       C  
ATOM    348  CZ  PHE A  55      32.476 -41.150 317.840  1.00 91.67           C  
ANISOU  348  CZ  PHE A  55    10439  13677  10715   2977    778    631       C  
ATOM    349  N   VAL A  56      35.779 -45.761 316.764  1.00 79.30           N  
ANISOU  349  N   VAL A  56     9073  11639   9419   1301    655    625       N  
ATOM    350  CA  VAL A  56      35.664 -46.569 317.971  1.00 73.30           C  
ANISOU  350  CA  VAL A  56     8300  10965   8585   1198    760    587       C  
ATOM    351  C   VAL A  56      37.001 -46.692 318.695  1.00 81.57           C  
ANISOU  351  C   VAL A  56     9647  11660   9684   1134    744    490       C  
ATOM    352  O   VAL A  56      37.092 -46.457 319.900  1.00 84.65           O  
ANISOU  352  O   VAL A  56    10134  12010  10019   1269    810    422       O  
ATOM    353  CB  VAL A  56      35.128 -47.978 317.647  1.00 68.34           C  
ANISOU  353  CB  VAL A  56     7479  10576   7910    854    785    658       C  
ATOM    354  CG1 VAL A  56      35.362 -48.926 318.816  1.00 78.30           C  
ANISOU  354  CG1 VAL A  56     8822  11814   9114    689    873    629       C  
ATOM    355  CG2 VAL A  56      33.651 -47.914 317.289  1.00 71.23           C  
ANISOU  355  CG2 VAL A  56     7496  11381   8188    910    822    752       C  
ATOM    356  N   VAL A  57      38.039 -47.051 317.947  1.00 79.24           N  
ANISOU  356  N   VAL A  57     9487  11140   9482    943    653    482       N  
ATOM    357  CA  VAL A  57      39.366 -47.260 318.514  1.00 79.88           C  
ANISOU  357  CA  VAL A  57     9815  10930   9607    866    624    400       C  
ATOM    358  C   VAL A  57      40.028 -45.947 318.928  1.00 81.50           C  
ANISOU  358  C   VAL A  57    10216  10891   9859   1092    578    326       C  
ATOM    359  O   VAL A  57      40.685 -45.870 319.968  1.00 81.00           O  
ANISOU  359  O   VAL A  57    10317  10681   9777   1127    588    240       O  
ATOM    360  CB  VAL A  57      40.283 -47.997 317.511  1.00 73.06           C  
ANISOU  360  CB  VAL A  57     9013   9933   8812    625    544    416       C  
ATOM    361  CG1 VAL A  57      41.694 -48.138 318.064  1.00 66.52           C  
ANISOU  361  CG1 VAL A  57     8409   8845   8022    577    508    338       C  
ATOM    362  CG2 VAL A  57      39.703 -49.360 317.164  1.00 63.69           C  
ANISOU  362  CG2 VAL A  57     7697   8931   7570    381    574    468       C  
ATOM    363  N   GLY A  58      39.838 -44.911 318.118  1.00 85.57           N  
ANISOU  363  N   GLY A  58    10729  11358  10426   1238    519    362       N  
ATOM    364  CA  GLY A  58      40.555 -43.662 318.300  1.00 87.09           C  
ANISOU  364  CA  GLY A  58    11149  11265  10677   1398    448    304       C  
ATOM    365  C   GLY A  58      39.901 -42.625 319.194  1.00 83.24           C  
ANISOU  365  C   GLY A  58    10735  10768  10126   1721    486    242       C  
ATOM    366  O   GLY A  58      40.597 -41.828 319.824  1.00 78.54           O  
ANISOU  366  O   GLY A  58    10381   9910   9550   1817    438    149       O  
ATOM    367  N   CYS A  59      38.573 -42.623 319.255  1.00 92.47           N  
ANISOU  367  N   CYS A  59    11695  12232  11206   1894    569    287       N  
ATOM    368  CA  CYS A  59      37.856 -41.591 320.002  1.00103.19           C  
ANISOU  368  CA  CYS A  59    13109  13615  12484   2264    612    230       C  
ATOM    369  C   CYS A  59      37.220 -42.095 321.296  1.00106.27           C  
ANISOU  369  C   CYS A  59    13401  14244  12733   2349    746    174       C  
ATOM    370  O   CYS A  59      37.246 -41.400 322.311  1.00114.72           O  
ANISOU  370  O   CYS A  59    14642  15214  13733   2591    772     64       O  
ATOM    371  CB  CYS A  59      36.778 -40.952 319.123  1.00102.29           C  
ANISOU  371  CB  CYS A  59    12830  13685  12350   2492    606    327       C  
ATOM    372  SG  CYS A  59      37.396 -39.679 317.998  1.00102.54           S  
ANISOU  372  SG  CYS A  59    13103  13356  12502   2586    454    371       S  
ATOM    373  N   ARG A  60      36.648 -43.295 321.267  1.00101.31           N  
ANISOU  373  N   ARG A  60    12514  13928  12052   2144    829    251       N  
ATOM    374  CA  ARG A  60      35.952 -43.813 322.441  1.00101.70           C  
ANISOU  374  CA  ARG A  60    12441  14249  11953   2200    971    234       C  
ATOM    375  C   ARG A  60      36.633 -45.042 323.041  1.00100.31           C  
ANISOU  375  C   ARG A  60    12322  14027  11766   1884   1000    224       C  
ATOM    376  O   ARG A  60      35.975 -45.899 323.629  1.00100.17           O  
ANISOU  376  O   ARG A  60    12136  14287  11638   1785   1114    277       O  
ATOM    377  CB  ARG A  60      34.496 -44.138 322.093  1.00103.01           C  
ANISOU  377  CB  ARG A  60    12233  14878  12027   2246   1063    350       C  
ATOM    378  CG  ARG A  60      33.645 -42.905 321.816  1.00108.35           C  
ANISOU  378  CG  ARG A  60    12834  15673  12659   2658   1063    355       C  
ATOM    379  CD  ARG A  60      32.172 -43.251 321.661  1.00113.13           C  
ANISOU  379  CD  ARG A  60    13026  16816  13144   2724   1167    468       C  
ATOM    380  NE  ARG A  60      31.365 -42.059 321.416  1.00125.30           N  
ANISOU  380  NE  ARG A  60    14494  18486  14627   3174   1166    472       N  
ATOM    381  CZ  ARG A  60      30.048 -42.069 321.233  1.00135.32           C  
ANISOU  381  CZ  ARG A  60    15390  20247  15779   3334   1243    566       C  
ATOM    382  NH1 ARG A  60      29.399 -40.933 321.016  1.00135.27           N  
ANISOU  382  NH1 ARG A  60    15353  20329  15716   3794   1233    565       N  
ATOM    383  NH2 ARG A  60      29.380 -43.213 321.268  1.00140.29           N  
ANISOU  383  NH2 ARG A  60    15680  21284  16340   3034   1325    667       N  
ATOM    384  N   MET A  61      37.952 -45.115 322.905  1.00 98.77           N  
ANISOU  384  N   MET A  61    12365  13490  11674   1733    896    167       N  
ATOM    385  CA  MET A  61      38.716 -46.219 323.477  1.00 91.15           C  
ANISOU  385  CA  MET A  61    11488  12451  10694   1482    908    153       C  
ATOM    386  C   MET A  61      40.032 -45.721 324.070  1.00 96.14           C  
ANISOU  386  C   MET A  61    12414  12750  11366   1522    821     31       C  
ATOM    387  O   MET A  61      40.689 -44.850 323.500  1.00 98.78           O  
ANISOU  387  O   MET A  61    12881  12849  11803   1573    711     -9       O  
ATOM    388  CB  MET A  61      38.977 -47.293 322.419  1.00 86.23           C  
ANISOU  388  CB  MET A  61    10780  11833  10152   1161    862    243       C  
ATOM    389  CG  MET A  61      39.626 -48.557 322.958  1.00 96.47           C  
ANISOU  389  CG  MET A  61    12169  13068  11416    922    880    245       C  
ATOM    390  SD  MET A  61      39.778 -49.852 321.709  1.00107.87           S  
ANISOU  390  SD  MET A  61    13543  14518  12927    582    830    335       S  
ATOM    391  CE  MET A  61      38.055 -50.178 321.344  1.00 68.92           C  
ANISOU  391  CE  MET A  61     8290   9981   7917    519    918    450       C  
ATOM    392  N   ARG A  62      40.408 -46.275 325.219  1.00 96.12           N  
ANISOU  392  N   ARG A  62    12510  12742  11269   1485    866    -19       N  
ATOM    393  CA  ARG A  62      41.622 -45.864 325.918  1.00 90.28           C  
ANISOU  393  CA  ARG A  62    12028  11736  10539   1517    779   -140       C  
ATOM    394  C   ARG A  62      42.872 -46.148 325.089  1.00 80.22           C  
ANISOU  394  C   ARG A  62    10833  10243   9402   1300    652   -130       C  
ATOM    395  O   ARG A  62      43.099 -47.277 324.656  1.00 75.08           O  
ANISOU  395  O   ARG A  62    10112   9641   8773   1088    661    -56       O  
ATOM    396  CB  ARG A  62      41.713 -46.565 327.275  1.00101.30           C  
ANISOU  396  CB  ARG A  62    13487  13218  11784   1512    855   -173       C  
ATOM    397  CG  ARG A  62      42.984 -46.267 328.052  1.00110.55           C  
ANISOU  397  CG  ARG A  62    14906  14156  12943   1527    753   -297       C  
ATOM    398  CD  ARG A  62      42.872 -46.709 329.508  1.00116.87           C  
ANISOU  398  CD  ARG A  62    15778  15073  13556   1602    836   -338       C  
ATOM    399  NE  ARG A  62      42.019 -45.819 330.294  1.00119.06           N  
ANISOU  399  NE  ARG A  62    16073  15461  13702   1891    915   -417       N  
ATOM    400  CZ  ARG A  62      40.745 -46.064 330.589  1.00121.96           C  
ANISOU  400  CZ  ARG A  62    16259  16131  13948   1992   1076   -344       C  
ATOM    401  NH1 ARG A  62      40.166 -47.180 330.168  1.00123.59           N  
ANISOU  401  NH1 ARG A  62    16258  16542  14157   1783   1165   -186       N  
ATOM    402  NH2 ARG A  62      40.050 -45.193 331.309  1.00117.85           N  
ANISOU  402  NH2 ARG A  62    15765  15719  13294   2299   1146   -431       N  
ATOM    403  N   GLN A  63      43.682 -45.115 324.879  1.00 83.15           N  
ANISOU  403  N   GLN A  63    11361  10376   9856   1356    535   -205       N  
ATOM    404  CA  GLN A  63      44.841 -45.203 323.995  1.00 87.48           C  
ANISOU  404  CA  GLN A  63    11953  10755  10530   1165    420   -184       C  
ATOM    405  C   GLN A  63      46.042 -45.880 324.646  1.00 85.98           C  
ANISOU  405  C   GLN A  63    11864  10491  10314   1038    370   -235       C  
ATOM    406  O   GLN A  63      46.560 -45.411 325.659  1.00 92.44           O  
ANISOU  406  O   GLN A  63    12835  11215  11075   1116    324   -341       O  
ATOM    407  CB  GLN A  63      45.242 -43.806 323.514  1.00 92.57           C  
ANISOU  407  CB  GLN A  63    12723  11183  11268   1240    313   -223       C  
ATOM    408  CG  GLN A  63      44.175 -43.098 322.694  1.00102.58           C  
ANISOU  408  CG  GLN A  63    13906  12502  12568   1384    342   -156       C  
ATOM    409  CD  GLN A  63      43.888 -43.794 321.376  1.00 99.40           C  
ANISOU  409  CD  GLN A  63    13305  12235  12229   1232    359    -23       C  
ATOM    410  OE1 GLN A  63      42.751 -44.177 321.099  1.00 94.53           O  
ANISOU  410  OE1 GLN A  63    12508  11842  11567   1284    443     45       O  
ATOM    411  NE2 GLN A  63      44.918 -43.953 320.552  1.00 96.41           N  
ANISOU  411  NE2 GLN A  63    12949  11742  11940   1042    276     13       N  
ATOM    412  N   THR A  64      46.479 -46.984 324.050  1.00 80.32           N  
ANISOU  412  N   THR A  64    11070   9821   9626    859    370   -163       N  
ATOM    413  CA  THR A  64      47.695 -47.666 324.475  1.00 82.14           C  
ANISOU  413  CA  THR A  64    11381   9993   9835    761    311   -196       C  
ATOM    414  C   THR A  64      48.665 -47.741 323.302  1.00 78.28           C  
ANISOU  414  C   THR A  64    10852   9435   9456    623    226   -156       C  
ATOM    415  O   THR A  64      48.497 -47.035 322.308  1.00 89.90           O  
ANISOU  415  O   THR A  64    12272  10868  11019    606    198   -117       O  
ATOM    416  CB  THR A  64      47.407 -49.086 325.000  1.00 90.83           C  
ANISOU  416  CB  THR A  64    12464  11213  10835    708    397   -148       C  
ATOM    417  OG1 THR A  64      46.927 -49.908 323.929  1.00 87.26           O  
ANISOU  417  OG1 THR A  64    11896  10833  10424    583    438    -49       O  
ATOM    418  CG2 THR A  64      46.366 -49.046 326.109  1.00100.61           C  
ANISOU  418  CG2 THR A  64    13711  12570  11948    829    503   -161       C  
ATOM    419  N   VAL A  65      49.677 -48.593 323.414  1.00 65.87           N  
ANISOU  419  N   VAL A  65     9304   7864   7861    543    187   -159       N  
ATOM    420  CA  VAL A  65      50.641 -48.763 322.333  1.00 64.52           C  
ANISOU  420  CA  VAL A  65     9074   7674   7765    435    121   -121       C  
ATOM    421  C   VAL A  65      50.077 -49.659 321.236  1.00 66.90           C  
ANISOU  421  C   VAL A  65     9282   8054   8083    365    182    -36       C  
ATOM    422  O   VAL A  65      50.183 -49.347 320.052  1.00 71.03           O  
ANISOU  422  O   VAL A  65     9729   8580   8679    307    158     12       O  
ATOM    423  CB  VAL A  65      51.971 -49.354 322.845  1.00 65.99           C  
ANISOU  423  CB  VAL A  65     9304   7867   7903    414     55   -160       C  
ATOM    424  CG1 VAL A  65      52.793 -49.920 321.690  1.00 63.96           C  
ANISOU  424  CG1 VAL A  65     8960   7655   7685    334     27   -107       C  
ATOM    425  CG2 VAL A  65      52.761 -48.298 323.604  1.00 65.80           C  
ANISOU  425  CG2 VAL A  65     9346   7772   7881    428    -47   -245       C  
ATOM    426  N   VAL A  66      49.464 -50.766 321.637  1.00 65.76           N  
ANISOU  426  N   VAL A  66     9158   7968   7860    357    257    -14       N  
ATOM    427  CA  VAL A  66      48.945 -51.737 320.683  1.00 67.32           C  
ANISOU  427  CA  VAL A  66     9302   8222   8057    263    299     52       C  
ATOM    428  C   VAL A  66      47.792 -51.166 319.855  1.00 72.31           C  
ANISOU  428  C   VAL A  66     9811   8925   8738    242    332    103       C  
ATOM    429  O   VAL A  66      47.669 -51.467 318.667  1.00 83.57           O  
ANISOU  429  O   VAL A  66    11171  10387  10196    162    320    147       O  
ATOM    430  CB  VAL A  66      48.477 -53.021 321.394  1.00 84.28           C  
ANISOU  430  CB  VAL A  66    11529  10392  10102    227    365     74       C  
ATOM    431  CG1 VAL A  66      48.108 -54.087 320.376  1.00 98.05           C  
ANISOU  431  CG1 VAL A  66    13262  12153  11839    102    382    125       C  
ATOM    432  CG2 VAL A  66      49.567 -53.534 322.321  1.00 90.02           C  
ANISOU  432  CG2 VAL A  66    12388  11055  10761    289    329     32       C  
ATOM    433  N   THR A  67      46.956 -50.335 320.471  1.00 68.72           N  
ANISOU  433  N   THR A  67     9328   8506   8277    335    370     93       N  
ATOM    434  CA  THR A  67      45.836 -49.731 319.751  1.00 67.80           C  
ANISOU  434  CA  THR A  67     9083   8483   8195    361    398    145       C  
ATOM    435  C   THR A  67      46.325 -48.702 318.738  1.00 75.99           C  
ANISOU  435  C   THR A  67    10102   9443   9328    381    321    161       C  
ATOM    436  O   THR A  67      45.588 -48.317 317.830  1.00 85.23           O  
ANISOU  436  O   THR A  67    11169  10686  10527    391    323    221       O  
ATOM    437  CB  THR A  67      44.829 -49.051 320.702  1.00 67.51           C  
ANISOU  437  CB  THR A  67     9021   8523   8108    510    464    127       C  
ATOM    438  OG1 THR A  67      45.452 -47.936 321.350  1.00 78.91           O  
ANISOU  438  OG1 THR A  67    10585   9825   9573    643    412     48       O  
ATOM    439  CG2 THR A  67      44.328 -50.034 321.746  1.00 68.86           C  
ANISOU  439  CG2 THR A  67     9202   8795   8166    476    554    134       C  
ATOM    440  N   THR A  68      47.567 -48.255 318.896  1.00 73.19           N  
ANISOU  440  N   THR A  68     9842   8956   9012    377    249    117       N  
ATOM    441  CA  THR A  68      48.159 -47.322 317.947  1.00 72.65           C  
ANISOU  441  CA  THR A  68     9767   8810   9028    353    176    150       C  
ATOM    442  C   THR A  68      48.512 -48.042 316.645  1.00 71.10           C  
ANISOU  442  C   THR A  68     9487   8686   8841    236    166    213       C  
ATOM    443  O   THR A  68      48.300 -47.505 315.556  1.00 61.32           O  
ANISOU  443  O   THR A  68     8188   7468   7643    219    145    283       O  
ATOM    444  CB  THR A  68      49.413 -46.638 318.529  1.00 66.28           C  
ANISOU  444  CB  THR A  68     9068   7866   8250    341     95     91       C  
ATOM    445  OG1 THR A  68      49.061 -45.935 319.726  1.00 83.13           O  
ANISOU  445  OG1 THR A  68    11308   9921  10357    461     95     14       O  
ATOM    446  CG2 THR A  68      50.000 -45.654 317.533  1.00 59.42           C  
ANISOU  446  CG2 THR A  68     8195   6919   7463    276     24    151       C  
ATOM    447  N   TRP A  69      49.038 -49.261 316.760  1.00 65.94           N  
ANISOU  447  N   TRP A  69     8850   8069   8135    174    180    188       N  
ATOM    448  CA  TRP A  69      49.353 -50.071 315.585  1.00 66.87           C  
ANISOU  448  CA  TRP A  69     8918   8253   8235     92    175    224       C  
ATOM    449  C   TRP A  69      48.096 -50.327 314.759  1.00 70.29           C  
ANISOU  449  C   TRP A  69     9268   8786   8654     55    207    277       C  
ATOM    450  O   TRP A  69      48.090 -50.129 313.546  1.00 84.31           O  
ANISOU  450  O   TRP A  69    10978  10615  10442     19    183    328       O  
ATOM    451  CB  TRP A  69      49.988 -51.408 315.979  1.00 69.09           C  
ANISOU  451  CB  TRP A  69     9275   8532   8445     73    186    178       C  
ATOM    452  CG  TRP A  69      51.213 -51.308 316.847  1.00 72.10           C  
ANISOU  452  CG  TRP A  69     9717   8859   8817    122    147    127       C  
ATOM    453  CD1 TRP A  69      51.410 -51.918 318.052  1.00 69.58           C  
ANISOU  453  CD1 TRP A  69     9493   8505   8438    170    158     77       C  
ATOM    454  CD2 TRP A  69      52.409 -50.565 316.574  1.00 67.40           C  
ANISOU  454  CD2 TRP A  69     9079   8266   8262    112     84    130       C  
ATOM    455  NE1 TRP A  69      52.651 -51.600 318.547  1.00 71.53           N  
ANISOU  455  NE1 TRP A  69     9754   8743   8683    207     97     40       N  
ATOM    456  CE2 TRP A  69      53.284 -50.770 317.660  1.00 61.64           C  
ANISOU  456  CE2 TRP A  69     8407   7518   7494    158     51     71       C  
ATOM    457  CE3 TRP A  69      52.824 -49.745 315.520  1.00 79.78           C  
ANISOU  457  CE3 TRP A  69    10562   9865   9885     56     51    188       C  
ATOM    458  CZ2 TRP A  69      54.547 -50.185 317.722  1.00 63.09           C  
ANISOU  458  CZ2 TRP A  69     8543   7732   7697    135    -21     62       C  
ATOM    459  CZ3 TRP A  69      54.080 -49.164 315.584  1.00 85.99           C  
ANISOU  459  CZ3 TRP A  69    11312  10667  10692     18     -9    190       C  
ATOM    460  CH2 TRP A  69      54.926 -49.388 316.677  1.00 80.48           C  
ANISOU  460  CH2 TRP A  69    10651   9969   9960     51    -48    124       C  
ATOM    461  N   VAL A  70      47.036 -50.767 315.431  1.00 63.43           N  
ANISOU  461  N   VAL A  70     8389   7966   7745     57    261    270       N  
ATOM    462  CA  VAL A  70      45.760 -51.058 314.783  1.00 59.28           C  
ANISOU  462  CA  VAL A  70     7754   7577   7194      0    286    320       C  
ATOM    463  C   VAL A  70      45.164 -49.811 314.131  1.00 67.01           C  
ANISOU  463  C   VAL A  70     8627   8613   8221     84    265    379       C  
ATOM    464  O   VAL A  70      44.536 -49.885 313.073  1.00 62.11           O  
ANISOU  464  O   VAL A  70     7905   8109   7586     39    247    433       O  
ATOM    465  CB  VAL A  70      44.746 -51.641 315.795  1.00 47.99           C  
ANISOU  465  CB  VAL A  70     6307   6222   5705    -23    356    316       C  
ATOM    466  CG1 VAL A  70      43.396 -51.886 315.139  1.00 59.67           C  
ANISOU  466  CG1 VAL A  70     7632   7889   7152   -104    375    376       C  
ATOM    467  CG2 VAL A  70      45.283 -52.927 316.395  1.00 47.38           C  
ANISOU  467  CG2 VAL A  70     6367   6065   5569   -109    373    278       C  
ATOM    468  N   LEU A  71      45.378 -48.663 314.764  1.00 70.75           N  
ANISOU  468  N   LEU A  71     9146   8991   8742    213    256    367       N  
ATOM    469  CA  LEU A  71      44.822 -47.405 314.281  1.00 72.65           C  
ANISOU  469  CA  LEU A  71     9338   9240   9024    330    232    423       C  
ATOM    470  C   LEU A  71      45.412 -47.016 312.926  1.00 69.45           C  
ANISOU  470  C   LEU A  71     8923   8811   8655    276    170    492       C  
ATOM    471  O   LEU A  71      44.684 -46.637 312.009  1.00 68.25           O  
ANISOU  471  O   LEU A  71     8679   8756   8495    311    154    569       O  
ATOM    472  CB  LEU A  71      45.061 -46.296 315.305  1.00 74.30           C  
ANISOU  472  CB  LEU A  71     9664   9298   9268    475    223    376       C  
ATOM    473  CG  LEU A  71      44.117 -45.095 315.233  1.00 83.27           C  
ANISOU  473  CG  LEU A  71    10782  10440  10416    665    221    415       C  
ATOM    474  CD1 LEU A  71      42.666 -45.548 315.289  1.00 86.74           C  
ANISOU  474  CD1 LEU A  71    11047  11125  10786    729    291    444       C  
ATOM    475  CD2 LEU A  71      44.416 -44.113 316.356  1.00 87.21           C  
ANISOU  475  CD2 LEU A  71    11449  10755  10931    808    206    336       C  
ATOM    476  N   HIS A  72      46.731 -47.116 312.804  1.00 68.43           N  
ANISOU  476  N   HIS A  72     8872   8580   8550    198    138    473       N  
ATOM    477  CA  HIS A  72      47.399 -46.856 311.535  1.00 65.19           C  
ANISOU  477  CA  HIS A  72     8439   8180   8152    131     95    546       C  
ATOM    478  C   HIS A  72      47.101 -47.972 310.541  1.00 70.58           C  
ANISOU  478  C   HIS A  72     9036   9019   8760     46    107    558       C  
ATOM    479  O   HIS A  72      47.014 -47.738 309.336  1.00 64.26           O  
ANISOU  479  O   HIS A  72     8180   8296   7939     25     80    634       O  
ATOM    480  CB  HIS A  72      48.910 -46.713 311.732  1.00 55.18           C  
ANISOU  480  CB  HIS A  72     7240   6814   6911     64     65    524       C  
ATOM    481  CG  HIS A  72      49.322 -45.398 312.315  1.00 70.81           C  
ANISOU  481  CG  HIS A  72     9316   8626   8962     98     20    532       C  
ATOM    482  ND1 HIS A  72      49.646 -44.307 311.537  1.00 74.85           N  
ANISOU  482  ND1 HIS A  72     9855   9067   9518     66    -27    632       N  
ATOM    483  CD2 HIS A  72      49.467 -44.997 313.601  1.00 86.29           C  
ANISOU  483  CD2 HIS A  72    11377  10462  10947    149      8    451       C  
ATOM    484  CE1 HIS A  72      49.971 -43.292 312.317  1.00 77.99           C  
ANISOU  484  CE1 HIS A  72    10380   9280   9972     84    -74    608       C  
ATOM    485  NE2 HIS A  72      49.870 -43.683 313.573  1.00 91.73           N  
ANISOU  485  NE2 HIS A  72    12164  10991  11698    141    -55    489       N  
ATOM    486  N   LEU A  73      46.937 -49.186 311.058  1.00 69.66           N  
ANISOU  486  N   LEU A  73     8935   8938   8595     -5    140    484       N  
ATOM    487  CA  LEU A  73      46.661 -50.348 310.223  1.00 63.93           C  
ANISOU  487  CA  LEU A  73     8180   8321   7791   -101    139    472       C  
ATOM    488  C   LEU A  73      45.273 -50.253 309.592  1.00 82.40           C  
ANISOU  488  C   LEU A  73    10398  10810  10100   -116    130    525       C  
ATOM    489  O   LEU A  73      45.012 -50.856 308.551  1.00 91.71           O  
ANISOU  489  O   LEU A  73    11538  12096  11212   -198    102    534       O  
ATOM    490  CB  LEU A  73      46.788 -51.634 311.042  1.00 57.45           C  
ANISOU  490  CB  LEU A  73     7449   7455   6924   -157    170    387       C  
ATOM    491  CG  LEU A  73      46.913 -52.943 310.262  1.00 68.98           C  
ANISOU  491  CG  LEU A  73     8965   8949   8296   -254    156    347       C  
ATOM    492  CD1 LEU A  73      48.081 -52.875 309.292  1.00 82.15           C  
ANISOU  492  CD1 LEU A  73    10650  10625   9939   -221    130    348       C  
ATOM    493  CD2 LEU A  73      47.076 -54.121 311.209  1.00 68.89           C  
ANISOU  493  CD2 LEU A  73     9091   8842   8243   -292    182    277       C  
ATOM    494  N   ALA A  74      44.388 -49.490 310.226  1.00 79.27           N  
ANISOU  494  N   ALA A  74     9938  10441   9739    -24    150    556       N  
ATOM    495  CA  ALA A  74      43.045 -49.278 309.699  1.00 78.34           C  
ANISOU  495  CA  ALA A  74     9668  10510   9587     -5    139    617       C  
ATOM    496  C   ALA A  74      42.999 -48.036 308.813  1.00 90.15           C  
ANISOU  496  C   ALA A  74    11126  12019  11110    113     93    712       C  
ATOM    497  O   ALA A  74      42.020 -47.804 308.102  1.00 82.74           O  
ANISOU  497  O   ALA A  74    10056  11253  10129    149     64    778       O  
ATOM    498  CB  ALA A  74      42.041 -49.159 310.834  1.00 56.38           C  
ANISOU  498  CB  ALA A  74     6817   7800   6804     65    195    606       C  
ATOM    499  N   LEU A  75      44.061 -47.240 308.860  1.00 89.89           N  
ANISOU  499  N   LEU A  75    11209  11807  11138    163     78    728       N  
ATOM    500  CA  LEU A  75      44.143 -46.027 308.056  1.00 86.57           C  
ANISOU  500  CA  LEU A  75    10799  11351  10744    254     33    836       C  
ATOM    501  C   LEU A  75      44.568 -46.349 306.628  1.00 78.40           C  
ANISOU  501  C   LEU A  75     9730  10410   9648    156     -3    896       C  
ATOM    502  O   LEU A  75      44.077 -45.747 305.674  1.00 74.59           O  
ANISOU  502  O   LEU A  75     9193  10016   9133    214    -43   1000       O  
ATOM    503  CB  LEU A  75      45.118 -45.030 308.683  1.00 84.36           C  
ANISOU  503  CB  LEU A  75    10670  10833  10549    300     24    838       C  
ATOM    504  CG  LEU A  75      45.250 -43.682 307.971  1.00 84.89           C  
ANISOU  504  CG  LEU A  75    10803  10803  10650    376    -27    963       C  
ATOM    505  CD1 LEU A  75      43.919 -42.947 307.954  1.00 86.07           C  
ANISOU  505  CD1 LEU A  75    10908  11007  10786    577    -39   1018       C  
ATOM    506  CD2 LEU A  75      46.328 -42.829 308.622  1.00 84.73           C  
ANISOU  506  CD2 LEU A  75    10951  10533  10710    352    -49    952       C  
ATOM    507  N   SER A  76      45.483 -47.303 306.487  1.00 75.69           N  
ANISOU  507  N   SER A  76     9427  10060   9273     32     11    830       N  
ATOM    508  CA  SER A  76      45.952 -47.717 305.171  1.00 81.41           C  
ANISOU  508  CA  SER A  76    10128  10890   9912    -42    -12    865       C  
ATOM    509  C   SER A  76      44.845 -48.438 304.409  1.00 91.28           C  
ANISOU  509  C   SER A  76    11279  12337  11065    -83    -42    856       C  
ATOM    510  O   SER A  76      44.757 -48.339 303.185  1.00107.77           O  
ANISOU  510  O   SER A  76    13325  14551  13074    -94    -81    922       O  
ATOM    511  CB  SER A  76      47.184 -48.617 305.291  1.00 77.50           C  
ANISOU  511  CB  SER A  76     9705  10352   9391   -120     16    779       C  
ATOM    512  OG  SER A  76      46.847 -49.874 305.852  1.00 85.91           O  
ANISOU  512  OG  SER A  76    10797  11425  10420   -172     33    662       O  
ATOM    513  N   ASP A  77      44.001 -49.160 305.138  1.00 80.37           N  
ANISOU  513  N   ASP A  77     9860  10997   9680   -123    -28    781       N  
ATOM    514  CA  ASP A  77      42.888 -49.878 304.528  1.00 77.03           C  
ANISOU  514  CA  ASP A  77     9330  10773   9165   -207    -68    769       C  
ATOM    515  C   ASP A  77      41.771 -48.923 304.117  1.00 79.59           C  
ANISOU  515  C   ASP A  77     9502  11256   9481    -97   -106    879       C  
ATOM    516  O   ASP A  77      40.993 -49.219 303.210  1.00 81.27           O  
ANISOU  516  O   ASP A  77     9604  11676   9600   -148   -165    905       O  
ATOM    517  CB  ASP A  77      42.346 -50.944 305.483  1.00 81.34           C  
ANISOU  517  CB  ASP A  77     9880  11318   9705   -320    -38    675       C  
ATOM    518  CG  ASP A  77      43.316 -52.090 305.689  1.00 97.71           C  
ANISOU  518  CG  ASP A  77    12122  13252  11752   -420    -20    568       C  
ATOM    519  OD1 ASP A  77      44.527 -51.897 305.448  1.00107.93           O  
ANISOU  519  OD1 ASP A  77    13509  14442  13058   -363     -9    561       O  
ATOM    520  OD2 ASP A  77      42.869 -53.184 306.095  1.00 99.91           O  
ANISOU  520  OD2 ASP A  77    12440  13531  11990   -555    -17    498       O  
ATOM    521  N   LEU A  78      41.694 -47.778 304.789  1.00 75.04           N  
ANISOU  521  N   LEU A  78     8934  10585   8993     68    -80    938       N  
ATOM    522  CA  LEU A  78      40.711 -46.761 304.437  1.00 72.57           C  
ANISOU  522  CA  LEU A  78     8507  10397   8670    235   -116   1049       C  
ATOM    523  C   LEU A  78      41.069 -46.136 303.095  1.00 88.16           C  
ANISOU  523  C   LEU A  78    10504  12396  10595    273   -175   1162       C  
ATOM    524  O   LEU A  78      40.199 -45.887 302.260  1.00 97.11           O  
ANISOU  524  O   LEU A  78    11514  13734  11651    336   -234   1243       O  
ATOM    525  CB  LEU A  78      40.628 -45.682 305.519  1.00 66.74           C  
ANISOU  525  CB  LEU A  78     7829   9504   8027    428    -76   1067       C  
ATOM    526  CG  LEU A  78      39.548 -44.615 305.318  1.00 62.66           C  
ANISOU  526  CG  LEU A  78     7215   9102   7493    663   -107   1171       C  
ATOM    527  CD1 LEU A  78      38.159 -45.218 305.464  1.00 56.26           C  
ANISOU  527  CD1 LEU A  78     6163   8608   6607    664   -103   1156       C  
ATOM    528  CD2 LEU A  78      39.739 -43.452 306.281  1.00 58.63           C  
ANISOU  528  CD2 LEU A  78     6848   8358   7069    871    -78   1176       C  
ATOM    529  N   LEU A  79      42.359 -45.885 302.895  1.00 88.12           N  
ANISOU  529  N   LEU A  79    10647  12210  10626    232   -159   1176       N  
ATOM    530  CA  LEU A  79      42.848 -45.358 301.628  1.00 87.02           C  
ANISOU  530  CA  LEU A  79    10539  12100  10426    239   -199   1296       C  
ATOM    531  C   LEU A  79      42.692 -46.396 300.522  1.00 85.55           C  
ANISOU  531  C   LEU A  79    10275  12133  10097    117   -236   1261       C  
ATOM    532  O   LEU A  79      42.385 -46.060 299.378  1.00 91.73           O  
ANISOU  532  O   LEU A  79    11008  13063  10781    154   -291   1363       O  
ATOM    533  CB  LEU A  79      44.313 -44.930 301.751  1.00 79.06           C  
ANISOU  533  CB  LEU A  79     9677  10883   9480    187   -164   1320       C  
ATOM    534  CG  LEU A  79      44.619 -43.838 302.776  1.00 78.52           C  
ANISOU  534  CG  LEU A  79     9726  10564   9544    275   -147   1348       C  
ATOM    535  CD1 LEU A  79      46.108 -43.525 302.802  1.00 76.24           C  
ANISOU  535  CD1 LEU A  79     9551  10117   9299    167   -126   1374       C  
ATOM    536  CD2 LEU A  79      43.809 -42.585 302.479  1.00 79.68           C  
ANISOU  536  CD2 LEU A  79     9895  10681   9700    457   -195   1486       C  
ATOM    537  N   ALA A  80      42.899 -47.660 300.879  1.00 71.36           N  
ANISOU  537  N   ALA A  80     8492  10344   8277    -21   -213   1113       N  
ATOM    538  CA  ALA A  80      42.815 -48.760 299.926  1.00 72.90           C  
ANISOU  538  CA  ALA A  80     8667  10701   8330   -145   -254   1043       C  
ATOM    539  C   ALA A  80      41.401 -48.929 299.381  1.00 82.93           C  
ANISOU  539  C   ALA A  80     9781  12217   9512   -161   -334   1065       C  
ATOM    540  O   ALA A  80      41.215 -49.264 298.212  1.00104.49           O  
ANISOU  540  O   ALA A  80    12480  15120  12102   -211   -400   1074       O  
ATOM    541  CB  ALA A  80      43.289 -50.053 300.570  1.00 70.89           C  
ANISOU  541  CB  ALA A  80     8506  10351   8077   -272   -217    880       C  
ATOM    542  N   SER A  81      40.408 -48.697 300.232  1.00 73.72           N  
ANISOU  542  N   SER A  81     8504  11095   8412   -116   -329   1073       N  
ATOM    543  CA  SER A  81      39.015 -48.820 299.822  1.00 75.35           C  
ANISOU  543  CA  SER A  81     8513  11584   8534   -130   -405   1103       C  
ATOM    544  C   SER A  81      38.482 -47.497 299.280  1.00 72.01           C  
ANISOU  544  C   SER A  81     7994  11269   8096     93   -447   1269       C  
ATOM    545  O   SER A  81      37.317 -47.395 298.897  1.00 70.16           O  
ANISOU  545  O   SER A  81     7568  11304   7785    137   -516   1320       O  
ATOM    546  CB  SER A  81      38.150 -49.302 300.990  1.00 77.84           C  
ANISOU  546  CB  SER A  81     8722  11953   8902   -193   -371   1039       C  
ATOM    547  OG  SER A  81      38.138 -48.355 302.043  1.00 85.99           O  
ANISOU  547  OG  SER A  81     9758  12858  10054     -4   -299   1087       O  
ATOM    548  N   ALA A  82      39.342 -46.485 299.250  1.00 72.89           N  
ANISOU  548  N   ALA A  82     8244  11173   8276    230   -411   1360       N  
ATOM    549  CA  ALA A  82      38.979 -45.192 298.684  1.00 82.58           C  
ANISOU  549  CA  ALA A  82     9449  12440   9486    447   -455   1533       C  
ATOM    550  C   ALA A  82      39.287 -45.164 297.189  1.00 95.52           C  
ANISOU  550  C   ALA A  82    11106  14204  10983    415   -519   1620       C  
ATOM    551  O   ALA A  82      38.638 -44.451 296.425  1.00 99.29           O  
ANISOU  551  O   ALA A  82    11511  14836  11380    562   -590   1758       O  
ATOM    552  CB  ALA A  82      39.709 -44.068 299.403  1.00 79.36           C  
ANISOU  552  CB  ALA A  82     9215  11722   9216    586   -396   1597       C  
ATOM    553  N   SER A  83      40.282 -45.947 296.782  1.00 93.08           N  
ANISOU  553  N   SER A  83    10897  13842  10629    244   -493   1540       N  
ATOM    554  CA  SER A  83      40.658 -46.048 295.377  1.00 87.78           C  
ANISOU  554  CA  SER A  83    10248  13308   9796    208   -540   1602       C  
ATOM    555  C   SER A  83      39.788 -47.076 294.668  1.00 92.90           C  
ANISOU  555  C   SER A  83    10768  14244  10284     95   -632   1508       C  
ATOM    556  O   SER A  83      39.672 -47.075 293.442  1.00 93.04           O  
ANISOU  556  O   SER A  83    10761  14454  10134    101   -703   1567       O  
ATOM    557  CB  SER A  83      42.134 -46.426 295.238  1.00 81.13           C  
ANISOU  557  CB  SER A  83     9558  12316   8952    104   -464   1552       C  
ATOM    558  OG  SER A  83      42.353 -47.761 295.663  1.00 77.10           O  
ANISOU  558  OG  SER A  83     9072  11789   8432    -46   -442   1352       O  
ATOM    559  N   LEU A  84      39.182 -47.956 295.457  1.00 86.83           N  
ANISOU  559  N   LEU A  84     9928  13505   9559    -23   -635   1365       N  
ATOM    560  CA  LEU A  84      38.348 -49.032 294.933  1.00 85.16           C  
ANISOU  560  CA  LEU A  84     9611  13538   9208   -191   -731   1257       C  
ATOM    561  C   LEU A  84      37.154 -48.569 294.079  1.00 93.56           C  
ANISOU  561  C   LEU A  84    10472  14934  10144   -111   -853   1368       C  
ATOM    562  O   LEU A  84      36.882 -49.174 293.042  1.00 96.66           O  
ANISOU  562  O   LEU A  84    10833  15535  10359   -220   -953   1323       O  
ATOM    563  CB  LEU A  84      37.850 -49.906 296.087  1.00 77.78           C  
ANISOU  563  CB  LEU A  84     8633  12560   8361   -345   -704   1122       C  
ATOM    564  CG  LEU A  84      37.242 -51.253 295.695  1.00 81.78           C  
ANISOU  564  CG  LEU A  84     9105  13230   8739   -603   -796    979       C  
ATOM    565  CD1 LEU A  84      38.200 -52.028 294.805  1.00 78.22           C  
ANISOU  565  CD1 LEU A  84     8861  12695   8162   -695   -816    872       C  
ATOM    566  CD2 LEU A  84      36.895 -52.059 296.935  1.00 86.52           C  
ANISOU  566  CD2 LEU A  84     9699  13736   9437   -768   -749    874       C  
ATOM    567  N   PRO A  85      36.433 -47.506 294.498  1.00 91.35           N  
ANISOU  567  N   PRO A  85    10060  14713   9937     98   -852   1505       N  
ATOM    568  CA  PRO A  85      35.313 -47.088 293.642  1.00 86.13           C  
ANISOU  568  CA  PRO A  85     9192  14398   9134    204   -976   1616       C  
ATOM    569  C   PRO A  85      35.736 -46.569 292.265  1.00 84.22           C  
ANISOU  569  C   PRO A  85     9030  14227   8741    298  -1037   1740       C  
ATOM    570  O   PRO A  85      34.904 -46.524 291.360  1.00 89.22           O  
ANISOU  570  O   PRO A  85     9510  15180   9210    334  -1161   1800       O  
ATOM    571  CB  PRO A  85      34.646 -45.970 294.456  1.00 82.01           C  
ANISOU  571  CB  PRO A  85     8563  13871   8728    472   -941   1740       C  
ATOM    572  CG  PRO A  85      35.689 -45.506 295.403  1.00 79.07           C  
ANISOU  572  CG  PRO A  85     8409  13098   8537    531   -809   1731       C  
ATOM    573  CD  PRO A  85      36.464 -46.732 295.752  1.00 83.53           C  
ANISOU  573  CD  PRO A  85     9087  13518   9132    255   -755   1549       C  
ATOM    574  N   PHE A  86      37.000 -46.187 292.110  1.00 86.60           N  
ANISOU  574  N   PHE A  86     9555  14264   9086    330   -952   1785       N  
ATOM    575  CA  PHE A  86      37.511 -45.775 290.805  1.00 78.70           C  
ANISOU  575  CA  PHE A  86     8640  13337   7925    388   -989   1909       C  
ATOM    576  C   PHE A  86      37.800 -46.993 289.935  1.00 80.85           C  
ANISOU  576  C   PHE A  86     8946  13758   8014    181  -1038   1756       C  
ATOM    577  O   PHE A  86      37.728 -46.922 288.709  1.00 95.06           O  
ANISOU  577  O   PHE A  86    10738  15768   9611    209  -1118   1824       O  
ATOM    578  CB  PHE A  86      38.776 -44.927 290.951  1.00 82.71           C  
ANISOU  578  CB  PHE A  86     9355  13538   8534    466   -875   2026       C  
ATOM    579  CG  PHE A  86      38.549 -43.608 291.632  1.00 91.18           C  
ANISOU  579  CG  PHE A  86    10458  14430   9758    683   -847   2186       C  
ATOM    580  CD1 PHE A  86      38.098 -42.513 290.915  1.00 89.65           C  
ANISOU  580  CD1 PHE A  86    10262  14317   9483    897   -913   2406       C  
ATOM    581  CD2 PHE A  86      38.796 -43.461 292.988  1.00 96.27           C  
ANISOU  581  CD2 PHE A  86    11158  14811  10610    687   -760   2114       C  
ATOM    582  CE1 PHE A  86      37.891 -41.296 291.537  1.00 95.83           C  
ANISOU  582  CE1 PHE A  86    11121  14896  10395   1119   -895   2544       C  
ATOM    583  CE2 PHE A  86      38.592 -42.246 293.616  1.00 95.62           C  
ANISOU  583  CE2 PHE A  86    11139  14541  10651    900   -741   2241       C  
ATOM    584  CZ  PHE A  86      38.138 -41.162 292.889  1.00 97.09           C  
ANISOU  584  CZ  PHE A  86    11347  14784  10760   1120   -809   2452       C  
ATOM    585  N   PHE A  87      38.132 -48.110 290.576  1.00 84.97           N  
ANISOU  585  N   PHE A  87     9528  14160   8596    -14   -994   1549       N  
ATOM    586  CA  PHE A  87      38.377 -49.356 289.860  1.00 77.30           C  
ANISOU  586  CA  PHE A  87     8634  13284   7453   -202  -1046   1371       C  
ATOM    587  C   PHE A  87      37.056 -49.964 289.403  1.00 85.40           C  
ANISOU  587  C   PHE A  87     9487  14624   8340   -323  -1208   1301       C  
ATOM    588  O   PHE A  87      37.007 -50.702 288.419  1.00 90.19           O  
ANISOU  588  O   PHE A  87    10137  15393   8737   -437  -1303   1201       O  
ATOM    589  CB  PHE A  87      39.148 -50.348 290.736  1.00 69.07           C  
ANISOU  589  CB  PHE A  87     7744  11982   6518   -350   -954   1179       C  
ATOM    590  CG  PHE A  87      39.447 -51.657 290.055  1.00 75.05           C  
ANISOU  590  CG  PHE A  87     8633  12785   7096   -514  -1007    980       C  
ATOM    591  CD1 PHE A  87      40.502 -51.764 289.164  1.00 82.19           C  
ANISOU  591  CD1 PHE A  87     9688  13685   7854   -455   -966    969       C  
ATOM    592  CD2 PHE A  87      38.676 -52.780 290.311  1.00 77.75           C  
ANISOU  592  CD2 PHE A  87     8964  13173   7405   -730  -1096    805       C  
ATOM    593  CE1 PHE A  87      40.781 -52.963 288.538  1.00 74.72           C  
ANISOU  593  CE1 PHE A  87     8892  12771   6725   -566  -1014    769       C  
ATOM    594  CE2 PHE A  87      38.951 -53.983 289.688  1.00 81.29           C  
ANISOU  594  CE2 PHE A  87     9586  13618   7681   -877  -1157    609       C  
ATOM    595  CZ  PHE A  87      40.005 -54.073 288.801  1.00 76.32           C  
ANISOU  595  CZ  PHE A  87     9122  12975   6901   -774  -1116    582       C  
ATOM    596  N   THR A  88      35.986 -49.648 290.125  1.00 87.45           N  
ANISOU  596  N   THR A  88     9542  14983   8701   -298  -1240   1349       N  
ATOM    597  CA  THR A  88      34.656 -50.112 289.758  1.00 94.11           C  
ANISOU  597  CA  THR A  88    10162  16177   9417   -419  -1397   1310       C  
ATOM    598  C   THR A  88      34.199 -49.422 288.476  1.00 94.34           C  
ANISOU  598  C   THR A  88    10085  16512   9247   -264  -1518   1460       C  
ATOM    599  O   THR A  88      33.575 -50.038 287.612  1.00 91.08           O  
ANISOU  599  O   THR A  88     9586  16389   8632   -403  -1670   1388       O  
ATOM    600  CB  THR A  88      33.633 -49.852 290.881  1.00103.48           C  
ANISOU  600  CB  THR A  88    11117  17447  10753   -397  -1383   1349       C  
ATOM    601  OG1 THR A  88      33.484 -48.441 291.080  1.00117.66           O  
ANISOU  601  OG1 THR A  88    12837  19238  12631    -72  -1336   1556       O  
ATOM    602  CG2 THR A  88      34.097 -50.493 292.179  1.00 96.05           C  
ANISOU  602  CG2 THR A  88    10292  16205   9998   -540  -1258   1220       C  
ATOM    603  N   TYR A  89      34.524 -48.138 288.361  1.00 91.71           N  
ANISOU  603  N   TYR A  89     9778  16104   8963     18  -1458   1669       N  
ATOM    604  CA  TYR A  89      34.220 -47.372 287.160  1.00 85.29           C  
ANISOU  604  CA  TYR A  89     8908  15538   7961    201  -1558   1847       C  
ATOM    605  C   TYR A  89      34.987 -47.938 285.967  1.00 91.35           C  
ANISOU  605  C   TYR A  89     9847  16350   8513     98  -1590   1780       C  
ATOM    606  O   TYR A  89      34.470 -47.984 284.853  1.00 92.05           O  
ANISOU  606  O   TYR A  89     9856  16753   8365    111  -1730   1816       O  
ATOM    607  CB  TYR A  89      34.559 -45.894 287.371  1.00 80.93           C  
ANISOU  607  CB  TYR A  89     8423  14806   7522    507  -1472   2089       C  
ATOM    608  CG  TYR A  89      34.069 -44.980 286.270  1.00 87.50           C  
ANISOU  608  CG  TYR A  89     9188  15886   8170    736  -1580   2310       C  
ATOM    609  CD1 TYR A  89      32.809 -44.399 286.334  1.00 88.90           C  
ANISOU  609  CD1 TYR A  89     9128  16328   8321    932  -1684   2423       C  
ATOM    610  CD2 TYR A  89      34.866 -44.694 285.168  1.00 94.69           C  
ANISOU  610  CD2 TYR A  89    10270  16790   8920    774  -1576   2416       C  
ATOM    611  CE1 TYR A  89      32.355 -43.560 285.331  1.00100.38           C  
ANISOU  611  CE1 TYR A  89    10533  18010   9597   1171  -1791   2635       C  
ATOM    612  CE2 TYR A  89      34.420 -43.858 284.160  1.00 91.35           C  
ANISOU  612  CE2 TYR A  89     9804  16590   8315    988  -1677   2636       C  
ATOM    613  CZ  TYR A  89      33.166 -43.293 284.246  1.00 98.36           C  
ANISOU  613  CZ  TYR A  89    10473  17717   9184   1192  -1789   2744       C  
ATOM    614  OH  TYR A  89      32.721 -42.461 283.244  1.00 96.21           O  
ANISOU  614  OH  TYR A  89    10169  17667   8720   1432  -1897   2972       O  
ATOM    615  N   PHE A  90      36.219 -48.375 286.220  1.00 88.87           N  
ANISOU  615  N   PHE A  90     9759  15743   8265     10  -1460   1679       N  
ATOM    616  CA  PHE A  90      37.070 -48.982 285.198  1.00 86.65           C  
ANISOU  616  CA  PHE A  90     9653  15492   7778    -64  -1460   1593       C  
ATOM    617  C   PHE A  90      36.409 -50.199 284.555  1.00 96.14           C  
ANISOU  617  C   PHE A  90    10822  16936   8770   -276  -1620   1382       C  
ATOM    618  O   PHE A  90      36.460 -50.373 283.339  1.00106.25           O  
ANISOU  618  O   PHE A  90    12147  18432   9790   -267  -1708   1374       O  
ATOM    619  CB  PHE A  90      38.420 -49.373 285.808  1.00 84.41           C  
ANISOU  619  CB  PHE A  90     9580  14870   7622   -118  -1291   1493       C  
ATOM    620  CG  PHE A  90      39.283 -50.214 284.906  1.00 83.78           C  
ANISOU  620  CG  PHE A  90     9677  14828   7328   -188  -1279   1354       C  
ATOM    621  CD1 PHE A  90      40.032 -49.629 283.900  1.00 81.54           C  
ANISOU  621  CD1 PHE A  90     9467  14637   6879    -56  -1233   1500       C  
ATOM    622  CD2 PHE A  90      39.363 -51.588 285.082  1.00 80.72           C  
ANISOU  622  CD2 PHE A  90     9401  14375   6896   -376  -1309   1082       C  
ATOM    623  CE1 PHE A  90      40.832 -50.397 283.077  1.00 87.31           C  
ANISOU  623  CE1 PHE A  90    10350  15432   7390    -88  -1209   1368       C  
ATOM    624  CE2 PHE A  90      40.160 -52.361 284.261  1.00 80.52           C  
ANISOU  624  CE2 PHE A  90     9562  14376   6657   -396  -1298    939       C  
ATOM    625  CZ  PHE A  90      40.895 -51.765 283.258  1.00 88.54           C  
ANISOU  625  CZ  PHE A  90    10623  15521   7497   -240  -1243   1078       C  
ATOM    626  N   LEU A  91      35.790 -51.037 285.381  1.00 92.58           N  
ANISOU  626  N   LEU A  91    10305  16446   8425   -478  -1660   1213       N  
ATOM    627  CA  LEU A  91      35.120 -52.238 284.899  1.00 90.15           C  
ANISOU  627  CA  LEU A  91     9986  16327   7940   -736  -1823   1003       C  
ATOM    628  C   LEU A  91      33.776 -51.905 284.261  1.00 98.25           C  
ANISOU  628  C   LEU A  91    10736  17778   8817   -733  -2014   1095       C  
ATOM    629  O   LEU A  91      33.306 -52.615 283.369  1.00 92.65           O  
ANISOU  629  O   LEU A  91    10021  17311   7871   -895  -2182    971       O  
ATOM    630  CB  LEU A  91      34.923 -53.234 286.043  1.00 78.49           C  
ANISOU  630  CB  LEU A  91     8545  14649   6629   -984  -1798    817       C  
ATOM    631  CG  LEU A  91      36.189 -53.693 286.766  1.00 96.83           C  
ANISOU  631  CG  LEU A  91    11134  16563   9094   -989  -1626    709       C  
ATOM    632  CD1 LEU A  91      35.844 -54.640 287.908  1.00101.31           C  
ANISOU  632  CD1 LEU A  91    11729  16953   9813  -1231  -1617    554       C  
ATOM    633  CD2 LEU A  91      37.147 -54.351 285.788  1.00 95.81           C  
ANISOU  633  CD2 LEU A  91    11268  16383   8753   -989  -1628    571       C  
ATOM    634  N   ALA A  92      33.162 -50.822 284.726  1.00 95.53           N  
ANISOU  634  N   ALA A  92    10169  17529   8600   -536  -1993   1306       N  
ATOM    635  CA  ALA A  92      31.840 -50.423 284.257  1.00 93.82           C  
ANISOU  635  CA  ALA A  92     9647  17742   8257   -485  -2166   1414       C  
ATOM    636  C   ALA A  92      31.858 -50.036 282.783  1.00106.77           C  
ANISOU  636  C   ALA A  92    11307  19647   9612   -350  -2284   1512       C  
ATOM    637  O   ALA A  92      30.854 -50.176 282.083  1.00 99.44           O  
ANISOU  637  O   ALA A  92    10175  19120   8486   -403  -2478   1515       O  
ATOM    638  CB  ALA A  92      31.309 -49.273 285.098  1.00 93.99           C  
ANISOU  638  CB  ALA A  92     9467  17773   8472   -228  -2097   1622       C  
ATOM    639  N   VAL A  93      33.002 -49.545 282.317  1.00112.58           N  
ANISOU  639  N   VAL A  93    12278  20182  10316   -185  -2166   1601       N  
ATOM    640  CA  VAL A  93      33.148 -49.148 280.923  1.00107.04           C  
ANISOU  640  CA  VAL A  93    11624  19714   9331    -48  -2250   1714       C  
ATOM    641  C   VAL A  93      33.944 -50.205 280.156  1.00110.69           C  
ANISOU  641  C   VAL A  93    12330  20139   9590   -223  -2260   1496       C  
ATOM    642  O   VAL A  93      34.685 -49.891 279.226  1.00122.19           O  
ANISOU  642  O   VAL A  93    13934  21629  10862    -94  -2222   1579       O  
ATOM    643  CB  VAL A  93      33.834 -47.772 280.799  1.00 97.15           C  
ANISOU  643  CB  VAL A  93    10460  18310   8141    264  -2117   2004       C  
ATOM    644  CG1 VAL A  93      33.398 -47.074 279.519  1.00118.78           C  
ANISOU  644  CG1 VAL A  93    13132  21394  10604    457  -2249   2205       C  
ATOM    645  CG2 VAL A  93      33.490 -46.904 281.995  1.00 81.36           C  
ANISOU  645  CG2 VAL A  93     8348  16131   6434    418  -2031   2143       C  
ATOM    646  N   GLY A  94      33.783 -51.461 280.562  1.00106.01           N  
ANISOU  646  N   GLY A  94    11789  19471   9018   -512  -2309   1220       N  
ATOM    647  CA  GLY A  94      34.392 -52.582 279.868  1.00 96.29           C  
ANISOU  647  CA  GLY A  94    10809  18200   7578   -674  -2346    975       C  
ATOM    648  C   GLY A  94      35.909 -52.598 279.889  1.00 91.85           C  
ANISOU  648  C   GLY A  94    10522  17329   7048   -561  -2138    956       C  
ATOM    649  O   GLY A  94      36.542 -52.725 278.841  1.00105.67           O  
ANISOU  649  O   GLY A  94    12427  19178   8544   -483  -2137    930       O  
ATOM    650  N   HIS A  95      36.485 -52.471 281.083  1.00 80.70           N  
ANISOU  650  N   HIS A  95     9155  15574   5933   -547  -1964    970       N  
ATOM    651  CA  HIS A  95      37.936 -52.512 281.272  1.00 85.75           C  
ANISOU  651  CA  HIS A  95    10018  15931   6633   -453  -1764    951       C  
ATOM    652  C   HIS A  95      38.664 -51.454 280.446  1.00 87.48           C  
ANISOU  652  C   HIS A  95    10257  16250   6732   -215  -1673   1194       C  
ATOM    653  O   HIS A  95      39.315 -51.773 279.451  1.00 86.06           O  
ANISOU  653  O   HIS A  95    10219  16184   6294   -169  -1662   1140       O  
ATOM    654  CB  HIS A  95      38.484 -53.902 280.931  1.00 94.12           C  
ANISOU  654  CB  HIS A  95    11330  16905   7527   -593  -1785    647       C  
ATOM    655  CG  HIS A  95      38.024 -54.980 281.862  1.00 98.89           C  
ANISOU  655  CG  HIS A  95    11987  17313   8272   -842  -1839    418       C  
ATOM    656  ND1 HIS A  95      36.727 -55.449 281.877  1.00100.06           N  
ANISOU  656  ND1 HIS A  95    12002  17632   8383  -1067  -2033    333       N  
ATOM    657  CD2 HIS A  95      38.689 -55.681 282.811  1.00 89.25           C  
ANISOU  657  CD2 HIS A  95    10939  15752   7222   -910  -1726    272       C  
ATOM    658  CE1 HIS A  95      36.614 -56.393 282.795  1.00 97.85           C  
ANISOU  658  CE1 HIS A  95    11822  17110   8247  -1284  -2032    151       C  
ATOM    659  NE2 HIS A  95      37.790 -56.553 283.376  1.00 92.39           N  
ANISOU  659  NE2 HIS A  95    11327  16096   7681  -1180  -1848    110       N  
ATOM    660  N   SER A  96      38.552 -50.198 280.867  1.00 85.07           N  
ANISOU  660  N   SER A  96     9824  15896   6602    -65  -1608   1463       N  
ATOM    661  CA  SER A  96      39.202 -49.093 280.171  1.00 78.75           C  
ANISOU  661  CA  SER A  96     9056  15153   5712    135  -1523   1733       C  
ATOM    662  C   SER A  96      39.429 -47.909 281.106  1.00 75.46           C  
ANISOU  662  C   SER A  96     8595  14489   5587    251  -1401   1964       C  
ATOM    663  O   SER A  96      38.505 -47.457 281.782  1.00 78.17           O  
ANISOU  663  O   SER A  96     8795  14811   6096    287  -1463   2028       O  
ATOM    664  CB  SER A  96      38.366 -48.658 278.964  1.00 84.40           C  
ANISOU  664  CB  SER A  96     9671  16244   6153    228  -1689   1869       C  
ATOM    665  OG  SER A  96      38.994 -47.602 278.257  1.00 80.57           O  
ANISOU  665  OG  SER A  96     9240  15808   5563    409  -1605   2150       O  
ATOM    666  N   TRP A  97      40.661 -47.413 281.148  1.00 77.02           N  
ANISOU  666  N   TRP A  97     8916  14512   5837    309  -1232   2083       N  
ATOM    667  CA  TRP A  97      40.979 -46.251 281.970  1.00 79.81           C  
ANISOU  667  CA  TRP A  97     9269  14607   6448    398  -1125   2301       C  
ATOM    668  C   TRP A  97      40.747 -44.964 281.187  1.00 91.33           C  
ANISOU  668  C   TRP A  97    10718  16182   7801    570  -1160   2626       C  
ATOM    669  O   TRP A  97      41.458 -44.676 280.225  1.00 91.02           O  
ANISOU  669  O   TRP A  97    10763  16258   7563    605  -1108   2764       O  
ATOM    670  CB  TRP A  97      42.423 -46.314 282.469  1.00 77.17           C  
ANISOU  670  CB  TRP A  97     9060  14028   6231    343   -937   2280       C  
ATOM    671  CG  TRP A  97      42.725 -45.276 283.501  1.00 85.53           C  
ANISOU  671  CG  TRP A  97    10136  14785   7579    384   -846   2445       C  
ATOM    672  CD1 TRP A  97      43.237 -44.030 283.287  1.00 92.07           C  
ANISOU  672  CD1 TRP A  97    11026  15520   8435    462   -780   2733       C  
ATOM    673  CD2 TRP A  97      42.519 -45.388 284.914  1.00 80.95           C  
ANISOU  673  CD2 TRP A  97     9530  13942   7283    340   -819   2331       C  
ATOM    674  NE1 TRP A  97      43.369 -43.361 284.481  1.00 88.42           N  
ANISOU  674  NE1 TRP A  97    10594  14739   8263    467   -724   2787       N  
ATOM    675  CE2 TRP A  97      42.934 -44.174 285.495  1.00 86.81           C  
ANISOU  675  CE2 TRP A  97    10329  14440   8214    406   -743   2541       C  
ATOM    676  CE3 TRP A  97      42.026 -46.399 285.744  1.00 86.65           C  
ANISOU  676  CE3 TRP A  97    10204  14610   8111    241   -853   2076       C  
ATOM    677  CZ2 TRP A  97      42.871 -43.943 286.868  1.00 90.71           C  
ANISOU  677  CZ2 TRP A  97    10828  14653   8985    397   -702   2487       C  
ATOM    678  CZ3 TRP A  97      41.965 -46.169 287.107  1.00 90.40           C  
ANISOU  678  CZ3 TRP A  97    10668  14821   8859    231   -800   2044       C  
ATOM    679  CH2 TRP A  97      42.385 -44.951 287.655  1.00 86.25           C  
ANISOU  679  CH2 TRP A  97    10195  14070   8506    319   -726   2240       C  
ATOM    680  N   GLU A  98      39.751 -44.189 281.606  1.00 92.52           N  
ANISOU  680  N   GLU A  98    10773  16309   8073    691  -1244   2755       N  
ATOM    681  CA  GLU A  98      39.350 -42.995 280.870  1.00 92.68           C  
ANISOU  681  CA  GLU A  98    10798  16437   7981    889  -1306   3063       C  
ATOM    682  C   GLU A  98      39.501 -41.723 281.699  1.00 95.41           C  
ANISOU  682  C   GLU A  98    11224  16450   8578   1015  -1233   3280       C  
ATOM    683  O   GLU A  98      38.809 -40.735 281.454  1.00 93.42           O  
ANISOU  683  O   GLU A  98    10964  16230   8299   1220  -1313   3503       O  
ATOM    684  CB  GLU A  98      37.899 -43.130 280.399  1.00 77.33           C  
ANISOU  684  CB  GLU A  98     8669  14825   5888    985  -1507   3047       C  
ATOM    685  CG  GLU A  98      37.634 -44.340 279.513  1.00 98.74           C  
ANISOU  685  CG  GLU A  98    11318  17872   8326    847  -1616   2830       C  
ATOM    686  CD  GLU A  98      38.120 -44.143 278.089  1.00102.81           C  
ANISOU  686  CD  GLU A  98    11931  18614   8519    906  -1629   2971       C  
ATOM    687  OE1 GLU A  98      38.298 -42.979 277.674  1.00 95.45           O  
ANISOU  687  OE1 GLU A  98    11068  17645   7555   1074  -1597   3275       O  
ATOM    688  OE2 GLU A  98      38.321 -45.153 277.382  1.00108.91           O  
ANISOU  688  OE2 GLU A  98    12731  19587   9063    785  -1668   2774       O  
ATOM    689  N   LEU A  99      40.405 -41.743 282.674  1.00 95.00           N  
ANISOU  689  N   LEU A  99    11263  16074   8756    905  -1090   3211       N  
ATOM    690  CA  LEU A  99      40.549 -40.609 283.581  1.00 89.39           C  
ANISOU  690  CA  LEU A  99    10653  15015   8294    998  -1032   3373       C  
ATOM    691  C   LEU A  99      41.947 -39.994 283.549  1.00 89.92           C  
ANISOU  691  C   LEU A  99    10907  14846   8414    902   -888   3533       C  
ATOM    692  O   LEU A  99      42.532 -39.709 284.593  1.00 96.57           O  
ANISOU  692  O   LEU A  99    11827  15371   9494    834   -799   3504       O  
ATOM    693  CB  LEU A  99      40.204 -41.030 285.011  1.00 95.32           C  
ANISOU  693  CB  LEU A  99    11334  15579   9306    958  -1010   3156       C  
ATOM    694  CG  LEU A  99      38.816 -41.639 285.227  1.00 97.55           C  
ANISOU  694  CG  LEU A  99    11404  16097   9563   1013  -1138   3002       C  
ATOM    695  CD1 LEU A  99      38.566 -41.891 286.708  1.00 67.38           C  
ANISOU  695  CD1 LEU A  99     7532  12068   6002    979  -1090   2835       C  
ATOM    696  CD2 LEU A  99      37.736 -40.745 284.635  1.00 86.40           C  
ANISOU  696  CD2 LEU A  99     9920  14870   8037   1269  -1268   3214       C  
ATOM    697  N   GLY A 100      42.476 -39.788 282.349  1.00 86.57           N  
ANISOU  697  N   GLY A 100    10542  14597   7755    886   -869   3706       N  
ATOM    698  CA  GLY A 100      43.757 -39.123 282.193  1.00 94.17           C  
ANISOU  698  CA  GLY A 100    11655  15391   8735    777   -736   3904       C  
ATOM    699  C   GLY A 100      44.953 -39.976 282.570  1.00102.51           C  
ANISOU  699  C   GLY A 100    12687  16421   9840    571   -597   3716       C  
ATOM    700  O   GLY A 100      44.817 -41.160 282.881  1.00100.55           O  
ANISOU  700  O   GLY A 100    12336  16273   9593    522   -604   3423       O  
ATOM    701  N   THR A 101      46.133 -39.364 282.551  1.00109.40           N  
ANISOU  701  N   THR A 101    13658  17161  10747    449   -474   3894       N  
ATOM    702  CA  THR A 101      47.379 -40.084 282.785  1.00103.85           C  
ANISOU  702  CA  THR A 101    12912  16492  10055    276   -335   3757       C  
ATOM    703  C   THR A 101      47.871 -39.935 284.223  1.00106.12           C  
ANISOU  703  C   THR A 101    13228  16435  10657    175   -277   3659       C  
ATOM    704  O   THR A 101      48.346 -40.896 284.829  1.00102.08           O  
ANISOU  704  O   THR A 101    12642  15931  10211    103   -220   3411       O  
ATOM    705  CB  THR A 101      48.487 -39.600 281.828  1.00 98.46           C  
ANISOU  705  CB  THR A 101    12268  15960   9181    175   -222   4012       C  
ATOM    706  OG1 THR A 101      47.980 -39.556 280.489  1.00108.41           O  
ANISOU  706  OG1 THR A 101    13528  17525  10138    286   -282   4143       O  
ATOM    707  CG2 THR A 101      49.687 -40.532 281.881  1.00 90.29           C  
ANISOU  707  CG2 THR A 101    11139  15079   8088     52    -82   3844       C  
ATOM    708  N   THR A 102      47.758 -38.726 284.763  1.00112.80           N  
ANISOU  708  N   THR A 102    14204  16972  11684    181   -301   3853       N  
ATOM    709  CA  THR A 102      48.240 -38.443 286.111  1.00116.91           C  
ANISOU  709  CA  THR A 102    14778  17154  12488     82   -259   3778       C  
ATOM    710  C   THR A 102      47.433 -39.196 287.163  1.00112.35           C  
ANISOU  710  C   THR A 102    14127  16493  12069    169   -313   3482       C  
ATOM    711  O   THR A 102      47.984 -39.670 288.156  1.00115.44           O  
ANISOU  711  O   THR A 102    14491  16754  12617     73   -256   3303       O  
ATOM    712  CB  THR A 102      48.190 -36.937 286.424  1.00130.68           C  
ANISOU  712  CB  THR A 102    16726  18553  14372     86   -293   4042       C  
ATOM    713  OG1 THR A 102      46.832 -36.482 286.388  1.00144.45           O  
ANISOU  713  OG1 THR A 102    18525  20236  16124    327   -419   4084       O  
ATOM    714  CG2 THR A 102      49.010 -36.155 285.408  1.00133.15           C  
ANISOU  714  CG2 THR A 102    17131  18931  14531    -42   -237   4366       C  
ATOM    715  N   PHE A 103      46.127 -39.311 286.940  1.00114.57           N  
ANISOU  715  N   PHE A 103    14364  16873  12295    347   -425   3441       N  
ATOM    716  CA  PHE A 103      45.255 -40.010 287.877  1.00116.24           C  
ANISOU  716  CA  PHE A 103    14484  17049  12634    416   -477   3187       C  
ATOM    717  C   PHE A 103      45.515 -41.514 287.841  1.00115.22           C  
ANISOU  717  C   PHE A 103    14233  17122  12423    316   -443   2916       C  
ATOM    718  O   PHE A 103      45.198 -42.230 288.791  1.00120.18           O  
ANISOU  718  O   PHE A 103    14809  17676  13180    296   -448   2694       O  
ATOM    719  CB  PHE A 103      43.785 -39.720 287.568  1.00125.50           C  
ANISOU  719  CB  PHE A 103    15604  18336  13745    624   -609   3236       C  
ATOM    720  CG  PHE A 103      42.924 -39.582 288.793  1.00136.75           C  
ANISOU  720  CG  PHE A 103    17001  19585  15374    734   -649   3121       C  
ATOM    721  CD1 PHE A 103      42.526 -40.699 289.510  1.00134.30           C  
ANISOU  721  CD1 PHE A 103    16554  19349  15124    677   -649   2851       C  
ATOM    722  CD2 PHE A 103      42.507 -38.332 289.224  1.00142.54           C  
ANISOU  722  CD2 PHE A 103    17860  20078  16223    902   -685   3287       C  
ATOM    723  CE1 PHE A 103      41.733 -40.574 290.636  1.00127.28           C  
ANISOU  723  CE1 PHE A 103    15623  18335  14402    777   -672   2758       C  
ATOM    724  CE2 PHE A 103      41.712 -38.200 290.351  1.00139.16           C  
ANISOU  724  CE2 PHE A 103    17400  19516  15957   1035   -711   3175       C  
ATOM    725  CZ  PHE A 103      41.326 -39.323 291.057  1.00129.33           C  
ANISOU  725  CZ  PHE A 103    15987  18387  14765    968   -699   2915       C  
ATOM    726  N   CYS A 104      46.091 -41.987 286.741  1.00110.37           N  
ANISOU  726  N   CYS A 104    13595  16758  11581    263   -408   2939       N  
ATOM    727  CA  CYS A 104      46.451 -43.394 286.613  1.00100.76           C  
ANISOU  727  CA  CYS A 104    12314  15712  10260    192   -374   2684       C  
ATOM    728  C   CYS A 104      47.609 -43.741 287.539  1.00 84.24           C  
ANISOU  728  C   CYS A 104    10241  13448   8317     81   -257   2573       C  
ATOM    729  O   CYS A 104      47.651 -44.828 288.116  1.00 74.56           O  
ANISOU  729  O   CYS A 104     8991  12208   7132     50   -246   2323       O  
ATOM    730  CB  CYS A 104      46.818 -43.732 285.166  1.00105.54           C  
ANISOU  730  CB  CYS A 104    12907  16637  10555    199   -361   2741       C  
ATOM    731  SG  CYS A 104      47.525 -45.382 284.934  1.00 86.69           S  
ANISOU  731  SG  CYS A 104    10501  14429   8009    145   -301   2435       S  
ATOM    732  N   LYS A 105      48.548 -42.811 287.674  1.00 83.09           N  
ANISOU  732  N   LYS A 105    10147  13176   8248     13   -176   2768       N  
ATOM    733  CA  LYS A 105      49.710 -43.014 288.530  1.00 87.70           C  
ANISOU  733  CA  LYS A 105    10726  13630   8966   -100    -74   2690       C  
ATOM    734  C   LYS A 105      49.320 -42.988 290.005  1.00 84.33           C  
ANISOU  734  C   LYS A 105    10328  12909   8805   -100   -104   2555       C  
ATOM    735  O   LYS A 105      49.761 -43.832 290.785  1.00 75.60           O  
ANISOU  735  O   LYS A 105     9194  11756   7774   -139    -62   2352       O  
ATOM    736  CB  LYS A 105      50.774 -41.951 288.251  1.00 87.72           C  
ANISOU  736  CB  LYS A 105    10764  13596   8971   -214      5   2956       C  
ATOM    737  CG  LYS A 105      51.388 -42.014 286.860  1.00 86.33           C  
ANISOU  737  CG  LYS A 105    10540  13743   8516   -233     70   3100       C  
ATOM    738  CD  LYS A 105      52.404 -40.896 286.666  1.00 91.59           C  
ANISOU  738  CD  LYS A 105    11235  14366   9199   -390    149   3391       C  
ATOM    739  CE  LYS A 105      52.983 -40.894 285.260  1.00 91.64           C  
ANISOU  739  CE  LYS A 105    11185  14725   8908   -409    226   3565       C  
ATOM    740  NZ  LYS A 105      53.795 -42.110 284.990  1.00 89.37           N  
ANISOU  740  NZ  LYS A 105    10764  14737   8458   -383    326   3368       N  
ATOM    741  N   LEU A 106      48.493 -42.016 290.378  1.00 85.28           N  
ANISOU  741  N   LEU A 106    10514  12839   9050    -35   -176   2671       N  
ATOM    742  CA  LEU A 106      48.065 -41.853 291.763  1.00 94.87           C  
ANISOU  742  CA  LEU A 106    11764  13785  10496    -10   -201   2560       C  
ATOM    743  C   LEU A 106      47.220 -43.025 292.246  1.00 93.94           C  
ANISOU  743  C   LEU A 106    11563  13741  10387     41   -239   2307       C  
ATOM    744  O   LEU A 106      47.439 -43.548 293.340  1.00 98.41           O  
ANISOU  744  O   LEU A 106    12129  14174  11087      0   -208   2138       O  
ATOM    745  CB  LEU A 106      47.281 -40.551 291.929  1.00 99.83           C  
ANISOU  745  CB  LEU A 106    12494  14219  11217    101   -272   2740       C  
ATOM    746  CG  LEU A 106      48.089 -39.260 291.806  1.00108.35           C  
ANISOU  746  CG  LEU A 106    13720  15100  12348     19   -247   2987       C  
ATOM    747  CD1 LEU A 106      47.187 -38.050 291.983  1.00110.15           C  
ANISOU  747  CD1 LEU A 106    14092  15106  12655    178   -331   3140       C  
ATOM    748  CD2 LEU A 106      49.215 -39.247 292.826  1.00108.10           C  
ANISOU  748  CD2 LEU A 106    13720  14878  12473   -147   -179   2911       C  
ATOM    749  N   HIS A 107      46.252 -43.426 291.429  1.00 87.34           N  
ANISOU  749  N   HIS A 107    10661  13123   9400    116   -313   2289       N  
ATOM    750  CA  HIS A 107      45.362 -44.528 291.773  1.00 78.19           C  
ANISOU  750  CA  HIS A 107     9422  12056   8230    122   -365   2069       C  
ATOM    751  C   HIS A 107      46.133 -45.823 292.000  1.00 78.84           C  
ANISOU  751  C   HIS A 107     9514  12164   8278     17   -305   1855       C  
ATOM    752  O   HIS A 107      45.820 -46.595 292.907  1.00 80.82           O  
ANISOU  752  O   HIS A 107     9756  12330   8620    -19   -308   1673       O  
ATOM    753  CB  HIS A 107      44.315 -44.734 290.678  1.00 66.21           C  
ANISOU  753  CB  HIS A 107     7826  10810   6520    184   -468   2098       C  
ATOM    754  CG  HIS A 107      43.561 -46.021 290.802  1.00 71.46           C  
ANISOU  754  CG  HIS A 107     8415  11609   7129    123   -528   1870       C  
ATOM    755  ND1 HIS A 107      42.512 -46.187 291.680  1.00 71.75           N  
ANISOU  755  ND1 HIS A 107     8369  11609   7282    135   -576   1786       N  
ATOM    756  CD2 HIS A 107      43.711 -47.206 290.164  1.00 83.16           C  
ANISOU  756  CD2 HIS A 107     9905  13253   8441     37   -547   1708       C  
ATOM    757  CE1 HIS A 107      42.044 -47.419 291.574  1.00 78.06           C  
ANISOU  757  CE1 HIS A 107     9124  12540   7993     25   -627   1596       C  
ATOM    758  NE2 HIS A 107      42.754 -48.057 290.662  1.00 86.36           N  
ANISOU  758  NE2 HIS A 107    10249  13692   8872    -32   -617   1537       N  
ATOM    759  N   SER A 108      47.145 -46.054 291.171  1.00 75.57           N  
ANISOU  759  N   SER A 108     9122  11874   7716    -17   -246   1885       N  
ATOM    760  CA  SER A 108      47.953 -47.262 291.276  1.00 80.29           C  
ANISOU  760  CA  SER A 108     9744  12513   8251    -65   -187   1688       C  
ATOM    761  C   SER A 108      48.857 -47.216 292.506  1.00 76.53           C  
ANISOU  761  C   SER A 108     9295  11820   7964   -107   -106   1639       C  
ATOM    762  O   SER A 108      49.110 -48.241 293.138  1.00 62.57           O  
ANISOU  762  O   SER A 108     7556   9994   6222   -122    -84   1443       O  
ATOM    763  CB  SER A 108      48.794 -47.456 290.010  1.00 76.17           C  
ANISOU  763  CB  SER A 108     9223  12227   7492    -51   -136   1743       C  
ATOM    764  OG  SER A 108      47.975 -47.626 288.866  1.00 83.15           O  
ANISOU  764  OG  SER A 108    10094  13328   8173    -11   -221   1760       O  
ATOM    765  N   SER A 109      49.334 -46.019 292.838  1.00 50.56           N  
ANISOU  765  N   SER A 109     6011   8404   4797   -129    -72   1821       N  
ATOM    766  CA  SER A 109      50.243 -45.829 293.963  1.00 72.53           C  
ANISOU  766  CA  SER A 109     8811  10998   7747   -186    -11   1793       C  
ATOM    767  C   SER A 109      49.600 -46.205 295.298  1.00 75.64           C  
ANISOU  767  C   SER A 109     9234  11193   8311   -171    -42   1633       C  
ATOM    768  O   SER A 109      50.270 -46.719 296.194  1.00 60.26           O  
ANISOU  768  O   SER A 109     7302   9152   6443   -199      2   1512       O  
ATOM    769  CB  SER A 109      50.725 -44.379 294.015  1.00 66.56           C  
ANISOU  769  CB  SER A 109     8084  10122   7085   -244      4   2026       C  
ATOM    770  OG  SER A 109      51.515 -44.062 292.883  1.00 72.98           O  
ANISOU  770  OG  SER A 109     8862  11128   7738   -292     55   2190       O  
ATOM    771  N   ILE A 110      48.302 -45.944 295.419  1.00 67.96           N  
ANISOU  771  N   ILE A 110     8256  10184   7380   -116   -115   1642       N  
ATOM    772  CA  ILE A 110      47.559 -46.251 296.636  1.00 68.33           C  
ANISOU  772  CA  ILE A 110     8309  10086   7566    -98   -137   1512       C  
ATOM    773  C   ILE A 110      47.614 -47.740 296.965  1.00 82.81           C  
ANISOU  773  C   ILE A 110    10151  11959   9353   -143   -124   1295       C  
ATOM    774  O   ILE A 110      47.820 -48.123 298.118  1.00 90.81           O  
ANISOU  774  O   ILE A 110    11200  12824  10479   -161    -94   1186       O  
ATOM    775  CB  ILE A 110      46.087 -45.808 296.515  1.00 58.42           C  
ANISOU  775  CB  ILE A 110     7004   8877   6317    -15   -215   1567       C  
ATOM    776  CG1 ILE A 110      45.999 -44.283 296.433  1.00 53.20           C  
ANISOU  776  CG1 ILE A 110     6386   8101   5724     68   -233   1774       C  
ATOM    777  CG2 ILE A 110      45.267 -46.321 297.689  1.00 64.48           C  
ANISOU  777  CG2 ILE A 110     7744   9568   7188     -8   -225   1424       C  
ATOM    778  CD1 ILE A 110      44.582 -43.757 296.308  1.00 63.98           C  
ANISOU  778  CD1 ILE A 110     7696   9529   7083    206   -309   1842       C  
ATOM    779  N   PHE A 111      47.432 -48.572 295.944  1.00 72.78           N  
ANISOU  779  N   PHE A 111     8871  10877   7905   -157   -151   1233       N  
ATOM    780  CA  PHE A 111      47.490 -50.022 296.100  1.00 71.10           C  
ANISOU  780  CA  PHE A 111     8717  10676   7621   -199   -152   1027       C  
ATOM    781  C   PHE A 111      48.837 -50.469 296.663  1.00 73.85           C  
ANISOU  781  C   PHE A 111     9130  10930   7999   -187    -69    951       C  
ATOM    782  O   PHE A 111      48.898 -51.318 297.554  1.00 71.33           O  
ANISOU  782  O   PHE A 111     8880  10488   7733   -203    -58    807       O  
ATOM    783  CB  PHE A 111      47.222 -50.704 294.755  1.00 66.09           C  
ANISOU  783  CB  PHE A 111     8094  10253   6764   -207   -202    979       C  
ATOM    784  CG  PHE A 111      47.480 -52.186 294.755  1.00 53.90           C  
ANISOU  784  CG  PHE A 111     6669   8692   5117   -239   -205    764       C  
ATOM    785  CD1 PHE A 111      46.519 -53.070 295.216  1.00 51.80           C  
ANISOU  785  CD1 PHE A 111     6450   8364   4867   -333   -273    626       C  
ATOM    786  CD2 PHE A 111      48.678 -52.698 294.276  1.00 55.51           C  
ANISOU  786  CD2 PHE A 111     6945   8948   5197   -170   -142    704       C  
ATOM    787  CE1 PHE A 111      46.749 -54.436 295.212  1.00 50.08           C  
ANISOU  787  CE1 PHE A 111     6394   8084   4552   -370   -286    432       C  
ATOM    788  CE2 PHE A 111      48.916 -54.064 294.271  1.00 52.18           C  
ANISOU  788  CE2 PHE A 111     6674   8482   4669   -161   -151    499       C  
ATOM    789  CZ  PHE A 111      47.948 -54.933 294.739  1.00 50.17           C  
ANISOU  789  CZ  PHE A 111     6510   8114   4440   -266   -228    362       C  
ATOM    790  N   PHE A 112      49.914 -49.892 296.139  1.00 72.34           N  
ANISOU  790  N   PHE A 112     8907  10816   7762   -159    -12   1062       N  
ATOM    791  CA  PHE A 112      51.259 -50.243 296.578  1.00 81.11           C  
ANISOU  791  CA  PHE A 112    10033  11906   8880   -136     66   1010       C  
ATOM    792  C   PHE A 112      51.611 -49.584 297.908  1.00 76.78           C  
ANISOU  792  C   PHE A 112     9474  11162   8537   -168     86   1044       C  
ATOM    793  O   PHE A 112      52.413 -50.115 298.676  1.00 70.55           O  
ANISOU  793  O   PHE A 112     8708  10315   7784   -147    124    949       O  
ATOM    794  CB  PHE A 112      52.288 -49.855 295.515  1.00 74.26           C  
ANISOU  794  CB  PHE A 112     9099  11246   7871   -114    126   1130       C  
ATOM    795  CG  PHE A 112      52.168 -50.638 294.242  1.00 76.51           C  
ANISOU  795  CG  PHE A 112     9411  11741   7918    -54    118   1064       C  
ATOM    796  CD1 PHE A 112      52.653 -51.933 294.160  1.00 78.99           C  
ANISOU  796  CD1 PHE A 112     9807  12099   8105     32    142    872       C  
ATOM    797  CD2 PHE A 112      51.575 -50.076 293.124  1.00 77.16           C  
ANISOU  797  CD2 PHE A 112     9459  11970   7888    -65     80   1191       C  
ATOM    798  CE1 PHE A 112      52.544 -52.654 292.985  1.00 85.78           C  
ANISOU  798  CE1 PHE A 112    10727  13138   8729     98    127    791       C  
ATOM    799  CE2 PHE A 112      51.463 -50.791 291.949  1.00 73.17           C  
ANISOU  799  CE2 PHE A 112     8990  11668   7144     -9     64   1119       C  
ATOM    800  CZ  PHE A 112      51.947 -52.081 291.878  1.00 76.03           C  
ANISOU  800  CZ  PHE A 112     9445  12064   7378     70     87    911       C  
ATOM    801  N   LEU A 113      51.016 -48.424 298.171  1.00 70.84           N  
ANISOU  801  N   LEU A 113     8701  10310   7905   -201     53   1175       N  
ATOM    802  CA  LEU A 113      51.241 -47.726 299.430  1.00 66.63           C  
ANISOU  802  CA  LEU A 113     8187   9574   7555   -228     57   1194       C  
ATOM    803  C   LEU A 113      50.668 -48.540 300.582  1.00 64.99           C  
ANISOU  803  C   LEU A 113     8033   9238   7423   -205     45   1027       C  
ATOM    804  O   LEU A 113      51.306 -48.700 301.620  1.00 53.47           O  
ANISOU  804  O   LEU A 113     6603   7670   6045   -209     69    960       O  
ATOM    805  CB  LEU A 113      50.618 -46.331 299.402  1.00 67.23           C  
ANISOU  805  CB  LEU A 113     8273   9549   7723   -234     17   1357       C  
ATOM    806  CG  LEU A 113      50.926 -45.444 300.609  1.00 67.02           C  
ANISOU  806  CG  LEU A 113     8301   9294   7868   -261     12   1382       C  
ATOM    807  CD1 LEU A 113      52.429 -45.289 300.787  1.00 75.06           C  
ANISOU  807  CD1 LEU A 113     9297  10326   8897   -354     53   1411       C  
ATOM    808  CD2 LEU A 113      50.259 -44.085 300.461  1.00 60.10           C  
ANISOU  808  CD2 LEU A 113     7481   8295   7058   -232    -35   1538       C  
ATOM    809  N   ASN A 114      49.460 -49.057 300.383  1.00 67.76           N  
ANISOU  809  N   ASN A 114     8388   9622   7734   -194      4    970       N  
ATOM    810  CA  ASN A 114      48.823 -49.925 301.363  1.00 67.94           C  
ANISOU  810  CA  ASN A 114     8458   9554   7803   -205     -3    829       C  
ATOM    811  C   ASN A 114      49.588 -51.232 301.539  1.00 68.83           C  
ANISOU  811  C   ASN A 114     8652   9657   7841   -204     26    684       C  
ATOM    812  O   ASN A 114      49.601 -51.814 302.623  1.00 86.84           O  
ANISOU  812  O   ASN A 114    10999  11813  10182   -207     39    589       O  
ATOM    813  CB  ASN A 114      47.376 -50.217 300.957  1.00 74.09           C  
ANISOU  813  CB  ASN A 114     9196  10423   8534   -230    -59    816       C  
ATOM    814  CG  ASN A 114      46.719 -51.256 301.845  1.00 87.94           C  
ANISOU  814  CG  ASN A 114    10995  12111  10308   -286    -64    683       C  
ATOM    815  OD1 ASN A 114      46.257 -50.948 302.944  1.00 99.79           O  
ANISOU  815  OD1 ASN A 114    12480  13517  11917   -275    -48    682       O  
ATOM    816  ND2 ASN A 114      46.669 -52.496 301.370  1.00 85.88           N  
ANISOU  816  ND2 ASN A 114    10806  11896   9929   -350    -85    570       N  
ATOM    817  N   MET A 115      50.231 -51.686 300.469  1.00 56.86           N  
ANISOU  817  N   MET A 115     7145   8279   6182   -179     37    671       N  
ATOM    818  CA  MET A 115      50.963 -52.946 300.504  1.00 61.32           C  
ANISOU  818  CA  MET A 115     7810   8840   6648   -130     62    528       C  
ATOM    819  C   MET A 115      52.193 -52.861 301.403  1.00 70.84           C  
ANISOU  819  C   MET A 115     9012   9982   7922    -72    114    518       C  
ATOM    820  O   MET A 115      52.351 -53.660 302.326  1.00 63.89           O  
ANISOU  820  O   MET A 115     8228   8980   7067    -41    119    409       O  
ATOM    821  CB  MET A 115      51.379 -53.363 299.095  1.00 56.08           C  
ANISOU  821  CB  MET A 115     7154   8364   5791    -81     67    514       C  
ATOM    822  CG  MET A 115      52.060 -54.716 299.041  1.00 64.46           C  
ANISOU  822  CG  MET A 115     8354   9413   6723     13     86    349       C  
ATOM    823  SD  MET A 115      52.807 -55.033 297.437  1.00 90.65           S  
ANISOU  823  SD  MET A 115    11666  12984   9791    125    117    336       S  
ATOM    824  CE  MET A 115      53.812 -53.563 297.258  1.00 54.23           C  
ANISOU  824  CE  MET A 115     6833   8536   5237    124    191    555       C  
ATOM    825  N   PHE A 116      53.060 -51.891 301.128  1.00 71.77           N  
ANISOU  825  N   PHE A 116     9018  10193   8060    -71    146    642       N  
ATOM    826  CA  PHE A 116      54.275 -51.705 301.914  1.00 75.27           C  
ANISOU  826  CA  PHE A 116     9419  10624   8558    -42    183    647       C  
ATOM    827  C   PHE A 116      53.955 -51.353 303.363  1.00 78.37           C  
ANISOU  827  C   PHE A 116     9849  10813   9116    -80    158    625       C  
ATOM    828  O   PHE A 116      54.620 -51.826 304.284  1.00 78.07           O  
ANISOU  828  O   PHE A 116     9842  10721   9099    -30    169    548       O  
ATOM    829  CB  PHE A 116      55.157 -50.614 301.300  1.00 78.11           C  
ANISOU  829  CB  PHE A 116     9639  11131   8909    -93    212    809       C  
ATOM    830  CG  PHE A 116      55.913 -51.055 300.078  1.00 78.61           C  
ANISOU  830  CG  PHE A 116     9639  11448   8783    -24    264    824       C  
ATOM    831  CD1 PHE A 116      56.996 -51.912 300.188  1.00 76.83           C  
ANISOU  831  CD1 PHE A 116     9392  11344   8456     99    311    733       C  
ATOM    832  CD2 PHE A 116      55.553 -50.600 298.821  1.00 85.82           C  
ANISOU  832  CD2 PHE A 116    10513  12495   9601    -57    268    933       C  
ATOM    833  CE1 PHE A 116      57.697 -52.317 299.067  1.00 75.71           C  
ANISOU  833  CE1 PHE A 116     9187  11461   8117    197    369    740       C  
ATOM    834  CE2 PHE A 116      56.250 -50.998 297.697  1.00 88.45           C  
ANISOU  834  CE2 PHE A 116    10788  13083   9734     19    324    945       C  
ATOM    835  CZ  PHE A 116      57.323 -51.859 297.820  1.00 85.76           C  
ANISOU  835  CZ  PHE A 116    10422  12871   9291    151    379    844       C  
ATOM    836  N   ALA A 117      52.937 -50.520 303.554  1.00 74.40           N  
ANISOU  836  N   ALA A 117     9345  10212   8713   -144    126    692       N  
ATOM    837  CA  ALA A 117      52.548 -50.076 304.887  1.00 69.57           C  
ANISOU  837  CA  ALA A 117     8772   9421   8239   -160    108    671       C  
ATOM    838  C   ALA A 117      52.084 -51.244 305.750  1.00 76.61           C  
ANISOU  838  C   ALA A 117     9762  10225   9122   -125    111    533       C  
ATOM    839  O   ALA A 117      52.492 -51.370 306.903  1.00 83.02           O  
ANISOU  839  O   ALA A 117    10616  10940   9988   -102    116    480       O  
ATOM    840  CB  ALA A 117      51.457 -49.021 304.797  1.00 58.70           C  
ANISOU  840  CB  ALA A 117     7381   7981   6941   -187     77    764       C  
ATOM    841  N   SER A 118      51.234 -52.096 305.187  1.00 73.49           N  
ANISOU  841  N   SER A 118     9411   9865   8648   -137    101    481       N  
ATOM    842  CA  SER A 118      50.710 -53.245 305.918  1.00 67.36           C  
ANISOU  842  CA  SER A 118     8749   8993   7852   -145    100    368       C  
ATOM    843  C   SER A 118      51.817 -54.230 306.284  1.00 66.15           C  
ANISOU  843  C   SER A 118     8697   8804   7634    -63    120    276       C  
ATOM    844  O   SER A 118      51.795 -54.831 307.357  1.00 77.13           O  
ANISOU  844  O   SER A 118    10186  10072   9046    -46    126    213       O  
ATOM    845  CB  SER A 118      49.627 -53.953 305.099  1.00 64.92           C  
ANISOU  845  CB  SER A 118     8470   8740   7458   -216     69    335       C  
ATOM    846  OG  SER A 118      48.482 -53.128 304.946  1.00 58.78           O  
ANISOU  846  OG  SER A 118     7585   8013   6735   -269     46    417       O  
ATOM    847  N   GLY A 119      52.787 -54.386 305.390  1.00 64.36           N  
ANISOU  847  N   GLY A 119     8441   8700   7313      7    134    276       N  
ATOM    848  CA  GLY A 119      53.886 -55.305 305.616  1.00 72.16           C  
ANISOU  848  CA  GLY A 119     9508   9694   8216    136    155    192       C  
ATOM    849  C   GLY A 119      54.856 -54.817 306.675  1.00 70.56           C  
ANISOU  849  C   GLY A 119     9239   9480   8089    184    166    215       C  
ATOM    850  O   GLY A 119      55.471 -55.617 307.382  1.00 58.30           O  
ANISOU  850  O   GLY A 119     7776   7879   6497    292    170    140       O  
ATOM    851  N   PHE A 120      54.994 -53.500 306.786  1.00 74.23           N  
ANISOU  851  N   PHE A 120     9564   9984   8655    104    161    321       N  
ATOM    852  CA  PHE A 120      55.902 -52.904 307.759  1.00 76.22           C  
ANISOU  852  CA  PHE A 120     9750  10232   8979    109    152    343       C  
ATOM    853  C   PHE A 120      55.270 -52.849 309.148  1.00 77.14           C  
ANISOU  853  C   PHE A 120     9958  10162   9188     88    130    299       C  
ATOM    854  O   PHE A 120      55.956 -53.005 310.158  1.00 77.82           O  
ANISOU  854  O   PHE A 120    10062  10221   9284    140    117    259       O  
ATOM    855  CB  PHE A 120      56.316 -51.499 307.315  1.00 73.90           C  
ANISOU  855  CB  PHE A 120     9307  10023   8748      2    144    472       C  
ATOM    856  CG  PHE A 120      57.164 -51.478 306.073  1.00 76.40           C  
ANISOU  856  CG  PHE A 120     9503  10567   8958     17    179    537       C  
ATOM    857  CD1 PHE A 120      57.846 -52.612 305.662  1.00 76.11           C  
ANISOU  857  CD1 PHE A 120     9472  10668   8776    165    214    459       C  
ATOM    858  CD2 PHE A 120      57.283 -50.321 305.321  1.00 83.35           C  
ANISOU  858  CD2 PHE A 120    10277  11526   9868   -103    180    680       C  
ATOM    859  CE1 PHE A 120      58.626 -52.593 304.523  1.00 74.36           C  
ANISOU  859  CE1 PHE A 120     9127  10692   8433    203    259    516       C  
ATOM    860  CE2 PHE A 120      58.063 -50.295 304.181  1.00 87.87           C  
ANISOU  860  CE2 PHE A 120    10727  12337  10323    -97    224    756       C  
ATOM    861  CZ  PHE A 120      58.735 -51.433 303.782  1.00 82.26           C  
ANISOU  861  CZ  PHE A 120     9998  11798   9460     61    268    670       C  
ATOM    862  N   LEU A 121      53.960 -52.626 309.190  1.00 71.54           N  
ANISOU  862  N   LEU A 121     9294   9355   8532     20    127    312       N  
ATOM    863  CA  LEU A 121      53.241 -52.528 310.455  1.00 66.77           C  
ANISOU  863  CA  LEU A 121     8762   8610   7999      7    121    280       C  
ATOM    864  C   LEU A 121      53.131 -53.883 311.145  1.00 68.32           C  
ANISOU  864  C   LEU A 121     9099   8732   8128     62    135    191       C  
ATOM    865  O   LEU A 121      53.235 -53.970 312.367  1.00 70.67           O  
ANISOU  865  O   LEU A 121     9457   8948   8447     93    134    159       O  
ATOM    866  CB  LEU A 121      51.847 -51.936 310.239  1.00 60.12           C  
ANISOU  866  CB  LEU A 121     7896   7736   7210    -57    123    327       C  
ATOM    867  CG  LEU A 121      51.797 -50.444 309.903  1.00 55.86           C  
ANISOU  867  CG  LEU A 121     7271   7200   6752    -87    101    422       C  
ATOM    868  CD1 LEU A 121      50.361 -49.975 309.742  1.00 62.86           C  
ANISOU  868  CD1 LEU A 121     8137   8075   7671    -96    101    463       C  
ATOM    869  CD2 LEU A 121      52.511 -49.631 310.970  1.00 49.94           C  
ANISOU  869  CD2 LEU A 121     6539   6361   6074    -81     77    415       C  
ATOM    870  N   LEU A 122      52.923 -54.938 310.363  1.00 61.77           N  
ANISOU  870  N   LEU A 122     8346   7919   7206     71    143    152       N  
ATOM    871  CA  LEU A 122      52.850 -56.285 310.919  1.00 64.08           C  
ANISOU  871  CA  LEU A 122     8821   8102   7424    113    148     75       C  
ATOM    872  C   LEU A 122      54.203 -56.707 311.475  1.00 75.81           C  
ANISOU  872  C   LEU A 122    10350   9596   8859    267    143     35       C  
ATOM    873  O   LEU A 122      54.280 -57.521 312.396  1.00 90.12           O  
ANISOU  873  O   LEU A 122    12312  11296  10633    327    142     -7       O  
ATOM    874  CB  LEU A 122      52.376 -57.286 309.865  1.00 66.36           C  
ANISOU  874  CB  LEU A 122     9216   8383   7614     81    140     30       C  
ATOM    875  CG  LEU A 122      50.913 -57.165 309.436  1.00 72.29           C  
ANISOU  875  CG  LEU A 122     9938   9138   8390    -85    131     59       C  
ATOM    876  CD1 LEU A 122      50.562 -58.241 308.423  1.00 76.07           C  
ANISOU  876  CD1 LEU A 122    10549   9601   8754   -133    102     -6       C  
ATOM    877  CD2 LEU A 122      49.989 -57.237 310.643  1.00 65.64           C  
ANISOU  877  CD2 LEU A 122     9133   8204   7604   -171    148     75       C  
ATOM    878  N   SER A 123      55.267 -56.149 310.907  1.00 71.35           N  
ANISOU  878  N   SER A 123     9643   9183   8283    330    140     61       N  
ATOM    879  CA  SER A 123      56.615 -56.388 311.404  1.00 78.01           C  
ANISOU  879  CA  SER A 123    10461  10104   9076    478    130     36       C  
ATOM    880  C   SER A 123      56.830 -55.646 312.717  1.00 74.71           C  
ANISOU  880  C   SER A 123     9994   9650   8743    447    102     55       C  
ATOM    881  O   SER A 123      57.394 -56.193 313.664  1.00 83.40           O  
ANISOU  881  O   SER A 123    11167  10723   9799    558     84     15       O  
ATOM    882  CB  SER A 123      57.660 -55.955 310.372  1.00 80.65           C  
ANISOU  882  CB  SER A 123    10616  10665   9363    525    140     74       C  
ATOM    883  OG  SER A 123      57.564 -56.731 309.191  1.00 82.67           O  
ANISOU  883  OG  SER A 123    10936  10969   9507    593    166     38       O  
ATOM    884  N   ALA A 124      56.370 -54.399 312.764  1.00 71.40           N  
ANISOU  884  N   ALA A 124     9472   9224   8433    310     93    112       N  
ATOM    885  CA  ALA A 124      56.505 -53.566 313.954  1.00 71.55           C  
ANISOU  885  CA  ALA A 124     9468   9192   8527    272     58    115       C  
ATOM    886  C   ALA A 124      55.739 -54.158 315.131  1.00 78.14           C  
ANISOU  886  C   ALA A 124    10461   9878   9351    303     68     68       C  
ATOM    887  O   ALA A 124      56.197 -54.104 316.271  1.00 82.06           O  
ANISOU  887  O   ALA A 124    10990  10353   9836    353     38     38       O  
ATOM    888  CB  ALA A 124      56.025 -52.152 313.667  1.00 57.19           C  
ANISOU  888  CB  ALA A 124     7562   7352   6817    139     44    180       C  
ATOM    889  N   ILE A 125      54.571 -54.724 314.845  1.00 68.53           N  
ANISOU  889  N   ILE A 125     9336   8579   8124    259    108     68       N  
ATOM    890  CA  ILE A 125      53.739 -55.335 315.873  1.00 57.15           C  
ANISOU  890  CA  ILE A 125     8035   7019   6660    254    133     46       C  
ATOM    891  C   ILE A 125      54.431 -56.538 316.508  1.00 64.44           C  
ANISOU  891  C   ILE A 125     9110   7894   7482    376    124      5       C  
ATOM    892  O   ILE A 125      54.453 -56.678 317.732  1.00 75.55           O  
ANISOU  892  O   ILE A 125    10596   9244   8864    417    121     -6       O  
ATOM    893  CB  ILE A 125      52.372 -55.772 315.301  1.00 46.80           C  
ANISOU  893  CB  ILE A 125     6765   5669   5348    146    171     67       C  
ATOM    894  CG1 ILE A 125      51.539 -54.545 314.928  1.00 42.44           C  
ANISOU  894  CG1 ILE A 125     6070   5167   4886     66    179    115       C  
ATOM    895  CG2 ILE A 125      51.616 -56.631 316.302  1.00 41.65           C  
ANISOU  895  CG2 ILE A 125     6263   4916   4648    117    204     60       C  
ATOM    896  CD1 ILE A 125      50.149 -54.876 314.434  1.00 44.65           C  
ANISOU  896  CD1 ILE A 125     6343   5462   5159    -40    208    142       C  
ATOM    897  N   SER A 126      55.005 -57.399 315.674  1.00 67.41           N  
ANISOU  897  N   SER A 126     9537   8291   7783    455    120    -18       N  
ATOM    898  CA  SER A 126      55.678 -58.599 316.158  1.00 78.80           C  
ANISOU  898  CA  SER A 126    11154   9672   9115    612    107    -56       C  
ATOM    899  C   SER A 126      56.939 -58.259 316.947  1.00 81.85           C  
ANISOU  899  C   SER A 126    11456  10165   9478    753     64    -65       C  
ATOM    900  O   SER A 126      57.281 -58.947 317.908  1.00 69.95           O  
ANISOU  900  O   SER A 126    10085   8596   7896    873     46    -79       O  
ATOM    901  CB  SER A 126      56.026 -59.525 314.991  1.00 73.65           C  
ANISOU  901  CB  SER A 126    10586   9023   8375    700    109    -94       C  
ATOM    902  OG  SER A 126      54.854 -59.993 314.347  1.00 89.63           O  
ANISOU  902  OG  SER A 126    12720  10937  10399    555    129    -97       O  
ATOM    903  N   LEU A 127      57.627 -57.198 316.537  1.00 81.01           N  
ANISOU  903  N   LEU A 127    11126  10226   9429    725     40    -49       N  
ATOM    904  CA  LEU A 127      58.847 -56.776 317.215  1.00 72.47           C  
ANISOU  904  CA  LEU A 127     9925   9285   8326    814    -16    -55       C  
ATOM    905  C   LEU A 127      58.543 -56.063 318.530  1.00 83.50           C  
ANISOU  905  C   LEU A 127    11336  10617   9772    742    -49    -60       C  
ATOM    906  O   LEU A 127      59.328 -56.131 319.477  1.00 81.98           O  
ANISOU  906  O   LEU A 127    11139  10487   9524    839   -103    -82       O  
ATOM    907  CB  LEU A 127      59.680 -55.871 316.305  1.00 58.89           C  
ANISOU  907  CB  LEU A 127     7960   7773   6644    760    -33    -22       C  
ATOM    908  CG  LEU A 127      60.392 -56.565 315.142  1.00 69.21           C  
ANISOU  908  CG  LEU A 127     9213   9229   7856    893     -5    -25       C  
ATOM    909  CD1 LEU A 127      61.222 -55.570 314.344  1.00 70.57           C  
ANISOU  909  CD1 LEU A 127     9117   9640   8057    809    -13     33       C  
ATOM    910  CD2 LEU A 127      61.260 -57.707 315.652  1.00 62.60           C  
ANISOU  910  CD2 LEU A 127     8463   8441   6882   1152    -25    -71       C  
ATOM    911  N   ASP A 128      57.404 -55.380 318.585  1.00 81.19           N  
ANISOU  911  N   ASP A 128    11059  10219   9569    593    -18    -44       N  
ATOM    912  CA  ASP A 128      56.984 -54.698 319.804  1.00 79.79           C  
ANISOU  912  CA  ASP A 128    10919   9977   9422    549    -37    -61       C  
ATOM    913  C   ASP A 128      56.654 -55.711 320.895  1.00 83.17           C  
ANISOU  913  C   ASP A 128    11535  10312   9752    643    -17    -75       C  
ATOM    914  O   ASP A 128      56.968 -55.501 322.066  1.00 85.76           O  
ANISOU  914  O   ASP A 128    11898  10649  10037    694    -56   -101       O  
ATOM    915  CB  ASP A 128      55.778 -53.799 319.532  1.00 84.85           C  
ANISOU  915  CB  ASP A 128    11535  10543  10162    416      2    -39       C  
ATOM    916  CG  ASP A 128      55.273 -53.107 320.781  1.00 88.93           C  
ANISOU  916  CG  ASP A 128    12108  10995  10688    407     -7    -70       C  
ATOM    917  OD1 ASP A 128      54.229 -53.535 321.316  1.00 88.82           O  
ANISOU  917  OD1 ASP A 128    12192  10914  10641    412     56    -64       O  
ATOM    918  OD2 ASP A 128      55.923 -52.139 321.231  1.00 89.50           O  
ANISOU  918  OD2 ASP A 128    12126  11091  10788    389    -78   -102       O  
ATOM    919  N   ARG A 129      56.022 -56.811 320.498  1.00 83.69           N  
ANISOU  919  N   ARG A 129    11737  10287   9775    652     40    -54       N  
ATOM    920  CA  ARG A 129      55.710 -57.902 321.414  1.00 71.62           C  
ANISOU  920  CA  ARG A 129    10420   8649   8145    719     63    -42       C  
ATOM    921  C   ARG A 129      56.983 -58.604 321.866  1.00 70.17           C  
ANISOU  921  C   ARG A 129    10301   8509   7854    921      4    -60       C  
ATOM    922  O   ARG A 129      57.113 -58.993 323.027  1.00 84.42           O  
ANISOU  922  O   ARG A 129    12228  10277   9572   1006    -12    -53       O  
ATOM    923  CB  ARG A 129      54.766 -58.908 320.750  1.00 68.83           C  
ANISOU  923  CB  ARG A 129    10211   8170   7772    641    122    -13       C  
ATOM    924  CG  ARG A 129      54.388 -60.100 321.622  1.00 67.95           C  
ANISOU  924  CG  ARG A 129    10352   7912   7552    669    148     21       C  
ATOM    925  CD  ARG A 129      53.127 -59.827 322.429  1.00 72.38           C  
ANISOU  925  CD  ARG A 129    10929   8446   8124    521    213     68       C  
ATOM    926  NE  ARG A 129      52.677 -61.006 323.163  1.00 88.24           N  
ANISOU  926  NE  ARG A 129    13185  10317  10024    500    248    127       N  
ATOM    927  CZ  ARG A 129      52.914 -61.222 324.453  1.00 90.95           C  
ANISOU  927  CZ  ARG A 129    13639  10644  10273    590    249    157       C  
ATOM    928  NH1 ARG A 129      53.595 -60.332 325.162  1.00 84.41           N  
ANISOU  928  NH1 ARG A 129    12692   9936   9445    706    207    113       N  
ATOM    929  NH2 ARG A 129      52.466 -62.325 325.037  1.00 86.64           N  
ANISOU  929  NH2 ARG A 129    13337   9960   9624    549    285    233       N  
ATOM    930  N   CYS A 130      57.920 -58.762 320.937  1.00 62.55           N  
ANISOU  930  N   CYS A 130     9243   7645   6878   1013    -26    -79       N  
ATOM    931  CA  CYS A 130      59.176 -59.449 321.216  1.00 69.30           C  
ANISOU  931  CA  CYS A 130    10126   8587   7618   1244    -81    -95       C  
ATOM    932  C   CYS A 130      60.004 -58.706 322.263  1.00 73.38           C  
ANISOU  932  C   CYS A 130    10510   9254   8115   1290   -159   -109       C  
ATOM    933  O   CYS A 130      60.551 -59.319 323.176  1.00 61.05           O  
ANISOU  933  O   CYS A 130     9050   7706   6439   1461   -203   -109       O  
ATOM    934  CB  CYS A 130      59.986 -59.622 319.930  1.00 60.04           C  
ANISOU  934  CB  CYS A 130     8831   7552   6430   1338    -85   -112       C  
ATOM    935  SG  CYS A 130      61.489 -60.613 320.113  1.00 82.63           S  
ANISOU  935  SG  CYS A 130    11719  10553   9123   1686   -140   -131       S  
ATOM    936  N   LEU A 131      60.090 -57.386 322.128  1.00 76.30           N  
ANISOU  936  N   LEU A 131    10672   9728   8589   1135   -186   -122       N  
ATOM    937  CA  LEU A 131      60.830 -56.571 323.085  1.00 80.31           C  
ANISOU  937  CA  LEU A 131    11065  10365   9084   1129   -278   -150       C  
ATOM    938  C   LEU A 131      60.158 -56.582 324.457  1.00 85.19           C  
ANISOU  938  C   LEU A 131    11853  10862   9656   1128   -279   -164       C  
ATOM    939  O   LEU A 131      60.828 -56.485 325.485  1.00 78.28           O  
ANISOU  939  O   LEU A 131    10972  10075   8695   1211   -360   -191       O  
ATOM    940  CB  LEU A 131      60.967 -55.131 322.580  1.00 76.58           C  
ANISOU  940  CB  LEU A 131    10385   9974   8737    929   -310   -158       C  
ATOM    941  CG  LEU A 131      61.942 -54.891 321.426  1.00 83.03           C  
ANISOU  941  CG  LEU A 131    10979  10993   9577    912   -329   -131       C  
ATOM    942  CD1 LEU A 131      61.924 -53.430 321.001  1.00 91.94           C  
ANISOU  942  CD1 LEU A 131    11954  12148  10830    676   -359   -117       C  
ATOM    943  CD2 LEU A 131      63.348 -55.317 321.818  1.00 79.49           C  
ANISOU  943  CD2 LEU A 131    10408  10785   9010   1080   -409   -141       C  
ATOM    944  N   GLN A 132      58.834 -56.709 324.460  1.00 84.34           N  
ANISOU  944  N   GLN A 132    11880  10578   9588   1035   -188   -142       N  
ATOM    945  CA  GLN A 132      58.051 -56.709 325.692  1.00 75.38           C  
ANISOU  945  CA  GLN A 132    10893   9351   8397   1026   -161   -143       C  
ATOM    946  C   GLN A 132      58.331 -57.951 326.537  1.00 73.76           C  
ANISOU  946  C   GLN A 132    10883   9109   8036   1198   -167   -108       C  
ATOM    947  O   GLN A 132      58.264 -57.905 327.765  1.00 74.52           O  
ANISOU  947  O   GLN A 132    11067   9209   8038   1246   -187   -113       O  
ATOM    948  CB  GLN A 132      56.557 -56.619 325.365  1.00 69.25           C  
ANISOU  948  CB  GLN A 132    10173   8448   7690    884    -53   -110       C  
ATOM    949  CG  GLN A 132      55.642 -56.460 326.569  1.00 67.80           C  
ANISOU  949  CG  GLN A 132    10098   8216   7447    865     -3   -105       C  
ATOM    950  CD  GLN A 132      54.175 -56.395 326.180  1.00 77.78           C  
ANISOU  950  CD  GLN A 132    11369   9414   8770    731    107    -63       C  
ATOM    951  OE1 GLN A 132      53.791 -56.815 325.088  1.00 93.18           O  
ANISOU  951  OE1 GLN A 132    13298  11324  10782    655    145    -28       O  
ATOM    952  NE2 GLN A 132      53.349 -55.862 327.072  1.00 73.68           N  
ANISOU  952  NE2 GLN A 132    10870   8908   8218    713    157    -70       N  
ATOM    953  N   VAL A 133      58.653 -59.056 325.871  1.00 71.87           N  
ANISOU  953  N   VAL A 133    10730   8823   7753   1304   -153    -74       N  
ATOM    954  CA  VAL A 133      58.895 -60.323 326.553  1.00 66.88           C  
ANISOU  954  CA  VAL A 133    10333   8110   6970   1484   -159    -28       C  
ATOM    955  C   VAL A 133      60.387 -60.608 326.744  1.00 77.91           C  
ANISOU  955  C   VAL A 133    11663   9672   8267   1726   -264    -50       C  
ATOM    956  O   VAL A 133      60.817 -61.013 327.824  1.00 80.27           O  
ANISOU  956  O   VAL A 133    12068   9998   8432   1880   -316    -30       O  
ATOM    957  CB  VAL A 133      58.257 -61.499 325.783  1.00 59.22           C  
ANISOU  957  CB  VAL A 133     9572   6940   5989   1470    -86     20       C  
ATOM    958  CG1 VAL A 133      58.515 -62.812 326.501  1.00 59.18           C  
ANISOU  958  CG1 VAL A 133     9859   6804   5821   1658   -100     78       C  
ATOM    959  CG2 VAL A 133      56.766 -61.270 325.611  1.00 54.54           C  
ANISOU  959  CG2 VAL A 133     9012   6230   5480   1219     11     51       C  
ATOM    960  N   VAL A 134      61.173 -60.394 325.693  1.00 82.70           N  
ANISOU  960  N   VAL A 134    12077  10418   8925   1767   -293    -82       N  
ATOM    961  CA  VAL A 134      62.597 -60.716 325.724  1.00 75.38           C  
ANISOU  961  CA  VAL A 134    11043   9702   7894   2013   -383    -95       C  
ATOM    962  C   VAL A 134      63.383 -59.746 326.603  1.00 65.39           C  
ANISOU  962  C   VAL A 134     9567   8668   6608   1994   -492   -130       C  
ATOM    963  O   VAL A 134      64.301 -60.150 327.317  1.00 64.35           O  
ANISOU  963  O   VAL A 134     9427   8683   6338   2207   -579   -126       O  
ATOM    964  CB  VAL A 134      63.199 -60.725 324.303  1.00 77.18           C  
ANISOU  964  CB  VAL A 134    11095  10060   8168   2055   -368   -113       C  
ATOM    965  CG1 VAL A 134      64.707 -60.929 324.352  1.00 87.52           C  
ANISOU  965  CG1 VAL A 134    12227  11664   9363   2312   -456   -123       C  
ATOM    966  CG2 VAL A 134      62.543 -61.809 323.464  1.00 80.71           C  
ANISOU  966  CG2 VAL A 134    11786  10278   8601   2108   -283    -98       C  
ATOM    967  N   ARG A 135      63.021 -58.469 326.559  1.00 66.30           N  
ANISOU  967  N   ARG A 135     9529   8812   6850   1742   -498   -167       N  
ATOM    968  CA  ARG A 135      63.726 -57.464 327.348  1.00 68.89           C  
ANISOU  968  CA  ARG A 135     9684   9330   7163   1678   -617   -216       C  
ATOM    969  C   ARG A 135      62.772 -56.654 328.223  1.00 67.11           C  
ANISOU  969  C   ARG A 135     9560   8961   6976   1507   -607   -254       C  
ATOM    970  O   ARG A 135      62.467 -55.500 327.918  1.00 61.50           O  
ANISOU  970  O   ARG A 135     8743   8233   6390   1297   -612   -293       O  
ATOM    971  CB  ARG A 135      64.522 -56.537 326.428  1.00 76.74           C  
ANISOU  971  CB  ARG A 135    10371  10533   8255   1543   -667   -235       C  
ATOM    972  CG  ARG A 135      65.467 -57.279 325.499  1.00 81.42           C  
ANISOU  972  CG  ARG A 135    10828  11316   8793   1728   -660   -200       C  
ATOM    973  CD  ARG A 135      66.485 -56.345 324.881  1.00 88.95           C  
ANISOU  973  CD  ARG A 135    11437  12563   9797   1598   -729   -203       C  
ATOM    974  NE  ARG A 135      67.339 -55.731 325.891  1.00 90.10           N  
ANISOU  974  NE  ARG A 135    11435  12920   9879   1557   -877   -238       N  
ATOM    975  CZ  ARG A 135      68.408 -56.317 326.420  1.00101.62           C  
ANISOU  975  CZ  ARG A 135    12791  14640  11182   1788   -967   -233       C  
ATOM    976  NH1 ARG A 135      68.752 -57.541 326.041  1.00104.34           N  
ANISOU  976  NH1 ARG A 135    13187  15041  11418   2104   -917   -196       N  
ATOM    977  NH2 ARG A 135      69.132 -55.683 327.333  1.00104.88           N  
ANISOU  977  NH2 ARG A 135    13058  15255  11535   1714  -1116   -271       N  
ATOM    978  N   PRO A 136      62.317 -57.259 329.331  1.00 67.17           N  
ANISOU  978  N   PRO A 136     9788   8872   6862   1614   -591   -237       N  
ATOM    979  CA  PRO A 136      61.302 -56.691 330.227  1.00 71.57           C  
ANISOU  979  CA  PRO A 136    10472   9306   7415   1504   -553   -265       C  
ATOM    980  C   PRO A 136      61.727 -55.374 330.871  1.00 69.41           C  
ANISOU  980  C   PRO A 136    10077   9146   7151   1395   -670   -364       C  
ATOM    981  O   PRO A 136      60.925 -54.442 330.940  1.00 66.48           O  
ANISOU  981  O   PRO A 136     9726   8671   6862   1244   -635   -412       O  
ATOM    982  CB  PRO A 136      61.132 -57.776 331.301  1.00 74.67           C  
ANISOU  982  CB  PRO A 136    11101   9646   7626   1685   -535   -207       C  
ATOM    983  CG  PRO A 136      61.705 -59.015 330.704  1.00 75.40           C  
ANISOU  983  CG  PRO A 136    11249   9732   7667   1869   -528   -138       C  
ATOM    984  CD  PRO A 136      62.813 -58.555 329.823  1.00 72.11           C  
ANISOU  984  CD  PRO A 136    10562   9515   7320   1877   -610   -181       C  
ATOM    985  N   VAL A 137      62.969 -55.307 331.342  1.00 59.71           N  
ANISOU  985  N   VAL A 137     8733   8128   5828   1478   -815   -397       N  
ATOM    986  CA  VAL A 137      63.455 -54.127 332.047  1.00 65.26           C  
ANISOU  986  CA  VAL A 137     9345   8937   6514   1357   -954   -501       C  
ATOM    987  C   VAL A 137      63.448 -52.891 331.149  1.00 69.24           C  
ANISOU  987  C   VAL A 137     9693   9412   7202   1107   -973   -545       C  
ATOM    988  O   VAL A 137      63.017 -51.816 331.567  1.00 72.95           O  
ANISOU  988  O   VAL A 137    10220   9785   7713    963  -1009   -629       O  
ATOM    989  CB  VAL A 137      64.879 -54.344 332.603  1.00 73.43           C  
ANISOU  989  CB  VAL A 137    10239  10253   7409   1476  -1122   -519       C  
ATOM    990  CG1 VAL A 137      65.300 -53.161 333.464  1.00 69.35           C  
ANISOU  990  CG1 VAL A 137     9668   9828   6852   1326  -1283   -639       C  
ATOM    991  CG2 VAL A 137      64.943 -55.632 333.407  1.00 72.53           C  
ANISOU  991  CG2 VAL A 137    10297  10159   7104   1757  -1107   -454       C  
ATOM    992  N   TRP A 138      63.917 -53.046 329.913  1.00 78.55           N  
ANISOU  992  N   TRP A 138    10697  10669   8480   1068   -948   -486       N  
ATOM    993  CA  TRP A 138      63.921 -51.939 328.960  1.00 69.30           C  
ANISOU  993  CA  TRP A 138     9385   9469   7476    828   -957   -496       C  
ATOM    994  C   TRP A 138      62.504 -51.513 328.596  1.00 61.55           C  
ANISOU  994  C   TRP A 138     8555   8221   6611    740   -830   -494       C  
ATOM    995  O   TRP A 138      62.181 -50.324 328.615  1.00 61.83           O  
ANISOU  995  O   TRP A 138     8610   8152   6732    571   -866   -550       O  
ATOM    996  CB  TRP A 138      64.690 -52.315 327.689  1.00 74.37           C  
ANISOU  996  CB  TRP A 138     9807  10280   8169    833   -935   -418       C  
ATOM    997  CG  TRP A 138      64.672 -51.234 326.640  1.00 78.56           C  
ANISOU  997  CG  TRP A 138    10205  10785   8861    582   -930   -400       C  
ATOM    998  CD1 TRP A 138      65.557 -50.203 326.511  1.00 81.55           C  
ANISOU  998  CD1 TRP A 138    10398  11307   9281    367  -1054   -416       C  
ATOM    999  CD2 TRP A 138      63.718 -51.078 325.578  1.00 63.59           C  
ANISOU  999  CD2 TRP A 138     8359   8710   7094    507   -802   -350       C  
ATOM   1000  NE1 TRP A 138      65.214 -49.416 325.436  1.00 73.42           N  
ANISOU 1000  NE1 TRP A 138     9320  10177   8398    169  -1004   -369       N  
ATOM   1001  CE2 TRP A 138      64.090 -49.931 324.848  1.00 69.34           C  
ANISOU 1001  CE2 TRP A 138     8941   9471   7935    267   -851   -330       C  
ATOM   1002  CE3 TRP A 138      62.588 -51.796 325.175  1.00 63.72           C  
ANISOU 1002  CE3 TRP A 138     8527   8549   7134    606   -659   -315       C  
ATOM   1003  CZ2 TRP A 138      63.371 -49.487 323.738  1.00 81.50           C  
ANISOU 1003  CZ2 TRP A 138    10489  10874   9601    156   -760   -273       C  
ATOM   1004  CZ3 TRP A 138      61.875 -51.352 324.073  1.00 81.26           C  
ANISOU 1004  CZ3 TRP A 138    10733  10658   9483    486   -576   -270       C  
ATOM   1005  CH2 TRP A 138      62.270 -50.209 323.367  1.00 80.45           C  
ANISOU 1005  CH2 TRP A 138    10490  10593   9483    279   -626   -248       C  
ATOM   1006  N   ALA A 139      61.666 -52.493 328.269  1.00 59.02           N  
ANISOU 1006  N   ALA A 139     8347   7793   6285    857   -690   -430       N  
ATOM   1007  CA  ALA A 139      60.307 -52.238 327.794  1.00 74.90           C  
ANISOU 1007  CA  ALA A 139    10456   9605   8398    783   -564   -410       C  
ATOM   1008  C   ALA A 139      59.483 -51.389 328.761  1.00 84.16           C  
ANISOU 1008  C   ALA A 139    11765  10658   9555    745   -565   -485       C  
ATOM   1009  O   ALA A 139      58.827 -50.435 328.348  1.00 85.94           O  
ANISOU 1009  O   ALA A 139    11994  10770   9889    634   -539   -506       O  
ATOM   1010  CB  ALA A 139      59.595 -53.556 327.521  1.00 75.08           C  
ANISOU 1010  CB  ALA A 139    10593   9555   8381    901   -435   -333       C  
ATOM   1011  N   GLN A 140      59.527 -51.732 330.044  1.00 89.56           N  
ANISOU 1011  N   GLN A 140    12569  11372  10087    861   -595   -526       N  
ATOM   1012  CA  GLN A 140      58.709 -51.048 331.044  1.00 84.23           C  
ANISOU 1012  CA  GLN A 140    12040  10606   9358    869   -580   -604       C  
ATOM   1013  C   GLN A 140      59.083 -49.574 331.191  1.00 76.07           C  
ANISOU 1013  C   GLN A 140    10986   9536   8382    738   -706   -717       C  
ATOM   1014  O   GLN A 140      58.289 -48.774 331.687  1.00 69.73           O  
ANISOU 1014  O   GLN A 140    10307   8615   7572    739   -685   -792       O  
ATOM   1015  CB  GLN A 140      58.828 -51.751 332.399  1.00 80.28           C  
ANISOU 1015  CB  GLN A 140    11671  10176   8655   1025   -597   -618       C  
ATOM   1016  CG  GLN A 140      60.197 -51.631 333.042  1.00 79.42           C  
ANISOU 1016  CG  GLN A 140    11502  10227   8445   1052   -777   -680       C  
ATOM   1017  CD  GLN A 140      60.307 -52.415 334.332  1.00 77.03           C  
ANISOU 1017  CD  GLN A 140    11337  10004   7926   1229   -793   -674       C  
ATOM   1018  OE1 GLN A 140      60.238 -51.849 335.423  1.00 85.40           O  
ANISOU 1018  OE1 GLN A 140    12498  11083   8867   1253   -857   -771       O  
ATOM   1019  NE2 GLN A 140      60.488 -53.726 334.215  1.00 59.17           N  
ANISOU 1019  NE2 GLN A 140     9104   7781   5598   1364   -741   -561       N  
ATOM   1020  N   ASN A 141      60.285 -49.217 330.749  1.00 70.54           N  
ANISOU 1020  N   ASN A 141    10135   8937   7730    625   -838   -727       N  
ATOM   1021  CA  ASN A 141      60.794 -47.865 330.945  1.00 67.44           C  
ANISOU 1021  CA  ASN A 141     9740   8504   7380    457   -986   -830       C  
ATOM   1022  C   ASN A 141      60.837 -47.017 329.674  1.00 77.15           C  
ANISOU 1022  C   ASN A 141    10872   9648   8795    263   -988   -787       C  
ATOM   1023  O   ASN A 141      61.143 -45.827 329.739  1.00 88.25           O  
ANISOU 1023  O   ASN A 141    12315  10965  10251     95  -1105   -859       O  
ATOM   1024  CB  ASN A 141      62.196 -47.921 331.563  1.00 74.87           C  
ANISOU 1024  CB  ASN A 141    10576   9655   8216    422  -1164   -877       C  
ATOM   1025  CG  ASN A 141      62.183 -48.407 333.002  1.00 85.13           C  
ANISOU 1025  CG  ASN A 141    12012  11021   9312    595  -1203   -946       C  
ATOM   1026  OD1 ASN A 141      61.395 -47.936 333.822  1.00 79.70           O  
ANISOU 1026  OD1 ASN A 141    11522  10202   8560    643  -1183  -1035       O  
ATOM   1027  ND2 ASN A 141      63.060 -49.356 333.314  1.00 87.78           N  
ANISOU 1027  ND2 ASN A 141    12248  11574   9531    710  -1257   -901       N  
ATOM   1028  N   HIS A 142      60.530 -47.612 328.523  1.00 82.92           N  
ANISOU 1028  N   HIS A 142    11499  10391   9615    278   -867   -669       N  
ATOM   1029  CA  HIS A 142      60.638 -46.877 327.260  1.00 75.72           C  
ANISOU 1029  CA  HIS A 142    10484   9427   8859    100   -867   -607       C  
ATOM   1030  C   HIS A 142      59.488 -47.110 326.274  1.00 75.49           C  
ANISOU 1030  C   HIS A 142    10474   9287   8923    146   -708   -523       C  
ATOM   1031  O   HIS A 142      59.269 -46.298 325.375  1.00 71.89           O  
ANISOU 1031  O   HIS A 142     9993   8735   8585     21   -702   -481       O  
ATOM   1032  CB  HIS A 142      61.968 -47.209 326.581  1.00 64.16           C  
ANISOU 1032  CB  HIS A 142     8781   8196   7401     12   -932   -539       C  
ATOM   1033  CG  HIS A 142      63.161 -46.679 327.310  1.00 71.08           C  
ANISOU 1033  CG  HIS A 142     9584   9209   8213   -109  -1114   -608       C  
ATOM   1034  ND1 HIS A 142      63.920 -47.453 328.163  1.00 71.17           N  
ANISOU 1034  ND1 HIS A 142     9536   9427   8078     18  -1183   -641       N  
ATOM   1035  CD2 HIS A 142      63.722 -45.444 327.330  1.00 77.93           C  
ANISOU 1035  CD2 HIS A 142    10437  10036   9136   -359  -1254   -650       C  
ATOM   1036  CE1 HIS A 142      64.898 -46.723 328.668  1.00 75.11           C  
ANISOU 1036  CE1 HIS A 142     9957  10039   8541   -150  -1360   -704       C  
ATOM   1037  NE2 HIS A 142      64.799 -45.500 328.177  1.00 78.16           N  
ANISOU 1037  NE2 HIS A 142    10377  10269   9052   -398  -1408   -713       N  
ATOM   1038  N   ARG A 143      58.756 -48.207 326.438  1.00 70.26           N  
ANISOU 1038  N   ARG A 143     9859   8638   8200    309   -587   -491       N  
ATOM   1039  CA  ARG A 143      57.618 -48.487 325.567  1.00 59.07           C  
ANISOU 1039  CA  ARG A 143     8450   7139   6853    335   -449   -417       C  
ATOM   1040  C   ARG A 143      56.449 -47.543 325.847  1.00 61.80           C  
ANISOU 1040  C   ARG A 143     8921   7322   7239    348   -410   -460       C  
ATOM   1041  O   ARG A 143      55.479 -47.927 326.498  1.00 74.76           O  
ANISOU 1041  O   ARG A 143    10655   8940   8810    466   -321   -476       O  
ATOM   1042  CB  ARG A 143      57.159 -49.937 325.731  1.00 61.55           C  
ANISOU 1042  CB  ARG A 143     8800   7504   7082    470   -344   -371       C  
ATOM   1043  CG  ARG A 143      57.343 -50.795 324.495  1.00 76.68           C  
ANISOU 1043  CG  ARG A 143    10614   9483   9036    461   -289   -283       C  
ATOM   1044  CD  ARG A 143      56.451 -52.026 324.545  1.00 83.86           C  
ANISOU 1044  CD  ARG A 143    11620  10357   9886    549   -175   -238       C  
ATOM   1045  NE  ARG A 143      55.038 -51.669 324.669  1.00 82.53           N  
ANISOU 1045  NE  ARG A 143    11512  10098   9748    526    -88   -231       N  
ATOM   1046  CZ  ARG A 143      54.036 -52.536 324.564  1.00 82.74           C  
ANISOU 1046  CZ  ARG A 143    11595  10101   9744    538     17   -178       C  
ATOM   1047  NH1 ARG A 143      54.284 -53.816 324.327  1.00 85.02           N  
ANISOU 1047  NH1 ARG A 143    11932  10398   9973    568     41   -134       N  
ATOM   1048  NH2 ARG A 143      52.785 -52.121 324.693  1.00 82.94           N  
ANISOU 1048  NH2 ARG A 143    11628  10097   9787    520     93   -167       N  
ATOM   1049  N   THR A 144      56.543 -46.311 325.355  1.00 59.22           N  
ANISOU 1049  N   THR A 144     8600   6889   7011    234   -473   -471       N  
ATOM   1050  CA  THR A 144      55.462 -45.343 325.518  1.00 68.63           C  
ANISOU 1050  CA  THR A 144     9924   7915   8238    284   -443   -511       C  
ATOM   1051  C   THR A 144      54.616 -45.221 324.251  1.00 80.38           C  
ANISOU 1051  C   THR A 144    11346   9367   9829    273   -352   -407       C  
ATOM   1052  O   THR A 144      55.025 -45.663 323.178  1.00 77.31           O  
ANISOU 1052  O   THR A 144    10821   9059   9495    187   -337   -313       O  
ATOM   1053  CB  THR A 144      55.998 -43.949 325.894  1.00 78.15           C  
ANISOU 1053  CB  THR A 144    11250   8968   9474    184   -586   -600       C  
ATOM   1054  OG1 THR A 144      54.946 -42.983 325.769  1.00100.24           O  
ANISOU 1054  OG1 THR A 144    14185  11584  12319    259   -552   -621       O  
ATOM   1055  CG2 THR A 144      57.142 -43.553 324.982  1.00 70.85           C  
ANISOU 1055  CG2 THR A 144    10207   8072   8641    -37   -683   -533       C  
ATOM   1056  N   VAL A 145      53.437 -44.621 324.388  1.00 77.59           N  
ANISOU 1056  N   VAL A 145    11084   8913   9484    382   -294   -426       N  
ATOM   1057  CA  VAL A 145      52.530 -44.418 323.263  1.00 76.48           C  
ANISOU 1057  CA  VAL A 145    10880   8755   9424    398   -219   -330       C  
ATOM   1058  C   VAL A 145      53.115 -43.431 322.253  1.00 83.71           C  
ANISOU 1058  C   VAL A 145    11792   9561  10453    256   -305   -273       C  
ATOM   1059  O   VAL A 145      52.960 -43.602 321.041  1.00 81.77           O  
ANISOU 1059  O   VAL A 145    11434   9366  10268    201   -266   -162       O  
ATOM   1060  CB  VAL A 145      51.150 -43.910 323.741  1.00 78.02           C  
ANISOU 1060  CB  VAL A 145    11163   8899   9583    583   -144   -368       C  
ATOM   1061  CG1 VAL A 145      50.278 -43.503 322.561  1.00 81.17           C  
ANISOU 1061  CG1 VAL A 145    11493   9284  10063    610    -95   -268       C  
ATOM   1062  CG2 VAL A 145      50.455 -44.972 324.581  1.00 76.88           C  
ANISOU 1062  CG2 VAL A 145    10986   8903   9321    691    -33   -384       C  
ATOM   1063  N   ALA A 146      53.797 -42.407 322.757  1.00 87.72           N  
ANISOU 1063  N   ALA A 146    12434   9919  10975    183   -427   -346       N  
ATOM   1064  CA  ALA A 146      54.409 -41.391 321.904  1.00 82.48           C  
ANISOU 1064  CA  ALA A 146    11798   9129  10412      9   -519   -281       C  
ATOM   1065  C   ALA A 146      55.487 -41.989 321.002  1.00 86.83           C  
ANISOU 1065  C   ALA A 146    12146   9851  10994   -175   -533   -179       C  
ATOM   1066  O   ALA A 146      55.676 -41.543 319.870  1.00 86.58           O  
ANISOU 1066  O   ALA A 146    12060   9799  11036   -294   -542    -63       O  
ATOM   1067  CB  ALA A 146      54.993 -40.270 322.752  1.00 70.51           C  
ANISOU 1067  CB  ALA A 146    10488   7413   8891    -71   -663   -393       C  
ATOM   1068  N   ALA A 147      56.191 -42.997 321.509  1.00 89.54           N  
ANISOU 1068  N   ALA A 147    12382  10374  11266   -178   -534   -216       N  
ATOM   1069  CA  ALA A 147      57.211 -43.684 320.725  1.00 90.56           C  
ANISOU 1069  CA  ALA A 147    12309  10703  11395   -293   -535   -132       C  
ATOM   1070  C   ALA A 147      56.566 -44.512 319.622  1.00 87.39           C  
ANISOU 1070  C   ALA A 147    11798  10401  11005   -220   -412    -35       C  
ATOM   1071  O   ALA A 147      57.091 -44.604 318.514  1.00 87.07           O  
ANISOU 1071  O   ALA A 147    11626  10466  10992   -318   -402     64       O  
ATOM   1072  CB  ALA A 147      58.070 -44.565 321.617  1.00 90.61           C  
ANISOU 1072  CB  ALA A 147    12251  10872  11305   -259   -571   -203       C  
ATOM   1073  N   ALA A 148      55.423 -45.114 319.940  1.00 86.69           N  
ANISOU 1073  N   ALA A 148    11762  10295  10881    -58   -320    -64       N  
ATOM   1074  CA  ALA A 148      54.674 -45.906 318.973  1.00 85.31           C  
ANISOU 1074  CA  ALA A 148    11504  10204  10707     -6   -217     12       C  
ATOM   1075  C   ALA A 148      54.175 -45.029 317.829  1.00 93.61           C  
ANISOU 1075  C   ALA A 148    12541  11189  11838    -58   -211    107       C  
ATOM   1076  O   ALA A 148      54.124 -45.460 316.677  1.00 96.30           O  
ANISOU 1076  O   ALA A 148    12776  11631  12184    -90   -168    193       O  
ATOM   1077  CB  ALA A 148      53.509 -46.610 319.654  1.00 68.65           C  
ANISOU 1077  CB  ALA A 148     9452   8094   8539    135   -131    -32       C  
ATOM   1078  N   HIS A 149      53.810 -43.794 318.158  1.00 94.03           N  
ANISOU 1078  N   HIS A 149    12722  11065  11939    -51   -260     89       N  
ATOM   1079  CA  HIS A 149      53.361 -42.835 317.159  1.00103.06           C  
ANISOU 1079  CA  HIS A 149    13893  12113  13153    -80   -270    188       C  
ATOM   1080  C   HIS A 149      54.524 -42.380 316.288  1.00103.28           C  
ANISOU 1080  C   HIS A 149    13856  12163  13223   -283   -332    284       C  
ATOM   1081  O   HIS A 149      54.366 -42.174 315.085  1.00112.49           O  
ANISOU 1081  O   HIS A 149    14962  13363  14415   -328   -309    406       O  
ATOM   1082  CB  HIS A 149      52.701 -41.627 317.829  1.00115.15           C  
ANISOU 1082  CB  HIS A 149    15623  13418  14712     15   -313    134       C  
ATOM   1083  CG  HIS A 149      52.326 -40.537 316.874  1.00130.51           C  
ANISOU 1083  CG  HIS A 149    17641  15224  16724      1   -341    242       C  
ATOM   1084  ND1 HIS A 149      51.256 -40.637 316.010  1.00139.03           N  
ANISOU 1084  ND1 HIS A 149    18654  16368  17803    119   -271    329       N  
ATOM   1085  CD2 HIS A 149      52.882 -39.323 316.643  1.00132.26           C  
ANISOU 1085  CD2 HIS A 149    18008  15241  17005   -123   -439    287       C  
ATOM   1086  CE1 HIS A 149      51.168 -39.533 315.291  1.00138.87           C  
ANISOU 1086  CE1 HIS A 149    18737  16191  17836     97   -321    427       C  
ATOM   1087  NE2 HIS A 149      52.142 -38.719 315.655  1.00136.31           N  
ANISOU 1087  NE2 HIS A 149    18556  15685  17551    -56   -422    408       N  
ATOM   1088  N   LYS A 150      55.692 -42.232 316.902  1.00 93.41           N  
ANISOU 1088  N   LYS A 150    12605  10921  11966   -411   -413    236       N  
ATOM   1089  CA  LYS A 150      56.872 -41.749 316.196  1.00 87.48           C  
ANISOU 1089  CA  LYS A 150    11768  10226  11245   -635   -475    333       C  
ATOM   1090  C   LYS A 150      57.390 -42.792 315.208  1.00 81.24           C  
ANISOU 1090  C   LYS A 150    10754   9709  10406   -652   -403    412       C  
ATOM   1091  O   LYS A 150      57.856 -42.451 314.120  1.00 85.07           O  
ANISOU 1091  O   LYS A 150    11147  10270  10905   -783   -399    542       O  
ATOM   1092  CB  LYS A 150      57.971 -41.369 317.191  1.00 93.75           C  
ANISOU 1092  CB  LYS A 150    12591  11000  12029   -776   -591    251       C  
ATOM   1093  CG  LYS A 150      58.811 -40.174 316.763  1.00114.24           C  
ANISOU 1093  CG  LYS A 150    15219  13505  14683  -1048   -695    341       C  
ATOM   1094  CD  LYS A 150      57.954 -38.922 316.616  1.00128.83           C  
ANISOU 1094  CD  LYS A 150    17322  15025  16603  -1042   -731    370       C  
ATOM   1095  CE  LYS A 150      58.788 -37.725 316.179  1.00132.21           C  
ANISOU 1095  CE  LYS A 150    17825  15321  17088  -1346   -841    476       C  
ATOM   1096  NZ  LYS A 150      57.967 -36.490 316.032  1.00126.39           N  
ANISOU 1096  NZ  LYS A 150    17386  14222  16414  -1315   -886    509       N  
ATOM   1097  N   VAL A 151      57.303 -44.062 315.591  1.00 69.76           N  
ANISOU 1097  N   VAL A 151     9231   8392   8881   -511   -344    337       N  
ATOM   1098  CA  VAL A 151      57.735 -45.158 314.730  1.00 73.35           C  
ANISOU 1098  CA  VAL A 151     9519   9080   9270   -479   -276    383       C  
ATOM   1099  C   VAL A 151      56.905 -45.215 313.449  1.00 87.12           C  
ANISOU 1099  C   VAL A 151    11241  10838  11021   -450   -205    477       C  
ATOM   1100  O   VAL A 151      57.451 -45.352 312.353  1.00 93.52           O  
ANISOU 1100  O   VAL A 151    11927  11806  11799   -513   -178    570       O  
ATOM   1101  CB  VAL A 151      57.647 -46.518 315.458  1.00 71.88           C  
ANISOU 1101  CB  VAL A 151     9335   8973   9004   -316   -234    280       C  
ATOM   1102  CG1 VAL A 151      57.797 -47.671 314.475  1.00 71.98           C  
ANISOU 1102  CG1 VAL A 151     9243   9164   8943   -243   -160    314       C  
ATOM   1103  CG2 VAL A 151      58.702 -46.605 316.551  1.00 68.77           C  
ANISOU 1103  CG2 VAL A 151     8918   8639   8571   -333   -310    205       C  
ATOM   1104  N   CYS A 152      55.588 -45.096 313.594  1.00 89.22           N  
ANISOU 1104  N   CYS A 152    11615  10969  11314   -349   -174    456       N  
ATOM   1105  CA  CYS A 152      54.671 -45.158 312.458  1.00 88.68           C  
ANISOU 1105  CA  CYS A 152    11522  10931  11243   -311   -121    537       C  
ATOM   1106  C   CYS A 152      54.969 -44.084 311.415  1.00 89.03           C  
ANISOU 1106  C   CYS A 152    11547  10955  11325   -432   -150    679       C  
ATOM   1107  O   CYS A 152      54.891 -44.342 310.215  1.00 85.38           O  
ANISOU 1107  O   CYS A 152    10999  10621  10820   -444   -111    768       O  
ATOM   1108  CB  CYS A 152      53.223 -45.028 312.933  1.00 86.23           C  
ANISOU 1108  CB  CYS A 152    11307  10504  10953   -184    -96    496       C  
ATOM   1109  SG  CYS A 152      52.644 -46.408 313.945  1.00 77.93           S  
ANISOU 1109  SG  CYS A 152    10271   9503   9837    -69    -39    371       S  
ATOM   1110  N   LEU A 153      55.313 -42.885 311.877  1.00 87.42           N  
ANISOU 1110  N   LEU A 153    11444  10580  11190   -529   -225    702       N  
ATOM   1111  CA  LEU A 153      55.629 -41.778 310.980  1.00 86.06           C  
ANISOU 1111  CA  LEU A 153    11296  10346  11056   -673   -262    854       C  
ATOM   1112  C   LEU A 153      56.849 -42.098 310.121  1.00 79.14           C  
ANISOU 1112  C   LEU A 153    10239   9706  10126   -825   -243    949       C  
ATOM   1113  O   LEU A 153      56.947 -41.662 308.973  1.00 80.26           O  
ANISOU 1113  O   LEU A 153    10339   9905  10252   -909   -226   1100       O  
ATOM   1114  CB  LEU A 153      55.866 -40.492 311.774  1.00 87.70           C  
ANISOU 1114  CB  LEU A 153    11687  10291  11342   -772   -362    842       C  
ATOM   1115  CG  LEU A 153      54.711 -40.023 312.661  1.00 89.07           C  
ANISOU 1115  CG  LEU A 153    12058  10232  11552   -591   -380    743       C  
ATOM   1116  CD1 LEU A 153      55.040 -38.688 313.314  1.00 89.36           C  
ANISOU 1116  CD1 LEU A 153    12319   9982  11652   -695   -491    727       C  
ATOM   1117  CD2 LEU A 153      53.416 -39.935 311.865  1.00 86.41           C  
ANISOU 1117  CD2 LEU A 153    11738   9885  11209   -424   -325    817       C  
ATOM   1118  N   VAL A 154      57.776 -42.864 310.684  1.00 67.99           N  
ANISOU 1118  N   VAL A 154     8713   8450   8670   -842   -243    865       N  
ATOM   1119  CA  VAL A 154      58.950 -43.302 309.945  1.00 68.61           C  
ANISOU 1119  CA  VAL A 154     8587   8810   8673   -936   -212    938       C  
ATOM   1120  C   VAL A 154      58.562 -44.378 308.935  1.00 69.87           C  
ANISOU 1120  C   VAL A 154     8656   9155   8736   -789   -116    948       C  
ATOM   1121  O   VAL A 154      59.026 -44.371 307.794  1.00 82.42           O  
ANISOU 1121  O   VAL A 154    10125  10931  10260   -849    -73   1065       O  
ATOM   1122  CB  VAL A 154      60.042 -43.843 310.892  1.00 70.23           C  
ANISOU 1122  CB  VAL A 154     8689   9152   8843   -953   -247    840       C  
ATOM   1123  CG1 VAL A 154      61.186 -44.460 310.103  1.00 65.00           C  
ANISOU 1123  CG1 VAL A 154     7786   8835   8076   -982   -198    906       C  
ATOM   1124  CG2 VAL A 154      60.552 -42.733 311.797  1.00 69.98           C  
ANISOU 1124  CG2 VAL A 154     8738   8962   8889  -1142   -362    831       C  
ATOM   1125  N   LEU A 155      57.693 -45.291 309.358  1.00 60.29           N  
ANISOU 1125  N   LEU A 155     7512   7891   7506   -609    -85    827       N  
ATOM   1126  CA  LEU A 155      57.257 -46.393 308.507  1.00 68.82           C  
ANISOU 1126  CA  LEU A 155     8547   9110   8490   -482    -13    808       C  
ATOM   1127  C   LEU A 155      56.519 -45.905 307.260  1.00 76.21           C  
ANISOU 1127  C   LEU A 155     9489  10052   9414   -506      9    927       C  
ATOM   1128  O   LEU A 155      56.708 -46.445 306.169  1.00 74.58           O  
ANISOU 1128  O   LEU A 155     9199  10035   9104   -480     57    969       O  
ATOM   1129  CB  LEU A 155      56.366 -47.353 309.298  1.00 68.41           C  
ANISOU 1129  CB  LEU A 155     8597   8964   8433   -337      3    668       C  
ATOM   1130  CG  LEU A 155      57.023 -48.020 310.507  1.00 77.94           C  
ANISOU 1130  CG  LEU A 155     9818  10173   9624   -278    -14    553       C  
ATOM   1131  CD1 LEU A 155      56.123 -49.097 311.093  1.00 82.02           C  
ANISOU 1131  CD1 LEU A 155    10443  10611  10111   -151     16    446       C  
ATOM   1132  CD2 LEU A 155      58.381 -48.594 310.133  1.00 79.50           C  
ANISOU 1132  CD2 LEU A 155     9875  10602   9729   -262      1    561       C  
ATOM   1133  N   TRP A 156      55.680 -44.886 307.425  1.00 76.72           N  
ANISOU 1133  N   TRP A 156     9663   9918   9568   -533    -30    979       N  
ATOM   1134  CA  TRP A 156      54.950 -44.309 306.300  1.00 74.48           C  
ANISOU 1134  CA  TRP A 156     9396   9633   9271   -537    -24   1108       C  
ATOM   1135  C   TRP A 156      55.899 -43.648 305.302  1.00 78.64           C  
ANISOU 1135  C   TRP A 156     9843  10279   9759   -686    -18   1275       C  
ATOM   1136  O   TRP A 156      55.701 -43.744 304.092  1.00 73.46           O  
ANISOU 1136  O   TRP A 156     9133   9761   9016   -674     17   1371       O  
ATOM   1137  CB  TRP A 156      53.915 -43.290 306.783  1.00 73.21           C  
ANISOU 1137  CB  TRP A 156     9381   9227   9207   -495    -72   1130       C  
ATOM   1138  CG  TRP A 156      52.652 -43.899 307.326  1.00 84.80           C  
ANISOU 1138  CG  TRP A 156    10887  10656  10679   -337    -56   1017       C  
ATOM   1139  CD1 TRP A 156      52.315 -44.052 308.640  1.00 80.33           C  
ANISOU 1139  CD1 TRP A 156    10391   9970  10162   -269    -64    891       C  
ATOM   1140  CD2 TRP A 156      51.554 -44.428 306.568  1.00 89.24           C  
ANISOU 1140  CD2 TRP A 156    11404  11325  11180   -246    -31   1028       C  
ATOM   1141  NE1 TRP A 156      51.080 -44.645 308.747  1.00 70.13           N  
ANISOU 1141  NE1 TRP A 156     9087   8714   8843   -151    -34    836       N  
ATOM   1142  CE2 TRP A 156      50.591 -44.886 307.490  1.00 77.87           C  
ANISOU 1142  CE2 TRP A 156     9993   9833   9760   -144    -20    915       C  
ATOM   1143  CE3 TRP A 156      51.293 -44.560 305.200  1.00 87.87           C  
ANISOU 1143  CE3 TRP A 156    11161  11305  10921   -250    -20   1124       C  
ATOM   1144  CZ2 TRP A 156      49.388 -45.466 307.089  1.00 81.81           C  
ANISOU 1144  CZ2 TRP A 156    10438  10438  10207    -73     -4    900       C  
ATOM   1145  CZ3 TRP A 156      50.097 -45.136 304.804  1.00 80.74           C  
ANISOU 1145  CZ3 TRP A 156    10220  10494   9963   -165    -15   1094       C  
ATOM   1146  CH2 TRP A 156      49.161 -45.582 305.745  1.00 81.48           C  
ANISOU 1146  CH2 TRP A 156    10328  10542  10089    -90     -9    986       C  
ATOM   1147  N   ALA A 157      56.926 -42.976 305.815  1.00 77.51           N  
ANISOU 1147  N   ALA A 157     9688  10093   9668   -842    -56   1314       N  
ATOM   1148  CA  ALA A 157      57.917 -42.326 304.965  1.00 73.08           C  
ANISOU 1148  CA  ALA A 157     9033   9666   9068  -1030    -48   1489       C  
ATOM   1149  C   ALA A 157      58.655 -43.355 304.114  1.00 83.85           C  
ANISOU 1149  C   ALA A 157    10196  11380  10283   -988     36   1495       C  
ATOM   1150  O   ALA A 157      58.938 -43.117 302.939  1.00 96.83           O  
ANISOU 1150  O   ALA A 157    11760  13194  11838  -1053     80   1646       O  
ATOM   1151  CB  ALA A 157      58.901 -41.530 305.806  1.00 68.06           C  
ANISOU 1151  CB  ALA A 157     8408   8940   8512  -1234   -117   1509       C  
ATOM   1152  N   LEU A 158      58.960 -44.500 304.715  1.00 79.54           N  
ANISOU 1152  N   LEU A 158     9587  10940   9695   -860     59   1331       N  
ATOM   1153  CA  LEU A 158      59.591 -45.597 303.992  1.00 78.11           C  
ANISOU 1153  CA  LEU A 158     9254  11066   9359   -755    137   1300       C  
ATOM   1154  C   LEU A 158      58.594 -46.266 303.056  1.00 75.36           C  
ANISOU 1154  C   LEU A 158     8964  10747   8921   -609    178   1273       C  
ATOM   1155  O   LEU A 158      58.971 -46.806 302.016  1.00 80.45           O  
ANISOU 1155  O   LEU A 158     9515  11636   9417   -551    240   1303       O  
ATOM   1156  CB  LEU A 158      60.171 -46.624 304.964  1.00 82.92           C  
ANISOU 1156  CB  LEU A 158     9822  11738   9945   -633    137   1133       C  
ATOM   1157  CG  LEU A 158      61.372 -46.163 305.790  1.00 90.19           C  
ANISOU 1157  CG  LEU A 158    10628  12733  10907   -764     93   1151       C  
ATOM   1158  CD1 LEU A 158      61.879 -47.297 306.666  1.00 87.62           C  
ANISOU 1158  CD1 LEU A 158    10266  12494  10532   -591     93    989       C  
ATOM   1159  CD2 LEU A 158      62.478 -45.641 304.886  1.00 91.15           C  
ANISOU 1159  CD2 LEU A 158    10540  13144  10949   -923    132   1321       C  
ATOM   1160  N   ALA A 159      57.320 -46.231 303.434  1.00 67.41           N  
ANISOU 1160  N   ALA A 159     8107   9512   7993   -550    139   1212       N  
ATOM   1161  CA  ALA A 159      56.263 -46.765 302.588  1.00 68.54           C  
ANISOU 1161  CA  ALA A 159     8299   9684   8060   -448    155   1191       C  
ATOM   1162  C   ALA A 159      56.134 -45.928 301.320  1.00 71.60           C  
ANISOU 1162  C   ALA A 159     8654  10161   8391   -521    164   1378       C  
ATOM   1163  O   ALA A 159      56.030 -46.467 300.222  1.00 62.70           O  
ANISOU 1163  O   ALA A 159     7484   9222   7117   -461    201   1393       O  
ATOM   1164  CB  ALA A 159      54.943 -46.806 303.339  1.00 67.96           C  
ANISOU 1164  CB  ALA A 159     8351   9388   8082   -388    111   1105       C  
ATOM   1165  N   VAL A 160      56.150 -44.609 301.485  1.00 76.01           N  
ANISOU 1165  N   VAL A 160     9256  10572   9053   -648    124   1520       N  
ATOM   1166  CA  VAL A 160      56.075 -43.686 300.357  1.00 79.26           C  
ANISOU 1166  CA  VAL A 160     9666  11032   9416   -731    127   1729       C  
ATOM   1167  C   VAL A 160      57.309 -43.811 299.467  1.00 86.62           C  
ANISOU 1167  C   VAL A 160    10441  12262  10211   -818    198   1836       C  
ATOM   1168  O   VAL A 160      57.209 -43.789 298.239  1.00 85.77           O  
ANISOU 1168  O   VAL A 160    10292  12329   9965   -805    235   1949       O  
ATOM   1169  CB  VAL A 160      55.935 -42.223 300.834  1.00 79.55           C  
ANISOU 1169  CB  VAL A 160     9831  10798   9598   -855     60   1858       C  
ATOM   1170  CG1 VAL A 160      56.015 -41.261 299.655  1.00 74.55           C  
ANISOU 1170  CG1 VAL A 160     9216  10206   8902   -958     64   2103       C  
ATOM   1171  CG2 VAL A 160      54.630 -42.035 301.593  1.00 76.87           C  
ANISOU 1171  CG2 VAL A 160     9638  10205   9364   -722      2   1764       C  
ATOM   1172  N   LEU A 161      58.470 -43.958 300.099  1.00 87.80           N  
ANISOU 1172  N   LEU A 161    10485  12495  10378   -897    216   1800       N  
ATOM   1173  CA  LEU A 161      59.738 -44.053 299.382  1.00 77.18           C  
ANISOU 1173  CA  LEU A 161     8948  11479   8899   -980    291   1905       C  
ATOM   1174  C   LEU A 161      59.793 -45.267 298.457  1.00 77.39           C  
ANISOU 1174  C   LEU A 161     8890  11793   8723   -785    371   1822       C  
ATOM   1175  O   LEU A 161      60.347 -45.197 297.362  1.00 83.96           O  
ANISOU 1175  O   LEU A 161     9602  12902   9396   -813    443   1951       O  
ATOM   1176  CB  LEU A 161      60.901 -44.104 300.375  1.00 71.81           C  
ANISOU 1176  CB  LEU A 161     8149  10862   8274  -1071    283   1853       C  
ATOM   1177  CG  LEU A 161      62.308 -44.172 299.780  1.00 86.88           C  
ANISOU 1177  CG  LEU A 161     9806  13161  10043  -1162    361   1965       C  
ATOM   1178  CD1 LEU A 161      62.590 -42.942 298.932  1.00103.37           C  
ANISOU 1178  CD1 LEU A 161    11864  15299  12114  -1416    374   2238       C  
ATOM   1179  CD2 LEU A 161      63.350 -44.321 300.876  1.00 82.86           C  
ANISOU 1179  CD2 LEU A 161     9167  12730   9587  -1224    333   1888       C  
ATOM   1180  N   ASN A 162      59.215 -46.378 298.899  1.00 74.54           N  
ANISOU 1180  N   ASN A 162     8608  11359   8356   -594    359   1607       N  
ATOM   1181  CA  ASN A 162      59.245 -47.610 298.121  1.00 74.09           C  
ANISOU 1181  CA  ASN A 162     8525  11519   8105   -402    417   1493       C  
ATOM   1182  C   ASN A 162      58.172 -47.664 297.038  1.00 81.36           C  
ANISOU 1182  C   ASN A 162     9536  12443   8931   -353    405   1522       C  
ATOM   1183  O   ASN A 162      58.189 -48.552 296.186  1.00 88.25           O  
ANISOU 1183  O   ASN A 162    10405  13508   9617   -216    447   1445       O  
ATOM   1184  CB  ASN A 162      59.105 -48.822 299.042  1.00 71.05           C  
ANISOU 1184  CB  ASN A 162     8223  11030   7743   -239    398   1256       C  
ATOM   1185  CG  ASN A 162      60.358 -49.087 299.849  1.00 81.32           C  
ANISOU 1185  CG  ASN A 162     9403  12442   9053   -216    422   1211       C  
ATOM   1186  OD1 ASN A 162      61.274 -49.767 299.385  1.00 83.12           O  
ANISOU 1186  OD1 ASN A 162     9514  12949   9118    -89    491   1180       O  
ATOM   1187  ND2 ASN A 162      60.405 -48.556 301.065  1.00 87.91           N  
ANISOU 1187  ND2 ASN A 162    10261  13077  10063   -319    363   1203       N  
ATOM   1188  N   THR A 163      57.237 -46.719 297.074  1.00 78.31           N  
ANISOU 1188  N   THR A 163     9239  11852   8662   -447    342   1627       N  
ATOM   1189  CA  THR A 163      56.187 -46.656 296.061  1.00 86.52           C  
ANISOU 1189  CA  THR A 163    10345  12918   9612   -401    316   1676       C  
ATOM   1190  C   THR A 163      56.500 -45.606 294.999  1.00 84.12           C  
ANISOU 1190  C   THR A 163     9985  12751   9225   -508    344   1931       C  
ATOM   1191  O   THR A 163      55.730 -45.412 294.057  1.00 65.50           O  
ANISOU 1191  O   THR A 163     7670  10447   6770   -472    320   2010       O  
ATOM   1192  CB  THR A 163      54.811 -46.347 296.678  1.00 80.23           C  
ANISOU 1192  CB  THR A 163     9674  11846   8965   -389    226   1635       C  
ATOM   1193  OG1 THR A 163      54.858 -45.086 297.358  1.00 86.06           O  
ANISOU 1193  OG1 THR A 163    10450  12374   9876   -503    192   1765       O  
ATOM   1194  CG2 THR A 163      54.407 -47.441 297.654  1.00 75.53           C  
ANISOU 1194  CG2 THR A 163     9137  11133   8427   -302    205   1402       C  
ATOM   1195  N   VAL A 164      57.632 -44.929 295.161  1.00 80.44           N  
ANISOU 1195  N   VAL A 164     9422  12352   8789   -653    389   2069       N  
ATOM   1196  CA  VAL A 164      58.078 -43.941 294.186  1.00 84.38           C  
ANISOU 1196  CA  VAL A 164     9867  12992   9202   -794    427   2337       C  
ATOM   1197  C   VAL A 164      58.294 -44.535 292.780  1.00 84.64           C  
ANISOU 1197  C   VAL A 164     9812  13385   8962   -693    507   2372       C  
ATOM   1198  O   VAL A 164      57.810 -43.963 291.805  1.00 79.73           O  
ANISOU 1198  O   VAL A 164     9235  12815   8245   -715    499   2541       O  
ATOM   1199  CB  VAL A 164      59.377 -43.237 294.654  1.00 75.22           C  
ANISOU 1199  CB  VAL A 164     8590  11881   8109  -1009    463   2469       C  
ATOM   1200  CG1 VAL A 164      59.930 -42.344 293.554  1.00 73.03           C  
ANISOU 1200  CG1 VAL A 164     8242  11796   7708  -1179    520   2761       C  
ATOM   1201  CG2 VAL A 164      59.119 -42.435 295.918  1.00 61.23           C  
ANISOU 1201  CG2 VAL A 164     6945   9733   6588  -1129    369   2458       C  
ATOM   1202  N   PRO A 165      59.004 -45.682 292.663  1.00 83.72           N  
ANISOU 1202  N   PRO A 165     9589  13519   8703   -559    581   2212       N  
ATOM   1203  CA  PRO A 165      59.216 -46.201 291.305  1.00 90.75           C  
ANISOU 1203  CA  PRO A 165    10416  14756   9309   -444    658   2238       C  
ATOM   1204  C   PRO A 165      57.929 -46.636 290.602  1.00 93.44           C  
ANISOU 1204  C   PRO A 165    10904  15043   9555   -315    590   2151       C  
ATOM   1205  O   PRO A 165      57.812 -46.476 289.386  1.00 95.43           O  
ANISOU 1205  O   PRO A 165    11143  15513   9604   -290    620   2269       O  
ATOM   1206  CB  PRO A 165      60.132 -47.412 291.528  1.00 86.50           C  
ANISOU 1206  CB  PRO A 165     9777  14432   8656   -275    733   2039       C  
ATOM   1207  CG  PRO A 165      60.759 -47.188 292.852  1.00 78.88           C  
ANISOU 1207  CG  PRO A 165     8749  13321   7900   -373    717   2011       C  
ATOM   1208  CD  PRO A 165      59.710 -46.505 293.663  1.00 78.55           C  
ANISOU 1208  CD  PRO A 165     8871  12870   8105   -485    601   2020       C  
ATOM   1209  N   TYR A 166      56.982 -47.180 291.360  1.00 84.20           N  
ANISOU 1209  N   TYR A 166     9863  13612   8519   -246    499   1954       N  
ATOM   1210  CA  TYR A 166      55.723 -47.647 290.789  1.00 78.29           C  
ANISOU 1210  CA  TYR A 166     9232  12828   7688   -153    419   1859       C  
ATOM   1211  C   TYR A 166      54.888 -46.483 290.269  1.00 83.61           C  
ANISOU 1211  C   TYR A 166     9942  13433   8394   -236    357   2079       C  
ATOM   1212  O   TYR A 166      54.094 -46.639 289.341  1.00 88.55           O  
ANISOU 1212  O   TYR A 166    10610  14167   8868   -171    309   2087       O  
ATOM   1213  CB  TYR A 166      54.936 -48.453 291.824  1.00 65.15           C  
ANISOU 1213  CB  TYR A 166     7674  10911   6169   -101    340   1621       C  
ATOM   1214  CG  TYR A 166      55.591 -49.770 292.170  1.00 71.06           C  
ANISOU 1214  CG  TYR A 166     8443  11714   6844     22    384   1390       C  
ATOM   1215  CD1 TYR A 166      55.260 -50.931 291.486  1.00 70.90           C  
ANISOU 1215  CD1 TYR A 166     8519  11796   6625    151    366   1207       C  
ATOM   1216  CD2 TYR A 166      56.552 -49.851 293.169  1.00 61.09           C  
ANISOU 1216  CD2 TYR A 166     7120  10397   5694     16    434   1355       C  
ATOM   1217  CE1 TYR A 166      55.860 -52.137 291.791  1.00 77.46           C  
ANISOU 1217  CE1 TYR A 166     9413  12640   7377    291    400    997       C  
ATOM   1218  CE2 TYR A 166      57.158 -51.053 293.480  1.00 54.67           C  
ANISOU 1218  CE2 TYR A 166     6339   9632   4800    166    470   1154       C  
ATOM   1219  CZ  TYR A 166      56.808 -52.193 292.789  1.00 71.93           C  
ANISOU 1219  CZ  TYR A 166     8648  11888   6793    313    456    977       C  
ATOM   1220  OH  TYR A 166      57.407 -53.394 293.093  1.00 73.67           O  
ANISOU 1220  OH  TYR A 166     8946  12122   6925    488    486    776       O  
ATOM   1221  N   PHE A 167      55.073 -45.317 290.878  1.00 76.45           N  
ANISOU 1221  N   PHE A 167     9033  12340   7674   -372    349   2256       N  
ATOM   1222  CA  PHE A 167      54.431 -44.095 290.415  1.00 76.84           C  
ANISOU 1222  CA  PHE A 167     9145  12295   7754   -435    295   2494       C  
ATOM   1223  C   PHE A 167      55.042 -43.654 289.089  1.00 89.39           C  
ANISOU 1223  C   PHE A 167    10675  14172   9119   -480    367   2721       C  
ATOM   1224  O   PHE A 167      54.344 -43.164 288.201  1.00 87.17           O  
ANISOU 1224  O   PHE A 167    10448  13942   8729   -446    322   2867       O  
ATOM   1225  CB  PHE A 167      54.572 -42.990 291.466  1.00 69.15           C  
ANISOU 1225  CB  PHE A 167     8230  11011   7032   -567    265   2605       C  
ATOM   1226  CG  PHE A 167      53.974 -41.672 291.055  1.00 73.49           C  
ANISOU 1226  CG  PHE A 167     8890  11414   7618   -612    206   2857       C  
ATOM   1227  CD1 PHE A 167      54.755 -40.693 290.459  1.00 73.83           C  
ANISOU 1227  CD1 PHE A 167     8936  11510   7607   -769    253   3133       C  
ATOM   1228  CD2 PHE A 167      52.632 -41.407 291.278  1.00 75.91           C  
ANISOU 1228  CD2 PHE A 167     9300  11536   8006   -492    103   2828       C  
ATOM   1229  CE1 PHE A 167      54.208 -39.480 290.083  1.00 61.67           C  
ANISOU 1229  CE1 PHE A 167     7541   9797   6094   -799    192   3375       C  
ATOM   1230  CE2 PHE A 167      52.080 -40.195 290.906  1.00 76.45           C  
ANISOU 1230  CE2 PHE A 167     9489  11462   8098   -487     44   3060       C  
ATOM   1231  CZ  PHE A 167      52.869 -39.231 290.306  1.00 72.41           C  
ANISOU 1231  CZ  PHE A 167     9020  10959   7533   -636     85   3334       C  
ATOM   1232  N   VAL A 168      56.352 -43.839 288.965  1.00 83.48           N  
ANISOU 1232  N   VAL A 168     9799  13634   8286   -546    480   2755       N  
ATOM   1233  CA  VAL A 168      57.094 -43.374 287.801  1.00 94.24           C  
ANISOU 1233  CA  VAL A 168    11074  15301   9432   -617    574   2994       C  
ATOM   1234  C   VAL A 168      56.852 -44.251 286.574  1.00 96.57           C  
ANISOU 1234  C   VAL A 168    11350  15920   9423   -439    604   2911       C  
ATOM   1235  O   VAL A 168      56.658 -43.743 285.469  1.00 94.03           O  
ANISOU 1235  O   VAL A 168    11042  15766   8919   -447    614   3111       O  
ATOM   1236  CB  VAL A 168      58.610 -43.323 288.097  1.00 95.20           C  
ANISOU 1236  CB  VAL A 168    11022  15604   9547   -747    693   3057       C  
ATOM   1237  CG1 VAL A 168      59.387 -42.907 286.858  1.00105.08           C  
ANISOU 1237  CG1 VAL A 168    12154  17226  10545   -826    808   3313       C  
ATOM   1238  CG2 VAL A 168      58.892 -42.371 289.250  1.00 79.64           C  
ANISOU 1238  CG2 VAL A 168     9083  13318   7857   -959    648   3150       C  
ATOM   1239  N   PHE A 169      56.853 -45.566 286.773  1.00 94.53           N  
ANISOU 1239  N   PHE A 169    11083  15734   9098   -277    609   2614       N  
ATOM   1240  CA  PHE A 169      56.746 -46.506 285.659  1.00 90.32           C  
ANISOU 1240  CA  PHE A 169    10558  15501   8260   -102    635   2493       C  
ATOM   1241  C   PHE A 169      55.306 -46.894 285.317  1.00 94.57           C  
ANISOU 1241  C   PHE A 169    11239  15933   8759    -12    496   2365       C  
ATOM   1242  O   PHE A 169      55.077 -47.900 284.646  1.00 99.85           O  
ANISOU 1242  O   PHE A 169    11956  16773   9208    130    481   2178       O  
ATOM   1243  CB  PHE A 169      57.560 -47.769 285.955  1.00 90.54           C  
ANISOU 1243  CB  PHE A 169    10537  15665   8200     45    710   2235       C  
ATOM   1244  CG  PHE A 169      59.042 -47.598 285.755  1.00 98.92           C  
ANISOU 1244  CG  PHE A 169    11404  17032   9148     21    868   2362       C  
ATOM   1245  CD1 PHE A 169      59.533 -46.662 284.860  1.00106.21           C  
ANISOU 1245  CD1 PHE A 169    12219  18206   9930    -97    951   2666       C  
ATOM   1246  CD2 PHE A 169      59.943 -48.378 286.462  1.00103.84           C  
ANISOU 1246  CD2 PHE A 169    11945  17713   9795    117    933   2189       C  
ATOM   1247  CE1 PHE A 169      60.895 -46.505 284.675  1.00110.26           C  
ANISOU 1247  CE1 PHE A 169    12518  19047  10329   -144   1102   2797       C  
ATOM   1248  CE2 PHE A 169      61.305 -48.225 286.282  1.00107.92           C  
ANISOU 1248  CE2 PHE A 169    12241  18566  10197    103   1077   2310       C  
ATOM   1249  CZ  PHE A 169      61.781 -47.288 285.388  1.00112.41           C  
ANISOU 1249  CZ  PHE A 169    12677  19408  10626    -40   1165   2615       C  
ATOM   1250  N   ARG A 170      54.341 -46.103 285.775  1.00 92.44           N  
ANISOU 1250  N   ARG A 170    11037  15396   8691    -90    389   2461       N  
ATOM   1251  CA  ARG A 170      52.953 -46.291 285.361  1.00 84.91           C  
ANISOU 1251  CA  ARG A 170    10172  14405   7686    -19    254   2394       C  
ATOM   1252  C   ARG A 170      52.644 -45.389 284.174  1.00 84.52           C  
ANISOU 1252  C   ARG A 170    10125  14527   7459    -22    236   2665       C  
ATOM   1253  O   ARG A 170      53.112 -44.252 284.112  1.00 83.38           O  
ANISOU 1253  O   ARG A 170     9964  14344   7373   -124    286   2943       O  
ATOM   1254  CB  ARG A 170      51.985 -46.006 286.512  1.00 74.57           C  
ANISOU 1254  CB  ARG A 170     8914  12752   6665    -55    148   2336       C  
ATOM   1255  CG  ARG A 170      51.610 -47.236 287.327  1.00 77.61           C  
ANISOU 1255  CG  ARG A 170     9338  13018   7133    -12    105   2019       C  
ATOM   1256  CD  ARG A 170      50.910 -48.280 286.470  1.00 61.87           C  
ANISOU 1256  CD  ARG A 170     7395  11204   4910     70     29   1837       C  
ATOM   1257  NE  ARG A 170      50.919 -49.599 287.100  1.00 75.80           N  
ANISOU 1257  NE  ARG A 170     9227  12873   6699     97     16   1538       N  
ATOM   1258  CZ  ARG A 170      49.838 -50.224 287.556  1.00 75.17           C  
ANISOU 1258  CZ  ARG A 170     9207  12663   6693     68    -96   1368       C  
ATOM   1259  NH1 ARG A 170      48.643 -49.659 287.446  1.00 82.87           N  
ANISOU 1259  NH1 ARG A 170    10146  13625   7717     33   -205   1458       N  
ATOM   1260  NH2 ARG A 170      49.951 -51.421 288.115  1.00 61.40           N  
ANISOU 1260  NH2 ARG A 170     7555  10811   4961     78   -101   1117       N  
ATOM   1261  N   ASP A 171      51.858 -45.900 283.233  1.00 82.99           N  
ANISOU 1261  N   ASP A 171     9969  14521   7043     79    156   2588       N  
ATOM   1262  CA  ASP A 171      51.531 -45.154 282.024  1.00 87.69           C  
ANISOU 1262  CA  ASP A 171    10574  15318   7427    104    130   2835       C  
ATOM   1263  C   ASP A 171      50.246 -45.680 281.392  1.00 94.61           C  
ANISOU 1263  C   ASP A 171    11495  16302   8151    203    -24   2706       C  
ATOM   1264  O   ASP A 171      49.894 -46.848 281.564  1.00 93.72           O  
ANISOU 1264  O   ASP A 171    11408  16200   8001    242    -80   2407       O  
ATOM   1265  CB  ASP A 171      52.689 -45.233 281.023  1.00 91.74           C  
ANISOU 1265  CB  ASP A 171    11029  16169   7658    116    276   2944       C  
ATOM   1266  CG  ASP A 171      52.534 -44.262 279.869  1.00 95.79           C  
ANISOU 1266  CG  ASP A 171    11555  16872   7968    111    274   3268       C  
ATOM   1267  OD1 ASP A 171      51.906 -43.200 280.062  1.00104.41           O  
ANISOU 1267  OD1 ASP A 171    12701  17760   9208     63    197   3484       O  
ATOM   1268  OD2 ASP A 171      53.044 -44.561 278.769  1.00 92.22           O  
ANISOU 1268  OD2 ASP A 171    11072  16773   7194    172    352   3309       O  
ATOM   1269  N   THR A 172      49.540 -44.810 280.675  1.00 96.95           N  
ANISOU 1269  N   THR A 172    11807  16672   8357    235   -103   2937       N  
ATOM   1270  CA  THR A 172      48.358 -45.221 279.926  1.00 94.87           C  
ANISOU 1270  CA  THR A 172    11557  16582   7907    325   -259   2848       C  
ATOM   1271  C   THR A 172      48.774 -45.722 278.548  1.00 73.79           C  
ANISOU 1271  C   THR A 172     8900  14291   4845    392   -224   2837       C  
ATOM   1272  O   THR A 172      49.562 -45.077 277.857  1.00 89.73           O  
ANISOU 1272  O   THR A 172    10911  16470   6714    390   -113   3082       O  
ATOM   1273  CB  THR A 172      47.344 -44.073 279.774  1.00 89.48           C  
ANISOU 1273  CB  THR A 172    10880  15834   7284    372   -376   3100       C  
ATOM   1274  OG1 THR A 172      47.967 -42.969 279.107  1.00 74.44           O  
ANISOU 1274  OG1 THR A 172     9012  13991   5280    365   -294   3448       O  
ATOM   1275  CG2 THR A 172      46.843 -43.615 281.136  1.00 78.94           C  
ANISOU 1275  CG2 THR A 172     9542  14141   6312    345   -414   3085       C  
ATOM   1276  N   ILE A 173      48.250 -46.879 278.158  1.00 79.60           N  
ANISOU 1276  N   ILE A 173     9668  15171   5407    440   -320   2550       N  
ATOM   1277  CA  ILE A 173      48.614 -47.486 276.882  1.00 85.92           C  
ANISOU 1277  CA  ILE A 173    10509  16326   5812    525   -297   2482       C  
ATOM   1278  C   ILE A 173      47.385 -47.764 276.021  1.00 86.68           C  
ANISOU 1278  C   ILE A 173    10630  16620   5683    574   -496   2411       C  
ATOM   1279  O   ILE A 173      46.488 -48.505 276.419  1.00 78.02           O  
ANISOU 1279  O   ILE A 173     9550  15434   4660    533   -642   2165       O  
ATOM   1280  CB  ILE A 173      49.390 -48.804 277.083  1.00 83.88           C  
ANISOU 1280  CB  ILE A 173    10309  16082   5478    557   -217   2155       C  
ATOM   1281  CG1 ILE A 173      50.603 -48.582 277.988  1.00 80.10           C  
ANISOU 1281  CG1 ILE A 173     9776  15441   5218    516    -33   2213       C  
ATOM   1282  CG2 ILE A 173      49.814 -49.388 275.741  1.00 78.85           C  
ANISOU 1282  CG2 ILE A 173     9732  15792   4436    677   -182   2070       C  
ATOM   1283  CD1 ILE A 173      51.395 -49.835 278.253  1.00 84.63           C  
ANISOU 1283  CD1 ILE A 173    10406  16024   5725    589     47   1909       C  
ATOM   1284  N   SER A 174      47.354 -47.175 274.832  1.00 97.90           N  
ANISOU 1284  N   SER A 174    12051  18220   6926    637   -494   2584       N  
ATOM   1285  CA  SER A 174      46.228 -47.360 273.922  1.00101.88           C  
ANISOU 1285  CA  SER A 174    12568  18887   7256    683   -678   2513       C  
ATOM   1286  C   SER A 174      46.260 -48.737 273.260  1.00 96.73           C  
ANISOU 1286  C   SER A 174    12011  18394   6349    708   -728   2159       C  
ATOM   1287  O   SER A 174      47.308 -49.174 272.789  1.00 85.53           O  
ANISOU 1287  O   SER A 174    10651  17058   4787    765   -584   2078       O  
ATOM   1288  CB  SER A 174      46.226 -46.265 272.853  1.00108.43           C  
ANISOU 1288  CB  SER A 174    13386  19827   7987    749   -654   2812       C  
ATOM   1289  OG  SER A 174      46.028 -44.982 273.423  1.00111.54           O  
ANISOU 1289  OG  SER A 174    13740  20032   8609    735   -644   3126       O  
ATOM   1290  N   ARG A 175      45.112 -49.411 273.224  1.00 84.91           N  
ANISOU 1290  N   ARG A 175    10530  16935   4796    664   -937   1948       N  
ATOM   1291  CA  ARG A 175      44.996 -50.712 272.574  1.00 91.70           C  
ANISOU 1291  CA  ARG A 175    11523  17905   5414    663  -1023   1602       C  
ATOM   1292  C   ARG A 175      44.500 -50.545 271.137  1.00 94.30           C  
ANISOU 1292  C   ARG A 175    11870  18470   5489    728  -1119   1640       C  
ATOM   1293  O   ARG A 175      44.321 -49.424 270.651  1.00 96.04           O  
ANISOU 1293  O   ARG A 175    12002  18770   5719    784  -1103   1941       O  
ATOM   1294  CB  ARG A 175      44.054 -51.627 273.359  1.00 97.70           C  
ANISOU 1294  CB  ARG A 175    12307  18563   6253    525  -1207   1331       C  
ATOM   1295  CG  ARG A 175      44.438 -51.816 274.818  1.00103.98           C  
ANISOU 1295  CG  ARG A 175    13088  19129   7291    456  -1129   1288       C  
ATOM   1296  CD  ARG A 175      44.387 -53.292 275.217  1.00112.64           C  
ANISOU 1296  CD  ARG A 175    14351  20067   8380    363  -1194    886       C  
ATOM   1297  NE  ARG A 175      43.082 -53.908 274.976  1.00113.32           N  
ANISOU 1297  NE  ARG A 175    14450  20230   8376    218  -1445    702       N  
ATOM   1298  CZ  ARG A 175      42.835 -55.207 275.140  1.00121.45           C  
ANISOU 1298  CZ  ARG A 175    15657  21137   9352     96  -1551    354       C  
ATOM   1299  NH1 ARG A 175      41.627 -55.700 274.892  1.00122.29           N  
ANISOU 1299  NH1 ARG A 175    15754  21339   9370    -78  -1790    210       N  
ATOM   1300  NH2 ARG A 175      43.806 -56.024 275.540  1.00132.06           N  
ANISOU 1300  NH2 ARG A 175    17193  22266  10718    145  -1424    152       N  
ATOM   1301  N   LEU A 176      44.286 -51.667 270.461  1.00100.02           N  
ANISOU 1301  N   LEU A 176    12735  19288   5981    721  -1222   1332       N  
ATOM   1302  CA  LEU A 176      43.811 -51.657 269.087  1.00109.50           C  
ANISOU 1302  CA  LEU A 176    13973  20718   6913    776  -1328   1327       C  
ATOM   1303  C   LEU A 176      42.297 -51.807 269.004  1.00112.03           C  
ANISOU 1303  C   LEU A 176    14230  21104   7232    666  -1597   1249       C  
ATOM   1304  O   LEU A 176      41.732 -51.813 267.913  1.00100.04           O  
ANISOU 1304  O   LEU A 176    12730  19784   5497    696  -1721   1236       O  
ATOM   1305  CB  LEU A 176      44.489 -52.772 268.295  1.00 98.03           C  
ANISOU 1305  CB  LEU A 176    12729  19335   5182    844  -1288   1038       C  
ATOM   1306  N   ASP A 177      41.646 -51.934 270.157  1.00 94.38           N  
ANISOU 1306  N   ASP A 177    11907  18721   5233    536  -1687   1198       N  
ATOM   1307  CA  ASP A 177      40.194 -52.060 270.198  1.00 95.39           C  
ANISOU 1307  CA  ASP A 177    11923  18931   5390    413  -1934   1135       C  
ATOM   1308  C   ASP A 177      39.537 -50.802 270.763  1.00114.06           C  
ANISOU 1308  C   ASP A 177    14056  21293   7987    453  -1949   1456       C  
ATOM   1309  O   ASP A 177      38.317 -50.740 270.901  1.00 95.01           O  
ANISOU 1309  O   ASP A 177    11496  18970   5634    380  -2133   1449       O  
ATOM   1310  CB  ASP A 177      39.783 -53.287 271.016  1.00 94.24           C  
ANISOU 1310  CB  ASP A 177    11850  18642   5314    208  -2054    802       C  
ATOM   1311  CG  ASP A 177      40.409 -53.312 272.402  1.00109.89           C  
ANISOU 1311  CG  ASP A 177    13824  20380   7548    172  -1913    811       C  
ATOM   1312  OD1 ASP A 177      40.756 -52.240 272.943  1.00102.70           O  
ANISOU 1312  OD1 ASP A 177    12783  19413   6823    265  -1778   1101       O  
ATOM   1313  OD2 ASP A 177      40.547 -54.421 272.958  1.00108.88           O  
ANISOU 1313  OD2 ASP A 177    13841  20098   7429     44  -1944    522       O  
ATOM   1314  N   GLY A 178      40.350 -49.805 271.097  1.00108.96           N  
ANISOU 1314  N   GLY A 178    13383  20541   7475    570  -1755   1735       N  
ATOM   1315  CA  GLY A 178      39.832 -48.544 271.597  1.00106.54           C  
ANISOU 1315  CA  GLY A 178    12915  20185   7381    642  -1758   2049       C  
ATOM   1316  C   GLY A 178      40.045 -48.343 273.086  1.00104.84           C  
ANISOU 1316  C   GLY A 178    12644  19726   7466    589  -1679   2096       C  
ATOM   1317  O   GLY A 178      40.022 -47.213 273.574  1.00114.53           O  
ANISOU 1317  O   GLY A 178    13798  20839   8877    677  -1618   2377       O  
ATOM   1318  N   ARG A 179      40.254 -49.438 273.811  1.00 93.98           N  
ANISOU 1318  N   ARG A 179    11327  18252   6131    449  -1683   1818       N  
ATOM   1319  CA  ARG A 179      40.444 -49.373 275.259  1.00 95.40           C  
ANISOU 1319  CA  ARG A 179    11461  18211   6578    386  -1617   1835       C  
ATOM   1320  C   ARG A 179      41.760 -48.703 275.635  1.00 92.85           C  
ANISOU 1320  C   ARG A 179    11205  17702   6372    467  -1379   2027       C  
ATOM   1321  O   ARG A 179      42.660 -48.564 274.807  1.00 91.73           O  
ANISOU 1321  O   ARG A 179    11152  17636   6064    542  -1258   2095       O  
ATOM   1322  CB  ARG A 179      40.384 -50.774 275.875  1.00 85.48           C  
ANISOU 1322  CB  ARG A 179    10287  16827   5365    205  -1665   1465       C  
ATOM   1323  CG  ARG A 179      39.009 -51.414 275.821  1.00 95.32           C  
ANISOU 1323  CG  ARG A 179    11437  18227   6553     52  -1909   1289       C  
ATOM   1324  CD  ARG A 179      39.055 -52.877 276.230  1.00100.15           C  
ANISOU 1324  CD  ARG A 179    12201  18677   7175   -152  -1954    915       C  
ATOM   1325  NE  ARG A 179      37.729 -53.490 276.191  1.00110.17           N  
ANISOU 1325  NE  ARG A 179    13370  20099   8388   -354  -2195    758       N  
ATOM   1326  CZ  ARG A 179      37.500 -54.790 276.348  1.00118.24           C  
ANISOU 1326  CZ  ARG A 179    14536  21028   9362   -579  -2299    436       C  
ATOM   1327  NH1 ARG A 179      36.259 -55.254 276.298  1.00114.29           N  
ANISOU 1327  NH1 ARG A 179    13917  20692   8816   -797  -2523    326       N  
ATOM   1328  NH2 ARG A 179      38.509 -55.626 276.553  1.00128.91           N  
ANISOU 1328  NH2 ARG A 179    16155  22119  10708   -587  -2180    228       N  
ATOM   1329  N   ILE A 180      41.861 -48.285 276.893  1.00 95.48           N  
ANISOU 1329  N   ILE A 180    11490  17717   7071    433  -1293   2084       N  
ATOM   1330  CA  ILE A 180      43.077 -47.668 277.408  1.00 91.16           C  
ANISOU 1330  CA  ILE A 180    10995  16945   6695    464  -1078   2240       C  
ATOM   1331  C   ILE A 180      43.532 -48.375 278.682  1.00 84.90           C  
ANISOU 1331  C   ILE A 180    10238  15842   6178    357   -990   2017       C  
ATOM   1332  O   ILE A 180      42.847 -48.336 279.703  1.00 86.25           O  
ANISOU 1332  O   ILE A 180    10340  15823   6610    300  -1043   1969       O  
ATOM   1333  CB  ILE A 180      42.874 -46.169 277.698  1.00 90.93           C  
ANISOU 1333  CB  ILE A 180    10906  16802   6842    551  -1053   2593       C  
ATOM   1334  CG1 ILE A 180      42.425 -45.435 276.432  1.00 79.95           C  
ANISOU 1334  CG1 ILE A 180     9500  15708   5168    678  -1143   2842       C  
ATOM   1335  CG2 ILE A 180      44.150 -45.559 278.255  1.00 84.47           C  
ANISOU 1335  CG2 ILE A 180    10150  15743   6201    532   -847   2743       C  
ATOM   1336  CD1 ILE A 180      42.137 -43.967 276.641  1.00 80.49           C  
ANISOU 1336  CD1 ILE A 180     9553  15646   5383    791  -1142   3194       C  
ATOM   1337  N   MET A 181      44.687 -49.028 278.613  1.00 84.66           N  
ANISOU 1337  N   MET A 181    10311  15784   6072    350   -855   1886       N  
ATOM   1338  CA  MET A 181      45.210 -49.770 279.753  1.00 92.66           C  
ANISOU 1338  CA  MET A 181    11376  16521   7310    275   -773   1673       C  
ATOM   1339  C   MET A 181      45.992 -48.878 280.711  1.00100.34           C  
ANISOU 1339  C   MET A 181    12306  17248   8569    275   -618   1862       C  
ATOM   1340  O   MET A 181      46.651 -47.929 280.290  1.00104.48           O  
ANISOU 1340  O   MET A 181    12810  17839   9050    325   -520   2122       O  
ATOM   1341  CB  MET A 181      46.103 -50.920 279.281  1.00 89.20           C  
ANISOU 1341  CB  MET A 181    11076  16166   6651    306   -704   1433       C  
ATOM   1342  CG  MET A 181      45.358 -52.058 278.608  1.00 95.66           C  
ANISOU 1342  CG  MET A 181    11996  17127   7224    268   -871   1158       C  
ATOM   1343  SD  MET A 181      46.420 -53.487 278.317  1.00136.92           S  
ANISOU 1343  SD  MET A 181    17443  22349  12231    339   -789    831       S  
ATOM   1344  CE  MET A 181      47.697 -52.756 277.297  1.00 84.96           C  
ANISOU 1344  CE  MET A 181    10821  16060   5400    524   -597   1065       C  
ATOM   1345  N   CYS A 182      45.910 -49.192 282.000  1.00 95.04           N  
ANISOU 1345  N   CYS A 182    11632  16296   8180    202   -604   1732       N  
ATOM   1346  CA  CYS A 182      46.703 -48.515 283.019  1.00 90.90           C  
ANISOU 1346  CA  CYS A 182    11088  15526   7925    186   -469   1854       C  
ATOM   1347  C   CYS A 182      47.599 -49.525 283.722  1.00 87.12           C  
ANISOU 1347  C   CYS A 182    10678  14911   7513    158   -374   1622       C  
ATOM   1348  O   CYS A 182      47.180 -50.174 284.682  1.00 98.65           O  
ANISOU 1348  O   CYS A 182    12165  16174   9142     97   -416   1437       O  
ATOM   1349  CB  CYS A 182      45.800 -47.810 284.029  1.00 92.89           C  
ANISOU 1349  CB  CYS A 182    11274  15561   8459    158   -534   1937       C  
ATOM   1350  SG  CYS A 182      46.671 -47.146 285.464  1.00131.16           S  
ANISOU 1350  SG  CYS A 182    16128  20065  13644    119   -398   2017       S  
ATOM   1351  N   TYR A 183      48.832 -49.657 283.244  1.00 73.65           N  
ANISOU 1351  N   TYR A 183     8995  13327   5661    215   -242   1644       N  
ATOM   1352  CA  TYR A 183      49.720 -50.704 283.732  1.00 68.46           C  
ANISOU 1352  CA  TYR A 183     8408  12597   5007    243   -156   1416       C  
ATOM   1353  C   TYR A 183      51.188 -50.283 283.672  1.00 70.93           C  
ANISOU 1353  C   TYR A 183     8657  13001   5290    290     23   1554       C  
ATOM   1354  O   TYR A 183      51.497 -49.114 283.437  1.00 65.72           O  
ANISOU 1354  O   TYR A 183     7908  12401   4662    252     79   1836       O  
ATOM   1355  CB  TYR A 183      49.496 -51.983 282.923  1.00 73.87           C  
ANISOU 1355  CB  TYR A 183     9224  13432   5411    304   -226   1153       C  
ATOM   1356  CG  TYR A 183      49.813 -53.257 283.668  1.00 81.29           C  
ANISOU 1356  CG  TYR A 183    10300  14183   6404    320   -216    858       C  
ATOM   1357  CD1 TYR A 183      49.316 -53.478 284.944  1.00 87.75           C  
ANISOU 1357  CD1 TYR A 183    11133  14703   7504    217   -262    773       C  
ATOM   1358  CD2 TYR A 183      50.596 -54.244 283.088  1.00 83.11           C  
ANISOU 1358  CD2 TYR A 183    10658  14533   6386    457   -160    667       C  
ATOM   1359  CE1 TYR A 183      49.601 -54.645 285.628  1.00 83.00           C  
ANISOU 1359  CE1 TYR A 183    10680  13912   6942    231   -256    523       C  
ATOM   1360  CE2 TYR A 183      50.885 -55.413 283.761  1.00 89.83           C  
ANISOU 1360  CE2 TYR A 183    11672  15184   7277    497   -159    403       C  
ATOM   1361  CZ  TYR A 183      50.386 -55.609 285.031  1.00 87.69           C  
ANISOU 1361  CZ  TYR A 183    11423  14601   7294    375   -209    340       C  
ATOM   1362  OH  TYR A 183      50.671 -56.773 285.706  1.00 88.38           O  
ANISOU 1362  OH  TYR A 183    11695  14472   7413    415   -210     97       O  
ATOM   1363  N   TYR A 184      52.086 -51.241 283.890  1.00 77.04           N  
ANISOU 1363  N   TYR A 184     9481  13791   5999    372    107   1359       N  
ATOM   1364  CA  TYR A 184      53.523 -50.975 283.877  1.00 84.87           C  
ANISOU 1364  CA  TYR A 184    10376  14924   6948    425    279   1468       C  
ATOM   1365  C   TYR A 184      54.030 -50.546 282.499  1.00 89.41           C  
ANISOU 1365  C   TYR A 184    10886  15870   7216    488    358   1645       C  
ATOM   1366  O   TYR A 184      53.576 -51.051 281.474  1.00 79.27           O  
ANISOU 1366  O   TYR A 184     9685  14772   5661    573    300   1551       O  
ATOM   1367  CB  TYR A 184      54.313 -52.213 284.325  1.00 84.74           C  
ANISOU 1367  CB  TYR A 184    10431  14881   6884    555    341   1201       C  
ATOM   1368  CG  TYR A 184      54.047 -52.701 285.736  1.00 81.10           C  
ANISOU 1368  CG  TYR A 184    10039  14072   6704    505    290   1038       C  
ATOM   1369  CD1 TYR A 184      54.702 -52.140 286.824  1.00 74.78           C  
ANISOU 1369  CD1 TYR A 184     9131  13132   6151    441    361   1142       C  
ATOM   1370  CD2 TYR A 184      53.168 -53.751 285.973  1.00 83.97           C  
ANISOU 1370  CD2 TYR A 184    10582  14256   7068    508    168    783       C  
ATOM   1371  CE1 TYR A 184      54.472 -52.596 288.111  1.00 75.20           C  
ANISOU 1371  CE1 TYR A 184     9252  12885   6437    407    317    998       C  
ATOM   1372  CE2 TYR A 184      52.933 -54.214 287.255  1.00 88.30           C  
ANISOU 1372  CE2 TYR A 184    11199  14498   7855    454    131    653       C  
ATOM   1373  CZ  TYR A 184      53.587 -53.633 288.320  1.00 82.84           C  
ANISOU 1373  CZ  TYR A 184    10396  13683   7397    418    209    762       C  
ATOM   1374  OH  TYR A 184      53.356 -54.090 289.597  1.00 73.88           O  
ANISOU 1374  OH  TYR A 184     9333  12259   6478    375    174    639       O  
ATOM   1375  N   ASN A 185      54.977 -49.612 282.492  1.00 91.43           N  
ANISOU 1375  N   ASN A 185    10995  16238   7504    428    488   1905       N  
ATOM   1376  CA  ASN A 185      55.736 -49.273 281.292  1.00 81.66           C  
ANISOU 1376  CA  ASN A 185     9670  15389   5967    482    608   2085       C  
ATOM   1377  C   ASN A 185      57.196 -49.055 281.672  1.00 81.78           C  
ANISOU 1377  C   ASN A 185     9518  15542   6011    463    783   2190       C  
ATOM   1378  O   ASN A 185      57.619 -47.931 281.945  1.00 70.62           O  
ANISOU 1378  O   ASN A 185     7990  14098   4743    287    837   2470       O  
ATOM   1379  CB  ASN A 185      55.165 -48.032 280.600  1.00 86.00           C  
ANISOU 1379  CB  ASN A 185    10199  15992   6486    369    565   2405       C  
ATOM   1380  CG  ASN A 185      55.892 -47.697 279.297  1.00101.93           C  
ANISOU 1380  CG  ASN A 185    12137  18431   8162    415    690   2611       C  
ATOM   1381  OD1 ASN A 185      56.669 -48.500 278.778  1.00 75.96           O  
ANISOU 1381  OD1 ASN A 185     8814  15413   4635    563    793   2469       O  
ATOM   1382  ND2 ASN A 185      55.633 -46.508 278.765  1.00 96.41           N  
ANISOU 1382  ND2 ASN A 185    11418  17765   7447    301    679   2940       N  
ATOM   1383  N   VAL A 186      57.959 -50.145 281.687  1.00 77.49           N  
ANISOU 1383  N   VAL A 186     8968  15151   5321    647    864   1960       N  
ATOM   1384  CA  VAL A 186      59.342 -50.131 282.155  1.00 82.74           C  
ANISOU 1384  CA  VAL A 186     9451  15977   6011    666   1020   2012       C  
ATOM   1385  C   VAL A 186      60.292 -49.412 281.196  1.00 92.88           C  
ANISOU 1385  C   VAL A 186    10536  17696   7059    629   1182   2301       C  
ATOM   1386  O   VAL A 186      61.458 -49.185 281.521  1.00 93.72           O  
ANISOU 1386  O   VAL A 186    10438  17957   7212    590   1305   2395       O  
ATOM   1387  CB  VAL A 186      59.867 -51.565 282.373  1.00 94.02           C  
ANISOU 1387  CB  VAL A 186    10944  17467   7311    934   1059   1677       C  
ATOM   1388  CG1 VAL A 186      60.919 -51.584 283.468  1.00101.20           C  
ANISOU 1388  CG1 VAL A 186    11697  18351   8405    925   1144   1678       C  
ATOM   1389  CG2 VAL A 186      58.724 -52.503 282.723  1.00 96.95           C  
ANISOU 1389  CG2 VAL A 186    11581  17499   7757    998    891   1376       C  
ATOM   1390  N   LEU A 187      59.797 -49.062 280.013  1.00 89.08           N  
ANISOU 1390  N   LEU A 187    10107  17328   6413    628   1150   2404       N  
ATOM   1391  CA  LEU A 187      60.625 -48.392 279.018  1.00 84.70           C  
ANISOU 1391  CA  LEU A 187     9388  17041   5754    578   1259   2623       C  
ATOM   1392  C   LEU A 187      60.338 -46.898 278.955  1.00 85.04           C  
ANISOU 1392  C   LEU A 187     9400  16957   5953    296   1230   2987       C  
ATOM   1393  O   LEU A 187      60.949 -46.175 278.168  1.00 82.87           O  
ANISOU 1393  O   LEU A 187     9010  16865   5612    204   1309   3210       O  
ATOM   1394  CB  LEU A 187      60.413 -49.015 277.638  1.00101.44           C  
ANISOU 1394  CB  LEU A 187    11592  19381   7571    785   1255   2490       C  
ATOM   1395  CG  LEU A 187      60.846 -50.469 277.460  1.00104.71           C  
ANISOU 1395  CG  LEU A 187    12064  19928   7793   1089   1292   2136       C  
ATOM   1396  CD1 LEU A 187      60.593 -50.916 276.029  1.00109.52           C  
ANISOU 1396  CD1 LEU A 187    12773  20735   8106   1258   1277   2038       C  
ATOM   1397  CD2 LEU A 187      62.311 -50.641 277.835  1.00 89.41           C  
ANISOU 1397  CD2 LEU A 187     9897  18195   5880   1160   1447   2145       C  
ATOM   1398  N   LEU A 188      59.406 -46.445 279.787  1.00 77.40           N  
ANISOU 1398  N   LEU A 188     8552  15666   5190    169   1113   3045       N  
ATOM   1399  CA  LEU A 188      58.947 -45.059 279.758  1.00 97.25           C  
ANISOU 1399  CA  LEU A 188    11105  17986   7858    -57   1055   3366       C  
ATOM   1400  C   LEU A 188      60.078 -44.060 279.992  1.00 98.49           C  
ANISOU 1400  C   LEU A 188    11103  18165   8156   -293   1159   3629       C  
ATOM   1401  O   LEU A 188      60.149 -43.029 279.322  1.00 99.11           O  
ANISOU 1401  O   LEU A 188    11187  18242   8228   -438   1167   3896       O  
ATOM   1402  CB  LEU A 188      57.846 -44.846 280.799  1.00 92.49           C  
ANISOU 1402  CB  LEU A 188    10647  16999   7494   -117    909   3336       C  
ATOM   1403  CG  LEU A 188      57.203 -43.457 280.826  1.00 86.28           C  
ANISOU 1403  CG  LEU A 188     9953  15960   6868   -292    825   3643       C  
ATOM   1404  CD1 LEU A 188      56.542 -43.147 279.491  1.00 80.41           C  
ANISOU 1404  CD1 LEU A 188     9288  15355   5909   -214    773   3758       C  
ATOM   1405  CD2 LEU A 188      56.200 -43.355 281.965  1.00 80.98           C  
ANISOU 1405  CD2 LEU A 188     9406  14833   6530   -302    670   3501       C  
ATOM   1406  N   LEU A 189      60.961 -44.371 280.935  1.00101.94           N  
ANISOU 1406  N   LEU A 189    11402  18622   8710   -337   1231   3548       N  
ATOM   1407  CA  LEU A 189      62.051 -43.465 281.283  1.00 99.53           C  
ANISOU 1407  CA  LEU A 189    10930  18337   8549   -594   1306   3773       C  
ATOM   1408  C   LEU A 189      63.406 -44.169 281.310  1.00107.22           C  
ANISOU 1408  C   LEU A 189    11653  19660   9425   -507   1438   3654       C  
ATOM   1409  O   LEU A 189      63.539 -45.260 281.866  1.00113.73           O  
ANISOU 1409  O   LEU A 189    12452  20542  10217   -303   1456   3387       O  
ATOM   1410  CB  LEU A 189      61.781 -42.806 282.637  1.00100.57           C  
ANISOU 1410  CB  LEU A 189    11133  18089   8990   -807   1228   3854       C  
ATOM   1411  N   ASN A 190      64.400 -43.525 280.704  1.00121.05           N  
ANISOU 1411  N   ASN A 190    13227  21644  11123   -654   1525   3859       N  
ATOM   1412  CA  ASN A 190      65.779 -44.015 280.667  1.00124.15           C  
ANISOU 1412  CA  ASN A 190    13339  22412  11420   -591   1645   3799       C  
ATOM   1413  C   ASN A 190      65.945 -45.466 280.206  1.00122.70           C  
ANISOU 1413  C   ASN A 190    13122  22507  10991   -193   1704   3493       C  
ATOM   1414  O   ASN A 190      66.395 -46.313 280.979  1.00136.92           O  
ANISOU 1414  O   ASN A 190    14845  24360  12818    -36   1727   3281       O  
ATOM   1415  CB  ASN A 190      66.422 -43.852 282.047  1.00130.32           C  
ANISOU 1415  CB  ASN A 190    13994  23083  12439   -760   1635   3792       C  
ATOM   1416  N   PRO A 191      65.592 -45.759 278.944  1.00118.90           N  
ANISOU 1416  N   PRO A 191    12719  22191  10265    -19   1723   3462       N  
ATOM   1417  CA  PRO A 191      65.821 -47.113 278.434  1.00116.44           C  
ANISOU 1417  CA  PRO A 191    12403  22128   9710    359   1774   3165       C  
ATOM   1418  C   PRO A 191      67.259 -47.301 277.960  1.00133.47           C  
ANISOU 1418  C   PRO A 191    14267  24726  11719    446   1909   3205       C  
ATOM   1419  O   PRO A 191      67.811 -46.421 277.297  1.00137.34           O  
ANISOU 1419  O   PRO A 191    14606  25411  12164    254   1968   3474       O  
ATOM   1420  CB  PRO A 191      64.838 -47.214 277.268  1.00104.19           C  
ANISOU 1420  CB  PRO A 191    11059  20564   7964    469   1723   3139       C  
ATOM   1421  CG  PRO A 191      64.742 -45.815 276.756  1.00105.52           C  
ANISOU 1421  CG  PRO A 191    11202  20701   8191    170   1719   3501       C  
ATOM   1422  CD  PRO A 191      64.923 -44.902 277.947  1.00115.73           C  
ANISOU 1422  CD  PRO A 191    12442  21734   9795   -142   1687   3681       C  
ATOM   1423  N   GLY A 192      67.860 -48.434 278.301  1.00136.32           N  
ANISOU 1423  N   GLY A 192    14555  25241  11999    739   1952   2944       N  
ATOM   1424  CA  GLY A 192      69.229 -48.709 277.907  1.00142.07           C  
ANISOU 1424  CA  GLY A 192    14993  26411  12576    871   2070   2964       C  
ATOM   1425  C   GLY A 192      69.353 -49.018 276.428  1.00145.59           C  
ANISOU 1425  C   GLY A 192    15439  27163  12714   1077   2138   2951       C  
ATOM   1426  O   GLY A 192      68.350 -49.058 275.714  1.00149.74           O  
ANISOU 1426  O   GLY A 192    16203  27547  13143   1118   2086   2910       O  
ATOM   1427  N   PRO A 193      70.591 -49.234 275.956  1.00132.60           N  
ANISOU 1427  N   PRO A 193    13519  25959  10904   1211   2249   2988       N  
ATOM   1428  CA  PRO A 193      70.863 -49.620 274.566  1.00133.27           C  
ANISOU 1428  CA  PRO A 193    13577  26388  10672   1447   2329   2961       C  
ATOM   1429  C   PRO A 193      70.147 -50.912 274.178  1.00141.94           C  
ANISOU 1429  C   PRO A 193    14971  27365  11597   1843   2285   2598       C  
ATOM   1430  O   PRO A 193      69.820 -51.113 273.008  1.00150.76           O  
ANISOU 1430  O   PRO A 193    16198  28605  12479   1979   2303   2562       O  
ATOM   1431  CB  PRO A 193      72.382 -49.811 274.546  1.00127.26           C  
ANISOU 1431  CB  PRO A 193    12452  26095   9807   1562   2439   3014       C  
ATOM   1432  CG  PRO A 193      72.880 -48.954 275.655  1.00123.38           C  
ANISOU 1432  CG  PRO A 193    11762  25529   9586   1206   2416   3216       C  
ATOM   1433  CD  PRO A 193      71.832 -49.038 276.724  1.00119.98           C  
ANISOU 1433  CD  PRO A 193    11598  24583   9406   1122   2298   3083       C  
ATOM   1434  N   ASP A 194      69.913 -51.774 275.162  1.00137.92           N  
ANISOU 1434  N   ASP A 194    14601  26603  11198   2014   2221   2331       N  
ATOM   1435  CA  ASP A 194      69.183 -53.018 274.945  1.00138.09           C  
ANISOU 1435  CA  ASP A 194    14951  26431  11085   2349   2154   1970       C  
ATOM   1436  C   ASP A 194      67.807 -52.940 275.603  1.00128.62           C  
ANISOU 1436  C   ASP A 194    14052  24748  10071   2183   2014   1888       C  
ATOM   1437  O   ASP A 194      67.691 -52.999 276.829  1.00123.89           O  
ANISOU 1437  O   ASP A 194    13475  23905   9694   2104   1966   1836       O  
ATOM   1438  CB  ASP A 194      69.976 -54.208 275.495  1.00137.91           C  
ANISOU 1438  CB  ASP A 194    14902  26484  11014   2719   2181   1704       C  
ATOM   1439  CG  ASP A 194      69.482 -55.545 274.964  1.00132.64           C  
ANISOU 1439  CG  ASP A 194    14572  25687  10138   3104   2130   1339       C  
ATOM   1440  OD1 ASP A 194      68.267 -55.688 274.709  1.00139.04           O  
ANISOU 1440  OD1 ASP A 194    15695  26195  10937   3040   2026   1225       O  
ATOM   1441  OD2 ASP A 194      70.316 -56.460 274.804  1.00123.33           O  
ANISOU 1441  OD2 ASP A 194    13353  24705   8804   3469   2182   1166       O  
ATOM   1442  N   ARG A 195      66.771 -52.803 274.782  1.00122.48           N  
ANISOU 1442  N   ARG A 195    13493  23855   9188   2133   1945   1881       N  
ATOM   1443  CA  ARG A 195      65.402 -52.743 275.277  1.00115.70           C  
ANISOU 1443  CA  ARG A 195    12910  22583   8469   1988   1797   1808       C  
ATOM   1444  C   ARG A 195      64.993 -54.065 275.909  1.00115.67           C  
ANISOU 1444  C   ARG A 195    13169  22320   8461   2235   1713   1427       C  
ATOM   1445  O   ARG A 195      64.394 -54.091 276.983  1.00118.14           O  
ANISOU 1445  O   ARG A 195    13593  22317   8979   2120   1627   1369       O  
ATOM   1446  CB  ARG A 195      64.426 -52.393 274.151  1.00121.91           C  
ANISOU 1446  CB  ARG A 195    13860  23356   9103   1917   1727   1871       C  
ATOM   1447  CG  ARG A 195      64.754 -51.127 273.383  1.00121.82           C  
ANISOU 1447  CG  ARG A 195    13644  23578   9064   1693   1802   2243       C  
ATOM   1448  CD  ARG A 195      63.602 -50.755 272.462  1.00120.42           C  
ANISOU 1448  CD  ARG A 195    13663  23319   8773   1618   1702   2304       C  
ATOM   1449  NE  ARG A 195      63.962 -49.698 271.523  1.00123.20           N  
ANISOU 1449  NE  ARG A 195    13857  23918   9036   1465   1781   2633       N  
ATOM   1450  CZ  ARG A 195      64.414 -49.916 270.292  1.00118.85           C  
ANISOU 1450  CZ  ARG A 195    13257  23703   8200   1628   1863   2634       C  
ATOM   1451  NH1 ARG A 195      64.562 -51.157 269.849  1.00110.93           N  
ANISOU 1451  NH1 ARG A 195    12358  22815   6976   1958   1872   2313       N  
ATOM   1452  NH2 ARG A 195      64.718 -48.895 269.504  1.00120.49           N  
ANISOU 1452  NH2 ARG A 195    13329  24116   8337   1462   1933   2955       N  
ATOM   1453  N   ASP A 196      65.321 -55.159 275.229  1.00110.57           N  
ANISOU 1453  N   ASP A 196    12637  21798   7575   2574   1736   1171       N  
ATOM   1454  CA  ASP A 196      64.955 -56.498 275.677  1.00119.89           C  
ANISOU 1454  CA  ASP A 196    14124  22707   8723   2824   1647    794       C  
ATOM   1455  C   ASP A 196      65.570 -56.827 277.033  1.00121.36           C  
ANISOU 1455  C   ASP A 196    14231  22775   9107   2887   1672    729       C  
ATOM   1456  O   ASP A 196      64.938 -57.469 277.871  1.00116.52           O  
ANISOU 1456  O   ASP A 196    13864  21808   8600   2914   1568    520       O  
ATOM   1457  CB  ASP A 196      65.386 -57.539 274.642  1.00125.81           C  
ANISOU 1457  CB  ASP A 196    14998  23631   9173   3188   1681    560       C  
ATOM   1458  CG  ASP A 196      64.918 -58.939 274.990  1.00128.08           C  
ANISOU 1458  CG  ASP A 196    15670  23580   9414   3427   1567    165       C  
ATOM   1459  OD1 ASP A 196      63.842 -59.345 274.501  1.00125.32           O  
ANISOU 1459  OD1 ASP A 196    15632  23020   8966   3389   1435     -3       O  
ATOM   1460  OD2 ASP A 196      65.625 -59.635 275.749  1.00127.31           O  
ANISOU 1460  OD2 ASP A 196    15571  23422   9377   3643   1599     28       O  
ATOM   1461  N   ALA A 197      66.805 -56.383 277.241  1.00120.20           N  
ANISOU 1461  N   ALA A 197    13734  22934   9002   2901   1801    914       N  
ATOM   1462  CA  ALA A 197      67.517 -56.650 278.485  1.00112.57           C  
ANISOU 1462  CA  ALA A 197    12649  21918   8206   2972   1826    872       C  
ATOM   1463  C   ALA A 197      66.947 -55.835 279.642  1.00106.87           C  
ANISOU 1463  C   ALA A 197    11896  20934   7775   2625   1769   1023       C  
ATOM   1464  O   ALA A 197      66.680 -56.371 280.719  1.00105.06           O  
ANISOU 1464  O   ALA A 197    11815  20423   7682   2676   1706    858       O  
ATOM   1465  CB  ALA A 197      68.999 -56.363 278.315  1.00101.13           C  
ANISOU 1465  CB  ALA A 197    10807  20919   6700   3062   1962   1040       C  
ATOM   1466  N   THR A 198      66.764 -54.539 279.414  1.00 99.66           N  
ANISOU 1466  N   THR A 198    10810  20103   6953   2279   1789   1339       N  
ATOM   1467  CA  THR A 198      66.250 -53.647 280.447  1.00101.86           C  
ANISOU 1467  CA  THR A 198    11058  20139   7506   1939   1736   1513       C  
ATOM   1468  C   THR A 198      64.767 -53.891 280.713  1.00 95.42           C  
ANISOU 1468  C   THR A 198    10581  18931   6744   1873   1593   1373       C  
ATOM   1469  O   THR A 198      64.255 -53.534 281.772  1.00 97.14           O  
ANISOU 1469  O   THR A 198    10840  18891   7176   1686   1532   1418       O  
ATOM   1470  CB  THR A 198      66.462 -52.170 280.071  1.00115.72           C  
ANISOU 1470  CB  THR A 198    12577  22049   9344   1586   1782   1898       C  
ATOM   1471  OG1 THR A 198      65.913 -51.923 278.772  1.00130.89           O  
ANISOU 1471  OG1 THR A 198    14593  24053  11085   1576   1770   1964       O  
ATOM   1472  CG2 THR A 198      67.944 -51.834 280.056  1.00120.42           C  
ANISOU 1472  CG2 THR A 198    12809  23019   9926   1576   1902   2058       C  
ATOM   1473  N   CYS A 199      64.080 -54.494 279.747  1.00101.52           N  
ANISOU 1473  N   CYS A 199    11586  19673   7313   2018   1532   1204       N  
ATOM   1474  CA  CYS A 199      62.683 -54.877 279.933  1.00101.18           C  
ANISOU 1474  CA  CYS A 199    11863  19292   7288   1969   1374   1038       C  
ATOM   1475  C   CYS A 199      62.566 -55.985 280.965  1.00100.74           C  
ANISOU 1475  C   CYS A 199    12012  18968   7296   2139   1315    739       C  
ATOM   1476  O   CYS A 199      61.643 -55.998 281.777  1.00100.78           O  
ANISOU 1476  O   CYS A 199    12175  18677   7439   2004   1204    685       O  
ATOM   1477  CB  CYS A 199      62.055 -55.336 278.615  1.00105.34           C  
ANISOU 1477  CB  CYS A 199    12589  19873   7564   2081   1311    907       C  
ATOM   1478  SG  CYS A 199      61.103 -54.073 277.751  1.00108.68           S  
ANISOU 1478  SG  CYS A 199    12974  20344   7977   1791   1247   1202       S  
ATOM   1479  N   ASN A 200      63.513 -56.914 280.925  1.00 99.90           N  
ANISOU 1479  N   ASN A 200    11907  18967   7083   2448   1385    552       N  
ATOM   1480  CA  ASN A 200      63.483 -58.078 281.797  1.00102.60           C  
ANISOU 1480  CA  ASN A 200    12486  19036   7462   2658   1327    255       C  
ATOM   1481  C   ASN A 200      64.122 -57.804 283.154  1.00100.05           C  
ANISOU 1481  C   ASN A 200    11979  18678   7359   2611   1380    342       C  
ATOM   1482  O   ASN A 200      63.607 -58.230 284.187  1.00 93.32           O  
ANISOU 1482  O   ASN A 200    11314  17510   6632   2597   1298    205       O  
ATOM   1483  CB  ASN A 200      64.183 -59.257 281.118  1.00 97.97           C  
ANISOU 1483  CB  ASN A 200    12024  18544   6657   3046   1362      9       C  
ATOM   1484  CG  ASN A 200      63.981 -60.563 281.860  1.00108.64           C  
ANISOU 1484  CG  ASN A 200    13718  19533   8028   3265   1271   -317       C  
ATOM   1485  OD1 ASN A 200      63.082 -60.684 282.692  1.00121.22           O  
ANISOU 1485  OD1 ASN A 200    15513  20787   9759   3111   1158   -397       O  
ATOM   1486  ND2 ASN A 200      64.815 -61.551 281.558  1.00103.21           N  
ANISOU 1486  ND2 ASN A 200    13108  18908   7198   3630   1312   -499       N  
ATOM   1487  N   SER A 201      65.243 -57.088 283.141  1.00 99.52           N  
ANISOU 1487  N   SER A 201    11542  18941   7330   2573   1509    573       N  
ATOM   1488  CA  SER A 201      66.010 -56.830 284.355  1.00105.41           C  
ANISOU 1488  CA  SER A 201    12074  19714   8264   2534   1559    658       C  
ATOM   1489  C   SER A 201      65.226 -56.003 285.369  1.00107.90           C  
ANISOU 1489  C   SER A 201    12398  19765   8836   2189   1491    799       C  
ATOM   1490  O   SER A 201      65.159 -56.355 286.546  1.00104.48           O  
ANISOU 1490  O   SER A 201    12047  19014   8639   2186   1414    685       O  
ATOM   1491  CB  SER A 201      67.323 -56.121 284.015  1.00 99.90           C  
ANISOU 1491  CB  SER A 201    10958  19453   7548   2497   1688    901       C  
ATOM   1492  OG  SER A 201      67.087 -54.817 283.515  1.00108.36           O  
ANISOU 1492  OG  SER A 201    11860  20637   8675   2143   1711   1208       O  
ATOM   1493  N   ARG A 202      64.633 -54.906 284.910  1.00102.47           N  
ANISOU 1493  N   ARG A 202    11642  19067   8225   1874   1466   1036       N  
ATOM   1494  CA  ARG A 202      63.936 -53.998 285.812  1.00105.63           C  
ANISOU 1494  CA  ARG A 202    12043  19090   9000   1519   1353   1178       C  
ATOM   1495  C   ARG A 202      62.530 -54.483 286.155  1.00106.81           C  
ANISOU 1495  C   ARG A 202    12526  18758   9299   1474   1175    982       C  
ATOM   1496  O   ARG A 202      61.930 -54.023 287.128  1.00106.52           O  
ANISOU 1496  O   ARG A 202    12528  18370   9575   1258   1076   1022       O  
ATOM   1497  CB  ARG A 202      63.878 -52.591 285.213  1.00109.20           C  
ANISOU 1497  CB  ARG A 202    12313  19704   9474   1218   1392   1525       C  
ATOM   1498  CG  ARG A 202      65.201 -51.846 285.290  1.00118.67           C  
ANISOU 1498  CG  ARG A 202    13154  21283  10651   1113   1539   1776       C  
ATOM   1499  CD  ARG A 202      65.017 -50.347 285.117  1.00120.23           C  
ANISOU 1499  CD  ARG A 202    13237  21458  10987    729   1533   2127       C  
ATOM   1500  NE  ARG A 202      64.692 -49.982 283.743  1.00122.94           N  
ANISOU 1500  NE  ARG A 202    13609  21980  11122    712   1559   2259       N  
ATOM   1501  CZ  ARG A 202      64.623 -48.730 283.302  1.00123.74           C  
ANISOU 1501  CZ  ARG A 202    13633  22083  11298    424   1556   2566       C  
ATOM   1502  NH1 ARG A 202      64.859 -47.721 284.129  1.00122.01           N  
ANISOU 1502  NH1 ARG A 202    13312  21726  11321    118   1543   2783       N  
ATOM   1503  NH2 ARG A 202      64.321 -48.487 282.034  1.00126.51           N  
ANISOU 1503  NH2 ARG A 202    14032  22555  11481    443   1559   2651       N  
ATOM   1504  N   GLN A 203      62.004 -55.412 285.363  1.00104.86           N  
ANISOU 1504  N   GLN A 203    12515  18508   8818   1670   1133    767       N  
ATOM   1505  CA  GLN A 203      60.703 -56.000 285.663  1.00101.13           C  
ANISOU 1505  CA  GLN A 203    12350  17614   8460   1614    961    566       C  
ATOM   1506  C   GLN A 203      60.831 -57.006 286.799  1.00100.75           C  
ANISOU 1506  C   GLN A 203    12466  17269   8547   1747    913    330       C  
ATOM   1507  O   GLN A 203      60.006 -57.038 287.714  1.00 85.27           O  
ANISOU 1507  O   GLN A 203    10628  14925   6846   1582    796    280       O  
ATOM   1508  CB  GLN A 203      60.107 -56.674 284.427  1.00 97.14           C  
ANISOU 1508  CB  GLN A 203    12058  17203   7646   1749    912    407       C  
ATOM   1509  CG  GLN A 203      58.719 -57.249 284.654  1.00 87.25           C  
ANISOU 1509  CG  GLN A 203    11098  15555   6496   1640    722    216       C  
ATOM   1510  CD  GLN A 203      57.717 -56.194 285.085  1.00 82.93           C  
ANISOU 1510  CD  GLN A 203    10468  14808   6234   1315    626    412       C  
ATOM   1511  OE1 GLN A 203      57.750 -55.060 284.607  1.00 82.03           O  
ANISOU 1511  OE1 GLN A 203    10161  14882   6123   1184    670    678       O  
ATOM   1512  NE2 GLN A 203      56.824 -56.560 285.998  1.00 83.60           N  
ANISOU 1512  NE2 GLN A 203    10705  14512   6548   1193    498    290       N  
ATOM   1513  N   ALA A 204      61.874 -57.827 286.730  1.00103.12           N  
ANISOU 1513  N   ALA A 204    12766  17764   8651   2063   1010    194       N  
ATOM   1514  CA  ALA A 204      62.162 -58.790 287.783  1.00 96.34           C  
ANISOU 1514  CA  ALA A 204    12063  16655   7888   2236    978    -10       C  
ATOM   1515  C   ALA A 204      62.660 -58.069 289.029  1.00 92.99           C  
ANISOU 1515  C   ALA A 204    11404  16167   7760   2078   1001    155       C  
ATOM   1516  O   ALA A 204      62.477 -58.544 290.146  1.00 87.95           O  
ANISOU 1516  O   ALA A 204    10899  15206   7310   2082    928     43       O  
ATOM   1517  CB  ALA A 204      63.185 -59.810 287.308  1.00 88.31           C  
ANISOU 1517  CB  ALA A 204    11104  15895   6554   2664   1079   -188       C  
ATOM   1518  N   ALA A 205      63.286 -56.914 288.826  1.00 91.69           N  
ANISOU 1518  N   ALA A 205    10903  16310   7626   1926   1096    425       N  
ATOM   1519  CA  ALA A 205      63.789 -56.111 289.934  1.00 89.35           C  
ANISOU 1519  CA  ALA A 205    10379  15974   7596   1738   1107    591       C  
ATOM   1520  C   ALA A 205      62.645 -55.583 290.790  1.00 85.72           C  
ANISOU 1520  C   ALA A 205    10043  15068   7459   1443    970    625       C  
ATOM   1521  O   ALA A 205      62.805 -55.374 291.990  1.00 91.22           O  
ANISOU 1521  O   ALA A 205    10694  15578   8387   1352    934    641       O  
ATOM   1522  CB  ALA A 205      64.635 -54.960 289.415  1.00 88.34           C  
ANISOU 1522  CB  ALA A 205     9894  16258   7414   1589   1226    882       C  
ATOM   1523  N   LEU A 206      61.490 -55.370 290.168  1.00 81.74           N  
ANISOU 1523  N   LEU A 206     9687  14420   6953   1309    893    634       N  
ATOM   1524  CA  LEU A 206      60.320 -54.881 290.887  1.00 79.70           C  
ANISOU 1524  CA  LEU A 206     9532  13781   6970   1060    769    666       C  
ATOM   1525  C   LEU A 206      59.564 -56.019 291.562  1.00 78.52           C  
ANISOU 1525  C   LEU A 206     9668  13281   6885   1139    665    410       C  
ATOM   1526  O   LEU A 206      59.173 -55.908 292.722  1.00 79.08           O  
ANISOU 1526  O   LEU A 206     9780  13066   7199   1023    603    397       O  
ATOM   1527  CB  LEU A 206      59.389 -54.120 289.942  1.00 76.77           C  
ANISOU 1527  CB  LEU A 206     9168  13439   6561    892    724    804       C  
ATOM   1528  CG  LEU A 206      59.934 -52.794 289.410  1.00 81.81           C  
ANISOU 1528  CG  LEU A 206     9560  14334   7188    739    806   1107       C  
ATOM   1529  CD1 LEU A 206      58.975 -52.180 288.402  1.00 80.42           C  
ANISOU 1529  CD1 LEU A 206     9433  14186   6937    627    754   1232       C  
ATOM   1530  CD2 LEU A 206      60.204 -51.832 290.557  1.00 80.36           C  
ANISOU 1530  CD2 LEU A 206     9250  13986   7298    533    795   1259       C  
ATOM   1531  N   ALA A 207      59.368 -57.114 290.833  1.00 76.42           N  
ANISOU 1531  N   ALA A 207     9612  13036   6388   1330    647    208       N  
ATOM   1532  CA  ALA A 207      58.626 -58.257 291.351  1.00 78.17           C  
ANISOU 1532  CA  ALA A 207    10144  12914   6644   1376    541    -32       C  
ATOM   1533  C   ALA A 207      59.348 -58.921 292.524  1.00 82.04           C  
ANISOU 1533  C   ALA A 207    10690  13258   7224   1529    562   -134       C  
ATOM   1534  O   ALA A 207      58.719 -59.306 293.511  1.00 71.32           O  
ANISOU 1534  O   ALA A 207     9492  11563   6043   1438    479   -214       O  
ATOM   1535  CB  ALA A 207      58.379 -59.270 290.245  1.00 60.25           C  
ANISOU 1535  CB  ALA A 207     8112  10701   4079   1548    510   -231       C  
ATOM   1536  N   VAL A 208      60.666 -59.054 292.412  1.00 81.74           N  
ANISOU 1536  N   VAL A 208    10509  13500   7050   1766    675   -122       N  
ATOM   1537  CA  VAL A 208      61.452 -59.704 293.455  1.00 85.54           C  
ANISOU 1537  CA  VAL A 208    11026  13895   7579   1960    695   -214       C  
ATOM   1538  C   VAL A 208      61.538 -58.845 294.716  1.00 87.05           C  
ANISOU 1538  C   VAL A 208    11033  13974   8067   1749    679    -62       C  
ATOM   1539  O   VAL A 208      61.274 -59.327 295.817  1.00 91.84           O  
ANISOU 1539  O   VAL A 208    11793  14283   8820   1745    615   -149       O  
ATOM   1540  CB  VAL A 208      62.876 -60.036 292.964  1.00 79.90           C  
ANISOU 1540  CB  VAL A 208    10160  13580   6618   2297    823   -231       C  
ATOM   1541  CG1 VAL A 208      63.769 -60.433 294.131  1.00 75.67           C  
ANISOU 1541  CG1 VAL A 208     9574  13017   6160   2476    842   -268       C  
ATOM   1542  CG2 VAL A 208      62.830 -61.144 291.920  1.00 73.96           C  
ANISOU 1542  CG2 VAL A 208     9675  12871   5555   2585    829   -445       C  
ATOM   1543  N   SER A 209      61.893 -57.574 294.551  1.00 79.77           N  
ANISOU 1543  N   SER A 209     9805  13280   7222   1564    732    166       N  
ATOM   1544  CA  SER A 209      62.049 -56.672 295.689  1.00 72.33           C  
ANISOU 1544  CA  SER A 209     8697  12244   6542   1358    711    305       C  
ATOM   1545  C   SER A 209      60.737 -56.481 296.457  1.00 73.74           C  
ANISOU 1545  C   SER A 209     9049  12013   6953   1139    599    283       C  
ATOM   1546  O   SER A 209      60.735 -56.433 297.688  1.00 77.41           O  
ANISOU 1546  O   SER A 209     9531  12281   7599   1085    559    270       O  
ATOM   1547  CB  SER A 209      62.592 -55.318 295.226  1.00 67.38           C  
ANISOU 1547  CB  SER A 209     7757  11906   5938   1167    777    558       C  
ATOM   1548  OG  SER A 209      61.709 -54.689 294.314  1.00 85.14           O  
ANISOU 1548  OG  SER A 209    10039  14138   8172    998    757    658       O  
ATOM   1549  N   LYS A 210      59.624 -56.385 295.733  1.00 68.17           N  
ANISOU 1549  N   LYS A 210     8461  11212   6228   1022    548    280       N  
ATOM   1550  CA  LYS A 210      58.320 -56.232 296.373  1.00 63.78           C  
ANISOU 1550  CA  LYS A 210     8040  10327   5866    829    448    262       C  
ATOM   1551  C   LYS A 210      57.931 -57.511 297.108  1.00 64.70           C  
ANISOU 1551  C   LYS A 210     8423  10169   5991    927    391     54       C  
ATOM   1552  O   LYS A 210      57.185 -57.470 298.085  1.00 72.13           O  
ANISOU 1552  O   LYS A 210     9441  10851   7113    794    330     42       O  
ATOM   1553  CB  LYS A 210      57.241 -55.861 295.347  1.00 74.63           C  
ANISOU 1553  CB  LYS A 210     9448  11720   7187    699    402    311       C  
ATOM   1554  CG  LYS A 210      56.778 -57.022 294.475  1.00 92.31           C  
ANISOU 1554  CG  LYS A 210    11908  13953   9211    815    363    126       C  
ATOM   1555  CD  LYS A 210      55.951 -56.560 293.283  1.00 97.03           C  
ANISOU 1555  CD  LYS A 210    12486  14674   9707    709    323    196       C  
ATOM   1556  CE  LYS A 210      54.572 -56.085 293.702  1.00 97.59           C  
ANISOU 1556  CE  LYS A 210    12576  14541   9963    487    222    246       C  
ATOM   1557  NZ  LYS A 210      53.715 -55.803 292.517  1.00 95.21           N  
ANISOU 1557  NZ  LYS A 210    12271  14373   9533    414    164    291       N  
ATOM   1558  N   PHE A 211      58.442 -58.645 296.637  1.00 66.89           N  
ANISOU 1558  N   PHE A 211     8854  10501   6059   1166    413   -105       N  
ATOM   1559  CA  PHE A 211      58.139 -59.933 297.250  1.00 74.46           C  
ANISOU 1559  CA  PHE A 211    10117  11174   6999   1270    354   -299       C  
ATOM   1560  C   PHE A 211      58.876 -60.097 298.576  1.00 80.69           C  
ANISOU 1560  C   PHE A 211    10884  11872   7904   1367    373   -300       C  
ATOM   1561  O   PHE A 211      58.355 -60.693 299.518  1.00 78.26           O  
ANISOU 1561  O   PHE A 211    10774  11266   7694   1327    314   -377       O  
ATOM   1562  CB  PHE A 211      58.495 -61.079 296.299  1.00 62.58           C  
ANISOU 1562  CB  PHE A 211     8827   9733   5216   1527    365   -479       C  
ATOM   1563  CG  PHE A 211      58.423 -62.439 296.933  1.00 74.38           C  
ANISOU 1563  CG  PHE A 211    10670  10921   6670   1673    310   -673       C  
ATOM   1564  CD1 PHE A 211      57.210 -62.959 297.355  1.00 81.84           C  
ANISOU 1564  CD1 PHE A 211    11865  11522   7708   1468    205   -750       C  
ATOM   1565  CD2 PHE A 211      59.567 -63.200 297.102  1.00 83.28           C  
ANISOU 1565  CD2 PHE A 211    11877  12113   7655   2019    363   -768       C  
ATOM   1566  CE1 PHE A 211      57.140 -64.211 297.939  1.00 77.26           C  
ANISOU 1566  CE1 PHE A 211    11636  10634   7087   1575    152   -909       C  
ATOM   1567  CE2 PHE A 211      59.504 -64.451 297.684  1.00 91.14           C  
ANISOU 1567  CE2 PHE A 211    13232  12791   8605   2170    307   -936       C  
ATOM   1568  CZ  PHE A 211      58.289 -64.957 298.103  1.00 85.92           C  
ANISOU 1568  CZ  PHE A 211    12848  11754   8044   1933    200  -1003       C  
ATOM   1569  N   LEU A 212      60.089 -59.559 298.641  1.00 79.22           N  
ANISOU 1569  N   LEU A 212    10444  11963   7695   1482    453   -203       N  
ATOM   1570  CA  LEU A 212      60.909 -59.669 299.838  1.00 73.45           C  
ANISOU 1570  CA  LEU A 212     9652  11209   7047   1589    464   -198       C  
ATOM   1571  C   LEU A 212      60.506 -58.641 300.891  1.00 78.53           C  
ANISOU 1571  C   LEU A 212    10164  11724   7948   1324    427    -70       C  
ATOM   1572  O   LEU A 212      60.073 -59.001 301.985  1.00 83.44           O  
ANISOU 1572  O   LEU A 212    10935  12081   8688   1288    374   -122       O  
ATOM   1573  CB  LEU A 212      62.389 -59.507 299.484  1.00 64.80           C  
ANISOU 1573  CB  LEU A 212     8303  10510   5808   1807    557   -145       C  
ATOM   1574  CG  LEU A 212      62.947 -60.488 298.449  1.00 80.40           C  
ANISOU 1574  CG  LEU A 212    10386  12668   7495   2135    613   -277       C  
ATOM   1575  CD1 LEU A 212      64.414 -60.206 298.157  1.00 79.92           C  
ANISOU 1575  CD1 LEU A 212    10005  13068   7294   2339    718   -196       C  
ATOM   1576  CD2 LEU A 212      62.758 -61.928 298.906  1.00 83.44           C  
ANISOU 1576  CD2 LEU A 212    11153  12749   7803   2371    557   -485       C  
ATOM   1577  N   LEU A 213      60.637 -57.364 300.546  1.00 76.28           N  
ANISOU 1577  N   LEU A 213     9622  11623   7739   1141    455    100       N  
ATOM   1578  CA  LEU A 213      60.435 -56.269 301.493  1.00 80.50           C  
ANISOU 1578  CA  LEU A 213    10030  12057   8497    915    422    221       C  
ATOM   1579  C   LEU A 213      59.027 -56.196 302.083  1.00 85.26           C  
ANISOU 1579  C   LEU A 213    10806  12331   9257    745    350    194       C  
ATOM   1580  O   LEU A 213      58.842 -55.690 303.190  1.00 89.55           O  
ANISOU 1580  O   LEU A 213    11329  12729   9966    638    317    230       O  
ATOM   1581  CB  LEU A 213      60.758 -54.932 300.820  1.00 82.07           C  
ANISOU 1581  CB  LEU A 213     9978  12481   8725    743    458    412       C  
ATOM   1582  CG  LEU A 213      62.158 -54.770 300.228  1.00 91.40           C  
ANISOU 1582  CG  LEU A 213    10918  14051   9758    848    541    488       C  
ATOM   1583  CD1 LEU A 213      62.305 -53.409 299.563  1.00 98.37           C  
ANISOU 1583  CD1 LEU A 213    11592  15105  10678    617    570    701       C  
ATOM   1584  CD2 LEU A 213      63.216 -54.963 301.300  1.00 84.61           C  
ANISOU 1584  CD2 LEU A 213     9948  13272   8928    948    539    462       C  
ATOM   1585  N   ALA A 214      58.038 -56.699 301.350  1.00 84.24           N  
ANISOU 1585  N   ALA A 214    10836  12109   9062    719    325    129       N  
ATOM   1586  CA  ALA A 214      56.644 -56.503 301.738  1.00 73.67           C  
ANISOU 1586  CA  ALA A 214     9598  10538   7856    535    263    131       C  
ATOM   1587  C   ALA A 214      55.886 -57.802 302.004  1.00 66.04           C  
ANISOU 1587  C   ALA A 214     8901   9348   6841    566    216    -25       C  
ATOM   1588  O   ALA A 214      54.671 -57.781 302.197  1.00 66.96           O  
ANISOU 1588  O   ALA A 214     9090   9317   7036    405    167    -28       O  
ATOM   1589  CB  ALA A 214      55.923 -55.695 300.669  1.00 78.61           C  
ANISOU 1589  CB  ALA A 214    10133  11265   8471    401    252    233       C  
ATOM   1590  N   PHE A 215      56.590 -58.929 302.022  1.00 65.29           N  
ANISOU 1590  N   PHE A 215     8962   9233   6612    770    229   -149       N  
ATOM   1591  CA  PHE A 215      55.922 -60.204 302.259  1.00 65.86           C  
ANISOU 1591  CA  PHE A 215     9340   9054   6629    783    177   -293       C  
ATOM   1592  C   PHE A 215      56.821 -61.237 302.933  1.00 76.51           C  
ANISOU 1592  C   PHE A 215    10865  10305   7902   1023    188   -395       C  
ATOM   1593  O   PHE A 215      56.554 -61.656 304.060  1.00 82.75           O  
ANISOU 1593  O   PHE A 215    11791  10875   8775    993    161   -415       O  
ATOM   1594  CB  PHE A 215      55.384 -60.767 300.945  1.00 70.15           C  
ANISOU 1594  CB  PHE A 215    10016   9628   7009    772    144   -381       C  
ATOM   1595  CG  PHE A 215      54.446 -61.923 301.123  1.00 65.86           C  
ANISOU 1595  CG  PHE A 215     9788   8806   6429    685     67   -512       C  
ATOM   1596  CD1 PHE A 215      53.145 -61.714 301.553  1.00 50.82           C  
ANISOU 1596  CD1 PHE A 215     7884   6771   4653    414     13   -469       C  
ATOM   1597  CD2 PHE A 215      54.861 -63.219 300.855  1.00 62.39           C  
ANISOU 1597  CD2 PHE A 215     9650   8240   5816    871     47   -674       C  
ATOM   1598  CE1 PHE A 215      52.275 -62.775 301.718  1.00 48.36           C  
ANISOU 1598  CE1 PHE A 215     7848   6223   4305    285    -60   -573       C  
ATOM   1599  CE2 PHE A 215      53.996 -64.287 301.017  1.00 57.96           C  
ANISOU 1599  CE2 PHE A 215     9412   7390   5219    750    -35   -788       C  
ATOM   1600  CZ  PHE A 215      52.700 -64.064 301.449  1.00 63.34           C  
ANISOU 1600  CZ  PHE A 215    10071   7959   6036    433    -89   -731       C  
ATOM   1601  N   LEU A 216      57.884 -61.646 302.247  1.00 76.31           N  
ANISOU 1601  N   LEU A 216    10033  10409   8552   2482    710     70       N  
ATOM   1602  CA  LEU A 216      58.745 -62.708 302.758  1.00 83.46           C  
ANISOU 1602  CA  LEU A 216    11114  11391   9208   3062    561   -213       C  
ATOM   1603  C   LEU A 216      59.489 -62.287 304.024  1.00 91.42           C  
ANISOU 1603  C   LEU A 216    11771  12636  10327   3010    710   -175       C  
ATOM   1604  O   LEU A 216      59.584 -63.057 304.980  1.00 83.06           O  
ANISOU 1604  O   LEU A 216    10952  11299   9309   3210    530   -258       O  
ATOM   1605  CB  LEU A 216      59.745 -63.151 301.690  1.00 76.19           C  
ANISOU 1605  CB  LEU A 216    10142  11004   7802   3622    591   -478       C  
ATOM   1606  CG  LEU A 216      60.463 -64.463 302.012  1.00 80.37           C  
ANISOU 1606  CG  LEU A 216    10962  11487   8087   4292    385   -785       C  
ATOM   1607  CD1 LEU A 216      59.454 -65.590 302.179  1.00 84.50           C  
ANISOU 1607  CD1 LEU A 216    12165  11220   8722   4359     -5   -852       C  
ATOM   1608  CD2 LEU A 216      61.482 -64.811 300.941  1.00 80.20           C  
ANISOU 1608  CD2 LEU A 216    10851  12026   7595   4862    491  -1041       C  
ATOM   1609  N   VAL A 217      60.018 -61.067 304.027  1.00 93.48           N  
ANISOU 1609  N   VAL A 217    11479  13403  10634   2724   1016    -37       N  
ATOM   1610  CA  VAL A 217      60.713 -60.545 305.200  1.00 88.91           C  
ANISOU 1610  CA  VAL A 217    10568  13058  10157   2599   1144     17       C  
ATOM   1611  C   VAL A 217      59.756 -60.295 306.378  1.00 86.07           C  
ANISOU 1611  C   VAL A 217    10407  12113  10184   2134   1124    189       C  
ATOM   1612  O   VAL A 217      60.092 -60.631 307.514  1.00 80.71           O  
ANISOU 1612  O   VAL A 217     9801  11345   9522   2209   1044    144       O  
ATOM   1613  CB  VAL A 217      61.497 -59.249 304.865  1.00 87.33           C  
ANISOU 1613  CB  VAL A 217     9727  13528   9925   2367   1457    141       C  
ATOM   1614  CG1 VAL A 217      61.990 -58.567 306.133  1.00 81.86           C  
ANISOU 1614  CG1 VAL A 217     8745  12964   9396   2092   1561    234       C  
ATOM   1615  CG2 VAL A 217      62.659 -59.562 303.933  1.00 85.69           C  
ANISOU 1615  CG2 VAL A 217     9272  13974   9312   2892   1507    -23       C  
ATOM   1616  N   PRO A 218      58.565 -59.711 306.125  1.00 83.86           N  
ANISOU 1616  N   PRO A 218    10211  11437  10215   1659   1205    401       N  
ATOM   1617  CA  PRO A 218      57.605 -59.658 307.235  1.00 79.99           C  
ANISOU 1617  CA  PRO A 218     9966  10345  10081   1299   1194    554       C  
ATOM   1618  C   PRO A 218      57.272 -61.031 307.821  1.00 77.08           C  
ANISOU 1618  C   PRO A 218    10121   9493   9674   1614    873    443       C  
ATOM   1619  O   PRO A 218      57.306 -61.184 309.039  1.00 81.58           O  
ANISOU 1619  O   PRO A 218    10791   9878  10327   1549    854    460       O  
ATOM   1620  CB  PRO A 218      56.368 -59.033 306.590  1.00 75.52           C  
ANISOU 1620  CB  PRO A 218     9424   9426   9842    853   1291    802       C  
ATOM   1621  CG  PRO A 218      56.925 -58.145 305.548  1.00 77.18           C  
ANISOU 1621  CG  PRO A 218     9192  10204   9927    780   1482    834       C  
ATOM   1622  CD  PRO A 218      58.118 -58.873 304.994  1.00 79.27           C  
ANISOU 1622  CD  PRO A 218     9416  10986   9716   1365   1362    559       C  
ATOM   1623  N   LEU A 219      56.965 -62.007 306.972  1.00 80.15           N  
ANISOU 1623  N   LEU A 219    10851   9676   9924   1937    612    335       N  
ATOM   1624  CA  LEU A 219      56.647 -63.353 307.445  1.00 80.11           C  
ANISOU 1624  CA  LEU A 219    11357   9186   9895   2246    271    236       C  
ATOM   1625  C   LEU A 219      57.810 -63.967 308.215  1.00 80.08           C  
ANISOU 1625  C   LEU A 219    11319   9464   9644   2679    178     32       C  
ATOM   1626  O   LEU A 219      57.605 -64.698 309.185  1.00 82.45           O  
ANISOU 1626  O   LEU A 219    11915   9390  10020   2755    -13     39       O  
ATOM   1627  CB  LEU A 219      56.264 -64.263 306.276  1.00 92.38           C  
ANISOU 1627  CB  LEU A 219    13284  10522  11295   2545     -8    115       C  
ATOM   1628  CG  LEU A 219      54.891 -64.028 305.646  1.00 96.04           C  
ANISOU 1628  CG  LEU A 219    13936  10510  12044   2131    -67    354       C  
ATOM   1629  CD1 LEU A 219      54.625 -65.051 304.550  1.00 93.27           C  
ANISOU 1629  CD1 LEU A 219    14021   9942  11475   2457   -408    195       C  
ATOM   1630  CD2 LEU A 219      53.801 -64.074 306.707  1.00 88.38           C  
ANISOU 1630  CD2 LEU A 219    13164   8913  11502   1755   -107    615       C  
ATOM   1631  N   ALA A 220      59.028 -63.667 307.779  1.00 80.83           N  
ANISOU 1631  N   ALA A 220    11031  10225   9455   2955    309   -116       N  
ATOM   1632  CA  ALA A 220      60.222 -64.185 308.437  1.00 79.28           C  
ANISOU 1632  CA  ALA A 220    10722  10357   9043   3373    226   -273       C  
ATOM   1633  C   ALA A 220      60.375 -63.595 309.837  1.00 67.17           C  
ANISOU 1633  C   ALA A 220     9019   8832   7669   3022    327   -130       C  
ATOM   1634  O   ALA A 220      60.672 -64.312 310.789  1.00 54.71           O  
ANISOU 1634  O   ALA A 220     7623   7109   6056   3214    132   -171       O  
ATOM   1635  CB  ALA A 220      61.460 -63.898 307.597  1.00 68.67           C  
ANISOU 1635  CB  ALA A 220     8945   9752   7396   3716    380   -412       C  
ATOM   1636  N   ILE A 221      60.169 -62.287 309.954  1.00 62.45           N  
ANISOU 1636  N   ILE A 221     8096   8392   7240   2502    622     40       N  
ATOM   1637  CA  ILE A 221      60.253 -61.606 311.241  1.00 64.31           C  
ANISOU 1637  CA  ILE A 221     8209   8615   7610   2116    746    161       C  
ATOM   1638  C   ILE A 221      59.161 -62.093 312.191  1.00 71.03           C  
ANISOU 1638  C   ILE A 221     9531   8774   8685   1906    633    267       C  
ATOM   1639  O   ILE A 221      59.429 -62.399 313.352  1.00 82.09           O  
ANISOU 1639  O   ILE A 221    11054  10091  10045   1908    537    270       O  
ATOM   1640  CB  ILE A 221      60.148 -60.075 311.075  1.00 54.27           C  
ANISOU 1640  CB  ILE A 221     6531   7583   6504   1589   1094    313       C  
ATOM   1641  CG1 ILE A 221      61.413 -59.528 310.409  1.00 49.00           C  
ANISOU 1641  CG1 ILE A 221     5336   7670   5611   1762   1206    249       C  
ATOM   1642  CG2 ILE A 221      59.929 -59.398 312.417  1.00 48.97           C  
ANISOU 1642  CG2 ILE A 221     5873   6729   6002   1136   1228    429       C  
ATOM   1643  CD1 ILE A 221      61.385 -58.031 310.183  1.00 52.00           C  
ANISOU 1643  CD1 ILE A 221     5296   8304   6156   1255   1520    408       C  
ATOM   1644  N   ILE A 222      57.934 -62.171 311.683  1.00 69.71           N  
ANISOU 1644  N   ILE A 222     9614   8122   8749   1718    637    381       N  
ATOM   1645  CA  ILE A 222      56.790 -62.636 312.462  1.00 64.51           C  
ANISOU 1645  CA  ILE A 222     9379   6791   8342   1512    547    530       C  
ATOM   1646  C   ILE A 222      57.022 -64.029 313.046  1.00 73.65           C  
ANISOU 1646  C   ILE A 222    10913   7719   9350   1930    185    424       C  
ATOM   1647  O   ILE A 222      56.786 -64.259 314.233  1.00 84.86           O  
ANISOU 1647  O   ILE A 222    12533   8871  10839   1796    145    513       O  
ATOM   1648  CB  ILE A 222      55.505 -62.652 311.605  1.00 50.38           C  
ANISOU 1648  CB  ILE A 222     7773   4545   6823   1317    540    686       C  
ATOM   1649  CG1 ILE A 222      55.075 -61.223 311.270  1.00 46.21           C  
ANISOU 1649  CG1 ILE A 222     6895   4123   6539    818    911    863       C  
ATOM   1650  CG2 ILE A 222      54.379 -63.380 312.322  1.00 43.82           C  
ANISOU 1650  CG2 ILE A 222     7391   3019   6242   1198    382    853       C  
ATOM   1651  CD1 ILE A 222      53.873 -61.148 310.358  1.00 57.90           C  
ANISOU 1651  CD1 ILE A 222     8488   5209   8302    605    897   1056       C  
ATOM   1652  N   ALA A 223      57.493 -64.949 312.212  1.00 71.74           N  
ANISOU 1652  N   ALA A 223    10777   7583   8897   2441    -70    235       N  
ATOM   1653  CA  ALA A 223      57.731 -66.321 312.646  1.00 76.94           C  
ANISOU 1653  CA  ALA A 223    11797   7999   9436   2882   -436    126       C  
ATOM   1654  C   ALA A 223      58.918 -66.406 313.599  1.00 86.31           C  
ANISOU 1654  C   ALA A 223    12794   9576  10424   3074   -471     50       C  
ATOM   1655  O   ALA A 223      58.919 -67.207 314.534  1.00 77.31           O  
ANISOU 1655  O   ALA A 223    11927   8167   9282   3195   -702     79       O  
ATOM   1656  CB  ALA A 223      57.956 -67.225 311.445  1.00 56.51           C  
ANISOU 1656  CB  ALA A 223     9382   5419   6669   3394   -672    -84       C  
ATOM   1657  N   SER A 224      59.927 -65.577 313.354  1.00 85.62           N  
ANISOU 1657  N   SER A 224    12227  10127  10179   3084   -260    -20       N  
ATOM   1658  CA  SER A 224      61.145 -65.593 314.155  1.00 74.92           C  
ANISOU 1658  CA  SER A 224    10626   9203   8637   3256   -313    -67       C  
ATOM   1659  C   SER A 224      60.912 -64.976 315.532  1.00 76.47           C  
ANISOU 1659  C   SER A 224    10843   9280   8933   2764   -211    101       C  
ATOM   1660  O   SER A 224      61.476 -65.431 316.528  1.00 78.31           O  
ANISOU 1660  O   SER A 224    11140   9557   9056   2873   -395    112       O  
ATOM   1661  CB  SER A 224      62.271 -64.852 313.429  1.00 71.34           C  
ANISOU 1661  CB  SER A 224     9622   9475   8008   3386   -120   -152       C  
ATOM   1662  OG  SER A 224      63.522 -65.078 314.051  1.00 89.65           O  
ANISOU 1662  OG  SER A 224    11696  12215  10151   3654   -238   -190       O  
ATOM   1663  N   SER A 225      60.079 -63.942 315.582  1.00 65.66           N  
ANISOU 1663  N   SER A 225     9430   7751   7766   2227     83    234       N  
ATOM   1664  CA  SER A 225      59.752 -63.286 316.841  1.00 65.26           C  
ANISOU 1664  CA  SER A 225     9447   7546   7804   1742    237    373       C  
ATOM   1665  C   SER A 225      58.769 -64.122 317.650  1.00 80.02           C  
ANISOU 1665  C   SER A 225    11827   8777   9799   1685     81    487       C  
ATOM   1666  O   SER A 225      58.681 -63.983 318.867  1.00 88.00           O  
ANISOU 1666  O   SER A 225    12986   9663  10787   1428    113    576       O  
ATOM   1667  CB  SER A 225      59.173 -61.892 316.595  1.00 72.85           C  
ANISOU 1667  CB  SER A 225    10190   8519   8971   1215    632    475       C  
ATOM   1668  OG  SER A 225      60.145 -61.029 316.029  1.00 89.94           O  
ANISOU 1668  OG  SER A 225    11860  11295  11020   1204    774    407       O  
ATOM   1669  N   HIS A 226      58.031 -64.989 316.966  1.00 89.50           N  
ANISOU 1669  N   HIS A 226    13308   9576  11120   1912    -95    493       N  
ATOM   1670  CA  HIS A 226      57.049 -65.847 317.619  1.00 91.87           C  
ANISOU 1670  CA  HIS A 226    14080   9251  11574   1867   -271    636       C  
ATOM   1671  C   HIS A 226      57.724 -66.993 318.369  1.00 88.31           C  
ANISOU 1671  C   HIS A 226    13840   8790  10926   2246   -639    580       C  
ATOM   1672  O   HIS A 226      57.224 -67.460 319.393  1.00 91.21           O  
ANISOU 1672  O   HIS A 226    14523   8786  11347   2114   -741    728       O  
ATOM   1673  CB  HIS A 226      56.059 -66.403 316.590  1.00 98.70           C  
ANISOU 1673  CB  HIS A 226    15151   9704  12648   1949   -387    675       C  
ATOM   1674  CG  HIS A 226      54.963 -67.230 317.188  1.00 97.64           C  
ANISOU 1674  CG  HIS A 226    14993   9365  12743   1600   -481    775       C  
ATOM   1675  ND1 HIS A 226      55.093 -68.582 317.422  1.00 95.07           N  
ANISOU 1675  ND1 HIS A 226    14799   8993  12328   1831   -783    705       N  
ATOM   1676  CD2 HIS A 226      53.715 -66.896 317.596  1.00 96.18           C  
ANISOU 1676  CD2 HIS A 226    14569   9084  12890   1101   -289    943       C  
ATOM   1677  CE1 HIS A 226      53.974 -69.045 317.950  1.00 94.19           C  
ANISOU 1677  CE1 HIS A 226    14590   8736  12460   1495   -731    849       C  
ATOM   1678  NE2 HIS A 226      53.122 -68.042 318.066  1.00 97.12           N  
ANISOU 1678  NE2 HIS A 226    14693   9107  13102   1091   -433    990       N  
ATOM   1679  N   ALA A 227      58.864 -67.438 317.852  1.00 84.85           N  
ANISOU 1679  N   ALA A 227    13209   8764  10266   2724   -827    386       N  
ATOM   1680  CA  ALA A 227      59.598 -68.548 318.449  1.00 78.70           C  
ANISOU 1680  CA  ALA A 227    12580   7996   9326   3142  -1193    336       C  
ATOM   1681  C   ALA A 227      60.400 -68.101 319.668  1.00 82.64           C  
ANISOU 1681  C   ALA A 227    12907   8831   9660   2954  -1164    399       C  
ATOM   1682  O   ALA A 227      60.586 -68.866 320.615  1.00 78.03           O  
ANISOU 1682  O   ALA A 227    12551   8092   9007   3061  -1430    476       O  
ATOM   1683  CB  ALA A 227      60.516 -69.188 317.418  1.00 62.48           C  
ANISOU 1683  CB  ALA A 227    10371   6247   7120   3754  -1373    111       C  
ATOM   1684  N   ALA A 228      60.877 -66.862 319.636  1.00 77.46           N  
ANISOU 1684  N   ALA A 228    11860   8631   8940   2656   -865    380       N  
ATOM   1685  CA  ALA A 228      61.645 -66.312 320.744  1.00 69.46           C  
ANISOU 1685  CA  ALA A 228    10683   7950   7757   2416   -844    437       C  
ATOM   1686  C   ALA A 228      60.761 -66.133 321.972  1.00 67.97           C  
ANISOU 1686  C   ALA A 228    10862   7341   7623   1946   -757    605       C  
ATOM   1687  O   ALA A 228      61.181 -66.412 323.097  1.00 74.21           O  
ANISOU 1687  O   ALA A 228    11780   8168   8247   1887   -933    679       O  
ATOM   1688  CB  ALA A 228      62.280 -64.990 320.346  1.00 56.21           C  
ANISOU 1688  CB  ALA A 228     8519   6811   6028   2173   -551    385       C  
ATOM   1689  N   VAL A 229      59.534 -65.674 321.745  1.00 55.92           N  
ANISOU 1689  N   VAL A 229     9500   5420   6328   1616   -481    683       N  
ATOM   1690  CA  VAL A 229      58.580 -65.432 322.823  1.00 71.94           C  
ANISOU 1690  CA  VAL A 229    11865   7033   8438   1173   -313    855       C  
ATOM   1691  C   VAL A 229      58.182 -66.717 323.547  1.00 85.27           C  
ANISOU 1691  C   VAL A 229    13987   8297  10114   1356   -637    980       C  
ATOM   1692  O   VAL A 229      58.260 -66.796 324.774  1.00 86.73           O  
ANISOU 1692  O   VAL A 229    14376   8431  10145   1161   -682   1081       O  
ATOM   1693  CB  VAL A 229      57.302 -64.746 322.296  1.00 59.89           C  
ANISOU 1693  CB  VAL A 229    10380   5146   7228    839     53    946       C  
ATOM   1694  CG1 VAL A 229      56.217 -64.739 323.363  1.00 65.88           C  
ANISOU 1694  CG1 VAL A 229    11520   5408   8105    474    220   1150       C  
ATOM   1695  CG2 VAL A 229      57.609 -63.330 321.834  1.00 46.54           C  
ANISOU 1695  CG2 VAL A 229     8290   3828   5565    548    409    867       C  
ATOM   1696  N   SER A 230      57.759 -67.717 322.778  1.00 79.49           N  
ANISOU 1696  N   SER A 230    13411   7258   9534   1717   -874    978       N  
ATOM   1697  CA  SER A 230      57.264 -68.974 323.333  1.00 85.09           C  
ANISOU 1697  CA  SER A 230    14433   7594  10303   1834  -1167   1085       C  
ATOM   1698  C   SER A 230      58.300 -69.679 324.208  1.00 88.89           C  
ANISOU 1698  C   SER A 230    15066   8199  10509   2136  -1548   1112       C  
ATOM   1699  O   SER A 230      57.955 -70.292 325.218  1.00 89.83           O  
ANISOU 1699  O   SER A 230    15365   8148  10618   1971  -1649   1235       O  
ATOM   1700  CB  SER A 230      56.818 -69.906 322.204  1.00 89.75           C  
ANISOU 1700  CB  SER A 230    14823   8181  11097   2013  -1282    946       C  
ATOM   1701  OG  SER A 230      56.304 -71.122 322.717  1.00102.31           O  
ANISOU 1701  OG  SER A 230    16463   9635  12777   1968  -1453    994       O  
ATOM   1702  N   LEU A 231      59.567 -69.586 323.816  1.00 83.09           N  
ANISOU 1702  N   LEU A 231    13981   7993   9595   2438  -1660    936       N  
ATOM   1703  CA  LEU A 231      60.652 -70.211 324.564  1.00 79.23           C  
ANISOU 1703  CA  LEU A 231    13459   7759   8884   2692  -2004    950       C  
ATOM   1704  C   LEU A 231      60.991 -69.408 325.815  1.00 81.25           C  
ANISOU 1704  C   LEU A 231    13686   8260   8927   2229  -1876   1051       C  
ATOM   1705  O   LEU A 231      61.315 -69.971 326.863  1.00 79.76           O  
ANISOU 1705  O   LEU A 231    13685   8039   8582   2229  -2144   1181       O  
ATOM   1706  CB  LEU A 231      61.893 -70.361 323.681  1.00 79.13           C  
ANISOU 1706  CB  LEU A 231    13040   8242   8785   3185  -2140    756       C  
ATOM   1707  CG  LEU A 231      63.164 -70.875 324.362  1.00103.59           C  
ANISOU 1707  CG  LEU A 231    15982  11689  11686   3462  -2475    789       C  
ATOM   1708  CD1 LEU A 231      62.923 -72.222 325.032  1.00120.16           C  
ANISOU 1708  CD1 LEU A 231    18486  13349  13820   3704  -2883    927       C  
ATOM   1709  CD2 LEU A 231      64.307 -70.966 323.364  1.00102.60           C  
ANISOU 1709  CD2 LEU A 231    15413  12048  11521   3970  -2533    612       C  
ATOM   1710  N   ARG A 232      60.913 -68.089 325.697  1.00 71.66           N  
ANISOU 1710  N   ARG A 232    12252   7275   7698   1825  -1480    993       N  
ATOM   1711  CA  ARG A 232      61.209 -67.202 326.811  1.00 75.89           C  
ANISOU 1711  CA  ARG A 232    12787   8028   8018   1349  -1331   1050       C  
ATOM   1712  C   ARG A 232      60.147 -67.325 327.902  1.00 86.77           C  
ANISOU 1712  C   ARG A 232    14653   8925   9390    980  -1223   1230       C  
ATOM   1713  O   ARG A 232      60.452 -67.223 329.090  1.00 79.78           O  
ANISOU 1713  O   ARG A 232    13939   8124   8251    727  -1296   1318       O  
ATOM   1714  CB  ARG A 232      61.311 -65.756 326.322  1.00 68.56           C  
ANISOU 1714  CB  ARG A 232    11525   7405   7121   1016   -926    935       C  
ATOM   1715  CG  ARG A 232      61.919 -64.798 327.326  1.00 72.27           C  
ANISOU 1715  CG  ARG A 232    11930   8194   7336    576   -832    943       C  
ATOM   1716  CD  ARG A 232      63.306 -65.248 327.747  1.00 71.40           C  
ANISOU 1716  CD  ARG A 232    11617   8534   6977    815  -1249    957       C  
ATOM   1717  NE  ARG A 232      64.000 -64.204 328.492  1.00 85.89           N  
ANISOU 1717  NE  ARG A 232    13316  10739   8579    380  -1182    951       N  
ATOM   1718  CZ  ARG A 232      64.872 -63.358 327.954  1.00104.58           C  
ANISOU 1718  CZ  ARG A 232    15208  13598  10929    333  -1118    868       C  
ATOM   1719  NH1 ARG A 232      65.167 -63.438 326.664  1.00103.92           N  
ANISOU 1719  NH1 ARG A 232    14732  13725  11028    713  -1083    783       N  
ATOM   1720  NH2 ARG A 232      65.453 -62.436 328.708  1.00118.45           N  
ANISOU 1720  NH2 ARG A 232    16894  15638  12475   -103  -1099    877       N  
ATOM   1721  N   LEU A 233      58.902 -67.553 327.490  1.00 86.17           N  
ANISOU 1721  N   LEU A 233    14798   8354   9590    944  -1053   1304       N  
ATOM   1722  CA  LEU A 233      57.798 -67.715 328.431  1.00 76.78           C  
ANISOU 1722  CA  LEU A 233    14043   6686   8442    624   -912   1511       C  
ATOM   1723  C   LEU A 233      57.868 -69.057 329.151  1.00 84.47           C  
ANISOU 1723  C   LEU A 233    15335   7438   9322    865  -1353   1676       C  
ATOM   1724  O   LEU A 233      57.451 -69.176 330.303  1.00 90.96           O  
ANISOU 1724  O   LEU A 233    16476   8072  10013    585  -1314   1848       O  
ATOM   1725  CB  LEU A 233      56.453 -67.587 327.715  1.00 66.41           C  
ANISOU 1725  CB  LEU A 233    12731   4982   7519    514   -613   1556       C  
ATOM   1726  CG  LEU A 233      56.083 -66.219 327.142  1.00 68.41           C  
ANISOU 1726  CG  LEU A 233    12759   5312   7922    198   -133   1477       C  
ATOM   1727  CD1 LEU A 233      54.667 -66.247 326.589  1.00 59.80           C  
ANISOU 1727  CD1 LEU A 233    11192   4225   7306     79     79   1431       C  
ATOM   1728  CD2 LEU A 233      56.229 -65.139 328.201  1.00 75.20           C  
ANISOU 1728  CD2 LEU A 233    13729   6289   8554   -271    194   1486       C  
ATOM   1729  N   GLN A 234      58.386 -70.068 328.463  1.00 79.73           N  
ANISOU 1729  N   GLN A 234    14643   6859   8791   1387  -1758   1619       N  
ATOM   1730  CA  GLN A 234      58.530 -71.391 329.054  1.00 77.31           C  
ANISOU 1730  CA  GLN A 234    14453   6450   8470   1605  -2147   1701       C  
ATOM   1731  C   GLN A 234      59.598 -71.364 330.137  1.00 86.56           C  
ANISOU 1731  C   GLN A 234    15746   7888   9253   1592  -2432   1816       C  
ATOM   1732  O   GLN A 234      59.455 -71.998 331.181  1.00 89.27           O  
ANISOU 1732  O   GLN A 234    16330   8092   9496   1479  -2607   1987       O  
ATOM   1733  CB  GLN A 234      58.885 -72.425 327.987  1.00 80.83           C  
ANISOU 1733  CB  GLN A 234    14643   6955   9113   2103  -2406   1520       C  
ATOM   1734  CG  GLN A 234      58.868 -73.859 328.483  1.00 99.87           C  
ANISOU 1734  CG  GLN A 234    17080   9262  11602   2241  -2694   1558       C  
ATOM   1735  CD  GLN A 234      59.346 -74.843 327.434  1.00109.22           C  
ANISOU 1735  CD  GLN A 234    18057  10512  12929   2696  -2905   1359       C  
ATOM   1736  OE1 GLN A 234      60.164 -74.507 326.577  1.00109.27           O  
ANISOU 1736  OE1 GLN A 234    17885  10758  12875   3026  -2951   1204       O  
ATOM   1737  NE2 GLN A 234      58.834 -76.067 327.493  1.00112.77           N  
ANISOU 1737  NE2 GLN A 234    18526  10769  13552   2711  -3012   1363       N  
ATOM   1738  N   HIS A 235      60.670 -70.625 329.875  1.00 87.63           N  
ANISOU 1738  N   HIS A 235    15487   8572   9236   1610  -2389   1643       N  
ATOM   1739  CA  HIS A 235      61.753 -70.471 330.837  1.00 86.32           C  
ANISOU 1739  CA  HIS A 235    15236   8819   8744   1500  -2605   1693       C  
ATOM   1740  C   HIS A 235      61.291 -69.653 332.040  1.00 90.35           C  
ANISOU 1740  C   HIS A 235    16031   9282   9016    877  -2332   1793       C  
ATOM   1741  O   HIS A 235      61.656 -69.944 333.180  1.00 96.89           O  
ANISOU 1741  O   HIS A 235    17070  10175   9569    724  -2569   1945       O  
ATOM   1742  CB  HIS A 235      62.966 -69.810 330.176  1.00 84.70           C  
ANISOU 1742  CB  HIS A 235    14498   9209   8474   1648  -2605   1509       C  
ATOM   1743  CG  HIS A 235      64.191 -69.791 331.035  1.00 99.54           C  
ANISOU 1743  CG  HIS A 235    16228  11526  10066   1603  -2920   1592       C  
ATOM   1744  ND1 HIS A 235      65.258 -68.950 330.796  1.00101.78           N  
ANISOU 1744  ND1 HIS A 235    16056  12375  10239   1544  -2889   1493       N  
ATOM   1745  CD2 HIS A 235      64.525 -70.515 332.131  1.00103.22           C  
ANISOU 1745  CD2 HIS A 235    16926  11951  10340   1591  -3299   1795       C  
ATOM   1746  CE1 HIS A 235      66.190 -69.153 331.707  1.00104.14           C  
ANISOU 1746  CE1 HIS A 235    16311  12957  10301   1491  -3244   1636       C  
ATOM   1747  NE2 HIS A 235      65.772 -70.098 332.530  1.00102.13           N  
ANISOU 1747  NE2 HIS A 235    16474  12347   9984   1518  -3500   1817       N  
ATOM   1748  N   ARG A 236      60.482 -68.631 331.776  1.00 76.91           N  
ANISOU 1748  N   ARG A 236    14346   7459   7416    523  -1830   1709       N  
ATOM   1749  CA  ARG A 236      59.958 -67.764 332.826  1.00 77.03           C  
ANISOU 1749  CA  ARG A 236    14650   7394   7225    -53  -1483   1764       C  
ATOM   1750  C   ARG A 236      58.976 -68.516 333.719  1.00 95.72           C  
ANISOU 1750  C   ARG A 236    17520   9279   9571   -170  -1499   2009       C  
ATOM   1751  O   ARG A 236      58.914 -68.280 334.926  1.00104.75           O  
ANISOU 1751  O   ARG A 236    18976  10424  10402   -536  -1435   2111       O  
ATOM   1752  CB  ARG A 236      59.287 -66.532 332.216  1.00 66.22           C  
ANISOU 1752  CB  ARG A 236    13149   5967   6045   -344   -927   1624       C  
ATOM   1753  CG  ARG A 236      58.722 -65.549 333.228  1.00 66.28           C  
ANISOU 1753  CG  ARG A 236    13456   5865   5863   -917   -502   1642       C  
ATOM   1754  CD  ARG A 236      58.269 -64.267 332.546  1.00 68.59           C  
ANISOU 1754  CD  ARG A 236    13536   6154   6369  -1167     12   1488       C  
ATOM   1755  NE  ARG A 236      59.386 -63.561 331.925  1.00 80.23           N  
ANISOU 1755  NE  ARG A 236    14555   8141   7788  -1124    -69   1295       N  
ATOM   1756  CZ  ARG A 236      59.254 -62.554 331.065  1.00 79.49           C  
ANISOU 1756  CZ  ARG A 236    14155   8137   7910  -1238    265   1161       C  
ATOM   1757  NH1 ARG A 236      58.049 -62.132 330.710  1.00 76.10           N  
ANISOU 1757  NH1 ARG A 236    13820   7311   7785  -1394    700   1195       N  
ATOM   1758  NH2 ARG A 236      60.331 -61.974 330.553  1.00 67.49           N  
ANISOU 1758  NH2 ARG A 236    12211   7109   6324  -1198    157   1023       N  
ATOM   1759  N   ALA A1238      58.215 -69.427 333.119  1.00 90.30           N  
ANISOU 1759  N   ALA A1238    16923   8182   9206    131  -1595   2113       N  
ATOM   1760  CA  ALA A1238      57.271 -70.244 333.868  1.00 86.02           C  
ANISOU 1760  CA  ALA A1238    16500   7376   8807     44  -1564   2226       C  
ATOM   1761  C   ALA A1238      58.004 -71.173 334.830  1.00 92.16           C  
ANISOU 1761  C   ALA A1238    17477   8233   9305    155  -2049   2390       C  
ATOM   1762  O   ALA A1238      57.508 -71.474 335.916  1.00102.52           O  
ANISOU 1762  O   ALA A1238    18964   9462  10528    -85  -1981   2502       O  
ATOM   1763  CB  ALA A1238      56.393 -71.045 332.922  1.00 79.47           C  
ANISOU 1763  CB  ALA A1238    15332   6380   8482    310  -1528   2142       C  
ATOM   1764  N   ASP A1239      59.188 -71.623 334.428  1.00 88.63           N  
ANISOU 1764  N   ASP A1239    16934   7998   8744    543  -2532   2394       N  
ATOM   1765  CA  ASP A1239      59.993 -72.508 335.263  1.00 96.73           C  
ANISOU 1765  CA  ASP A1239    18012   9173   9567    681  -3014   2531       C  
ATOM   1766  C   ASP A1239      60.640 -71.749 336.420  1.00 97.74           C  
ANISOU 1766  C   ASP A1239    18378   9597   9162    265  -3067   2643       C  
ATOM   1767  O   ASP A1239      60.891 -72.316 337.483  1.00 93.94           O  
ANISOU 1767  O   ASP A1239    18031   9167   8494    158  -3308   2791       O  
ATOM   1768  CB  ASP A1239      61.065 -73.205 334.423  1.00 99.02           C  
ANISOU 1768  CB  ASP A1239    17967   9676   9979   1256  -3454   2447       C  
ATOM   1769  CG  ASP A1239      60.474 -74.113 333.360  1.00 96.88           C  
ANISOU 1769  CG  ASP A1239    17478   9143  10190   1622  -3409   2296       C  
ATOM   1770  OD1 ASP A1239      61.097 -74.258 332.287  1.00 99.60           O  
ANISOU 1770  OD1 ASP A1239    17538   9637  10666   2041  -3535   2130       O  
ATOM   1771  OD2 ASP A1239      59.386 -74.682 333.597  1.00 97.50           O  
ANISOU 1771  OD2 ASP A1239    17634   8918  10492   1467  -3234   2332       O  
ATOM   1772  N   LEU A1240      60.903 -70.465 336.208  1.00 96.93           N  
ANISOU 1772  N   LEU A1240    18066   9804   8960    -18  -2712   2425       N  
ATOM   1773  CA  LEU A1240      61.505 -69.626 337.238  1.00 96.40           C  
ANISOU 1773  CA  LEU A1240    18093  10082   8454   -478  -2672   2410       C  
ATOM   1774  C   LEU A1240      60.488 -69.213 338.293  1.00 98.63           C  
ANISOU 1774  C   LEU A1240    18894  10071   8510   -985  -2294   2514       C  
ATOM   1775  O   LEU A1240      60.816 -69.107 339.474  1.00102.39           O  
ANISOU 1775  O   LEU A1240    19659  10684   8561  -1313  -2416   2619       O  
ATOM   1776  CB  LEU A1240      62.131 -68.383 336.613  1.00 99.45           C  
ANISOU 1776  CB  LEU A1240    18078  10873   8837   -611  -2434   2143       C  
ATOM   1777  CG  LEU A1240      63.310 -68.637 335.678  1.00101.02           C  
ANISOU 1777  CG  LEU A1240    17726  11471   9185   -154  -2776   2049       C  
ATOM   1778  CD1 LEU A1240      63.608 -67.392 334.865  1.00102.94           C  
ANISOU 1778  CD1 LEU A1240    17577  12018   9517   -286  -2437   1806       C  
ATOM   1779  CD2 LEU A1240      64.532 -69.072 336.472  1.00 95.34           C  
ANISOU 1779  CD2 LEU A1240    16933  11116   8175   -115  -3311   2198       C  
ATOM   1780  N   GLY A1241      59.256 -68.975 337.857  1.00104.72           N  
ANISOU 1780  N   GLY A1241    19782  10444   9565  -1050  -1828   2498       N  
ATOM   1781  CA  GLY A1241      58.202 -68.525 338.747  1.00102.79           C  
ANISOU 1781  CA  GLY A1241    19768   9995   9294  -1455  -1336   2473       C  
ATOM   1782  C   GLY A1241      57.769 -69.587 339.737  1.00100.54           C  
ANISOU 1782  C   GLY A1241    19635   9567   8999  -1425  -1513   2641       C  
ATOM   1783  O   GLY A1241      57.366 -69.277 340.858  1.00 87.98           O  
ANISOU 1783  O   GLY A1241    18281   7972   7174  -1770  -1278   2645       O  
ATOM   1784  N   LEU A1242      57.859 -70.847 339.323  1.00107.11           N  
ANISOU 1784  N   LEU A1242    20315  10290  10092  -1004  -1919   2765       N  
ATOM   1785  CA  LEU A1242      57.453 -71.964 340.170  1.00106.26           C  
ANISOU 1785  CA  LEU A1242    20299  10049  10026   -956  -2106   2944       C  
ATOM   1786  C   LEU A1242      58.544 -72.347 341.164  1.00110.20           C  
ANISOU 1786  C   LEU A1242    20994  10791  10087  -1030  -2581   3101       C  
ATOM   1787  O   LEU A1242      58.397 -73.306 341.923  1.00107.90           O  
ANISOU 1787  O   LEU A1242    20785  10423   9791   -993  -2799   3277       O  
ATOM   1788  CB  LEU A1242      57.079 -73.174 339.313  1.00109.48           C  
ANISOU 1788  CB  LEU A1242    20415  10255  10928   -504  -2319   2973       C  
ATOM   1789  CG  LEU A1242      55.812 -73.022 338.470  1.00119.90           C  
ANISOU 1789  CG  LEU A1242    21456  11378  12722   -457  -1883   2853       C  
ATOM   1790  CD1 LEU A1242      55.588 -74.256 337.612  1.00126.09           C  
ANISOU 1790  CD1 LEU A1242    21951  12029  13930    -50  -2141   2855       C  
ATOM   1791  CD2 LEU A1242      54.609 -72.759 339.364  1.00122.10           C  
ANISOU 1791  CD2 LEU A1242    21789  11573  13031   -770  -1443   2915       C  
ATOM   1792  N   GLN A1243      59.641 -71.598 341.154  1.00115.48           N  
ANISOU 1792  N   GLN A1243    21676  11797  10405  -1145  -2749   3040       N  
ATOM   1793  CA  GLN A1243      60.710 -71.809 342.120  1.00122.23           C  
ANISOU 1793  CA  GLN A1243    22616  12973  10852  -1269  -3188   3163       C  
ATOM   1794  C   GLN A1243      60.471 -70.965 343.364  1.00124.33           C  
ANISOU 1794  C   GLN A1243    23239  13323  10678  -1842  -2881   3128       C  
ATOM   1795  O   GLN A1243      60.173 -69.773 343.274  1.00118.94           O  
ANISOU 1795  O   GLN A1243    22651  12666   9877  -2151  -2429   2930       O  
ATOM   1796  CB  GLN A1243      62.073 -71.481 341.508  1.00130.69           C  
ANISOU 1796  CB  GLN A1243    23393  14458  11804  -1091  -3567   3102       C  
ATOM   1797  CG  GLN A1243      62.483 -72.407 340.374  1.00137.72           C  
ANISOU 1797  CG  GLN A1243    23902  15315  13112   -462  -3915   3112       C  
ATOM   1798  CD  GLN A1243      63.886 -72.127 339.872  1.00142.46           C  
ANISOU 1798  CD  GLN A1243    24127  16389  13610   -253  -4292   3058       C  
ATOM   1799  OE1 GLN A1243      64.701 -71.531 340.576  1.00142.25           O  
ANISOU 1799  OE1 GLN A1243    24092  16744  13211   -574  -4442   3078       O  
ATOM   1800  NE2 GLN A1243      64.174 -72.553 338.647  1.00145.21           N  
ANISOU 1800  NE2 GLN A1243    24123  16735  14316    285  -4430   2970       N  
ATOM   1801  N   HIS A1244      60.601 -71.600 344.523  1.00131.23           N  
ANISOU 1801  N   HIS A1244    24298  14231  11331  -1970  -3116   3303       N  
ATOM   1802  CA  HIS A1244      60.379 -70.947 345.806  1.00135.02           C  
ANISOU 1802  CA  HIS A1244    25142  14778  11381  -2482  -2864   3267       C  
ATOM   1803  C   HIS A1244      61.329 -69.773 346.033  1.00132.70           C  
ANISOU 1803  C   HIS A1244    24875  14856  10687  -2826  -2889   3092       C  
ATOM   1804  O   HIS A1244      60.937 -68.746 346.586  1.00122.69           O  
ANISOU 1804  O   HIS A1244    23863  13576   9178  -3241  -2453   2904       O  
ATOM   1805  CB  HIS A1244      60.530 -71.966 346.936  1.00147.57           C  
ANISOU 1805  CB  HIS A1244    26885  16381  12805  -2511  -3219   3522       C  
ATOM   1806  CG  HIS A1244      61.797 -72.759 346.862  1.00151.84           C  
ANISOU 1806  CG  HIS A1244    27164  17182  13347  -2241  -3895   3689       C  
ATOM   1807  ND1 HIS A1244      61.999 -73.755 345.929  1.00142.97           N  
ANISOU 1807  ND1 HIS A1244    25701  15958  12661  -1709  -4207   3779       N  
ATOM   1808  CD2 HIS A1244      62.932 -72.699 347.598  1.00162.67           C  
ANISOU 1808  CD2 HIS A1244    28517  18911  14379  -2413  -4303   3767       C  
ATOM   1809  CE1 HIS A1244      63.201 -74.275 346.096  1.00153.27           C  
ANISOU 1809  CE1 HIS A1244    26777  17551  13909  -1539  -4751   3905       C  
ATOM   1810  NE2 HIS A1244      63.788 -73.652 347.103  1.00167.34           N  
ANISOU 1810  NE2 HIS A1244    28731  19622  15229  -1966  -4831   3918       N  
ATOM   1811  N   ARG A1245      62.576 -69.935 345.599  1.00141.52           N  
ANISOU 1811  N   ARG A1245    25682  16311  11779  -2634  -3396   3137       N  
ATOM   1812  CA  ARG A1245      63.605 -68.919 345.804  1.00141.65           C  
ANISOU 1812  CA  ARG A1245    25619  16738  11463  -2944  -3512   2995       C  
ATOM   1813  C   ARG A1245      63.282 -67.624 345.065  1.00144.70           C  
ANISOU 1813  C   ARG A1245    25981  17119  11880  -3127  -3019   2711       C  
ATOM   1814  O   ARG A1245      63.441 -66.532 345.611  1.00136.30           O  
ANISOU 1814  O   ARG A1245    25079  16187  10522  -3578  -2791   2522       O  
ATOM   1815  CB  ARG A1245      64.969 -69.448 345.356  1.00135.70           C  
ANISOU 1815  CB  ARG A1245    24408  16360  10791  -2614  -4150   3121       C  
ATOM   1816  N   ASN A1246      62.829 -67.755 343.823  1.00147.78           N  
ANISOU 1816  N   ASN A1246    26163  17335  12649  -2776  -2857   2678       N  
ATOM   1817  CA  ASN A1246      62.496 -66.597 343.003  1.00151.50           C  
ANISOU 1817  CA  ASN A1246    26565  17787  13212  -2911  -2382   2436       C  
ATOM   1818  C   ASN A1246      61.062 -66.133 343.230  1.00155.06           C  
ANISOU 1818  C   ASN A1246    27296  17809  13813  -3115  -1688   2314       C  
ATOM   1819  O   ASN A1246      60.251 -66.116 342.304  1.00159.06           O  
ANISOU 1819  O   ASN A1246    27671  18042  14721  -2903  -1355   2273       O  
ATOM   1820  CB  ASN A1246      62.713 -66.916 341.523  1.00155.21           C  
ANISOU 1820  CB  ASN A1246    26568  18292  14114  -2408  -2504   2415       C  
ATOM   1821  CG  ASN A1246      64.123 -67.387 341.230  1.00158.31           C  
ANISOU 1821  CG  ASN A1246    26503  19125  14523  -2102  -3127   2478       C  
ATOM   1822  OD1 ASN A1246      65.093 -66.865 341.782  1.00165.25           O  
ANISOU 1822  OD1 ASN A1246    27323  20395  15070  -2383  -3378   2466       O  
ATOM   1823  ND2 ASN A1246      64.245 -68.387 340.364  1.00154.95           N  
ANISOU 1823  ND2 ASN A1246    25756  18628  14491  -1522  -3385   2556       N  
ATOM   1824  N   ILE A1247      60.759 -65.753 344.467  1.00160.21           N  
ANISOU 1824  N   ILE A1247    28286  18410  14178  -3506  -1480   2247       N  
ATOM   1825  CA  ILE A1247      59.415 -65.310 344.825  1.00151.35           C  
ANISOU 1825  CA  ILE A1247    27370  16923  13213  -3663   -836   2109       C  
ATOM   1826  C   ILE A1247      59.278 -63.789 344.786  1.00148.79           C  
ANISOU 1826  C   ILE A1247    27082  16616  12837  -4012   -344   1779       C  
ATOM   1827  O   ILE A1247      58.343 -63.259 344.188  1.00138.89           O  
ANISOU 1827  O   ILE A1247    25690  15119  11964  -3941    165   1622       O  
ATOM   1828  CB  ILE A1247      59.016 -65.810 346.227  1.00146.75           C  
ANISOU 1828  CB  ILE A1247    27147  16241  12370  -3839   -850   2215       C  
ATOM   1829  N   PHE A1248      60.210 -63.092 345.429  1.00156.86           N  
ANISOU 1829  N   PHE A1248    28240  17924  13435  -4373   -524   1668       N  
ATOM   1830  CA  PHE A1248      60.170 -61.634 345.493  1.00154.77           C  
ANISOU 1830  CA  PHE A1248    28036  17659  13109  -4734   -110   1346       C  
ATOM   1831  C   PHE A1248      61.302 -61.007 344.710  1.00154.94           C  
ANISOU 1831  C   PHE A1248    27746  18052  13072  -4798   -369   1276       C  
ATOM   1832  O   PHE A1248      61.746 -59.904 345.025  1.00148.79           O  
ANISOU 1832  O   PHE A1248    27037  17400  12098  -5174   -274   1061       O  
ATOM   1833  CB  PHE A1248      60.233 -61.157 346.940  1.00156.35           C  
ANISOU 1833  CB  PHE A1248    28677  17847  12883  -5161    -52   1231       C  
ATOM   1834  CG  PHE A1248      58.958 -61.341 347.683  1.00155.17           C  
ANISOU 1834  CG  PHE A1248    28825  17330  12803  -5157    386   1198       C  
ATOM   1835  CD1 PHE A1248      57.748 -61.285 347.018  1.00152.26           C  
ANISOU 1835  CD1 PHE A1248    28274  16658  12921  -4890    872   1124       C  
ATOM   1836  CD2 PHE A1248      58.965 -61.578 349.044  1.00148.85           C  
ANISOU 1836  CD2 PHE A1248    28438  16523  11597  -5398    293   1248       C  
ATOM   1837  CE1 PHE A1248      56.568 -61.456 347.697  1.00147.37           C  
ANISOU 1837  CE1 PHE A1248    27844  15763  12386  -4843   1252   1104       C  
ATOM   1838  CE2 PHE A1248      57.788 -61.750 349.730  1.00142.01           C  
ANISOU 1838  CE2 PHE A1248    27820  15359  10778  -5375    703   1228       C  
ATOM   1839  CZ  PHE A1248      56.586 -61.690 349.056  1.00141.58           C  
ANISOU 1839  CZ  PHE A1248    27547  15029  11217  -5087   1182   1158       C  
ATOM   1840  N   GLU A1249      61.778 -61.717 343.696  1.00158.59           N  
ANISOU 1840  N   GLU A1249    27858  18694  13706  -4422   -717   1457       N  
ATOM   1841  CA  GLU A1249      62.859 -61.204 342.874  1.00166.24           C  
ANISOU 1841  CA  GLU A1249    28453  20075  14634  -4423   -992   1404       C  
ATOM   1842  C   GLU A1249      62.332 -60.145 341.925  1.00163.25           C  
ANISOU 1842  C   GLU A1249    27899  19570  14558  -4491   -441   1185       C  
ATOM   1843  O   GLU A1249      61.205 -60.242 341.441  1.00165.33           O  
ANISOU 1843  O   GLU A1249    28155  19447  15214  -4307     12   1169       O  
ATOM   1844  CB  GLU A1249      63.527 -62.326 342.091  1.00178.41           C  
ANISOU 1844  CB  GLU A1249    29578  21841  16370  -3907  -1536   1623       C  
ATOM   1845  CG  GLU A1249      64.836 -61.920 341.439  1.00187.65           C  
ANISOU 1845  CG  GLU A1249    30156  23510  17632  -3821  -1902   1552       C  
ATOM   1846  CD  GLU A1249      65.474 -63.068 340.686  1.00190.80           C  
ANISOU 1846  CD  GLU A1249    30062  24097  18335  -3221  -2383   1730       C  
ATOM   1847  OE1 GLU A1249      64.811 -64.122 340.559  1.00189.53           O  
ANISOU 1847  OE1 GLU A1249    30024  23630  18359  -2872  -2402   1872       O  
ATOM   1848  OE2 GLU A1249      66.629 -62.918 340.226  1.00192.99           O  
ANISOU 1848  OE2 GLU A1249    29834  24816  18677  -3096  -2733   1733       O  
ATOM   1849  N   MET A1250      63.149 -59.131 341.663  1.00142.21           N  
ANISOU 1849  N   MET A1250    24990  17223  11821  -4732   -498   1011       N  
ATOM   1850  CA  MET A1250      62.720 -58.023 340.820  1.00123.72           C  
ANISOU 1850  CA  MET A1250    22411  14767   9830  -4819     13    787       C  
ATOM   1851  C   MET A1250      63.818 -57.501 339.888  1.00112.40           C  
ANISOU 1851  C   MET A1250    20322  13780   8605  -4733   -259    712       C  
ATOM   1852  O   MET A1250      64.999 -57.504 340.236  1.00 98.60           O  
ANISOU 1852  O   MET A1250    18429  12446   6588  -4845   -770    765       O  
ATOM   1853  CB  MET A1250      62.193 -56.887 341.698  1.00118.86           C  
ANISOU 1853  CB  MET A1250    22210  13890   9060  -5305    470    544       C  
ATOM   1854  CG  MET A1250      63.151 -56.443 342.791  1.00127.57           C  
ANISOU 1854  CG  MET A1250    23546  15248   9676  -5725    112    478       C  
ATOM   1855  SD  MET A1250      62.392 -55.298 343.962  1.00135.10           S  
ANISOU 1855  SD  MET A1250    25025  15776  10532  -6194    635    174       S  
ATOM   1856  CE  MET A1250      61.084 -56.317 344.639  1.00107.50           C  
ANISOU 1856  CE  MET A1250    21859  11843   7142  -5922    897    270       C  
ATOM   1857  N   LEU A1251      63.403 -57.049 338.705  1.00110.73           N  
ANISOU 1857  N   LEU A1251    19707  13483   8881  -4546     87    617       N  
ATOM   1858  CA  LEU A1251      64.309 -56.525 337.677  1.00112.48           C  
ANISOU 1858  CA  LEU A1251    19274  14110   9353  -4437    -82    560       C  
ATOM   1859  C   LEU A1251      65.387 -57.539 337.276  1.00118.33           C  
ANISOU 1859  C   LEU A1251    19562  15276  10122  -4002   -698    742       C  
ATOM   1860  O   LEU A1251      66.578 -57.300 337.479  1.00119.77           O  
ANISOU 1860  O   LEU A1251    19498  15898  10111  -4130  -1113    781       O  
ATOM   1861  CB  LEU A1251      64.961 -55.216 338.149  1.00108.21           C  
ANISOU 1861  CB  LEU A1251    18786  13771   8558  -4985    -75    400       C  
ATOM   1862  CG  LEU A1251      64.043 -54.001 338.311  1.00 98.34           C  
ANISOU 1862  CG  LEU A1251    17864  12134   7366  -5390    562    179       C  
ATOM   1863  CD1 LEU A1251      64.840 -52.776 338.735  1.00 94.26           C  
ANISOU 1863  CD1 LEU A1251    17380  11836   6598  -5914    468     22       C  
ATOM   1864  CD2 LEU A1251      63.291 -53.732 337.020  1.00 92.53           C  
ANISOU 1864  CD2 LEU A1251    16736  11208   7211  -5124    995    144       C  
ATOM   1865  N   ARG A1252      64.957 -58.662 336.703  1.00125.87           N  
ANISOU 1865  N   ARG A1252    20409  16080  11336  -3488   -755    862       N  
ATOM   1866  CA  ARG A1252      65.862 -59.714 336.235  1.00135.10           C  
ANISOU 1866  CA  ARG A1252    21165  17581  12588  -2992  -1281   1021       C  
ATOM   1867  C   ARG A1252      66.378 -59.438 334.828  1.00135.74           C  
ANISOU 1867  C   ARG A1252    20567  17969  13041  -2672  -1258    962       C  
ATOM   1868  O   ARG A1252      65.713 -58.782 334.024  1.00133.62           O  
ANISOU 1868  O   ARG A1252    20172  17536  13060  -2701   -818    834       O  
ATOM   1869  CB  ARG A1252      65.162 -61.079 336.264  1.00142.91           C  
ANISOU 1869  CB  ARG A1252    22388  18231  13681  -2580  -1369   1165       C  
ATOM   1870  CG  ARG A1252      64.585 -61.471 337.634  1.00157.16           C  
ANISOU 1870  CG  ARG A1252    24863  19727  15124  -2861  -1382   1268       C  
ATOM   1871  CD  ARG A1252      63.896 -62.852 337.622  1.00162.48           C  
ANISOU 1871  CD  ARG A1252    25736  20057  15942  -2452  -1499   1448       C  
ATOM   1872  NE  ARG A1252      64.458 -63.745 336.611  1.00162.84           N  
ANISOU 1872  NE  ARG A1252    25303  20276  16293  -1857  -1841   1512       N  
ATOM   1873  CZ  ARG A1252      65.502 -64.544 336.805  1.00161.95           C  
ANISOU 1873  CZ  ARG A1252    24996  20465  16072  -1589  -2402   1659       C  
ATOM   1874  NH1 ARG A1252      65.942 -65.308 335.810  1.00163.46           N  
ANISOU 1874  NH1 ARG A1252    24765  20777  16567  -1016  -2634   1685       N  
ATOM   1875  NH2 ARG A1252      66.106 -64.575 337.989  1.00158.24           N  
ANISOU 1875  NH2 ARG A1252    24764  20172  15190  -1892  -2728   1785       N  
ATOM   1876  N   ILE A1253      67.570 -59.947 334.539  1.00135.43           N  
ANISOU 1876  N   ILE A1253    20081  18381  12994  -2365  -1730   1078       N  
ATOM   1877  CA  ILE A1253      68.178 -59.778 333.229  1.00122.12           C  
ANISOU 1877  CA  ILE A1253    17734  17047  11620  -2020  -1731   1048       C  
ATOM   1878  C   ILE A1253      68.628 -61.120 332.656  1.00120.17           C  
ANISOU 1878  C   ILE A1253    17214  16923  11524  -1348  -2076   1171       C  
ATOM   1879  O   ILE A1253      68.527 -61.352 331.450  1.00135.26           O  
ANISOU 1879  O   ILE A1253    18782  18872  13738   -928  -1939   1113       O  
ATOM   1880  CB  ILE A1253      69.385 -58.819 333.287  1.00117.95           C  
ANISOU 1880  CB  ILE A1253    16794  17046  10975  -2320  -1919   1065       C  
ATOM   1881  CG1 ILE A1253      69.040 -57.569 334.103  1.00103.22           C  
ANISOU 1881  CG1 ILE A1253    15305  15027   8885  -3022  -1670    941       C  
ATOM   1882  CG2 ILE A1253      69.819 -58.435 331.884  1.00126.98           C  
ANISOU 1882  CG2 ILE A1253    17276  18520  12452  -2034  -1786   1025       C  
ATOM   1883  CD1 ILE A1253      70.180 -56.590 334.240  1.00101.15           C  
ANISOU 1883  CD1 ILE A1253    14697  15235   8502  -3389  -1890    967       C  
ATOM   1884  N   ASP A1254      69.106 -62.006 333.527  1.00109.79           N  
ANISOU 1884  N   ASP A1254    16075  15650   9989  -1250  -2522   1342       N  
ATOM   1885  CA  ASP A1254      69.702 -63.269 333.092  1.00110.83           C  
ANISOU 1885  CA  ASP A1254    15932  15920  10258   -614  -2901   1474       C  
ATOM   1886  C   ASP A1254      68.675 -64.349 332.744  1.00110.76           C  
ANISOU 1886  C   ASP A1254    16231  15412  10442   -208  -2807   1457       C  
ATOM   1887  O   ASP A1254      68.866 -65.523 333.064  1.00104.98           O  
ANISOU 1887  O   ASP A1254    15610  14585   9693    138  -3171   1603       O  
ATOM   1888  CB  ASP A1254      70.660 -63.796 334.168  1.00121.40           C  
ANISOU 1888  CB  ASP A1254    17308  17499  11320   -674  -3455   1703       C  
ATOM   1889  CG  ASP A1254      69.974 -64.040 335.502  1.00125.58           C  
ANISOU 1889  CG  ASP A1254    18529  17653  11532  -1058  -3515   1775       C  
ATOM   1890  OD1 ASP A1254      68.943 -63.391 335.774  1.00126.43           O  
ANISOU 1890  OD1 ASP A1254    19054  17417  11567  -1446  -3090   1634       O  
ATOM   1891  OD2 ASP A1254      70.472 -64.879 336.285  1.00127.32           O  
ANISOU 1891  OD2 ASP A1254    18868  17927  11580   -967  -3979   1990       O  
ATOM   1892  N   GLU A1255      67.594 -63.952 332.078  1.00116.65           N  
ANISOU 1892  N   GLU A1255    17102  15830  11392   -259  -2342   1301       N  
ATOM   1893  CA  GLU A1255      66.606 -64.907 331.588  1.00119.60           C  
ANISOU 1893  CA  GLU A1255    17718  15733  11993    113  -2256   1292       C  
ATOM   1894  C   GLU A1255      67.010 -65.442 330.218  1.00118.58           C  
ANISOU 1894  C   GLU A1255    17142  15773  12141    725  -2322   1221       C  
ATOM   1895  O   GLU A1255      66.718 -66.588 329.878  1.00109.31           O  
ANISOU 1895  O   GLU A1255    16091  14333  11108   1185  -2493   1252       O  
ATOM   1896  CB  GLU A1255      65.215 -64.269 331.518  1.00116.37           C  
ANISOU 1896  CB  GLU A1255    17647  14871  11696   -231  -1743   1197       C  
ATOM   1897  CG  GLU A1255      64.486 -64.209 332.852  1.00118.43           C  
ANISOU 1897  CG  GLU A1255    18494  14785  11717   -677  -1656   1285       C  
ATOM   1898  CD  GLU A1255      63.031 -63.797 332.708  1.00110.89           C  
ANISOU 1898  CD  GLU A1255    17850  13332  10949   -905  -1143   1234       C  
ATOM   1899  OE1 GLU A1255      62.673 -63.214 331.663  1.00106.52           O  
ANISOU 1899  OE1 GLU A1255    17035  12760  10677   -860   -829   1115       O  
ATOM   1900  OE2 GLU A1255      62.245 -64.060 333.643  1.00112.55           O  
ANISOU 1900  OE2 GLU A1255    18555  13177  11032  -1129  -1052   1339       O  
ATOM   1901  N   GLY A1256      67.688 -64.607 329.437  1.00133.53           N  
ANISOU 1901  N   GLY A1256    18531  18104  14100    724  -2185   1128       N  
ATOM   1902  CA  GLY A1256      68.140 -64.999 328.114  1.00139.70           C  
ANISOU 1902  CA  GLY A1256    18874  19109  15098   1286  -2199   1052       C  
ATOM   1903  C   GLY A1256      69.397 -65.846 328.160  1.00146.12           C  
ANISOU 1903  C   GLY A1256    19366  20289  15863   1759  -2645   1166       C  
ATOM   1904  O   GLY A1256      69.844 -66.368 327.139  1.00150.25           O  
ANISOU 1904  O   GLY A1256    19559  20987  16543   2312  -2686   1107       O  
ATOM   1905  N   GLY A1257      69.967 -65.983 329.353  1.00151.06           N  
ANISOU 1905  N   GLY A1257    20096  21031  16269   1542  -2977   1338       N  
ATOM   1906  CA  GLY A1257      71.178 -66.762 329.533  1.00152.63           C  
ANISOU 1906  CA  GLY A1257    19978  21572  16443   1948  -3430   1501       C  
ATOM   1907  C   GLY A1257      72.419 -65.987 329.138  1.00165.25           C  
ANISOU 1907  C   GLY A1257    20921  23827  18039   1933  -3460   1548       C  
ATOM   1908  O   GLY A1257      72.342 -64.806 328.797  1.00150.30           O  
ANISOU 1908  O   GLY A1257    18848  22116  16141   1559  -3148   1454       O  
ATOM   1909  N   GLY A1258      73.566 -66.656 329.183  1.00185.80           N  
ANISOU 1909  N   GLY A1258    23145  26778  20672   2343  -3839   1719       N  
ATOM   1910  CA  GLY A1258      74.829 -66.028 328.842  1.00189.95           C  
ANISOU 1910  CA  GLY A1258    22994  27954  21225   2368  -3909   1828       C  
ATOM   1911  C   GLY A1258      75.440 -65.288 330.016  1.00196.58           C  
ANISOU 1911  C   GLY A1258    23809  29055  21828   1748  -4172   2025       C  
ATOM   1912  O   GLY A1258      74.799 -65.113 331.052  1.00200.00           O  
ANISOU 1912  O   GLY A1258    24789  29163  22040   1252  -4222   2029       O  
ATOM   1913  N   SER A1259      76.686 -64.854 329.852  1.00198.37           N  
ANISOU 1913  N   SER A1259    23406  29874  22093   1768  -4343   2199       N  
ATOM   1914  CA  SER A1259      77.386 -64.120 330.900  1.00192.32           C  
ANISOU 1914  CA  SER A1259    22566  29397  21108   1167  -4648   2408       C  
ATOM   1915  C   SER A1259      76.855 -62.695 331.022  1.00187.22           C  
ANISOU 1915  C   SER A1259    22099  28708  20328    459  -4320   2248       C  
ATOM   1916  O   SER A1259      76.120 -62.221 330.156  1.00188.50           O  
ANISOU 1916  O   SER A1259    22286  28717  20619    481  -3856   2016       O  
ATOM   1917  CB  SER A1259      78.890 -64.100 330.626  1.00193.28           C  
ANISOU 1917  CB  SER A1259    21905  30171  21363   1416  -4942   2683       C  
ATOM   1918  OG  SER A1259      79.173 -63.491 329.378  1.00190.04           O  
ANISOU 1918  OG  SER A1259    20948  30101  21156   1621  -4585   2591       O  
ATOM   1919  N   GLY A1260      77.232 -62.017 332.102  1.00183.95           N  
ANISOU 1919  N   GLY A1260    21822  28414  19655   -173  -4578   2377       N  
ATOM   1920  CA  GLY A1260      76.781 -60.658 332.343  1.00173.32           C  
ANISOU 1920  CA  GLY A1260    20692  26994  18166   -870  -4302   2223       C  
ATOM   1921  C   GLY A1260      77.913 -59.649 332.350  1.00167.73           C  
ANISOU 1921  C   GLY A1260    19441  26840  17450  -1233  -4492   2392       C  
ATOM   1922  O   GLY A1260      78.004 -58.811 333.248  1.00166.80           O  
ANISOU 1922  O   GLY A1260    19582  26717  17077  -1906  -4627   2410       O  
ATOM   1923  N   GLY A1261      78.778 -59.728 331.344  1.00173.42           N  
ANISOU 1923  N   GLY A1261    19413  28034  18444   -790  -4499   2520       N  
ATOM   1924  CA  GLY A1261      79.906 -58.821 331.238  1.00175.56           C  
ANISOU 1924  CA  GLY A1261    19072  28869  18763  -1084  -4683   2732       C  
ATOM   1925  C   GLY A1261      79.719 -57.776 330.155  1.00177.08           C  
ANISOU 1925  C   GLY A1261    18924  29211  19148  -1185  -4221   2585       C  
ATOM   1926  O   GLY A1261      80.324 -56.705 330.203  1.00164.64           O  
ANISOU 1926  O   GLY A1261    17025  27960  17572  -1655  -4294   2697       O  
ATOM   1927  N   ASP A1262      78.877 -58.089 329.175  1.00182.85           N  
ANISOU 1927  N   ASP A1262    22409  25968  21098   4579   1324  -2048       N  
ATOM   1928  CA  ASP A1262      78.625 -57.175 328.067  1.00185.54           C  
ANISOU 1928  CA  ASP A1262    22799  26226  21472   4056   1605  -2097       C  
ATOM   1929  C   ASP A1262      77.285 -56.463 328.229  1.00181.42           C  
ANISOU 1929  C   ASP A1262    22635  25518  20779   3690   1475  -1915       C  
ATOM   1930  O   ASP A1262      76.524 -56.330 327.272  1.00184.04           O  
ANISOU 1930  O   ASP A1262    23335  25599  20992   3399   1660  -1830       O  
ATOM   1931  CB  ASP A1262      78.669 -57.925 326.731  1.00190.82           C  
ANISOU 1931  CB  ASP A1262    23753  26651  22097   4046   1982  -2096       C  
ATOM   1932  CG  ASP A1262      77.652 -59.048 326.653  1.00190.46           C  
ANISOU 1932  CG  ASP A1262    24289  26251  21826   4200   1955  -1882       C  
ATOM   1933  OD1 ASP A1262      77.272 -59.585 327.715  1.00191.85           O  
ANISOU 1933  OD1 ASP A1262    24584  26390  21921   4479   1688  -1758       O  
ATOM   1934  OD2 ASP A1262      77.233 -59.393 325.528  1.00187.84           O  
ANISOU 1934  OD2 ASP A1262    24312  25669  21390   4034   2219  -1855       O  
ATOM   1935  N   GLU A1263      77.008 -55.996 329.443  1.00165.74           N  
ANISOU 1935  N   GLU A1263    20534  23664  18776   3721   1147  -1870       N  
ATOM   1936  CA  GLU A1263      75.741 -55.334 329.739  1.00145.46           C  
ANISOU 1936  CA  GLU A1263    18268  20929  16070   3411   1009  -1709       C  
ATOM   1937  C   GLU A1263      75.716 -53.878 329.283  1.00127.25           C  
ANISOU 1937  C   GLU A1263    15802  18702  13845   2943   1116  -1793       C  
ATOM   1938  O   GLU A1263      74.650 -53.324 329.016  1.00119.74           O  
ANISOU 1938  O   GLU A1263    15161  17555  12779   2647   1109  -1666       O  
ATOM   1939  CB  GLU A1263      75.438 -55.409 331.237  1.00144.36           C  
ANISOU 1939  CB  GLU A1263    18115  20873  15864   3629    650  -1626       C  
ATOM   1940  CG  GLU A1263      74.799 -56.717 331.675  1.00144.20           C  
ANISOU 1940  CG  GLU A1263    18524  20596  15671   3965    577  -1444       C  
ATOM   1941  CD  GLU A1263      73.397 -56.897 331.121  1.00140.31           C  
ANISOU 1941  CD  GLU A1263    18534  19733  15043   3695    684  -1287       C  
ATOM   1942  OE1 GLU A1263      72.741 -55.879 330.810  1.00135.08           O  
ANISOU 1942  OE1 GLU A1263    17897  19041  14385   3294    684  -1277       O  
ATOM   1943  OE2 GLU A1263      72.951 -58.056 330.996  1.00141.52           O  
ANISOU 1943  OE2 GLU A1263    19053  19623  15094   3890    769  -1191       O  
ATOM   1944  N   ALA A1264      76.890 -53.262 329.193  1.00125.17           N  
ANISOU 1944  N   ALA A1264    15054  18716  13788   2884   1228  -2022       N  
ATOM   1945  CA  ALA A1264      76.983 -51.863 328.791  1.00120.14           C  
ANISOU 1945  CA  ALA A1264    14270  18134  13243   2437   1388  -2122       C  
ATOM   1946  C   ALA A1264      76.978 -51.709 327.272  1.00134.62           C  
ANISOU 1946  C   ALA A1264    16345  19765  15039   2189   1795  -2125       C  
ATOM   1947  O   ALA A1264      76.910 -50.594 326.753  1.00128.93           O  
ANISOU 1947  O   ALA A1264    15653  18999  14338   1817   1988  -2162       O  
ATOM   1948  CB  ALA A1264      78.233 -51.228 329.383  1.00107.81           C  
ANISOU 1948  CB  ALA A1264    12075  16949  11941   2436   1365  -2410       C  
ATOM   1949  N   GLU A1265      77.045 -52.833 326.564  1.00145.97           N  
ANISOU 1949  N   GLU A1265    17997  21062  16401   2407   1939  -2084       N  
ATOM   1950  CA  GLU A1265      77.127 -52.819 325.107  1.00145.14           C  
ANISOU 1950  CA  GLU A1265    18145  20771  16230   2219   2332  -2103       C  
ATOM   1951  C   GLU A1265      75.838 -53.291 324.436  1.00139.65           C  
ANISOU 1951  C   GLU A1265    18064  19745  15253   2168   2304  -1888       C  
ATOM   1952  O   GLU A1265      75.706 -53.211 323.215  1.00142.19           O  
ANISOU 1952  O   GLU A1265    18686  19890  15448   2001   2581  -1882       O  
ATOM   1953  CB  GLU A1265      78.297 -53.686 324.632  1.00151.51           C  
ANISOU 1953  CB  GLU A1265    18710  21674  17183   2473   2583  -2276       C  
ATOM   1954  CG  GLU A1265      79.677 -53.115 324.931  1.00159.47           C  
ANISOU 1954  CG  GLU A1265    19072  23013  18507   2454   2714  -2568       C  
ATOM   1955  CD  GLU A1265      80.170 -53.453 326.325  1.00163.90           C  
ANISOU 1955  CD  GLU A1265    19184  23877  19214   2806   2332  -2653       C  
ATOM   1956  OE1 GLU A1265      79.460 -54.181 327.051  1.00167.55           O  
ANISOU 1956  OE1 GLU A1265    19890  24259  19514   3080   2006  -2459       O  
ATOM   1957  OE2 GLU A1265      81.271 -52.994 326.695  1.00165.54           O  
ANISOU 1957  OE2 GLU A1265    18804  24401  19693   2813   2365  -2930       O  
ATOM   1958  N   LYS A1266      74.893 -53.779 325.233  1.00131.52           N  
ANISOU 1958  N   LYS A1266    17221  18631  14121   2307   1979  -1734       N  
ATOM   1959  CA  LYS A1266      73.647 -54.322 324.698  1.00117.76           C  
ANISOU 1959  CA  LYS A1266    15998  16596  12150   2267   1930  -1582       C  
ATOM   1960  C   LYS A1266      72.697 -53.238 324.197  1.00111.47           C  
ANISOU 1960  C   LYS A1266    15461  15675  11216   1918   1903  -1501       C  
ATOM   1961  O   LYS A1266      72.486 -52.227 324.866  1.00104.03           O  
ANISOU 1961  O   LYS A1266    14367  14825  10334   1760   1755  -1475       O  
ATOM   1962  CB  LYS A1266      72.936 -55.170 325.756  1.00106.14           C  
ANISOU 1962  CB  LYS A1266    14635  15053  10642   2503   1640  -1470       C  
ATOM   1963  CG  LYS A1266      73.581 -56.521 326.007  1.00109.79           C  
ANISOU 1963  CG  LYS A1266    15052  15514  11147   2902   1689  -1501       C  
ATOM   1964  CD  LYS A1266      72.800 -57.324 327.034  1.00111.38           C  
ANISOU 1964  CD  LYS A1266    15457  15583  11279   3115   1456  -1373       C  
ATOM   1965  CE  LYS A1266      73.448 -58.678 327.283  1.00116.84           C  
ANISOU 1965  CE  LYS A1266    16168  16235  11991   3551   1527  -1385       C  
ATOM   1966  NZ  LYS A1266      72.697 -59.486 328.285  1.00109.87           N  
ANISOU 1966  NZ  LYS A1266    15556  15170  11017   3762   1360  -1250       N  
ATOM   1967  N   LEU A1267      72.127 -53.460 323.015  1.00111.77           N  
ANISOU 1967  N   LEU A1267    15905  15503  11058   1819   2037  -1468       N  
ATOM   1968  CA  LEU A1267      71.078 -52.589 322.496  1.00104.36           C  
ANISOU 1968  CA  LEU A1267    15280  14429   9944   1566   1957  -1380       C  
ATOM   1969  C   LEU A1267      69.794 -52.836 323.274  1.00 99.50           C  
ANISOU 1969  C   LEU A1267    14790  13726   9290   1594   1611  -1280       C  
ATOM   1970  O   LEU A1267      69.596 -53.928 323.812  1.00 95.73           O  
ANISOU 1970  O   LEU A1267    14323  13204   8847   1795   1515  -1274       O  
ATOM   1971  CB  LEU A1267      70.862 -52.822 321.000  1.00 95.79           C  
ANISOU 1971  CB  LEU A1267    14608  13164   8624   1497   2167  -1395       C  
ATOM   1972  CG  LEU A1267      71.899 -52.168 320.086  1.00 96.03           C  
ANISOU 1972  CG  LEU A1267    14621  13224   8643   1367   2555  -1474       C  
ATOM   1973  CD1 LEU A1267      71.613 -52.484 318.627  1.00107.50           C  
ANISOU 1973  CD1 LEU A1267    16558  14480   9808   1329   2748  -1481       C  
ATOM   1974  CD2 LEU A1267      71.926 -50.664 320.317  1.00 88.03           C  
ANISOU 1974  CD2 LEU A1267    13514  12263   7670   1128   2571  -1439       C  
ATOM   1975  N   PHE A1268      68.928 -51.825 323.321  1.00 96.18           N  
ANISOU 1975  N   PHE A1268    14480  13260   8803   1398   1458  -1207       N  
ATOM   1976  CA  PHE A1268      67.773 -51.826 324.216  1.00 90.51           C  
ANISOU 1976  CA  PHE A1268    13795  12487   8107   1391   1152  -1135       C  
ATOM   1977  C   PHE A1268      68.277 -52.097 325.630  1.00 89.23           C  
ANISOU 1977  C   PHE A1268    13302  12468   8132   1539   1049  -1134       C  
ATOM   1978  O   PHE A1268      67.874 -53.064 326.277  1.00 83.41           O  
ANISOU 1978  O   PHE A1268    12615  11663   7415   1703    938  -1112       O  
ATOM   1979  CB  PHE A1268      66.730 -52.864 323.785  1.00 81.91           C  
ANISOU 1979  CB  PHE A1268    13016  11209   6897   1452   1057  -1147       C  
ATOM   1980  CG  PHE A1268      66.346 -52.772 322.334  1.00 90.56           C  
ANISOU 1980  CG  PHE A1268    14448  12190   7770   1361   1137  -1181       C  
ATOM   1981  CD1 PHE A1268      65.435 -51.821 321.905  1.00 89.56           C  
ANISOU 1981  CD1 PHE A1268    14501  12011   7517   1212    986  -1142       C  
ATOM   1982  CD2 PHE A1268      66.894 -53.637 321.400  1.00 98.61           C  
ANISOU 1982  CD2 PHE A1268    15627  13152   8689   1450   1357  -1257       C  
ATOM   1983  CE1 PHE A1268      65.080 -51.733 320.573  1.00 87.85           C  
ANISOU 1983  CE1 PHE A1268    14631  11698   7049   1172   1025  -1173       C  
ATOM   1984  CE2 PHE A1268      66.542 -53.554 320.067  1.00 77.12           C  
ANISOU 1984  CE2 PHE A1268    13255  10327   5721   1377   1421  -1296       C  
ATOM   1985  CZ  PHE A1268      65.634 -52.600 319.654  1.00 76.49           C  
ANISOU 1985  CZ  PHE A1268    13367  10208   5489   1248   1241  -1252       C  
ATOM   1986  N   ASN A1269      69.172 -51.225 326.087  1.00 93.36           N  
ANISOU 1986  N   ASN A1269    13510  13183   8779   1478   1101  -1170       N  
ATOM   1987  CA  ASN A1269      69.966 -51.445 327.292  1.00101.26           C  
ANISOU 1987  CA  ASN A1269    14155  14381   9939   1653   1015  -1214       C  
ATOM   1988  C   ASN A1269      69.158 -51.670 328.567  1.00105.64           C  
ANISOU 1988  C   ASN A1269    14730  14903  10505   1738    742  -1131       C  
ATOM   1989  O   ASN A1269      68.082 -51.100 328.749  1.00101.97           O  
ANISOU 1989  O   ASN A1269    14417  14327   9999   1569    612  -1060       O  
ATOM   1990  CB  ASN A1269      70.913 -50.262 327.504  1.00103.54           C  
ANISOU 1990  CB  ASN A1269    14095  14883  10364   1497   1105  -1311       C  
ATOM   1991  CG  ASN A1269      71.899 -50.503 328.626  1.00115.02           C  
ANISOU 1991  CG  ASN A1269    15133  16593  11976   1703   1002  -1412       C  
ATOM   1992  OD1 ASN A1269      72.456 -51.593 328.749  1.00117.39           O  
ANISOU 1992  OD1 ASN A1269    15362  16946  12297   1998   1009  -1447       O  
ATOM   1993  ND2 ASN A1269      72.106 -49.493 329.462  1.00118.59           N  
ANISOU 1993  ND2 ASN A1269    15321  17208  12529   1568    893  -1469       N  
ATOM   1994  N   GLN A1270      69.698 -52.507 329.448  1.00103.30           N  
ANISOU 1994  N   GLN A1270    14296  14697  10258   2022    667  -1144       N  
ATOM   1995  CA  GLN A1270      69.079 -52.791 330.736  1.00 98.02           C  
ANISOU 1995  CA  GLN A1270    13680  13988   9575   2139    449  -1065       C  
ATOM   1996  C   GLN A1270      70.118 -52.794 331.854  1.00 93.80           C  
ANISOU 1996  C   GLN A1270    12818  13711   9112   2373    327  -1122       C  
ATOM   1997  O   GLN A1270      69.937 -53.459 332.873  1.00 85.71           O  
ANISOU 1997  O   GLN A1270    11880  12653   8032   2613    186  -1058       O  
ATOM   1998  CB  GLN A1270      68.352 -54.137 330.697  1.00 93.60           C  
ANISOU 1998  CB  GLN A1270    13465  13175   8926   2310    474   -996       C  
ATOM   1999  CG  GLN A1270      67.200 -54.199 329.712  1.00 85.24           C  
ANISOU 1999  CG  GLN A1270    12711  11879   7797   2088    536   -983       C  
ATOM   2000  CD  GLN A1270      66.528 -55.557 329.693  1.00 90.26           C  
ANISOU 2000  CD  GLN A1270    13658  12262   8376   2223    595   -966       C  
ATOM   2001  OE1 GLN A1270      65.317 -55.657 329.506  1.00 95.46           O  
ANISOU 2001  OE1 GLN A1270    14533  12728   9010   2059    562   -970       O  
ATOM   2002  NE2 GLN A1270      67.313 -56.610 329.885  1.00 88.76           N  
ANISOU 2002  NE2 GLN A1270    13485  12065   8176   2527    694   -966       N  
ATOM   2003  N   ASP A1271      71.204 -52.051 331.658  1.00 96.27           N  
ANISOU 2003  N   ASP A1271    12762  14275   9540   2305    388  -1258       N  
ATOM   2004  CA  ASP A1271      72.309 -52.039 332.615  1.00102.72           C  
ANISOU 2004  CA  ASP A1271    13194  15392  10444   2537    251  -1376       C  
ATOM   2005  C   ASP A1271      71.904 -51.381 333.933  1.00104.18           C  
ANISOU 2005  C   ASP A1271    13321  15661  10604   2493     -6  -1349       C  
ATOM   2006  O   ASP A1271      71.981 -50.162 334.082  1.00 97.08           O  
ANISOU 2006  O   ASP A1271    12220  14880   9786   2211    -23  -1430       O  
ATOM   2007  CB  ASP A1271      73.523 -51.320 332.020  1.00102.20           C  
ANISOU 2007  CB  ASP A1271    12709  15572  10549   2406    418  -1583       C  
ATOM   2008  CG  ASP A1271      74.819 -51.661 332.740  1.00111.37           C  
ANISOU 2008  CG  ASP A1271    13429  17063  11823   2730    297  -1760       C  
ATOM   2009  OD1 ASP A1271      74.767 -52.085 333.914  1.00111.57           O  
ANISOU 2009  OD1 ASP A1271    13453  17170  11769   3016     19  -1717       O  
ATOM   2010  OD2 ASP A1271      75.897 -51.495 332.131  1.00118.58           O  
ANISOU 2010  OD2 ASP A1271    13998  18156  12902   2708    482  -1956       O  
ATOM   2011  N   VAL A1272      71.486 -52.203 334.889  1.00103.78           N  
ANISOU 2011  N   VAL A1272    13479  15524  10429   2773   -176  -1239       N  
ATOM   2012  CA  VAL A1272      71.024 -51.713 336.181  1.00109.13           C  
ANISOU 2012  CA  VAL A1272    14181  16242  11042   2759   -402  -1199       C  
ATOM   2013  C   VAL A1272      72.188 -51.269 337.064  1.00114.57           C  
ANISOU 2013  C   VAL A1272    14439  17310  11781   2919   -602  -1373       C  
ATOM   2014  O   VAL A1272      72.106 -50.251 337.752  1.00110.67           O  
ANISOU 2014  O   VAL A1272    13795  16945  11312   2725   -730  -1440       O  
ATOM   2015  CB  VAL A1272      70.202 -52.788 336.921  1.00102.75           C  
ANISOU 2015  CB  VAL A1272    13796  15183  10063   3013   -467  -1026       C  
ATOM   2016  CG1 VAL A1272      69.702 -52.257 338.255  1.00 91.43           C  
ANISOU 2016  CG1 VAL A1272    12428  13770   8543   2986   -666   -986       C  
ATOM   2017  CG2 VAL A1272      69.037 -53.247 336.056  1.00 98.58           C  
ANISOU 2017  CG2 VAL A1272    13643  14298   9515   2831   -275   -913       C  
ATOM   2018  N   ASP A1273      73.276 -52.031 337.029  1.00120.40           N  
ANISOU 2018  N   ASP A1273    14967  18235  12543   3280   -633  -1468       N  
ATOM   2019  CA  ASP A1273      74.438 -51.756 337.871  1.00119.45           C  
ANISOU 2019  CA  ASP A1273    14399  18514  12474   3501   -868  -1675       C  
ATOM   2020  C   ASP A1273      75.096 -50.419 337.534  1.00118.32           C  
ANISOU 2020  C   ASP A1273    13775  18627  12553   3120   -798  -1923       C  
ATOM   2021  O   ASP A1273      75.565 -49.711 338.425  1.00115.18           O  
ANISOU 2021  O   ASP A1273    13066  18507  12189   3098  -1011  -2095       O  
ATOM   2022  CB  ASP A1273      75.462 -52.887 337.744  1.00126.28           C  
ANISOU 2022  CB  ASP A1273    15117  19518  13347   3990   -895  -1741       C  
ATOM   2023  CG  ASP A1273      74.889 -54.238 338.123  1.00128.35           C  
ANISOU 2023  CG  ASP A1273    15888  19497  13381   4391   -929  -1500       C  
ATOM   2024  OD1 ASP A1273      73.664 -54.429 337.967  1.00132.56           O  
ANISOU 2024  OD1 ASP A1273    16886  19668  13812   4201   -801  -1298       O  
ATOM   2025  OD2 ASP A1273      75.660 -55.111 338.576  1.00123.40           O  
ANISOU 2025  OD2 ASP A1273    15199  19003  12683   4901  -1071  -1528       O  
ATOM   2026  N   ALA A1274      75.124 -50.079 336.249  1.00123.17           N  
ANISOU 2026  N   ALA A1274    14361  19133  13305   2817   -482  -1952       N  
ATOM   2027  CA  ALA A1274      75.758 -48.845 335.794  1.00116.63           C  
ANISOU 2027  CA  ALA A1274    13141  18484  12691   2434   -320  -2183       C  
ATOM   2028  C   ALA A1274      75.050 -47.610 336.342  1.00105.25           C  
ANISOU 2028  C   ALA A1274    11764  16994  11235   2068   -384  -2165       C  
ATOM   2029  O   ALA A1274      75.690 -46.609 336.665  1.00 94.32           O  
ANISOU 2029  O   ALA A1274     9995  15842   9999   1851   -392  -2402       O  
ATOM   2030  CB  ALA A1274      75.794 -48.798 334.276  1.00113.16           C  
ANISOU 2030  CB  ALA A1274    12796  17862  12336   2205     67  -2168       C  
ATOM   2031  N   ALA A1275      73.728 -47.688 336.444  1.00105.30           N  
ANISOU 2031  N   ALA A1275    12243  16690  11078   1993   -413  -1908       N  
ATOM   2032  CA  ALA A1275      72.934 -46.574 336.946  1.00110.78           C  
ANISOU 2032  CA  ALA A1275    13042  17295  11754   1672   -461  -1868       C  
ATOM   2033  C   ALA A1275      73.150 -46.375 338.441  1.00119.80           C  
ANISOU 2033  C   ALA A1275    14021  18661  12836   1816   -775  -1962       C  
ATOM   2034  O   ALA A1275      73.118 -45.249 338.935  1.00117.37           O  
ANISOU 2034  O   ALA A1275    13570  18438  12590   1541   -809  -2076       O  
ATOM   2035  CB  ALA A1275      71.459 -46.796 336.649  1.00105.79           C  
ANISOU 2035  CB  ALA A1275    12920  16288  10989   1588   -414  -1599       C  
ATOM   2036  N   VAL A1276      73.373 -47.476 339.154  1.00122.59           N  
ANISOU 2036  N   VAL A1276    14435  19095  13049   2260   -996  -1914       N  
ATOM   2037  CA  VAL A1276      73.577 -47.436 340.599  1.00121.19           C  
ANISOU 2037  CA  VAL A1276    14178  19123  12745   2477  -1323  -1985       C  
ATOM   2038  C   VAL A1276      74.858 -46.683 340.957  1.00119.40           C  
ANISOU 2038  C   VAL A1276    13359  19330  12678   2426  -1447  -2340       C  
ATOM   2039  O   VAL A1276      74.884 -45.910 341.917  1.00119.34           O  
ANISOU 2039  O   VAL A1276    13226  19480  12637   2318  -1633  -2468       O  
ATOM   2040  CB  VAL A1276      73.628 -48.859 341.198  1.00120.78           C  
ANISOU 2040  CB  VAL A1276    14369  19043  12478   3024  -1509  -1848       C  
ATOM   2041  CG1 VAL A1276      73.946 -48.808 342.684  1.00120.65           C  
ANISOU 2041  CG1 VAL A1276    14294  19263  12284   3296  -1867  -1932       C  
ATOM   2042  CG2 VAL A1276      72.309 -49.578 340.959  1.00115.53           C  
ANISOU 2042  CG2 VAL A1276    14285  17935  11674   3028  -1363  -1540       C  
ATOM   2043  N   ARG A1277      75.914 -46.903 340.179  1.00114.95           N  
ANISOU 2043  N   ARG A1277    12418  18957  12299   2488  -1326  -2525       N  
ATOM   2044  CA  ARG A1277      77.173 -46.200 340.395  1.00113.48           C  
ANISOU 2044  CA  ARG A1277    11602  19188  12326   2402  -1394  -2920       C  
ATOM   2045  C   ARG A1277      76.999 -44.704 340.150  1.00112.46           C  
ANISOU 2045  C   ARG A1277    11344  19019  12367   1817  -1177  -3057       C  
ATOM   2046  O   ARG A1277      77.609 -43.877 340.828  1.00113.29           O  
ANISOU 2046  O   ARG A1277    11056  19412  12576   1668  -1304  -3359       O  
ATOM   2047  CB  ARG A1277      78.273 -46.751 339.484  1.00116.92           C  
ANISOU 2047  CB  ARG A1277    11670  19791  12964   2553  -1229  -3096       C  
ATOM   2048  CG  ARG A1277      78.363 -48.269 339.429  1.00119.52           C  
ANISOU 2048  CG  ARG A1277    12204  20064  13142   3107  -1339  -2919       C  
ATOM   2049  CD  ARG A1277      79.631 -48.707 338.705  1.00125.68           C  
ANISOU 2049  CD  ARG A1277    12509  21088  14158   3280  -1211  -3170       C  
ATOM   2050  NE  ARG A1277      79.537 -50.066 338.177  1.00126.75           N  
ANISOU 2050  NE  ARG A1277    12942  21029  14186   3678  -1137  -2953       N  
ATOM   2051  CZ  ARG A1277      79.263 -50.355 336.909  1.00125.70           C  
ANISOU 2051  CZ  ARG A1277    13031  20615  14115   3508   -758  -2825       C  
ATOM   2052  NH1 ARG A1277      79.197 -51.619 336.512  1.00123.58           N  
ANISOU 2052  NH1 ARG A1277    13035  20175  13744   3879   -702  -2653       N  
ATOM   2053  NH2 ARG A1277      79.060 -49.380 336.033  1.00122.53           N  
ANISOU 2053  NH2 ARG A1277    12609  20090  13857   2978   -428  -2873       N  
ATOM   2054  N   GLY A1278      76.162 -44.365 339.173  1.00113.56           N  
ANISOU 2054  N   GLY A1278    11831  18792  12523   1500   -850  -2845       N  
ATOM   2055  CA  GLY A1278      75.896 -42.978 338.840  1.00121.54           C  
ANISOU 2055  CA  GLY A1278    12826  19688  13666    977   -602  -2921       C  
ATOM   2056  C   GLY A1278      75.088 -42.276 339.912  1.00128.32           C  
ANISOU 2056  C   GLY A1278    13871  20483  14401    845   -794  -2860       C  
ATOM   2057  O   GLY A1278      75.292 -41.091 340.179  1.00125.03           O  
ANISOU 2057  O   GLY A1278    13254  20142  14110    494   -715  -3062       O  
ATOM   2058  N   ILE A1279      74.164 -43.013 340.524  1.00132.88           N  
ANISOU 2058  N   ILE A1279    14848  20899  14740   1114  -1009  -2591       N  
ATOM   2059  CA  ILE A1279      73.346 -42.491 341.615  1.00133.64           C  
ANISOU 2059  CA  ILE A1279    15161  20917  14698   1035  -1185  -2520       C  
ATOM   2060  C   ILE A1279      74.218 -42.095 342.804  1.00137.29           C  
ANISOU 2060  C   ILE A1279    15235  21771  15157   1107  -1471  -2829       C  
ATOM   2061  O   ILE A1279      74.047 -41.021 343.382  1.00141.27           O  
ANISOU 2061  O   ILE A1279    15680  22301  15694    811  -1481  -2956       O  
ATOM   2062  CB  ILE A1279      72.289 -43.523 342.072  1.00131.45           C  
ANISOU 2062  CB  ILE A1279    15377  20395  14172   1343  -1326  -2203       C  
ATOM   2063  CG1 ILE A1279      71.220 -43.709 340.994  1.00121.31           C  
ANISOU 2063  CG1 ILE A1279    14476  18718  12899   1197  -1068  -1938       C  
ATOM   2064  CG2 ILE A1279      71.640 -43.091 343.376  1.00133.87           C  
ANISOU 2064  CG2 ILE A1279    15868  20674  14323   1320  -1522  -2175       C  
ATOM   2065  CD1 ILE A1279      70.128 -44.684 341.379  1.00113.99           C  
ANISOU 2065  CD1 ILE A1279    14009  17525  11778   1431  -1147  -1671       C  
ATOM   2066  N   LEU A1280      75.163 -42.963 343.153  1.00130.20           N  
ANISOU 2066  N   LEU A1280    14072  21182  14216   1516  -1710  -2965       N  
ATOM   2067  CA  LEU A1280      76.072 -42.704 344.264  1.00130.77           C  
ANISOU 2067  CA  LEU A1280    13741  21681  14264   1659  -2047  -3293       C  
ATOM   2068  C   LEU A1280      77.060 -41.590 343.928  1.00141.57           C  
ANISOU 2068  C   LEU A1280    14527  23313  15949   1263  -1894  -3710       C  
ATOM   2069  O   LEU A1280      77.630 -40.965 344.822  1.00139.48           O  
ANISOU 2069  O   LEU A1280    13923  23364  15708   1198  -2116  -4033       O  
ATOM   2070  CB  LEU A1280      76.828 -43.979 344.645  1.00125.44           C  
ANISOU 2070  CB  LEU A1280    12942  21263  13455   2263  -2355  -3325       C  
ATOM   2071  CG  LEU A1280      75.972 -45.171 345.081  1.00117.56           C  
ANISOU 2071  CG  LEU A1280    12536  20001  12129   2694  -2489  -2942       C  
ATOM   2072  CD1 LEU A1280      76.848 -46.363 345.441  1.00111.27           C  
ANISOU 2072  CD1 LEU A1280    11611  19463  11204   3317  -2779  -2995       C  
ATOM   2073  CD2 LEU A1280      75.072 -44.792 346.248  1.00118.81           C  
ANISOU 2073  CD2 LEU A1280    13074  20030  12037   2649  -2651  -2823       C  
ATOM   2074  N   ARG A1281      77.258 -41.347 342.637  1.00152.02           N  
ANISOU 2074  N   ARG A1281    15755  24496  17508    989  -1496  -3718       N  
ATOM   2075  CA  ARG A1281      78.151 -40.286 342.186  1.00158.90           C  
ANISOU 2075  CA  ARG A1281    16131  25541  18702    563  -1238  -4104       C  
ATOM   2076  C   ARG A1281      77.521 -38.913 342.397  1.00160.15           C  
ANISOU 2076  C   ARG A1281    16446  25502  18903     58  -1055  -4127       C  
ATOM   2077  O   ARG A1281      78.222 -37.925 342.619  1.00164.42           O  
ANISOU 2077  O   ARG A1281    16577  26242  19652   -277   -965  -4509       O  
ATOM   2078  CB  ARG A1281      78.512 -40.478 340.711  1.00160.93           C  
ANISOU 2078  CB  ARG A1281    16331  25655  19160    436   -817  -4077       C  
ATOM   2079  N   ASN A1282      76.195 -38.859 342.328  1.00156.40           N  
ANISOU 2079  N   ASN A1282    16553  24627  18244      6   -989  -3737       N  
ATOM   2080  CA  ASN A1282      75.466 -37.613 342.527  1.00146.35           C  
ANISOU 2080  CA  ASN A1282    15493  23122  16994   -418   -817  -3711       C  
ATOM   2081  C   ASN A1282      75.258 -37.331 344.011  1.00145.71           C  
ANISOU 2081  C   ASN A1282    15409  23202  16752   -351  -1170  -3815       C  
ATOM   2082  O   ASN A1282      74.878 -38.219 344.774  1.00146.39           O  
ANISOU 2082  O   ASN A1282    15705  23331  16587     47  -1502  -3646       O  
ATOM   2083  CB  ASN A1282      74.120 -37.661 341.799  1.00132.25           C  
ANISOU 2083  CB  ASN A1282    14296  20856  15097   -479   -610  -3278       C  
ATOM   2084  CG  ASN A1282      73.518 -36.283 341.588  1.00126.94           C  
ANISOU 2084  CG  ASN A1282    13813  19906  14512   -938   -319  -3263       C  
ATOM   2085  OD1 ASN A1282      73.596 -35.414 342.457  1.00128.41           O  
ANISOU 2085  OD1 ASN A1282    13876  20183  14730  -1146   -379  -3463       O  
ATOM   2086  ND2 ASN A1282      72.913 -36.077 340.423  1.00123.18           N  
ANISOU 2086  ND2 ASN A1282    13659  19085  14059  -1077     -4  -3030       N  
ATOM   2087  N   ALA A1283      75.506 -36.090 344.413  1.00139.66           N  
ANISOU 2087  N   ALA A1283    14440  22503  16120   -749  -1069  -4099       N  
ATOM   2088  CA  ALA A1283      75.399 -35.703 345.815  1.00132.50           C  
ANISOU 2088  CA  ALA A1283    13509  21769  15067   -732  -1385  -4255       C  
ATOM   2089  C   ALA A1283      73.947 -35.528 346.250  1.00124.72           C  
ANISOU 2089  C   ALA A1283    13114  20404  13871   -752  -1382  -3896       C  
ATOM   2090  O   ALA A1283      73.657 -35.435 347.443  1.00130.98           O  
ANISOU 2090  O   ALA A1283    14015  21281  14471   -659  -1650  -3938       O  
ATOM   2091  CB  ALA A1283      76.181 -34.423 346.066  1.00135.19           C  
ANISOU 2091  CB  ALA A1283    13420  22303  15644  -1184  -1247  -4721       C  
ATOM   2092  N   LYS A1284      73.038 -35.485 345.281  1.00110.01           N  
ANISOU 2092  N   LYS A1284    11626  18130  12042   -864  -1080  -3562       N  
ATOM   2093  CA  LYS A1284      71.624 -35.271 345.567  1.00101.82           C  
ANISOU 2093  CA  LYS A1284    11100  16722  10863   -903  -1040  -3248       C  
ATOM   2094  C   LYS A1284      70.856 -36.577 345.750  1.00 98.05           C  
ANISOU 2094  C   LYS A1284    10974  16124  10155   -479  -1239  -2915       C  
ATOM   2095  O   LYS A1284      69.923 -36.649 346.549  1.00101.49           O  
ANISOU 2095  O   LYS A1284    11742  16398  10422   -404  -1345  -2757       O  
ATOM   2096  CB  LYS A1284      70.973 -34.452 344.450  1.00106.11           C  
ANISOU 2096  CB  LYS A1284    11871  16884  11562  -1236   -630  -3085       C  
ATOM   2097  CG  LYS A1284      70.770 -32.984 344.780  1.00111.56           C  
ANISOU 2097  CG  LYS A1284    12583  17443  12361  -1656   -428  -3237       C  
ATOM   2098  CD  LYS A1284      69.871 -32.320 343.748  1.00120.53           C  
ANISOU 2098  CD  LYS A1284    14077  18144  13577  -1865    -72  -2986       C  
ATOM   2099  CE  LYS A1284      69.482 -30.912 344.169  1.00124.21           C  
ANISOU 2099  CE  LYS A1284    14656  18417  14121  -2226    126  -3084       C  
ATOM   2100  NZ  LYS A1284      68.509 -30.302 343.219  1.00118.86           N  
ANISOU 2100  NZ  LYS A1284    14376  17301  13483  -2347    428  -2810       N  
ATOM   2101  N   LEU A1285      71.254 -37.606 345.009  1.00 94.67           N  
ANISOU 2101  N   LEU A1285    10483  15756   9730   -219  -1252  -2826       N  
ATOM   2102  CA  LEU A1285      70.493 -38.850 344.957  1.00 92.54           C  
ANISOU 2102  CA  LEU A1285    10576  15305   9277    136  -1350  -2508       C  
ATOM   2103  C   LEU A1285      70.958 -39.892 345.973  1.00 99.54           C  
ANISOU 2103  C   LEU A1285    11439  16442   9941    582  -1704  -2544       C  
ATOM   2104  O   LEU A1285      70.173 -40.735 346.406  1.00 98.04           O  
ANISOU 2104  O   LEU A1285    11635  16068   9549    842  -1793  -2302       O  
ATOM   2105  CB  LEU A1285      70.560 -39.443 343.547  1.00 87.87           C  
ANISOU 2105  CB  LEU A1285    10010  14589   8788    183  -1145  -2368       C  
ATOM   2106  CG  LEU A1285      70.059 -38.548 342.411  1.00 90.12           C  
ANISOU 2106  CG  LEU A1285    10410  14597   9235   -182   -800  -2288       C  
ATOM   2107  CD1 LEU A1285      70.173 -39.260 341.071  1.00 99.83           C  
ANISOU 2107  CD1 LEU A1285    11698  15726  10507    -86   -632  -2159       C  
ATOM   2108  CD2 LEU A1285      68.627 -38.103 342.665  1.00 86.17           C  
ANISOU 2108  CD2 LEU A1285    10310  13761   8671   -303   -754  -2071       C  
ATOM   2109  N   LYS A1286      72.231 -39.833 346.351  1.00105.35           N  
ANISOU 2109  N   LYS A1286    11729  17588  10713    680  -1896  -2859       N  
ATOM   2110  CA  LYS A1286      72.810 -40.839 347.242  1.00111.96           C  
ANISOU 2110  CA  LYS A1286    12523  18696  11321   1173  -2265  -2909       C  
ATOM   2111  C   LYS A1286      72.155 -40.918 348.632  1.00111.77           C  
ANISOU 2111  C   LYS A1286    12860  18619  10990   1336  -2499  -2823       C  
ATOM   2112  O   LYS A1286      71.794 -42.012 349.069  1.00110.50           O  
ANISOU 2112  O   LYS A1286    13053  18354  10577   1740  -2632  -2602       O  
ATOM   2113  CB  LYS A1286      74.316 -40.607 347.401  1.00114.94           C  
ANISOU 2113  CB  LYS A1286    12281  19567  11825   1228  -2454  -3329       C  
ATOM   2114  CG  LYS A1286      74.987 -41.626 348.305  1.00125.45           C  
ANISOU 2114  CG  LYS A1286    13547  21213  12904   1802  -2883  -3400       C  
ATOM   2115  CD  LYS A1286      76.458 -41.321 348.512  1.00135.11           C  
ANISOU 2115  CD  LYS A1286    14090  22967  14280   1856  -3108  -3874       C  
ATOM   2116  CE  LYS A1286      77.092 -42.340 349.445  1.00141.07           C  
ANISOU 2116  CE  LYS A1286    14810  24044  14748   2499  -3586  -3936       C  
ATOM   2117  NZ  LYS A1286      78.533 -42.054 349.684  1.00156.29           N  
ANISOU 2117  NZ  LYS A1286    16012  26535  16836   2584  -3858  -4447       N  
ATOM   2118  N   PRO A1287      72.002 -39.778 349.339  1.00108.14           N  
ANISOU 2118  N   PRO A1287    12346  18204  10537   1025  -2518  -2999       N  
ATOM   2119  CA  PRO A1287      71.395 -39.917 350.669  1.00108.42           C  
ANISOU 2119  CA  PRO A1287    12763  18180  10252   1202  -2723  -2916       C  
ATOM   2120  C   PRO A1287      69.933 -40.352 350.608  1.00102.72           C  
ANISOU 2120  C   PRO A1287    12625  16972   9430   1206  -2511  -2525       C  
ATOM   2121  O   PRO A1287      69.447 -40.998 351.536  1.00102.19           O  
ANISOU 2121  O   PRO A1287    12958  16803   9067   1491  -2640  -2378       O  
ATOM   2122  CB  PRO A1287      71.520 -38.510 351.261  1.00108.58           C  
ANISOU 2122  CB  PRO A1287    12584  18319  10351    799  -2723  -3205       C  
ATOM   2123  CG  PRO A1287      71.568 -37.613 350.081  1.00108.02           C  
ANISOU 2123  CG  PRO A1287    12261  18132  10648    339  -2370  -3273       C  
ATOM   2124  CD  PRO A1287      72.331 -38.372 349.038  1.00107.11           C  
ANISOU 2124  CD  PRO A1287    11875  18146  10675    519  -2334  -3272       C  
ATOM   2125  N   VAL A1288      69.249 -40.000 349.525  1.00 94.99           N  
ANISOU 2125  N   VAL A1288    11699  15699   8693    899  -2182  -2378       N  
ATOM   2126  CA  VAL A1288      67.870 -40.422 349.320  1.00 91.05           C  
ANISOU 2126  CA  VAL A1288    11671  14764   8158    887  -1979  -2055       C  
ATOM   2127  C   VAL A1288      67.821 -41.924 349.066  1.00 95.02           C  
ANISOU 2127  C   VAL A1288    12393  15183   8525   1297  -2021  -1849       C  
ATOM   2128  O   VAL A1288      66.930 -42.621 349.553  1.00 98.52           O  
ANISOU 2128  O   VAL A1288    13275  15361   8799   1457  -1977  -1641       O  
ATOM   2129  CB  VAL A1288      67.219 -39.678 348.141  1.00 92.76           C  
ANISOU 2129  CB  VAL A1288    11861  14726   8658    504  -1664  -1975       C  
ATOM   2130  CG1 VAL A1288      65.741 -40.022 348.048  1.00 90.73           C  
ANISOU 2130  CG1 VAL A1288    12037  14054   8381    484  -1494  -1703       C  
ATOM   2131  CG2 VAL A1288      67.413 -38.177 348.289  1.00 97.86           C  
ANISOU 2131  CG2 VAL A1288    12286  15442   9454    105  -1582  -2191       C  
ATOM   2132  N   TYR A1289      68.795 -42.412 348.305  1.00 97.65           N  
ANISOU 2132  N   TYR A1289    12427  15730   8947   1453  -2071  -1923       N  
ATOM   2133  CA  TYR A1289      68.900 -43.831 347.981  1.00 99.60           C  
ANISOU 2133  CA  TYR A1289    12848  15912   9083   1851  -2097  -1753       C  
ATOM   2134  C   TYR A1289      69.104 -44.676 349.238  1.00 99.43           C  
ANISOU 2134  C   TYR A1289    13089  15974   8717   2307  -2357  -1714       C  
ATOM   2135  O   TYR A1289      68.585 -45.788 349.343  1.00 95.98           O  
ANISOU 2135  O   TYR A1289    13060  15290   8117   2588  -2297  -1487       O  
ATOM   2136  CB  TYR A1289      70.049 -44.060 346.994  1.00 99.40           C  
ANISOU 2136  CB  TYR A1289    12395  16140   9231   1926  -2103  -1892       C  
ATOM   2137  CG  TYR A1289      70.136 -45.465 346.437  1.00 99.08           C  
ANISOU 2137  CG  TYR A1289    12526  15995   9123   2292  -2068  -1718       C  
ATOM   2138  CD1 TYR A1289      69.365 -45.851 345.348  1.00 93.10           C  
ANISOU 2138  CD1 TYR A1289    11976  14916   8483   2161  -1794  -1526       C  
ATOM   2139  CD2 TYR A1289      71.000 -46.400 346.991  1.00 98.42           C  
ANISOU 2139  CD2 TYR A1289    12403  16138   8856   2785  -2317  -1762       C  
ATOM   2140  CE1 TYR A1289      69.445 -47.132 344.833  1.00 86.82           C  
ANISOU 2140  CE1 TYR A1289    11347  14010   7630   2472  -1739  -1390       C  
ATOM   2141  CE2 TYR A1289      71.087 -47.683 346.482  1.00 92.67           C  
ANISOU 2141  CE2 TYR A1289    11857  15284   8069   3128  -2256  -1602       C  
ATOM   2142  CZ  TYR A1289      70.308 -48.043 345.404  1.00 89.07           C  
ANISOU 2142  CZ  TYR A1289    11608  14492   7741   2950  -1952  -1421       C  
ATOM   2143  OH  TYR A1289      70.393 -49.319 344.897  1.00 93.95           O  
ANISOU 2143  OH  TYR A1289    12420  14972   8305   3269  -1870  -1284       O  
ATOM   2144  N   ASP A1290      69.857 -44.137 350.191  1.00100.05           N  
ANISOU 2144  N   ASP A1290    12954  16388   8672   2379  -2636  -1946       N  
ATOM   2145  CA  ASP A1290      70.161 -44.848 351.427  1.00105.44           C  
ANISOU 2145  CA  ASP A1290    13891  17195   8977   2852  -2933  -1933       C  
ATOM   2146  C   ASP A1290      68.964 -44.880 352.371  1.00104.67           C  
ANISOU 2146  C   ASP A1290    14377  16752   8642   2822  -2833  -1738       C  
ATOM   2147  O   ASP A1290      68.842 -45.778 353.205  1.00101.57           O  
ANISOU 2147  O   ASP A1290    14417  16267   7908   3233  -2940  -1598       O  
ATOM   2148  CB  ASP A1290      71.360 -44.205 352.127  1.00120.22           C  
ANISOU 2148  CB  ASP A1290    15314  19574  10791   2932  -3298  -2293       C  
ATOM   2149  CG  ASP A1290      72.576 -44.111 351.227  1.00128.36           C  
ANISOU 2149  CG  ASP A1290    15714  20958  12101   2926  -3361  -2540       C  
ATOM   2150  OD1 ASP A1290      72.676 -44.914 350.276  1.00133.20           O  
ANISOU 2150  OD1 ASP A1290    16320  21462  12829   3067  -3214  -2397       O  
ATOM   2151  OD2 ASP A1290      73.431 -43.234 351.471  1.00126.71           O  
ANISOU 2151  OD2 ASP A1290    15012  21127  12005   2763  -3534  -2898       O  
ATOM   2152  N   SER A1291      68.082 -43.896 352.233  1.00105.41           N  
ANISOU 2152  N   SER A1291    14499  16635   8915   2345  -2604  -1732       N  
ATOM   2153  CA  SER A1291      66.910 -43.784 353.094  1.00 94.10           C  
ANISOU 2153  CA  SER A1291    13565  14871   7317   2254  -2463  -1586       C  
ATOM   2154  C   SER A1291      65.853 -44.831 352.756  1.00 93.51           C  
ANISOU 2154  C   SER A1291    13953  14351   7224   2350  -2181  -1288       C  
ATOM   2155  O   SER A1291      65.175 -45.354 353.641  1.00 85.98           O  
ANISOU 2155  O   SER A1291    13505  13146   6018   2508  -2104  -1146       O  
ATOM   2156  CB  SER A1291      66.301 -42.384 352.985  1.00 92.44           C  
ANISOU 2156  CB  SER A1291    13207  14573   7343   1726  -2292  -1688       C  
ATOM   2157  OG  SER A1291      67.255 -41.383 353.295  1.00101.90           O  
ANISOU 2157  OG  SER A1291    13985  16154   8578   1586  -2505  -1994       O  
ATOM   2158  N   LEU A1292      65.721 -45.133 351.469  1.00 97.57           N  
ANISOU 2158  N   LEU A1292    14305  14761   8006   2241  -2007  -1213       N  
ATOM   2159  CA  LEU A1292      64.669 -46.023 350.994  1.00 95.43           C  
ANISOU 2159  CA  LEU A1292    14401  14073   7783   2251  -1720   -984       C  
ATOM   2160  C   LEU A1292      64.974 -47.493 351.266  1.00100.79           C  
ANISOU 2160  C   LEU A1292    15417  14674   8205   2737  -1757   -842       C  
ATOM   2161  O   LEU A1292      66.122 -47.872 351.501  1.00 80.20           O  
ANISOU 2161  O   LEU A1292    12668  12372   5432   3098  -2026   -912       O  
ATOM   2162  CB  LEU A1292      64.440 -45.814 349.496  1.00 95.01           C  
ANISOU 2162  CB  LEU A1292    14070  13953   8077   1975  -1548   -976       C  
ATOM   2163  CG  LEU A1292      64.126 -44.383 349.058  1.00 95.06           C  
ANISOU 2163  CG  LEU A1292    13787  13992   8340   1522  -1477  -1089       C  
ATOM   2164  CD1 LEU A1292      63.918 -44.311 347.551  1.00 96.08           C  
ANISOU 2164  CD1 LEU A1292    13727  14036   8741   1328  -1317  -1055       C  
ATOM   2165  CD2 LEU A1292      62.908 -43.852 349.801  1.00 83.85           C  
ANISOU 2165  CD2 LEU A1292    12649  12296   6914   1305  -1328  -1043       C  
ATOM   2166  N   ASP A1293      63.928 -48.311 351.236  1.00 95.24           N  
ANISOU 2166  N   ASP A1293    15158  13550   7481   2747  -1472   -657       N  
ATOM   2167  CA  ASP A1293      64.068 -49.757 351.341  1.00 88.33           C  
ANISOU 2167  CA  ASP A1293    14664  12502   6396   3167  -1410   -501       C  
ATOM   2168  C   ASP A1293      64.321 -50.353 349.960  1.00 90.43           C  
ANISOU 2168  C   ASP A1293    14710  12760   6890   3172  -1322   -479       C  
ATOM   2169  O   ASP A1293      64.305 -49.637 348.959  1.00 78.03           O  
ANISOU 2169  O   ASP A1293    12735  11296   5615   2846  -1298   -571       O  
ATOM   2170  CB  ASP A1293      62.818 -50.374 351.966  1.00 84.44           C  
ANISOU 2170  CB  ASP A1293    14771  11523   5788   3137  -1082   -345       C  
ATOM   2171  CG  ASP A1293      61.550 -49.996 351.222  1.00 90.90           C  
ANISOU 2171  CG  ASP A1293    15524  12056   6959   2659   -772   -353       C  
ATOM   2172  OD1 ASP A1293      60.921 -48.982 351.590  1.00 89.81           O  
ANISOU 2172  OD1 ASP A1293    15313  11889   6921   2341   -728   -424       O  
ATOM   2173  OD2 ASP A1293      61.182 -50.709 350.265  1.00 90.28           O  
ANISOU 2173  OD2 ASP A1293    15461  11788   7055   2613   -583   -304       O  
ATOM   2174  N   ALA A1294      64.536 -51.665 349.914  1.00 96.34           N  
ANISOU 2174  N   ALA A1294    15768  13356   7481   3550  -1251   -351       N  
ATOM   2175  CA  ALA A1294      64.884 -52.360 348.676  1.00 93.18           C  
ANISOU 2175  CA  ALA A1294    15204  12949   7252   3615  -1170   -335       C  
ATOM   2176  C   ALA A1294      63.854 -52.164 347.563  1.00 85.85           C  
ANISOU 2176  C   ALA A1294    14195  11779   6647   3168   -894   -339       C  
ATOM   2177  O   ALA A1294      64.213 -52.053 346.392  1.00 77.78           O  
ANISOU 2177  O   ALA A1294    12838  10884   5829   3056   -898   -401       O  
ATOM   2178  CB  ALA A1294      65.073 -53.845 348.951  1.00 81.14           C  
ANISOU 2178  CB  ALA A1294    14142  11201   5484   4087  -1074   -180       C  
ATOM   2179  N   VAL A1295      62.577 -52.120 347.931  1.00 93.29           N  
ANISOU 2179  N   VAL A1295    15442  12377   7627   2927   -656   -288       N  
ATOM   2180  CA  VAL A1295      61.505 -51.978 346.950  1.00 91.04           C  
ANISOU 2180  CA  VAL A1295    15086  11865   7639   2537   -425   -318       C  
ATOM   2181  C   VAL A1295      61.478 -50.576 346.344  1.00 93.71           C  
ANISOU 2181  C   VAL A1295    14962  12434   8209   2181   -549   -437       C  
ATOM   2182  O   VAL A1295      61.316 -50.416 345.134  1.00 84.74           O  
ANISOU 2182  O   VAL A1295    13604  11309   7285   1993   -503   -480       O  
ATOM   2183  CB  VAL A1295      60.129 -52.284 347.576  1.00 82.34           C  
ANISOU 2183  CB  VAL A1295    14394  10342   6549   2372   -126   -275       C  
ATOM   2184  CG1 VAL A1295      59.027 -52.149 346.535  1.00 82.38           C  
ANISOU 2184  CG1 VAL A1295    14265  10155   6880   1994     68   -352       C  
ATOM   2185  CG2 VAL A1295      60.124 -53.675 348.183  1.00 76.00           C  
ANISOU 2185  CG2 VAL A1295    14124   9248   5503   2710     66   -149       C  
ATOM   2186  N   ARG A1296      61.640 -49.564 347.191  1.00102.93           N  
ANISOU 2186  N   ARG A1296    16025  13768   9315   2100   -696   -491       N  
ATOM   2187  CA  ARG A1296      61.588 -48.177 346.740  1.00 96.10           C  
ANISOU 2187  CA  ARG A1296    14782  13077   8655   1762   -775   -599       C  
ATOM   2188  C   ARG A1296      62.884 -47.749 346.056  1.00 89.69           C  
ANISOU 2188  C   ARG A1296    13555  12636   7889   1812   -967   -692       C  
ATOM   2189  O   ARG A1296      62.925 -46.723 345.379  1.00 90.73           O  
ANISOU 2189  O   ARG A1296    13391  12877   8206   1535   -976   -773       O  
ATOM   2190  CB  ARG A1296      61.280 -47.245 347.914  1.00 87.70           C  
ANISOU 2190  CB  ARG A1296    13775  12032   7516   1635   -825   -644       C  
ATOM   2191  CG  ARG A1296      59.860 -47.369 348.438  1.00 81.74           C  
ANISOU 2191  CG  ARG A1296    13354  10899   6803   1475   -578   -592       C  
ATOM   2192  CD  ARG A1296      59.609 -46.396 349.570  1.00 77.90           C  
ANISOU 2192  CD  ARG A1296    12921  10436   6240   1345   -612   -646       C  
ATOM   2193  NE  ARG A1296      58.211 -46.386 349.989  1.00 77.52           N  
ANISOU 2193  NE  ARG A1296    13135  10028   6291   1148   -341   -626       N  
ATOM   2194  CZ  ARG A1296      57.706 -47.183 350.925  1.00 83.74           C  
ANISOU 2194  CZ  ARG A1296    14370  10549   6898   1280   -155   -555       C  
ATOM   2195  NH1 ARG A1296      58.484 -48.062 351.542  1.00 88.70           N  
ANISOU 2195  NH1 ARG A1296    15274  11226   7203   1648   -238   -472       N  
ATOM   2196  NH2 ARG A1296      56.421 -47.102 351.244  1.00 86.28           N  
ANISOU 2196  NH2 ARG A1296    14874  10545   7363   1057    129   -575       N  
ATOM   2197  N   ARG A1297      63.940 -48.536 346.239  1.00 84.20           N  
ANISOU 2197  N   ARG A1297    12848  12117   7028   2175  -1099   -687       N  
ATOM   2198  CA  ARG A1297      65.197 -48.296 345.542  1.00 87.54           C  
ANISOU 2198  CA  ARG A1297    12856  12881   7526   2241  -1241   -802       C  
ATOM   2199  C   ARG A1297      65.078 -48.719 344.084  1.00 94.15           C  
ANISOU 2199  C   ARG A1297    13623  13613   8537   2154  -1076   -769       C  
ATOM   2200  O   ARG A1297      65.663 -48.101 343.195  1.00 95.77           O  
ANISOU 2200  O   ARG A1297    13492  14002   8895   1999  -1080   -866       O  
ATOM   2201  CB  ARG A1297      66.347 -49.047 346.213  1.00 89.54           C  
ANISOU 2201  CB  ARG A1297    13097  13367   7557   2702  -1452   -826       C  
ATOM   2202  CG  ARG A1297      66.846 -48.410 347.496  1.00 88.48           C  
ANISOU 2202  CG  ARG A1297    12891  13481   7248   2796  -1703   -935       C  
ATOM   2203  CD  ARG A1297      67.964 -49.232 348.113  1.00 93.61           C  
ANISOU 2203  CD  ARG A1297    13537  14375   7658   3320  -1955   -966       C  
ATOM   2204  NE  ARG A1297      68.501 -48.601 349.314  1.00109.32           N  
ANISOU 2204  NE  ARG A1297    15430  16649   9459   3425  -2246  -1110       N  
ATOM   2205  CZ  ARG A1297      69.476 -49.115 350.056  1.00111.27           C  
ANISOU 2205  CZ  ARG A1297    15652  17167   9459   3901  -2547  -1177       C  
ATOM   2206  NH1 ARG A1297      70.027 -50.275 349.721  1.00109.93           N  
ANISOU 2206  NH1 ARG A1297    15556  17001   9213   4328  -2575  -1096       N  
ATOM   2207  NH2 ARG A1297      69.901 -48.470 351.133  1.00114.55           N  
ANISOU 2207  NH2 ARG A1297    15975  17853   9695   3968  -2831  -1338       N  
ATOM   2208  N   ALA A1298      64.311 -49.779 343.851  1.00 88.80           N  
ANISOU 2208  N   ALA A1298    13288  12624   7828   2243   -906   -646       N  
ATOM   2209  CA  ALA A1298      64.102 -50.302 342.510  1.00 92.20           C  
ANISOU 2209  CA  ALA A1298    13710  12931   8392   2174   -752   -627       C  
ATOM   2210  C   ALA A1298      63.304 -49.323 341.654  1.00102.69           C  
ANISOU 2210  C   ALA A1298    14910  14187   9921   1772   -673   -667       C  
ATOM   2211  O   ALA A1298      63.503 -49.236 340.441  1.00104.04           O  
ANISOU 2211  O   ALA A1298    14939  14396  10195   1676   -618   -699       O  
ATOM   2212  CB  ALA A1298      63.400 -51.650 342.573  1.00 88.44           C  
ANISOU 2212  CB  ALA A1298    13647  12118   7838   2336   -573   -520       C  
ATOM   2213  N   ALA A1299      62.402 -48.585 342.293  1.00 99.97           N  
ANISOU 2213  N   ALA A1299    14640  13728   9616   1562   -663   -665       N  
ATOM   2214  CA  ALA A1299      61.592 -47.597 341.591  1.00 96.79           C  
ANISOU 2214  CA  ALA A1299    14135  13250   9392   1229   -611   -698       C  
ATOM   2215  C   ALA A1299      62.414 -46.354 341.275  1.00 85.52           C  
ANISOU 2215  C   ALA A1299    12384  12083   8026   1083   -699   -779       C  
ATOM   2216  O   ALA A1299      62.175 -45.682 340.273  1.00 73.18           O  
ANISOU 2216  O   ALA A1299    10726  10499   6580    883   -645   -796       O  
ATOM   2217  CB  ALA A1299      60.367 -47.231 342.412  1.00 98.81           C  
ANISOU 2217  CB  ALA A1299    14563  13291   9691   1072   -552   -685       C  
ATOM   2218  N   LEU A1300      63.382 -46.054 342.136  1.00 87.96           N  
ANISOU 2218  N   LEU A1300    12542  12631   8247   1187   -826   -842       N  
ATOM   2219  CA  LEU A1300      64.266 -44.913 341.926  1.00 93.50           C  
ANISOU 2219  CA  LEU A1300    12914  13587   9026   1029   -878   -966       C  
ATOM   2220  C   LEU A1300      65.187 -45.163 340.736  1.00 92.33           C  
ANISOU 2220  C   LEU A1300    12568  13575   8936   1074   -821  -1012       C  
ATOM   2221  O   LEU A1300      65.507 -44.244 339.981  1.00 92.19           O  
ANISOU 2221  O   LEU A1300    12371  13625   9032    852   -737  -1081       O  
ATOM   2222  CB  LEU A1300      65.091 -44.629 343.183  1.00 92.41           C  
ANISOU 2222  CB  LEU A1300    12635  13697   8778   1142  -1053  -1072       C  
ATOM   2223  CG  LEU A1300      65.974 -43.379 343.148  1.00 79.86           C  
ANISOU 2223  CG  LEU A1300    10683  12368   7292    929  -1089  -1256       C  
ATOM   2224  CD1 LEU A1300      65.123 -42.118 343.138  1.00 67.68           C  
ANISOU 2224  CD1 LEU A1300     9189  10665   5860    579   -983  -1255       C  
ATOM   2225  CD2 LEU A1300      66.945 -43.369 344.318  1.00 77.65           C  
ANISOU 2225  CD2 LEU A1300    10225  12392   6887   1111  -1312  -1407       C  
ATOM   2226  N   ILE A1301      65.605 -46.415 340.576  1.00 94.30           N  
ANISOU 2226  N   ILE A1301    12887  13840   9104   1365   -833   -972       N  
ATOM   2227  CA  ILE A1301      66.456 -46.811 339.460  1.00 93.01           C  
ANISOU 2227  CA  ILE A1301    12566  13783   8992   1438   -752  -1017       C  
ATOM   2228  C   ILE A1301      65.713 -46.656 338.136  1.00 84.39           C  
ANISOU 2228  C   ILE A1301    11606  12482   7977   1232   -584   -955       C  
ATOM   2229  O   ILE A1301      66.278 -46.186 337.147  1.00 74.07           O  
ANISOU 2229  O   ILE A1301    10147  11256   6741   1110   -477  -1015       O  
ATOM   2230  CB  ILE A1301      66.945 -48.265 339.620  1.00 90.05           C  
ANISOU 2230  CB  ILE A1301    12290  13422   8502   1826   -788   -974       C  
ATOM   2231  CG1 ILE A1301      67.839 -48.385 340.858  1.00 86.44           C  
ANISOU 2231  CG1 ILE A1301    11685  13221   7938   2094   -999  -1052       C  
ATOM   2232  CG2 ILE A1301      67.690 -48.727 338.378  1.00 68.24           C  
ANISOU 2232  CG2 ILE A1301     9399  10725   5806   1890   -663  -1017       C  
ATOM   2233  CD1 ILE A1301      68.287 -49.798 341.163  1.00 79.01           C  
ANISOU 2233  CD1 ILE A1301    10898  12271   6850   2541  -1052   -988       C  
ATOM   2234  N   ASN A1302      64.441 -47.047 338.130  1.00 78.64           N  
ANISOU 2234  N   ASN A1302    11166  11484   7229   1196   -557   -853       N  
ATOM   2235  CA  ASN A1302      63.586 -46.878 336.961  1.00 74.90           C  
ANISOU 2235  CA  ASN A1302    10824  10824   6810   1023   -457   -817       C  
ATOM   2236  C   ASN A1302      63.481 -45.417 336.533  1.00 86.67           C  
ANISOU 2236  C   ASN A1302    12207  12346   8379    754   -430   -846       C  
ATOM   2237  O   ASN A1302      63.485 -45.115 335.341  1.00 95.46           O  
ANISOU 2237  O   ASN A1302    13350  13419   9500    661   -339   -842       O  
ATOM   2238  CB  ASN A1302      62.190 -47.440 337.235  1.00 67.88           C  
ANISOU 2238  CB  ASN A1302    10198   9668   5925   1011   -453   -759       C  
ATOM   2239  CG  ASN A1302      62.129 -48.947 337.090  1.00 69.56           C  
ANISOU 2239  CG  ASN A1302    10598   9758   6074   1224   -388   -733       C  
ATOM   2240  OD1 ASN A1302      63.142 -49.601 336.843  1.00 66.16           O  
ANISOU 2240  OD1 ASN A1302    10112   9444   5581   1420   -365   -740       O  
ATOM   2241  ND2 ASN A1302      60.935 -49.507 337.247  1.00 59.20           N  
ANISOU 2241  ND2 ASN A1302     9503   8197   4792   1182   -336   -722       N  
ATOM   2242  N   MET A1303      63.387 -44.515 337.508  1.00 82.41           N  
ANISOU 2242  N   MET A1303    11580  11856   7875    641   -493   -872       N  
ATOM   2243  CA  MET A1303      63.333 -43.085 337.221  1.00 82.50           C  
ANISOU 2243  CA  MET A1303    11512  11872   7962    390   -438   -902       C  
ATOM   2244  C   MET A1303      64.626 -42.614 336.571  1.00 89.81           C  
ANISOU 2244  C   MET A1303    12226  12985   8915    325   -327   -994       C  
ATOM   2245  O   MET A1303      64.606 -41.790 335.657  1.00101.25           O  
ANISOU 2245  O   MET A1303    13716  14363  10392    154   -192   -988       O  
ATOM   2246  CB  MET A1303      63.065 -42.282 338.493  1.00 82.04           C  
ANISOU 2246  CB  MET A1303    11403  11834   7936    285   -510   -936       C  
ATOM   2247  CG  MET A1303      61.656 -42.429 339.034  1.00 86.78           C  
ANISOU 2247  CG  MET A1303    12214  12208   8552    273   -553   -862       C  
ATOM   2248  SD  MET A1303      61.327 -41.295 340.395  1.00 97.90           S  
ANISOU 2248  SD  MET A1303    13586  13613   9999    113   -588   -910       S  
ATOM   2249  CE  MET A1303      61.636 -39.719 339.604  1.00 57.41           C  
ANISOU 2249  CE  MET A1303     8348   8498   4966   -144   -476   -952       C  
ATOM   2250  N   VAL A1304      65.749 -43.140 337.047  1.00 78.67           N  
ANISOU 2250  N   VAL A1304    10596  11803   7492    473   -371  -1090       N  
ATOM   2251  CA  VAL A1304      67.042 -42.833 336.451  1.00 87.44           C  
ANISOU 2251  CA  VAL A1304    11448  13109   8667    420   -243  -1223       C  
ATOM   2252  C   VAL A1304      67.087 -43.359 335.018  1.00 92.08           C  
ANISOU 2252  C   VAL A1304    12172  13590   9223    456    -82  -1165       C  
ATOM   2253  O   VAL A1304      67.668 -42.734 334.132  1.00103.05           O  
ANISOU 2253  O   VAL A1304    13499  14998  10659    299    119  -1226       O  
ATOM   2254  CB  VAL A1304      68.200 -43.436 337.272  1.00 87.13           C  
ANISOU 2254  CB  VAL A1304    11115  13362   8630    636   -369  -1362       C  
ATOM   2255  CG1 VAL A1304      69.543 -43.095 336.642  1.00 85.34           C  
ANISOU 2255  CG1 VAL A1304    10556  13350   8520    558   -212  -1549       C  
ATOM   2256  CG2 VAL A1304      68.147 -42.934 338.703  1.00 84.20           C  
ANISOU 2256  CG2 VAL A1304    10646  13104   8241    618   -553  -1430       C  
ATOM   2257  N   PHE A1305      66.451 -44.504 334.792  1.00 87.12           N  
ANISOU 2257  N   PHE A1305    11760  12832   8510    650   -146  -1058       N  
ATOM   2258  CA  PHE A1305      66.384 -45.092 333.459  1.00 82.58           C  
ANISOU 2258  CA  PHE A1305    11353  12145   7879    693    -15  -1013       C  
ATOM   2259  C   PHE A1305      65.514 -44.275 332.506  1.00 84.58           C  
ANISOU 2259  C   PHE A1305    11842  12200   8096    496     64   -940       C  
ATOM   2260  O   PHE A1305      65.795 -44.199 331.310  1.00 95.25           O  
ANISOU 2260  O   PHE A1305    13295  13504   9392    454    224   -939       O  
ATOM   2261  CB  PHE A1305      65.850 -46.524 333.535  1.00 88.61           C  
ANISOU 2261  CB  PHE A1305    12302  12799   8567    929    -95   -944       C  
ATOM   2262  CG  PHE A1305      66.907 -47.554 333.815  1.00 97.62           C  
ANISOU 2262  CG  PHE A1305    13294  14096   9699   1193    -93  -1000       C  
ATOM   2263  CD1 PHE A1305      68.223 -47.339 333.438  1.00 97.79           C  
ANISOU 2263  CD1 PHE A1305    13041  14330   9784   1206     18  -1120       C  
ATOM   2264  CD2 PHE A1305      66.582 -48.743 334.450  1.00 93.97           C  
ANISOU 2264  CD2 PHE A1305    12977  13554   9173   1438   -181   -942       C  
ATOM   2265  CE1 PHE A1305      69.197 -48.290 333.693  1.00 94.72           C  
ANISOU 2265  CE1 PHE A1305    12488  14100   9403   1491      1  -1186       C  
ATOM   2266  CE2 PHE A1305      67.551 -49.697 334.708  1.00 88.48           C  
ANISOU 2266  CE2 PHE A1305    12178  12987   8452   1734   -186   -979       C  
ATOM   2267  CZ  PHE A1305      68.860 -49.470 334.329  1.00 91.09           C  
ANISOU 2267  CZ  PHE A1305    12199  13557   8854   1776   -116  -1104       C  
ATOM   2268  N   GLN A1306      64.461 -43.664 333.039  1.00 85.09           N  
ANISOU 2268  N   GLN A1306    12007  12144   8178    399    -49   -882       N  
ATOM   2269  CA  GLN A1306      63.474 -42.981 332.208  1.00 81.39           C  
ANISOU 2269  CA  GLN A1306    11778  11482   7664    286    -34   -807       C  
ATOM   2270  C   GLN A1306      63.858 -41.547 331.838  1.00 85.91           C  
ANISOU 2270  C   GLN A1306    12347  12041   8254     82    122   -815       C  
ATOM   2271  O   GLN A1306      63.565 -41.096 330.731  1.00 96.37           O  
ANISOU 2271  O   GLN A1306    13901  13232   9483     39    214   -758       O  
ATOM   2272  CB  GLN A1306      62.110 -42.981 332.907  1.00 73.54           C  
ANISOU 2272  CB  GLN A1306    10882  10352   6709    289   -208   -760       C  
ATOM   2273  CG  GLN A1306      61.466 -44.358 333.015  1.00 73.05           C  
ANISOU 2273  CG  GLN A1306    10914  10216   6627    448   -301   -758       C  
ATOM   2274  CD  GLN A1306      60.204 -44.354 333.858  1.00 69.48           C  
ANISOU 2274  CD  GLN A1306    10514   9631   6255    420   -418   -750       C  
ATOM   2275  OE1 GLN A1306      59.615 -43.302 334.111  1.00 59.40           O  
ANISOU 2275  OE1 GLN A1306     9235   8297   5038    299   -455   -735       O  
ATOM   2276  NE2 GLN A1306      59.786 -45.534 334.303  1.00 61.37           N  
ANISOU 2276  NE2 GLN A1306     9548   8533   5237    531   -444   -768       N  
ATOM   2277  N   MET A1307      64.507 -40.829 332.751  1.00 86.70           N  
ANISOU 2277  N   MET A1307    12217  12266   8459    -39    159   -895       N  
ATOM   2278  CA  MET A1307      64.809 -39.420 332.502  1.00 87.29           C  
ANISOU 2278  CA  MET A1307    12307  12289   8571   -266    346   -920       C  
ATOM   2279  C   MET A1307      66.262 -39.031 332.789  1.00 87.43           C  
ANISOU 2279  C   MET A1307    12013  12511   8696   -399    525  -1094       C  
ATOM   2280  O   MET A1307      66.677 -37.910 332.492  1.00 78.73           O  
ANISOU 2280  O   MET A1307    10919  11354   7641   -621    755  -1148       O  
ATOM   2281  CB  MET A1307      63.866 -38.533 333.321  1.00 87.82           C  
ANISOU 2281  CB  MET A1307    12433  12242   8692   -363    243   -878       C  
ATOM   2282  CG  MET A1307      63.965 -38.721 334.824  1.00 93.08           C  
ANISOU 2282  CG  MET A1307    12867  13056   9445   -351     88   -958       C  
ATOM   2283  SD  MET A1307      62.587 -37.956 335.706  1.00129.53           S  
ANISOU 2283  SD  MET A1307    17612  17491  14110   -421    -33   -891       S  
ATOM   2284  CE  MET A1307      62.666 -36.280 335.079  1.00122.96           C  
ANISOU 2284  CE  MET A1307    16908  16503  13307   -657    201   -881       C  
ATOM   2285  N   GLY A1308      67.034 -39.951 333.358  1.00 92.87           N  
ANISOU 2285  N   GLY A1308    12428  13430   9430   -257    430  -1198       N  
ATOM   2286  CA  GLY A1308      68.436 -39.690 333.632  1.00 92.55           C  
ANISOU 2286  CA  GLY A1308    12020  13630   9514   -350    559  -1411       C  
ATOM   2287  C   GLY A1308      68.673 -39.127 335.020  1.00103.75           C  
ANISOU 2287  C   GLY A1308    13178  15215  11028   -435    419  -1547       C  
ATOM   2288  O   GLY A1308      67.729 -38.751 335.713  1.00103.86           O  
ANISOU 2288  O   GLY A1308    13337  15115  11010   -465    279  -1458       O  
ATOM   2289  N   GLU A1309      69.938 -39.064 335.421  1.00114.19           N  
ANISOU 2289  N   GLU A1309    14102  16815  12471   -472    456  -1786       N  
ATOM   2290  CA  GLU A1309      70.304 -38.584 336.750  1.00116.32           C  
ANISOU 2290  CA  GLU A1309    14088  17293  12813   -536    292  -1966       C  
ATOM   2291  C   GLU A1309      69.970 -37.108 336.936  1.00115.75           C  
ANISOU 2291  C   GLU A1309    14091  17078  12812   -881    451  -2010       C  
ATOM   2292  O   GLU A1309      69.567 -36.686 338.019  1.00125.98           O  
ANISOU 2292  O   GLU A1309    15372  18399  14097   -926    284  -2040       O  
ATOM   2293  CB  GLU A1309      71.794 -38.809 337.005  1.00123.72           C  
ANISOU 2293  CB  GLU A1309    14535  18589  13883   -498    293  -2264       C  
ATOM   2294  CG  GLU A1309      72.264 -40.226 336.735  1.00133.69           C  
ANISOU 2294  CG  GLU A1309    15712  19990  15095   -138    178  -2237       C  
ATOM   2295  CD  GLU A1309      73.746 -40.401 336.991  1.00143.51           C  
ANISOU 2295  CD  GLU A1309    16424  21608  16496    -73    163  -2560       C  
ATOM   2296  OE1 GLU A1309      74.312 -39.607 337.772  1.00143.61           O  
ANISOU 2296  OE1 GLU A1309    16108  21832  16623   -243    108  -2818       O  
ATOM   2297  OE2 GLU A1309      74.346 -41.328 336.408  1.00146.32           O  
ANISOU 2297  OE2 GLU A1309    16671  22052  16871    149    206  -2581       O  
ATOM   2298  N   THR A1310      70.146 -36.329 335.874  1.00111.40           N  
ANISOU 2298  N   THR A1310    13657  16352  12317  -1118    798  -2013       N  
ATOM   2299  CA  THR A1310      69.913 -34.891 335.927  1.00107.27           C  
ANISOU 2299  CA  THR A1310    13247  15647  11863  -1447   1017  -2054       C  
ATOM   2300  C   THR A1310      68.443 -34.568 336.183  1.00102.85           C  
ANISOU 2300  C   THR A1310    13070  14818  11189  -1402    883  -1807       C  
ATOM   2301  O   THR A1310      68.121 -33.657 336.946  1.00106.43           O  
ANISOU 2301  O   THR A1310    13535  15212  11692  -1573    882  -1860       O  
ATOM   2302  CB  THR A1310      70.360 -34.205 334.622  1.00101.60           C  
ANISOU 2302  CB  THR A1310    12678  14738  11188  -1672   1462  -2069       C  
ATOM   2303  OG1 THR A1310      71.691 -34.621 334.293  1.00 96.18           O  
ANISOU 2303  OG1 THR A1310    11624  14293  10629  -1701   1616  -2308       O  
ATOM   2304  CG2 THR A1310      70.327 -32.691 334.773  1.00 99.86           C  
ANISOU 2304  CG2 THR A1310    12550  14333  11059  -2026   1740  -2157       C  
ATOM   2305  N   GLY A1311      67.556 -35.323 335.542  1.00 94.72           N  
ANISOU 2305  N   GLY A1311    12335  13633  10022  -1176    776  -1564       N  
ATOM   2306  CA  GLY A1311      66.127 -35.107 335.678  1.00 90.92           C  
ANISOU 2306  CA  GLY A1311    12176  12909   9461  -1111    645  -1358       C  
ATOM   2307  C   GLY A1311      65.589 -35.527 337.032  1.00 92.90           C  
ANISOU 2307  C   GLY A1311    12332  13255   9710   -997    351  -1364       C  
ATOM   2308  O   GLY A1311      64.749 -34.841 337.614  1.00 90.69           O  
ANISOU 2308  O   GLY A1311    12181  12830   9447  -1075    313  -1315       O  
ATOM   2309  N   VAL A1312      66.072 -36.661 337.530  1.00 89.93           N  
ANISOU 2309  N   VAL A1312    11762  13105   9302   -796    164  -1420       N  
ATOM   2310  CA  VAL A1312      65.654 -37.168 338.832  1.00 95.19           C  
ANISOU 2310  CA  VAL A1312    12391  13853   9923   -658    -90  -1421       C  
ATOM   2311  C   VAL A1312      66.115 -36.225 339.941  1.00103.96           C  
ANISOU 2311  C   VAL A1312    13305  15098  11099   -847   -105  -1610       C  
ATOM   2312  O   VAL A1312      65.404 -36.008 340.924  1.00 99.13           O  
ANISOU 2312  O   VAL A1312    12789  14421  10454   -852   -222  -1585       O  
ATOM   2313  CB  VAL A1312      66.204 -38.587 339.086  1.00 95.19           C  
ANISOU 2313  CB  VAL A1312    12267  14054   9847   -366   -263  -1437       C  
ATOM   2314  CG1 VAL A1312      65.813 -39.078 340.472  1.00 86.25           C  
ANISOU 2314  CG1 VAL A1312    11166  12978   8628   -209   -493  -1430       C  
ATOM   2315  CG2 VAL A1312      65.697 -39.548 338.022  1.00 90.61           C  
ANISOU 2315  CG2 VAL A1312    11899  13324   9204   -198   -235  -1271       C  
ATOM   2316  N   ALA A1313      67.301 -35.651 339.766  1.00106.83           N  
ANISOU 2316  N   ALA A1313    13390  15638  11561  -1023     37  -1825       N  
ATOM   2317  CA  ALA A1313      67.844 -34.700 340.730  1.00101.68           C  
ANISOU 2317  CA  ALA A1313    12515  15131  10988  -1245     43  -2065       C  
ATOM   2318  C   ALA A1313      67.159 -33.340 340.609  1.00103.32           C  
ANISOU 2318  C   ALA A1313    12939  15055  11263  -1535    264  -2023       C  
ATOM   2319  O   ALA A1313      67.415 -32.433 341.402  1.00111.57           O  
ANISOU 2319  O   ALA A1313    13864  16153  12374  -1755    303  -2211       O  
ATOM   2320  CB  ALA A1313      69.348 -34.555 340.544  1.00100.80           C  
ANISOU 2320  CB  ALA A1313    11990  15310  11000  -1359    143  -2359       C  
ATOM   2321  N   GLY A1314      66.289 -33.205 339.612  1.00102.82           N  
ANISOU 2321  N   GLY A1314    13203  14690  11172  -1515    399  -1789       N  
ATOM   2322  CA  GLY A1314      65.543 -31.978 339.400  1.00 97.24           C  
ANISOU 2322  CA  GLY A1314    12756  13680  10509  -1714    598  -1710       C  
ATOM   2323  C   GLY A1314      64.323 -31.875 340.297  1.00 86.08           C  
ANISOU 2323  C   GLY A1314    11517  12130   9061  -1641    426  -1601       C  
ATOM   2324  O   GLY A1314      63.853 -30.778 340.594  1.00 84.87           O  
ANISOU 2324  O   GLY A1314    11492  11789   8965  -1818    555  -1610       O  
ATOM   2325  N   PHE A1315      63.808 -33.024 340.723  1.00 95.15           N  
ANISOU 2325  N   PHE A1315    12681  13349  10122  -1384    169  -1505       N  
ATOM   2326  CA  PHE A1315      62.669 -33.068 341.635  1.00106.51           C  
ANISOU 2326  CA  PHE A1315    14270  14660  11537  -1314     35  -1424       C  
ATOM   2327  C   PHE A1315      63.133 -32.900 343.078  1.00 99.63           C  
ANISOU 2327  C   PHE A1315    13234  13980  10640  -1384    -74  -1609       C  
ATOM   2328  O   PHE A1315      63.255 -33.877 343.816  1.00102.90           O  
ANISOU 2328  O   PHE A1315    13594  14556  10948  -1191   -279  -1623       O  
ATOM   2329  CB  PHE A1315      61.905 -34.385 341.480  1.00113.08           C  
ANISOU 2329  CB  PHE A1315    15219  15452  12293  -1037   -138  -1264       C  
ATOM   2330  CG  PHE A1315      61.304 -34.582 340.118  1.00114.19           C  
ANISOU 2330  CG  PHE A1315    15535  15414  12440   -953    -79  -1105       C  
ATOM   2331  CD1 PHE A1315      60.625 -33.553 339.487  1.00116.97           C  
ANISOU 2331  CD1 PHE A1315    16069  15527  12846  -1051     54  -1027       C  
ATOM   2332  CD2 PHE A1315      61.427 -35.797 339.463  1.00107.63           C  
ANISOU 2332  CD2 PHE A1315    14706  14649  11538   -756   -162  -1040       C  
ATOM   2333  CE1 PHE A1315      60.073 -33.733 338.234  1.00112.63           C  
ANISOU 2333  CE1 PHE A1315    15701  14833  12261   -936     66   -892       C  
ATOM   2334  CE2 PHE A1315      60.879 -35.983 338.210  1.00102.80           C  
ANISOU 2334  CE2 PHE A1315    14265  13889  10906   -679   -129   -920       C  
ATOM   2335  CZ  PHE A1315      60.201 -34.950 337.594  1.00106.43           C  
ANISOU 2335  CZ  PHE A1315    14905  14135  11399   -760    -32   -847       C  
ATOM   2336  N   THR A1316      63.388 -31.659 343.476  1.00 88.80           N  
ANISOU 2336  N   THR A1316    11817  12575   9347  -1651     72  -1755       N  
ATOM   2337  CA  THR A1316      63.956 -31.380 344.790  1.00 94.57           C  
ANISOU 2337  CA  THR A1316    12375  13515  10043  -1748    -32  -1982       C  
ATOM   2338  C   THR A1316      62.991 -31.701 345.932  1.00 95.07           C  
ANISOU 2338  C   THR A1316    12619  13497  10005  -1626   -185  -1910       C  
ATOM   2339  O   THR A1316      63.322 -32.475 346.831  1.00 91.84           O  
ANISOU 2339  O   THR A1316    12146  13296   9452  -1461   -401  -1975       O  
ATOM   2340  CB  THR A1316      64.392 -29.908 344.903  1.00 90.88           C  
ANISOU 2340  CB  THR A1316    11839  12993   9700  -2105    204  -2180       C  
ATOM   2341  OG1 THR A1316      65.348 -29.612 343.876  1.00 99.92           O  
ANISOU 2341  OG1 THR A1316    12826  14196  10945  -2246    403  -2273       O  
ATOM   2342  CG2 THR A1316      65.020 -29.644 346.259  1.00 86.91           C  
ANISOU 2342  CG2 THR A1316    11135  12739   9146  -2210     66  -2459       C  
ATOM   2343  N   ASN A1317      61.801 -31.108 345.893  1.00 95.26           N  
ANISOU 2343  N   ASN A1317    12886  13208  10099  -1690    -60  -1778       N  
ATOM   2344  CA  ASN A1317      60.806 -31.306 346.946  1.00 95.95           C  
ANISOU 2344  CA  ASN A1317    13154  13174  10128  -1613   -133  -1726       C  
ATOM   2345  C   ASN A1317      60.336 -32.753 347.067  1.00 89.24           C  
ANISOU 2345  C   ASN A1317    12398  12341   9169  -1321   -296  -1584       C  
ATOM   2346  O   ASN A1317      59.986 -33.209 348.156  1.00 86.27           O  
ANISOU 2346  O   ASN A1317    12136  11968   8675  -1230   -380  -1595       O  
ATOM   2347  CB  ASN A1317      59.596 -30.399 346.715  1.00100.73           C  
ANISOU 2347  CB  ASN A1317    13964  13434  10875  -1716     51  -1622       C  
ATOM   2348  CG  ASN A1317      59.869 -28.955 347.084  1.00102.97           C  
ANISOU 2348  CG  ASN A1317    14241  13646  11238  -2004    233  -1776       C  
ATOM   2349  OD1 ASN A1317      60.671 -28.671 347.973  1.00 97.45           O  
ANISOU 2349  OD1 ASN A1317    13412  13143  10470  -2138    191  -1989       O  
ATOM   2350  ND2 ASN A1317      59.196 -28.034 346.405  1.00112.11           N  
ANISOU 2350  ND2 ASN A1317    15548  14516  12532  -2087    432  -1682       N  
ATOM   2351  N   SER A1318      60.324 -33.469 345.947  1.00 81.23           N  
ANISOU 2351  N   SER A1318    11369  11314   8182  -1183   -310  -1457       N  
ATOM   2352  CA  SER A1318      59.887 -34.859 345.937  1.00 80.23           C  
ANISOU 2352  CA  SER A1318    11342  11173   7971   -928   -423  -1334       C  
ATOM   2353  C   SER A1318      60.904 -35.767 346.622  1.00 76.46           C  
ANISOU 2353  C   SER A1318    10770  10972   7308   -754   -598  -1413       C  
ATOM   2354  O   SER A1318      60.534 -36.681 347.360  1.00 73.61           O  
ANISOU 2354  O   SER A1318    10570  10580   6818   -570   -675  -1357       O  
ATOM   2355  CB  SER A1318      59.638 -35.332 344.503  1.00 82.53           C  
ANISOU 2355  CB  SER A1318    11645  11380   8333   -841   -391  -1205       C  
ATOM   2356  OG  SER A1318      58.554 -34.634 343.916  1.00 85.77           O  
ANISOU 2356  OG  SER A1318    12175  11533   8882   -923   -282  -1124       O  
ATOM   2357  N   LEU A1319      62.185 -35.512 346.373  1.00 73.24           N  
ANISOU 2357  N   LEU A1319    10109  10826   6892   -800   -645  -1552       N  
ATOM   2358  CA  LEU A1319      63.255 -36.271 347.011  1.00 76.77           C  
ANISOU 2358  CA  LEU A1319    10413  11581   7174   -605   -848  -1663       C  
ATOM   2359  C   LEU A1319      63.267 -36.028 348.516  1.00 80.84           C  
ANISOU 2359  C   LEU A1319    11003  12179   7535   -598   -968  -1779       C  
ATOM   2360  O   LEU A1319      63.485 -36.948 349.303  1.00 74.74           O  
ANISOU 2360  O   LEU A1319    10327  11519   6551   -333  -1143  -1767       O  
ATOM   2361  CB  LEU A1319      64.613 -35.905 346.408  1.00 76.28           C  
ANISOU 2361  CB  LEU A1319    10000  11792   7191   -694   -850  -1845       C  
ATOM   2362  CG  LEU A1319      64.884 -36.378 344.978  1.00 82.44           C  
ANISOU 2362  CG  LEU A1319    10710  12549   8064   -640   -750  -1751       C  
ATOM   2363  CD1 LEU A1319      66.230 -35.865 344.488  1.00 67.64           C  
ANISOU 2363  CD1 LEU A1319     8480  10924   6294   -782   -688  -1972       C  
ATOM   2364  CD2 LEU A1319      64.820 -37.895 344.895  1.00 64.64           C  
ANISOU 2364  CD2 LEU A1319     8560  10320   5682   -293   -884  -1614       C  
ATOM   2365  N   ARG A1320      63.024 -34.780 348.904  1.00 88.17           N  
ANISOU 2365  N   ARG A1320    11924  13031   8547   -879   -859  -1887       N  
ATOM   2366  CA  ARG A1320      62.983 -34.395 350.309  1.00 94.15           C  
ANISOU 2366  CA  ARG A1320    12775  13846   9154   -916   -947  -2018       C  
ATOM   2367  C   ARG A1320      61.846 -35.107 351.035  1.00 94.62           C  
ANISOU 2367  C   ARG A1320    13205  13667   9078   -747   -932  -1842       C  
ATOM   2368  O   ARG A1320      61.921 -35.357 352.239  1.00 97.87           O  
ANISOU 2368  O   ARG A1320    13773  14153   9260   -631  -1054  -1902       O  
ATOM   2369  CB  ARG A1320      62.831 -32.875 350.438  1.00102.69           C  
ANISOU 2369  CB  ARG A1320    13803  14830  10385  -1278   -772  -2160       C  
ATOM   2370  CG  ARG A1320      62.913 -32.348 351.864  1.00112.24           C  
ANISOU 2370  CG  ARG A1320    15086  16123  11438  -1359   -855  -2345       C  
ATOM   2371  CD  ARG A1320      61.582 -31.771 352.324  1.00116.26           C  
ANISOU 2371  CD  ARG A1320    15899  16275  11999  -1488   -655  -2242       C  
ATOM   2372  NE  ARG A1320      61.254 -30.523 351.641  1.00116.71           N  
ANISOU 2372  NE  ARG A1320    15906  16129  12311  -1788   -403  -2262       N  
ATOM   2373  CZ  ARG A1320      60.150 -29.816 351.866  1.00122.79           C  
ANISOU 2373  CZ  ARG A1320    16887  16583  13185  -1917   -203  -2194       C  
ATOM   2374  NH1 ARG A1320      59.262 -30.235 352.757  1.00124.77           N  
ANISOU 2374  NH1 ARG A1320    17393  16687  13329  -1808   -202  -2120       N  
ATOM   2375  NH2 ARG A1320      59.934 -28.690 351.199  1.00124.99           N  
ANISOU 2375  NH2 ARG A1320    17140  16673  13676  -2145     20  -2204       N  
ATOM   2376  N   MET A1321      60.797 -35.440 350.290  1.00 86.91           N  
ANISOU 2376  N   MET A1321    12378  12403   8241   -734   -775  -1643       N  
ATOM   2377  CA  MET A1321      59.628 -36.100 350.856  1.00 83.09           C  
ANISOU 2377  CA  MET A1321    12218  11655   7696   -624   -692  -1504       C  
ATOM   2378  C   MET A1321      59.853 -37.601 351.010  1.00 88.65           C  
ANISOU 2378  C   MET A1321    13063  12412   8206   -299   -803  -1402       C  
ATOM   2379  O   MET A1321      59.403 -38.208 351.982  1.00 89.32           O  
ANISOU 2379  O   MET A1321    13446  12382   8109   -162   -784  -1354       O  
ATOM   2380  CB  MET A1321      58.400 -35.833 349.985  1.00 77.91           C  
ANISOU 2380  CB  MET A1321    11614  10690   7296   -744   -492  -1383       C  
ATOM   2381  CG  MET A1321      57.163 -35.422 350.765  1.00 79.51           C  
ANISOU 2381  CG  MET A1321    12034  10613   7561   -850   -323  -1374       C  
ATOM   2382  SD  MET A1321      57.485 -34.076 351.924  1.00104.18           S  
ANISOU 2382  SD  MET A1321    15168  13799  10615  -1069   -299  -1557       S  
ATOM   2383  CE  MET A1321      58.172 -32.830 350.838  1.00116.18           C  
ANISOU 2383  CE  MET A1321    16389  15419  12333  -1292   -273  -1637       C  
ATOM   2384  N   LEU A1322      60.549 -38.195 350.046  1.00 90.43           N  
ANISOU 2384  N   LEU A1322    13109  12787   8464   -173   -887  -1367       N  
ATOM   2385  CA  LEU A1322      60.879 -39.614 350.106  1.00 85.35           C  
ANISOU 2385  CA  LEU A1322    12593  12195   7643    155   -985  -1275       C  
ATOM   2386  C   LEU A1322      61.857 -39.891 351.245  1.00 81.21           C  
ANISOU 2386  C   LEU A1322    12098  11935   6822    376  -1212  -1377       C  
ATOM   2387  O   LEU A1322      61.800 -40.939 351.889  1.00 79.66           O  
ANISOU 2387  O   LEU A1322    12189  11685   6392    665  -1260  -1285       O  
ATOM   2388  CB  LEU A1322      61.470 -40.086 348.776  1.00 69.53           C  
ANISOU 2388  CB  LEU A1322    10368  10299   5752    227  -1012  -1238       C  
ATOM   2389  CG  LEU A1322      60.535 -40.061 347.565  1.00 72.89           C  
ANISOU 2389  CG  LEU A1322    10808  10479   6409     90   -835  -1130       C  
ATOM   2390  CD1 LEU A1322      61.305 -40.342 346.283  1.00 67.12           C  
ANISOU 2390  CD1 LEU A1322     9859   9891   5752    139   -864  -1125       C  
ATOM   2391  CD2 LEU A1322      59.407 -41.067 347.748  1.00 68.11           C  
ANISOU 2391  CD2 LEU A1322    10510   9584   5786    200   -718  -1003       C  
ATOM   2392  N   GLN A1323      62.749 -38.938 351.490  1.00 68.78           N  
ANISOU 2392  N   GLN A1323    10241  10642   5253    245  -1348  -1581       N  
ATOM   2393  CA  GLN A1323      63.784 -39.096 352.502  1.00 76.33           C  
ANISOU 2393  CA  GLN A1323    11145  11919   5937    458  -1624  -1737       C  
ATOM   2394  C   GLN A1323      63.204 -39.024 353.912  1.00 81.20           C  
ANISOU 2394  C   GLN A1323    12139  12415   6299    507  -1634  -1733       C  
ATOM   2395  O   GLN A1323      63.788 -39.552 354.857  1.00 79.25           O  
ANISOU 2395  O   GLN A1323    12032  12350   5730    805  -1863  -1783       O  
ATOM   2396  CB  GLN A1323      64.870 -38.032 352.319  1.00 85.95           C  
ANISOU 2396  CB  GLN A1323    11907  13472   7278    248  -1739  -2014       C  
ATOM   2397  CG  GLN A1323      66.143 -38.290 353.109  1.00 95.62           C  
ANISOU 2397  CG  GLN A1323    12942  15119   8269    502  -2084  -2232       C  
ATOM   2398  CD  GLN A1323      67.280 -37.375 352.694  1.00103.10           C  
ANISOU 2398  CD  GLN A1323    13357  16404   9414    273  -2157  -2544       C  
ATOM   2399  OE1 GLN A1323      67.174 -36.640 351.710  1.00105.64           O  
ANISOU 2399  OE1 GLN A1323    13489  16618  10031    -54  -1919  -2560       O  
ATOM   2400  NE2 GLN A1323      68.377 -37.416 353.442  1.00101.64           N  
ANISOU 2400  NE2 GLN A1323    12935  16625   9061    451  -2479  -2809       N  
ATOM   2401  N   GLN A1324      62.054 -38.370 354.048  1.00 75.34           N  
ANISOU 2401  N   GLN A1324    11575  11362   5689    235  -1385  -1678       N  
ATOM   2402  CA  GLN A1324      61.373 -38.278 355.337  1.00 82.47           C  
ANISOU 2402  CA  GLN A1324    12868  12092   6374    246  -1320  -1669       C  
ATOM   2403  C   GLN A1324      60.209 -39.260 355.421  1.00 87.85           C  
ANISOU 2403  C   GLN A1324    13966  12386   7026    365  -1082  -1440       C  
ATOM   2404  O   GLN A1324      59.405 -39.204 356.353  1.00 87.98           O  
ANISOU 2404  O   GLN A1324    14339  12168   6922    327   -922  -1411       O  
ATOM   2405  CB  GLN A1324      60.868 -36.858 355.583  1.00 85.78           C  
ANISOU 2405  CB  GLN A1324    13217  12411   6963   -139  -1170  -1796       C  
ATOM   2406  CG  GLN A1324      61.958 -35.804 355.609  1.00 83.84           C  
ANISOU 2406  CG  GLN A1324    12592  12506   6757   -317  -1344  -2063       C  
ATOM   2407  CD  GLN A1324      61.401 -34.407 355.791  1.00 83.21           C  
ANISOU 2407  CD  GLN A1324    12486  12270   6860   -702  -1144  -2175       C  
ATOM   2408  OE1 GLN A1324      60.232 -34.233 356.138  1.00 80.14           O  
ANISOU 2408  OE1 GLN A1324    12382  11549   6518   -795   -914  -2069       O  
ATOM   2409  NE2 GLN A1324      62.235 -33.403 355.553  1.00 81.75           N  
ANISOU 2409  NE2 GLN A1324    11956  12308   6798   -934  -1201  -2406       N  
ATOM   2410  N   LYS A1325      60.126 -40.143 354.428  1.00 82.74           N  
ANISOU 2410  N   LYS A1325    13268  11667   6504    486  -1033  -1302       N  
ATOM   2411  CA  LYS A1325      59.115 -41.199 354.369  1.00 79.43           C  
ANISOU 2411  CA  LYS A1325    13199  10891   6088    590   -796  -1120       C  
ATOM   2412  C   LYS A1325      57.681 -40.667 354.299  1.00 78.13           C  
ANISOU 2412  C   LYS A1325    13126  10374   6185    290   -483  -1100       C  
ATOM   2413  O   LYS A1325      56.731 -41.371 354.647  1.00 79.34           O  
ANISOU 2413  O   LYS A1325    13611  10210   6325    324   -241  -1011       O  
ATOM   2414  CB  LYS A1325      59.264 -42.144 355.565  1.00 77.05           C  
ANISOU 2414  CB  LYS A1325    13364  10533   5380    920   -829  -1050       C  
ATOM   2415  CG  LYS A1325      60.615 -42.842 355.621  1.00 83.76           C  
ANISOU 2415  CG  LYS A1325    14146  11716   5964   1303  -1154  -1058       C  
ATOM   2416  CD  LYS A1325      60.629 -43.967 356.641  1.00 96.01           C  
ANISOU 2416  CD  LYS A1325    16247  13133   7100   1695  -1150   -934       C  
ATOM   2417  CE  LYS A1325      61.892 -44.799 356.508  1.00115.38           C  
ANISOU 2417  CE  LYS A1325    18621  15887   9331   2131  -1464   -920       C  
ATOM   2418  NZ  LYS A1325      62.045 -45.351 355.133  1.00122.39           N  
ANISOU 2418  NZ  LYS A1325    19228  16773  10500   2130  -1410   -854       N  
ATOM   2419  N   ARG A1326      57.529 -39.431 353.836  1.00 64.82           N  
ANISOU 2419  N   ARG A1326    11144   8734   4750      2   -468  -1195       N  
ATOM   2420  CA  ARG A1326      56.210 -38.850 353.616  1.00 72.14           C  
ANISOU 2420  CA  ARG A1326    12087   9358   5964   -251   -207  -1189       C  
ATOM   2421  C   ARG A1326      55.732 -39.212 352.210  1.00 78.58           C  
ANISOU 2421  C   ARG A1326    12715  10080   7063   -281   -148  -1115       C  
ATOM   2422  O   ARG A1326      55.835 -38.412 351.280  1.00 74.36           O  
ANISOU 2422  O   ARG A1326    11896   9623   6733   -423   -196  -1145       O  
ATOM   2423  CB  ARG A1326      56.254 -37.333 353.820  1.00 69.04           C  
ANISOU 2423  CB  ARG A1326    11519   9030   5683   -510   -210  -1320       C  
ATOM   2424  CG  ARG A1326      56.633 -36.924 355.242  1.00 77.40           C  
ANISOU 2424  CG  ARG A1326    12778  10172   6460   -508   -262  -1427       C  
ATOM   2425  CD  ARG A1326      57.287 -35.550 355.302  1.00 72.76           C  
ANISOU 2425  CD  ARG A1326    11934   9785   5924   -726   -362  -1599       C  
ATOM   2426  NE  ARG A1326      56.357 -34.468 354.988  1.00 77.07           N  
ANISOU 2426  NE  ARG A1326    12412  10099   6773  -1001   -139  -1623       N  
ATOM   2427  CZ  ARG A1326      56.657 -33.176 355.084  1.00 77.76           C  
ANISOU 2427  CZ  ARG A1326    12350  10250   6943  -1231   -126  -1765       C  
ATOM   2428  NH1 ARG A1326      57.863 -32.800 355.488  1.00 66.89           N  
ANISOU 2428  NH1 ARG A1326    10843   9184   5389  -1254   -326  -1929       N  
ATOM   2429  NH2 ARG A1326      55.752 -32.256 354.777  1.00 64.72           N  
ANISOU 2429  NH2 ARG A1326    10676   8353   5563  -1431     89  -1763       N  
ATOM   2430  N   TRP A1327      55.209 -40.428 352.073  1.00 72.78           N  
ANISOU 2430  N   TRP A1327    12173   9162   6318   -144    -30  -1027       N  
ATOM   2431  CA  TRP A1327      54.920 -41.014 350.767  1.00 71.05           C  
ANISOU 2431  CA  TRP A1327    11803   8893   6301   -125    -15   -975       C  
ATOM   2432  C   TRP A1327      53.771 -40.331 350.028  1.00 74.34           C  
ANISOU 2432  C   TRP A1327    12049   9133   7063   -342    108  -1020       C  
ATOM   2433  O   TRP A1327      53.944 -39.879 348.894  1.00 73.28           O  
ANISOU 2433  O   TRP A1327    11665   9104   7076   -391      1  -1018       O  
ATOM   2434  CB  TRP A1327      54.614 -42.505 350.920  1.00 75.99           C  
ANISOU 2434  CB  TRP A1327    12711   9336   6825     57    117   -900       C  
ATOM   2435  CG  TRP A1327      55.568 -43.228 351.824  1.00 87.64           C  
ANISOU 2435  CG  TRP A1327    14447  10924   7927    329     18   -841       C  
ATOM   2436  CD1 TRP A1327      55.255 -43.918 352.959  1.00 84.56           C  
ANISOU 2436  CD1 TRP A1327    14489  10329   7310    454    184   -796       C  
ATOM   2437  CD2 TRP A1327      56.991 -43.327 351.675  1.00 89.53           C  
ANISOU 2437  CD2 TRP A1327    14543  11506   7967    536   -269   -831       C  
ATOM   2438  NE1 TRP A1327      56.391 -44.446 353.521  1.00 83.09           N  
ANISOU 2438  NE1 TRP A1327    14463  10342   6766    764    -17   -741       N  
ATOM   2439  CE2 TRP A1327      57.470 -44.097 352.753  1.00 88.99           C  
ANISOU 2439  CE2 TRP A1327    14826  11443   7543    819   -308   -777       C  
ATOM   2440  CE3 TRP A1327      57.905 -42.842 350.734  1.00 81.09           C  
ANISOU 2440  CE3 TRP A1327    13090  10733   6988    516   -479   -875       C  
ATOM   2441  CZ2 TRP A1327      58.822 -44.395 352.915  1.00 86.69           C  
ANISOU 2441  CZ2 TRP A1327    14465  11473   7000   1106   -596   -781       C  
ATOM   2442  CZ3 TRP A1327      59.246 -43.136 350.899  1.00 74.88           C  
ANISOU 2442  CZ3 TRP A1327    12215  10254   5983    756   -720   -894       C  
ATOM   2443  CH2 TRP A1327      59.691 -43.903 351.981  1.00 78.41           C  
ANISOU 2443  CH2 TRP A1327    12970  10731   6092   1059   -799   -855       C  
ATOM   2444  N   ASP A1328      52.603 -40.261 350.664  1.00 72.73           N  
ANISOU 2444  N   ASP A1328    11992   8660   6983   -454    337  -1066       N  
ATOM   2445  CA  ASP A1328      51.422 -39.667 350.037  1.00 67.91           C  
ANISOU 2445  CA  ASP A1328    11203   7882   6716   -619    442  -1135       C  
ATOM   2446  C   ASP A1328      51.680 -38.230 349.591  1.00 76.08           C  
ANISOU 2446  C   ASP A1328    12009   9046   7852   -732    317  -1157       C  
ATOM   2447  O   ASP A1328      51.144 -37.777 348.579  1.00 80.07           O  
ANISOU 2447  O   ASP A1328    12322   9516   8584   -776    281  -1172       O  
ATOM   2448  CB  ASP A1328      50.223 -39.706 350.991  1.00 60.59           C  
ANISOU 2448  CB  ASP A1328    10453   6659   5910   -731    734  -1216       C  
ATOM   2449  CG  ASP A1328      49.695 -41.112 351.209  1.00 76.13           C  
ANISOU 2449  CG  ASP A1328    12643   8417   7866   -667    944  -1219       C  
ATOM   2450  OD1 ASP A1328      49.964 -41.989 350.364  1.00 68.90           O  
ANISOU 2450  OD1 ASP A1328    11678   7557   6944   -561    860  -1179       O  
ATOM   2451  OD2 ASP A1328      49.002 -41.339 352.223  1.00 87.93           O  
ANISOU 2451  OD2 ASP A1328    14383   9669   9359   -735   1225  -1270       O  
ATOM   2452  N   GLU A1329      52.512 -37.524 350.347  1.00 77.51           N  
ANISOU 2452  N   GLU A1329    12232   9368   7850   -768    254  -1171       N  
ATOM   2453  CA  GLU A1329      52.865 -36.146 350.026  1.00 80.96           C  
ANISOU 2453  CA  GLU A1329    12493   9904   8366   -900    185  -1207       C  
ATOM   2454  C   GLU A1329      53.767 -36.079 348.795  1.00 75.79           C  
ANISOU 2454  C   GLU A1329    11639   9456   7701   -850     10  -1158       C  
ATOM   2455  O   GLU A1329      53.709 -35.124 348.018  1.00 63.97           O  
ANISOU 2455  O   GLU A1329    10010   7950   6344   -940      2  -1159       O  
ATOM   2456  CB  GLU A1329      53.549 -35.488 351.223  1.00 80.51           C  
ANISOU 2456  CB  GLU A1329    12533   9949   8109   -975    175  -1279       C  
ATOM   2457  CG  GLU A1329      52.977 -34.137 351.604  1.00 84.86           C  
ANISOU 2457  CG  GLU A1329    13070  10361   8812  -1173    310  -1358       C  
ATOM   2458  CD  GLU A1329      53.298 -33.764 353.036  1.00 81.12           C  
ANISOU 2458  CD  GLU A1329    12779   9913   8129  -1244    355  -1453       C  
ATOM   2459  OE1 GLU A1329      53.552 -34.684 353.841  1.00 68.69           O  
ANISOU 2459  OE1 GLU A1329    11410   8380   6309  -1113    329  -1439       O  
ATOM   2460  OE2 GLU A1329      53.298 -32.556 353.358  1.00 70.67           O  
ANISOU 2460  OE2 GLU A1329    11426   8559   6867  -1418    422  -1542       O  
ATOM   2461  N   ALA A1330      54.604 -37.097 348.626  1.00 69.36           N  
ANISOU 2461  N   ALA A1330    10834   8808   6711   -694   -107  -1115       N  
ATOM   2462  CA  ALA A1330      55.486 -37.179 347.470  1.00 71.31           C  
ANISOU 2462  CA  ALA A1330    10905   9244   6945   -639   -239  -1079       C  
ATOM   2463  C   ALA A1330      54.701 -37.589 346.228  1.00 70.42           C  
ANISOU 2463  C   ALA A1330    10749   9003   7003   -596   -222  -1020       C  
ATOM   2464  O   ALA A1330      55.013 -37.167 345.114  1.00 56.75           O  
ANISOU 2464  O   ALA A1330     8898   7338   5326   -612   -277   -993       O  
ATOM   2465  CB  ALA A1330      56.618 -38.160 347.734  1.00 63.95           C  
ANISOU 2465  CB  ALA A1330     9986   8530   5781   -459   -366  -1067       C  
ATOM   2466  N   ALA A1331      53.678 -38.411 346.434  1.00 71.47           N  
ANISOU 2466  N   ALA A1331    10995   8947   7213   -548   -133  -1019       N  
ATOM   2467  CA  ALA A1331      52.830 -38.883 345.346  1.00 70.01           C  
ANISOU 2467  CA  ALA A1331    10752   8649   7198   -512   -133  -1015       C  
ATOM   2468  C   ALA A1331      52.038 -37.738 344.728  1.00 76.16           C  
ANISOU 2468  C   ALA A1331    11419   9333   8184   -602   -137  -1043       C  
ATOM   2469  O   ALA A1331      51.857 -37.681 343.512  1.00 83.77           O  
ANISOU 2469  O   ALA A1331    12301  10314   9214   -549   -230  -1023       O  
ATOM   2470  CB  ALA A1331      51.891 -39.966 345.842  1.00 62.03           C  
ANISOU 2470  CB  ALA A1331     9871   7441   6254   -483      7  -1060       C  
ATOM   2471  N   VAL A1332      51.563 -36.833 345.576  1.00 78.43           N  
ANISOU 2471  N   VAL A1332    11731   9515   8556   -714    -37  -1089       N  
ATOM   2472  CA  VAL A1332      50.816 -35.666 345.124  1.00 75.30           C  
ANISOU 2472  CA  VAL A1332    11254   9007   8351   -768    -26  -1111       C  
ATOM   2473  C   VAL A1332      51.704 -34.754 344.285  1.00 79.86           C  
ANISOU 2473  C   VAL A1332    11793   9704   8845   -778   -111  -1039       C  
ATOM   2474  O   VAL A1332      51.286 -34.239 343.246  1.00 88.13           O  
ANISOU 2474  O   VAL A1332    12808  10697   9981   -721   -170  -1007       O  
ATOM   2475  CB  VAL A1332      50.240 -34.874 346.319  1.00 69.62           C  
ANISOU 2475  CB  VAL A1332    10591   8140   7724   -891    134  -1179       C  
ATOM   2476  CG1 VAL A1332      49.702 -33.526 345.866  1.00 59.90           C  
ANISOU 2476  CG1 VAL A1332     9297   6802   6660   -922    146  -1185       C  
ATOM   2477  CG2 VAL A1332      49.160 -35.683 347.019  1.00 54.90           C  
ANISOU 2477  CG2 VAL A1332     8770   6100   5990   -899    280  -1268       C  
ATOM   2478  N   ASN A1333      52.941 -34.578 344.737  1.00 72.58           N  
ANISOU 2478  N   ASN A1333    10886   8946   7746   -843   -111  -1029       N  
ATOM   2479  CA  ASN A1333      53.894 -33.705 344.067  1.00 77.12           C  
ANISOU 2479  CA  ASN A1333    11422   9623   8256   -904   -123   -998       C  
ATOM   2480  C   ASN A1333      54.328 -34.250 342.708  1.00 86.12           C  
ANISOU 2480  C   ASN A1333    12531  10854   9335   -790   -216   -926       C  
ATOM   2481  O   ASN A1333      54.405 -33.508 341.728  1.00 81.74           O  
ANISOU 2481  O   ASN A1333    12006  10255   8797   -793   -201   -875       O  
ATOM   2482  CB  ASN A1333      55.119 -33.488 344.958  1.00 72.15           C  
ANISOU 2482  CB  ASN A1333    10759   9177   7479  -1013   -107  -1067       C  
ATOM   2483  CG  ASN A1333      55.988 -32.336 344.489  1.00 73.82           C  
ANISOU 2483  CG  ASN A1333    10920   9446   7684  -1156    -38  -1093       C  
ATOM   2484  OD1 ASN A1333      55.668 -31.169 344.719  1.00 60.37           O  
ANISOU 2484  OD1 ASN A1333     9270   7599   6068  -1289     83  -1122       O  
ATOM   2485  ND2 ASN A1333      57.100 -32.659 343.838  1.00 89.69           N  
ANISOU 2485  ND2 ASN A1333    12835  11646   9599  -1140    -79  -1095       N  
ATOM   2486  N   LEU A1334      54.605 -35.549 342.654  1.00 81.25           N  
ANISOU 2486  N   LEU A1334    11895  10343   8633   -680   -292   -918       N  
ATOM   2487  CA  LEU A1334      55.063 -36.189 341.426  1.00 69.15           C  
ANISOU 2487  CA  LEU A1334    10344   8900   7029   -572   -366   -865       C  
ATOM   2488  C   LEU A1334      53.972 -36.243 340.361  1.00 78.87           C  
ANISOU 2488  C   LEU A1334    11618   9991   8360   -480   -426   -836       C  
ATOM   2489  O   LEU A1334      54.264 -36.310 339.166  1.00 80.17           O  
ANISOU 2489  O   LEU A1334    11813  10194   8455   -409   -475   -786       O  
ATOM   2490  CB  LEU A1334      55.568 -37.602 341.722  1.00 63.43           C  
ANISOU 2490  CB  LEU A1334     9610   8295   6194   -460   -414   -871       C  
ATOM   2491  CG  LEU A1334      56.872 -37.689 342.518  1.00 71.80           C  
ANISOU 2491  CG  LEU A1334    10606   9563   7113   -472   -423   -907       C  
ATOM   2492  CD1 LEU A1334      57.184 -39.129 342.895  1.00 72.89           C  
ANISOU 2492  CD1 LEU A1334    10790   9772   7134   -300   -474   -896       C  
ATOM   2493  CD2 LEU A1334      58.015 -37.084 341.721  1.00 63.19           C  
ANISOU 2493  CD2 LEU A1334     9402   8627   5979   -532   -409   -917       C  
ATOM   2494  N   ALA A1335      52.716 -36.212 340.797  1.00 81.30           N  
ANISOU 2494  N   ALA A1335    11922  10140   8827   -476   -422   -887       N  
ATOM   2495  CA  ALA A1335      51.584 -36.299 339.879  1.00 77.71           C  
ANISOU 2495  CA  ALA A1335    11454   9579   8491   -370   -519   -912       C  
ATOM   2496  C   ALA A1335      51.349 -34.978 339.154  1.00 75.18           C  
ANISOU 2496  C   ALA A1335    11191   9181   8192   -338   -547   -856       C  
ATOM   2497  O   ALA A1335      50.669 -34.937 338.129  1.00 85.30           O  
ANISOU 2497  O   ALA A1335    12493  10418   9498   -198   -676   -856       O  
ATOM   2498  CB  ALA A1335      50.329 -36.723 340.627  1.00 86.25           C  
ANISOU 2498  CB  ALA A1335    12470  10525   9776   -386   -482  -1030       C  
ATOM   2499  N   LYS A1336      51.910 -33.900 339.692  1.00 73.93           N  
ANISOU 2499  N   LYS A1336    11081   8999   8010   -458   -423   -818       N  
ATOM   2500  CA  LYS A1336      51.795 -32.587 339.069  1.00 78.64           C  
ANISOU 2500  CA  LYS A1336    11795   9480   8607   -434   -389   -749       C  
ATOM   2501  C   LYS A1336      53.095 -32.204 338.370  1.00 87.40           C  
ANISOU 2501  C   LYS A1336    13007  10668   9530   -491   -305   -667       C  
ATOM   2502  O   LYS A1336      53.660 -31.142 338.627  1.00101.90           O  
ANISOU 2502  O   LYS A1336    14916  12450  11353   -626   -143   -650       O  
ATOM   2503  CB  LYS A1336      51.422 -31.525 340.106  1.00 80.09           C  
ANISOU 2503  CB  LYS A1336    11985   9525   8920   -551   -254   -785       C  
ATOM   2504  CG  LYS A1336      50.108 -31.789 340.821  1.00 89.47           C  
ANISOU 2504  CG  LYS A1336    13068  10607  10320   -511   -281   -884       C  
ATOM   2505  CD  LYS A1336      48.954 -31.898 339.837  1.00 93.61           C  
ANISOU 2505  CD  LYS A1336    13556  11058  10952   -294   -453   -903       C  
ATOM   2506  CE  LYS A1336      47.642 -32.173 340.555  1.00 98.56           C  
ANISOU 2506  CE  LYS A1336    14023  11586  11842   -279   -449  -1051       C  
ATOM   2507  NZ  LYS A1336      46.516 -32.374 339.601  1.00 94.35           N  
ANISOU 2507  NZ  LYS A1336    13384  11027  11438    -62   -656  -1128       N  
ATOM   2508  N   SER A1337      53.565 -33.079 337.488  1.00 83.53           N  
ANISOU 2508  N   SER A1337    12526  10296   8913   -405   -385   -637       N  
ATOM   2509  CA  SER A1337      54.794 -32.829 336.745  1.00 92.74           C  
ANISOU 2509  CA  SER A1337    13781  11536   9919   -460   -274   -579       C  
ATOM   2510  C   SER A1337      54.581 -33.085 335.260  1.00 90.80           C  
ANISOU 2510  C   SER A1337    13701  11258   9541   -278   -366   -501       C  
ATOM   2511  O   SER A1337      53.531 -33.579 334.854  1.00 84.73           O  
ANISOU 2511  O   SER A1337    12935  10452   8806   -108   -557   -516       O  
ATOM   2512  CB  SER A1337      55.931 -33.708 337.271  1.00 93.43           C  
ANISOU 2512  CB  SER A1337    13706  11840   9952   -551   -241   -642       C  
ATOM   2513  OG  SER A1337      55.672 -35.079 337.024  1.00 83.77           O  
ANISOU 2513  OG  SER A1337    12429  10701   8701   -415   -384   -655       O  
ATOM   2514  N   ARG A1338      55.580 -32.745 334.452  1.00 93.57           N  
ANISOU 2514  N   ARG A1338    14190  11623   9741   -321   -221   -440       N  
ATOM   2515  CA  ARG A1338      55.520 -33.014 333.021  1.00 94.42           C  
ANISOU 2515  CA  ARG A1338    14506  11701   9669   -151   -282   -363       C  
ATOM   2516  C   ARG A1338      55.807 -34.487 332.753  1.00 89.87           C  
ANISOU 2516  C   ARG A1338    13803  11301   9043    -92   -394   -418       C  
ATOM   2517  O   ARG A1338      55.319 -35.062 331.780  1.00 84.77           O  
ANISOU 2517  O   ARG A1338    13270  10649   8290     80   -543   -403       O  
ATOM   2518  CB  ARG A1338      56.511 -32.130 332.260  1.00 94.92           C  
ANISOU 2518  CB  ARG A1338    14803  11680   9584   -238    -17   -284       C  
ATOM   2519  N   TRP A1339      56.603 -35.087 333.632  1.00 89.39           N  
ANISOU 2519  N   TRP A1339    13521  11394   9048   -219   -328   -490       N  
ATOM   2520  CA  TRP A1339      56.954 -36.499 333.532  1.00 90.64           C  
ANISOU 2520  CA  TRP A1339    13569  11701   9167   -153   -403   -539       C  
ATOM   2521  C   TRP A1339      55.714 -37.390 333.584  1.00 94.63           C  
ANISOU 2521  C   TRP A1339    14043  12168   9743    -22   -611   -586       C  
ATOM   2522  O   TRP A1339      55.553 -38.290 332.761  1.00 90.41           O  
ANISOU 2522  O   TRP A1339    13564  11662   9126     92   -700   -605       O  
ATOM   2523  CB  TRP A1339      57.934 -36.875 334.648  1.00 93.45           C  
ANISOU 2523  CB  TRP A1339    13704  12220   9582   -267   -323   -609       C  
ATOM   2524  CG  TRP A1339      58.112 -38.351 334.853  1.00 95.04           C  
ANISOU 2524  CG  TRP A1339    13808  12539   9766   -163   -408   -652       C  
ATOM   2525  CD1 TRP A1339      58.531 -39.264 333.930  1.00 90.21           C  
ANISOU 2525  CD1 TRP A1339    13242  11985   9048    -59   -410   -646       C  
ATOM   2526  CD2 TRP A1339      57.897 -39.079 336.069  1.00 98.47           C  
ANISOU 2526  CD2 TRP A1339    14126  13016  10273   -144   -472   -703       C  
ATOM   2527  NE1 TRP A1339      58.578 -40.518 334.492  1.00 94.69           N  
ANISOU 2527  NE1 TRP A1339    13725  12621   9634     28   -469   -689       N  
ATOM   2528  CE2 TRP A1339      58.195 -40.430 335.805  1.00100.39           C  
ANISOU 2528  CE2 TRP A1339    14363  13328  10453    -15   -504   -717       C  
ATOM   2529  CE3 TRP A1339      57.476 -38.719 337.353  1.00 90.06           C  
ANISOU 2529  CE3 TRP A1339    13001  11915   9303   -216   -482   -735       C  
ATOM   2530  CZ2 TRP A1339      58.085 -41.423 336.778  1.00 95.19           C  
ANISOU 2530  CZ2 TRP A1339    13667  12686   9815     55   -537   -748       C  
ATOM   2531  CZ3 TRP A1339      57.368 -39.705 338.316  1.00 85.90           C  
ANISOU 2531  CZ3 TRP A1339    12440  11416   8783   -152   -518   -769       C  
ATOM   2532  CH2 TRP A1339      57.671 -41.041 338.024  1.00 88.51           C  
ANISOU 2532  CH2 TRP A1339    12792  11798   9041    -11   -541   -769       C  
ATOM   2533  N   TYR A1340      54.834 -37.127 334.545  1.00 99.96           N  
ANISOU 2533  N   TYR A1340    14629  12770  10581    -55   -664   -630       N  
ATOM   2534  CA  TYR A1340      53.607 -37.904 334.679  1.00 85.45           C  
ANISOU 2534  CA  TYR A1340    12728  10879   8862     29   -813   -718       C  
ATOM   2535  C   TYR A1340      52.563 -37.511 333.633  1.00 75.81           C  
ANISOU 2535  C   TYR A1340    11605   9568   7633    174   -979   -729       C  
ATOM   2536  O   TYR A1340      51.734 -38.330 333.234  1.00 75.98           O  
ANISOU 2536  O   TYR A1340    11577   9590   7704    264  -1128   -836       O  
ATOM   2537  CB  TYR A1340      53.020 -37.741 336.083  1.00 75.75           C  
ANISOU 2537  CB  TYR A1340    11375   9588   7819    -65   -771   -778       C  
ATOM   2538  CG  TYR A1340      51.676 -38.413 336.253  1.00 62.74           C  
ANISOU 2538  CG  TYR A1340     9644   7853   6341    -16   -867   -903       C  
ATOM   2539  CD1 TYR A1340      51.588 -39.778 336.486  1.00 67.26           C  
ANISOU 2539  CD1 TYR A1340    10174   8446   6937    -13   -851   -983       C  
ATOM   2540  CD2 TYR A1340      50.496 -37.683 336.175  1.00 66.01           C  
ANISOU 2540  CD2 TYR A1340    10018   8155   6908     29   -953   -959       C  
ATOM   2541  CE1 TYR A1340      50.364 -40.399 336.639  1.00 80.73           C  
ANISOU 2541  CE1 TYR A1340    11792  10055   8828    -10   -888  -1136       C  
ATOM   2542  CE2 TYR A1340      49.266 -38.297 336.326  1.00 76.16           C  
ANISOU 2542  CE2 TYR A1340    11170   9374   8391     54  -1024  -1124       C  
ATOM   2543  CZ  TYR A1340      49.207 -39.655 336.559  1.00 81.99           C  
ANISOU 2543  CZ  TYR A1340    11861  10128   9164     13   -977  -1221       C  
ATOM   2544  OH  TYR A1340      47.986 -40.271 336.711  1.00 84.90           O  
ANISOU 2544  OH  TYR A1340    12087  10413   9758     -4   -998  -1422       O  
ATOM   2545  N   ASN A1341      52.608 -36.257 333.195  1.00 77.83           N  
ANISOU 2545  N   ASN A1341    12008   9742   7820    205   -953   -634       N  
ATOM   2546  CA  ASN A1341      51.626 -35.736 332.247  1.00 89.06           C  
ANISOU 2546  CA  ASN A1341    13561  11076   9203    401  -1136   -629       C  
ATOM   2547  C   ASN A1341      51.788 -36.306 330.838  1.00 88.28           C  
ANISOU 2547  C   ASN A1341    13634  11033   8876    553  -1256   -616       C  
ATOM   2548  O   ASN A1341      50.805 -36.503 330.123  1.00 78.27           O  
ANISOU 2548  O   ASN A1341    12390   9759   7590    738  -1498   -695       O  
ATOM   2549  CB  ASN A1341      51.705 -34.208 332.199  1.00101.54           C  
ANISOU 2549  CB  ASN A1341    15323  12513  10742    415  -1034   -506       C  
ATOM   2550  CG  ASN A1341      50.870 -33.613 331.079  1.00114.59           C  
ANISOU 2550  CG  ASN A1341    17192  14069  12277    683  -1228   -463       C  
ATOM   2551  OD1 ASN A1341      49.647 -33.515 331.185  1.00117.90           O  
ANISOU 2551  OD1 ASN A1341    17498  14453  12846    827  -1433   -557       O  
ATOM   2552  ND2 ASN A1341      51.530 -33.204 330.001  1.00118.29           N  
ANISOU 2552  ND2 ASN A1341    17981  14492  12472    766  -1159   -331       N  
ATOM   2553  N   GLN A1342      53.029 -36.574 330.447  1.00 87.71           N  
ANISOU 2553  N   GLN A1342    13670  11025   8632    479  -1090   -539       N  
ATOM   2554  CA  GLN A1342      53.319 -37.033 329.093  1.00 83.52           C  
ANISOU 2554  CA  GLN A1342    13352  10528   7854    607  -1148   -515       C  
ATOM   2555  C   GLN A1342      53.314 -38.556 328.982  1.00 87.55           C  
ANISOU 2555  C   GLN A1342    13725  11156   8382    607  -1226   -642       C  
ATOM   2556  O   GLN A1342      52.904 -39.110 327.961  1.00100.45           O  
ANISOU 2556  O   GLN A1342    15474  12814   9879    747  -1391   -703       O  
ATOM   2557  CB  GLN A1342      54.665 -36.473 328.627  1.00 91.06           C  
ANISOU 2557  CB  GLN A1342    14514  11463   8623    522   -874   -382       C  
ATOM   2558  CG  GLN A1342      54.697 -34.952 328.542  1.00109.80           C  
ANISOU 2558  CG  GLN A1342    17106  13670  10943    521   -745   -257       C  
ATOM   2559  CD  GLN A1342      56.056 -34.410 328.142  1.00127.03           C  
ANISOU 2559  CD  GLN A1342    19472  15812  12982    380   -405   -166       C  
ATOM   2560  OE1 GLN A1342      57.020 -35.161 327.994  1.00129.23           O  
ANISOU 2560  OE1 GLN A1342    19666  16213  13223    286   -276   -205       O  
ATOM   2561  NE2 GLN A1342      56.139 -33.095 327.965  1.00130.02           N  
ANISOU 2561  NE2 GLN A1342    20104  16004  13295    364   -232    -58       N  
ATOM   2562  N   THR A1343      53.776 -39.231 330.030  1.00 86.74           N  
ANISOU 2562  N   THR A1343    13407  11118   8431    461  -1106   -685       N  
ATOM   2563  CA  THR A1343      53.815 -40.692 330.047  1.00 88.50           C  
ANISOU 2563  CA  THR A1343    13533  11412   8680    462  -1130   -793       C  
ATOM   2564  C   THR A1343      53.276 -41.244 331.363  1.00 85.87           C  
ANISOU 2564  C   THR A1343    12980  11060   8589    373  -1117   -888       C  
ATOM   2565  O   THR A1343      54.049 -41.634 332.236  1.00 90.72           O  
ANISOU 2565  O   THR A1343    13514  11718   9237    291   -969   -858       O  
ATOM   2566  CB  THR A1343      55.245 -41.225 329.834  1.00 89.37           C  
ANISOU 2566  CB  THR A1343    13686  11614   8658    421   -939   -732       C  
ATOM   2567  OG1 THR A1343      56.111 -40.693 330.846  1.00 86.02           O  
ANISOU 2567  OG1 THR A1343    13142  11232   8309    297   -770   -669       O  
ATOM   2568  CG2 THR A1343      55.771 -40.829 328.462  1.00 76.51           C  
ANISOU 2568  CG2 THR A1343    12312   9980   6780    496   -898   -657       C  
ATOM   2569  N   PRO A1344      51.943 -41.293 331.501  1.00 84.88           N  
ANISOU 2569  N   PRO A1344    12760  10865   8625    401  -1268  -1017       N  
ATOM   2570  CA  PRO A1344      51.285 -41.669 332.758  1.00 84.82           C  
ANISOU 2570  CA  PRO A1344    12573  10793   8860    300  -1211  -1116       C  
ATOM   2571  C   PRO A1344      51.483 -43.132 333.155  1.00 82.30           C  
ANISOU 2571  C   PRO A1344    12225  10471   8575    254  -1102  -1199       C  
ATOM   2572  O   PRO A1344      51.649 -43.412 334.341  1.00 86.57           O  
ANISOU 2572  O   PRO A1344    12718  10969   9206    172   -956  -1186       O  
ATOM   2573  CB  PRO A1344      49.807 -41.386 332.473  1.00 95.64           C  
ANISOU 2573  CB  PRO A1344    13841  12103  10395    361  -1402  -1274       C  
ATOM   2574  CG  PRO A1344      49.679 -41.516 330.999  1.00 96.69           C  
ANISOU 2574  CG  PRO A1344    14094  12297  10346    513  -1599  -1310       C  
ATOM   2575  CD  PRO A1344      50.970 -41.005 330.433  1.00 93.77           C  
ANISOU 2575  CD  PRO A1344    13946  11974   9707    546  -1505  -1098       C  
ATOM   2576  N   ASN A1345      51.466 -44.041 332.185  1.00 80.32           N  
ANISOU 2576  N   ASN A1345    12038  10248   8234    317  -1164  -1281       N  
ATOM   2577  CA  ASN A1345      51.550 -45.471 332.473  1.00 88.94           C  
ANISOU 2577  CA  ASN A1345    13137  11294   9364    282  -1040  -1373       C  
ATOM   2578  C   ASN A1345      52.830 -45.871 333.204  1.00 97.73           C  
ANISOU 2578  C   ASN A1345    14313  12443  10377    286   -852  -1226       C  
ATOM   2579  O   ASN A1345      52.776 -46.541 334.235  1.00105.32           O  
ANISOU 2579  O   ASN A1345    15273  13320  11423    247   -712  -1247       O  
ATOM   2580  CB  ASN A1345      51.425 -46.280 331.181  1.00 93.61           C  
ANISOU 2580  CB  ASN A1345    13809  11912   9844    350  -1135  -1489       C  
ATOM   2581  CG  ASN A1345      50.005 -46.318 330.654  1.00107.36           C  
ANISOU 2581  CG  ASN A1345    15441  13623  11729    346  -1331  -1725       C  
ATOM   2582  OD1 ASN A1345      49.045 -46.215 331.418  1.00 99.67           O  
ANISOU 2582  OD1 ASN A1345    14300  12567  11001    262  -1320  -1852       O  
ATOM   2583  ND2 ASN A1345      49.864 -46.471 329.342  1.00117.39           N  
ANISOU 2583  ND2 ASN A1345    16795  14963  12844    443  -1511  -1808       N  
ATOM   2584  N   ARG A1346      53.977 -45.458 332.672  1.00 91.23           N  
ANISOU 2584  N   ARG A1346    13552  11740   9370    344   -842  -1091       N  
ATOM   2585  CA  ARG A1346      55.261 -45.791 333.280  1.00 83.02           C  
ANISOU 2585  CA  ARG A1346    12519  10780   8246    376   -701   -986       C  
ATOM   2586  C   ARG A1346      55.518 -44.949 334.528  1.00 83.83           C  
ANISOU 2586  C   ARG A1346    12531  10910   8411    311   -661   -915       C  
ATOM   2587  O   ARG A1346      56.374 -45.284 335.348  1.00 83.37           O  
ANISOU 2587  O   ARG A1346    12452  10917   8308    350   -579   -865       O  
ATOM   2588  CB  ARG A1346      56.401 -45.601 332.275  1.00 78.15           C  
ANISOU 2588  CB  ARG A1346    11956  10288   7450    436   -674   -911       C  
ATOM   2589  CG  ARG A1346      56.680 -44.149 331.914  1.00 76.16           C  
ANISOU 2589  CG  ARG A1346    11701  10087   7148    382   -697   -829       C  
ATOM   2590  CD  ARG A1346      57.904 -44.022 331.019  1.00 77.09           C  
ANISOU 2590  CD  ARG A1346    11881  10305   7105    412   -590   -771       C  
ATOM   2591  NE  ARG A1346      58.238 -42.626 330.749  1.00 77.24           N  
ANISOU 2591  NE  ARG A1346    11932  10334   7081    334   -541   -697       N  
ATOM   2592  CZ  ARG A1346      59.284 -42.229 330.029  1.00 75.09           C  
ANISOU 2592  CZ  ARG A1346    11719  10119   6692    312   -389   -655       C  
ATOM   2593  NH1 ARG A1346      60.107 -43.124 329.500  1.00 68.87           N  
ANISOU 2593  NH1 ARG A1346    10939   9404   5824    378   -292   -680       N  
ATOM   2594  NH2 ARG A1346      59.507 -40.936 329.838  1.00 70.54           N  
ANISOU 2594  NH2 ARG A1346    11208   9505   6090    219   -300   -596       N  
ATOM   2595  N   ALA A1347      54.771 -43.857 334.664  1.00 77.25           N  
ANISOU 2595  N   ALA A1347    11651  10030   7671    231   -731   -920       N  
ATOM   2596  CA  ALA A1347      54.931 -42.953 335.798  1.00 71.42           C  
ANISOU 2596  CA  ALA A1347    10843   9302   6993    148   -687   -872       C  
ATOM   2597  C   ALA A1347      54.080 -43.392 336.981  1.00 76.24           C  
ANISOU 2597  C   ALA A1347    11440   9786   7743    103   -633   -939       C  
ATOM   2598  O   ALA A1347      54.555 -43.416 338.114  1.00 76.87           O  
ANISOU 2598  O   ALA A1347    11523   9887   7797     89   -556   -903       O  
ATOM   2599  CB  ALA A1347      54.581 -41.527 335.399  1.00 54.18           C  
ANISOU 2599  CB  ALA A1347     8651   7097   4839     92   -746   -838       C  
ATOM   2600  N   LYS A1348      52.824 -43.737 336.711  1.00 76.31           N  
ANISOU 2600  N   LYS A1348    11436   9663   7896     81   -667  -1057       N  
ATOM   2601  CA  LYS A1348      51.897 -44.167 337.755  1.00 80.23           C  
ANISOU 2601  CA  LYS A1348    11924  10002   8558      8   -559  -1153       C  
ATOM   2602  C   LYS A1348      52.385 -45.439 338.446  1.00 86.19           C  
ANISOU 2602  C   LYS A1348    12811  10705   9233     55   -404  -1137       C  
ATOM   2603  O   LYS A1348      52.118 -45.657 339.628  1.00 93.65           O  
ANISOU 2603  O   LYS A1348    13828  11535  10221     14   -264  -1145       O  
ATOM   2604  CB  LYS A1348      50.498 -44.390 337.174  1.00 89.61           C  
ANISOU 2604  CB  LYS A1348    13023  11079   9945    -30   -620  -1337       C  
ATOM   2605  CG  LYS A1348      49.421 -44.636 338.221  1.00 96.97           C  
ANISOU 2605  CG  LYS A1348    13911  11830  11105   -145   -467  -1473       C  
ATOM   2606  CD  LYS A1348      48.098 -45.034 337.585  1.00107.85           C  
ANISOU 2606  CD  LYS A1348    15144  13124  12711   -192   -521  -1718       C  
ATOM   2607  CE  LYS A1348      47.593 -43.965 336.627  1.00117.02           C  
ANISOU 2607  CE  LYS A1348    16160  14386  13917   -118   -785  -1753       C  
ATOM   2608  NZ  LYS A1348      46.302 -44.352 335.991  1.00115.70           N  
ANISOU 2608  NZ  LYS A1348    15806  14183  13974   -134   -895  -2034       N  
ATOM   2609  N   ARG A1349      53.109 -46.273 337.704  1.00 91.12           N  
ANISOU 2609  N   ARG A1349    13501  11397   9724    159   -415  -1108       N  
ATOM   2610  CA  ARG A1349      53.639 -47.519 338.246  1.00 88.77           C  
ANISOU 2610  CA  ARG A1349    13361  11038   9328    255   -271  -1079       C  
ATOM   2611  C   ARG A1349      54.760 -47.251 339.252  1.00 87.45           C  
ANISOU 2611  C   ARG A1349    13233  10989   9006    347   -258   -944       C  
ATOM   2612  O   ARG A1349      54.912 -47.976 340.236  1.00 77.73           O  
ANISOU 2612  O   ARG A1349    12164   9665   7703    429   -138   -912       O  
ATOM   2613  CB  ARG A1349      54.139 -48.420 337.112  1.00 76.59           C  
ANISOU 2613  CB  ARG A1349    11871   9538   7691    355   -285  -1093       C  
ATOM   2614  CG  ARG A1349      54.583 -49.808 337.553  1.00 83.80           C  
ANISOU 2614  CG  ARG A1349    12979  10345   8515    481   -117  -1071       C  
ATOM   2615  CD  ARG A1349      54.894 -50.688 336.351  1.00105.87           C  
ANISOU 2615  CD  ARG A1349    15829  13150  11248    554   -110  -1117       C  
ATOM   2616  NE  ARG A1349      55.479 -51.970 336.736  1.00118.69           N  
ANISOU 2616  NE  ARG A1349    17658  14670  12767    715     60  -1073       N  
ATOM   2617  CZ  ARG A1349      56.780 -52.239 336.699  1.00114.24           C  
ANISOU 2617  CZ  ARG A1349    17119  14248  12037    919     45   -955       C  
ATOM   2618  NH1 ARG A1349      57.221 -53.434 337.067  1.00110.68           N  
ANISOU 2618  NH1 ARG A1349    16881  13677  11493   1103    198   -915       N  
ATOM   2619  NH2 ARG A1349      57.640 -51.316 336.291  1.00108.41           N  
ANISOU 2619  NH2 ARG A1349    16194  13760  11236    943   -104   -891       N  
ATOM   2620  N   VAL A1350      55.533 -46.199 339.003  1.00 88.92           N  
ANISOU 2620  N   VAL A1350    13282  11372   9130    339   -378   -880       N  
ATOM   2621  CA  VAL A1350      56.644 -45.833 339.875  1.00 82.88           C  
ANISOU 2621  CA  VAL A1350    12487  10769   8236    408   -403   -806       C  
ATOM   2622  C   VAL A1350      56.160 -45.106 341.128  1.00 81.22           C  
ANISOU 2622  C   VAL A1350    12295  10496   8070    310   -376   -814       C  
ATOM   2623  O   VAL A1350      56.606 -45.400 342.238  1.00 83.74           O  
ANISOU 2623  O   VAL A1350    12713  10836   8269    401   -350   -783       O  
ATOM   2624  CB  VAL A1350      57.663 -44.943 339.133  1.00 82.26           C  
ANISOU 2624  CB  VAL A1350    12237  10911   8108    388   -492   -780       C  
ATOM   2625  CG1 VAL A1350      58.683 -44.369 340.105  1.00 87.84           C  
ANISOU 2625  CG1 VAL A1350    12846  11800   8730    408   -531   -769       C  
ATOM   2626  CG2 VAL A1350      58.350 -45.734 338.030  1.00 79.15           C  
ANISOU 2626  CG2 VAL A1350    11846  10590   7637    508   -485   -771       C  
ATOM   2627  N   ILE A1351      55.244 -44.161 340.940  1.00 75.59           N  
ANISOU 2627  N   ILE A1351    11505   9703   7514    147   -387   -859       N  
ATOM   2628  CA  ILE A1351      54.697 -43.378 342.044  1.00 77.61           C  
ANISOU 2628  CA  ILE A1351    11773   9879   7836     35   -338   -880       C  
ATOM   2629  C   ILE A1351      53.973 -44.260 343.059  1.00 86.44           C  
ANISOU 2629  C   ILE A1351    13081  10791   8970     50   -180   -912       C  
ATOM   2630  O   ILE A1351      54.158 -44.110 344.267  1.00 91.40           O  
ANISOU 2630  O   ILE A1351    13821  11403   9503     58   -124   -890       O  
ATOM   2631  CB  ILE A1351      53.724 -42.297 341.532  1.00 77.05           C  
ANISOU 2631  CB  ILE A1351    11590   9729   7955   -107   -368   -930       C  
ATOM   2632  CG1 ILE A1351      54.434 -41.361 340.552  1.00 91.96           C  
ANISOU 2632  CG1 ILE A1351    13371  11772   9798   -120   -474   -882       C  
ATOM   2633  CG2 ILE A1351      53.139 -41.506 342.692  1.00 72.27           C  
ANISOU 2633  CG2 ILE A1351    11002   9022   7433   -221   -287   -963       C  
ATOM   2634  CD1 ILE A1351      53.526 -40.320 339.933  1.00 93.78           C  
ANISOU 2634  CD1 ILE A1351    13548  11912  10174   -194   -518   -906       C  
ATOM   2635  N   THR A1352      53.152 -45.179 342.560  1.00 81.94           N  
ANISOU 2635  N   THR A1352    12567  10053   8511     45    -89   -979       N  
ATOM   2636  CA  THR A1352      52.396 -46.081 343.421  1.00 88.65           C  
ANISOU 2636  CA  THR A1352    13624  10657   9404     27    133  -1032       C  
ATOM   2637  C   THR A1352      53.332 -46.971 344.236  1.00 95.12           C  
ANISOU 2637  C   THR A1352    14697  11483   9963    219    199   -924       C  
ATOM   2638  O   THR A1352      53.052 -47.285 345.394  1.00 92.29           O  
ANISOU 2638  O   THR A1352    14574  10958   9534    232    371   -911       O  
ATOM   2639  CB  THR A1352      51.428 -46.961 342.603  1.00 88.90           C  
ANISOU 2639  CB  THR A1352    13639  10519   9621    -34    229  -1167       C  
ATOM   2640  OG1 THR A1352      50.560 -46.124 341.830  1.00 94.41           O  
ANISOU 2640  OG1 THR A1352    14091  11240  10540   -158    113  -1280       O  
ATOM   2641  CG2 THR A1352      50.587 -47.838 343.518  1.00 88.86           C  
ANISOU 2641  CG2 THR A1352    13851  10215   9695   -102    532  -1251       C  
ATOM   2642  N   THR A1353      54.449 -47.362 343.627  1.00 86.76           N  
ANISOU 2642  N   THR A1353    13604  10611   8751    388     68   -849       N  
ATOM   2643  CA  THR A1353      55.459 -48.165 344.308  1.00 84.02           C  
ANISOU 2643  CA  THR A1353    13462  10314   8146    635     75   -749       C  
ATOM   2644  C   THR A1353      55.990 -47.432 345.539  1.00 82.26           C  
ANISOU 2644  C   THR A1353    13280  10213   7764    680     -4   -705       C  
ATOM   2645  O   THR A1353      56.184 -48.034 346.594  1.00 75.44           O  
ANISOU 2645  O   THR A1353    12702   9259   6702    843     75   -648       O  
ATOM   2646  CB  THR A1353      56.633 -48.516 343.370  1.00 71.02           C  
ANISOU 2646  CB  THR A1353    11690   8893   6402    805    -73   -704       C  
ATOM   2647  OG1 THR A1353      56.159 -49.333 342.292  1.00 76.27           O  
ANISOU 2647  OG1 THR A1353    12378   9428   7175    780     15   -752       O  
ATOM   2648  CG2 THR A1353      57.723 -49.266 344.124  1.00 70.54           C  
ANISOU 2648  CG2 THR A1353    11803   8917   6080   1109   -106   -613       C  
ATOM   2649  N   PHE A1354      56.208 -46.128 345.401  1.00 77.50           N  
ANISOU 2649  N   PHE A1354    12420   9796   7230    540   -149   -738       N  
ATOM   2650  CA  PHE A1354      56.662 -45.308 346.516  1.00 71.40           C  
ANISOU 2650  CA  PHE A1354    11654   9148   6328    536   -228   -740       C  
ATOM   2651  C   PHE A1354      55.623 -45.256 347.635  1.00 82.73           C  
ANISOU 2651  C   PHE A1354    13334  10323   7775    440    -38   -758       C  
ATOM   2652  O   PHE A1354      55.975 -45.164 348.810  1.00 96.33           O  
ANISOU 2652  O   PHE A1354    15238  12075   9289    530    -51   -739       O  
ATOM   2653  CB  PHE A1354      56.992 -43.889 346.043  1.00 62.24           C  
ANISOU 2653  CB  PHE A1354    10183   8186   5279    358   -361   -794       C  
ATOM   2654  CG  PHE A1354      58.280 -43.787 345.271  1.00 68.67           C  
ANISOU 2654  CG  PHE A1354    10773   9285   6034    447   -521   -795       C  
ATOM   2655  CD1 PHE A1354      59.320 -44.674 345.504  1.00 64.62           C  
ANISOU 2655  CD1 PHE A1354    10301   8925   5329    709   -608   -767       C  
ATOM   2656  CD2 PHE A1354      58.452 -42.798 344.311  1.00 75.13           C  
ANISOU 2656  CD2 PHE A1354    11353  10203   6991    281   -561   -830       C  
ATOM   2657  CE1 PHE A1354      60.509 -44.577 344.795  1.00 68.88           C  
ANISOU 2657  CE1 PHE A1354    10592   9730   5849    783   -729   -800       C  
ATOM   2658  CE2 PHE A1354      59.639 -42.697 343.597  1.00 61.61           C  
ANISOU 2658  CE2 PHE A1354     9441   8728   5240    334   -648   -851       C  
ATOM   2659  CZ  PHE A1354      60.668 -43.588 343.839  1.00 60.82           C  
ANISOU 2659  CZ  PHE A1354     9328   8796   4983    575   -730   -849       C  
ATOM   2660  N   ARG A1355      54.346 -45.321 347.267  1.00 76.09           N  
ANISOU 2660  N   ARG A1355    12497   9237   7177    264    140   -817       N  
ATOM   2661  CA  ARG A1355      53.264 -45.256 348.247  1.00 72.19           C  
ANISOU 2661  CA  ARG A1355    12203   8472   6753    138    376   -867       C  
ATOM   2662  C   ARG A1355      53.089 -46.558 349.022  1.00 78.21           C  
ANISOU 2662  C   ARG A1355    13374   8993   7351    279    607   -820       C  
ATOM   2663  O   ARG A1355      53.288 -46.600 350.235  1.00102.87           O  
ANISOU 2663  O   ARG A1355    16784  12057  10245    369    678   -773       O  
ATOM   2664  CB  ARG A1355      51.942 -44.896 347.565  1.00 61.37           C  
ANISOU 2664  CB  ARG A1355    10646   6936   5736    -89    486   -987       C  
ATOM   2665  CG  ARG A1355      51.805 -43.436 347.179  1.00 57.23           C  
ANISOU 2665  CG  ARG A1355     9834   6547   5365   -232    338  -1028       C  
ATOM   2666  CD  ARG A1355      50.392 -43.134 346.699  1.00 63.25           C  
ANISOU 2666  CD  ARG A1355    10441   7128   6464   -400    443  -1161       C  
ATOM   2667  NE  ARG A1355      49.400 -43.327 347.751  1.00 71.86           N  
ANISOU 2667  NE  ARG A1355    11696   7950   7659   -509    728  -1248       N  
ATOM   2668  CZ  ARG A1355      48.091 -43.170 347.582  1.00 90.23           C  
ANISOU 2668  CZ  ARG A1355    13884  10094  10306   -657    871  -1408       C  
ATOM   2669  NH1 ARG A1355      47.260 -43.365 348.597  1.00 98.26           N  
ANISOU 2669  NH1 ARG A1355    15060  10856  11419   -770   1179  -1499       N  
ATOM   2670  NH2 ARG A1355      47.613 -42.817 346.397  1.00103.44           N  
ANISOU 2670  NH2 ARG A1355    15262  11843  12199   -681    708  -1489       N  
ATOM   2671  N   THR A1356      52.703 -47.614 348.313  1.00 72.82           N  
ANISOU 2671  N   THR A1356    12747   8153   6769    300    739   -841       N  
ATOM   2672  CA  THR A1356      52.380 -48.893 348.939  1.00 78.41           C  
ANISOU 2672  CA  THR A1356    13875   8554   7363    398   1038   -812       C  
ATOM   2673  C   THR A1356      53.605 -49.596 349.518  1.00 89.06           C  
ANISOU 2673  C   THR A1356    15522   9996   8319    748    944   -651       C  
ATOM   2674  O   THR A1356      53.512 -50.290 350.533  1.00 96.74           O  
ANISOU 2674  O   THR A1356    16945  10735   9076    882   1162   -584       O  
ATOM   2675  CB  THR A1356      51.704 -49.847 347.936  1.00 80.66           C  
ANISOU 2675  CB  THR A1356    14120   8651   7873    312   1205   -909       C  
ATOM   2676  OG1 THR A1356      52.667 -50.292 346.972  1.00 79.80           O  
ANISOU 2676  OG1 THR A1356    13899   8752   7668    495    990   -840       O  
ATOM   2677  CG2 THR A1356      50.553 -49.146 347.226  1.00 80.16           C  
ANISOU 2677  CG2 THR A1356    13701   8560   8198     18   1215  -1096       C  
ATOM   2678  N   GLY A1357      54.750 -49.414 348.868  1.00 90.71           N  
ANISOU 2678  N   GLY A1357    15491  10539   8434    910    628   -598       N  
ATOM   2679  CA  GLY A1357      55.959 -50.117 349.251  1.00 66.04           C  
ANISOU 2679  CA  GLY A1357    12569   7547   4977   1280    496   -475       C  
ATOM   2680  C   GLY A1357      55.935 -51.544 348.739  1.00 86.28           C  
ANISOU 2680  C   GLY A1357    15368   9897   7517   1439    679   -427       C  
ATOM   2681  O   GLY A1357      56.705 -52.388 349.195  1.00 78.72           O  
ANISOU 2681  O   GLY A1357    14708   8928   6273   1784    664   -312       O  
ATOM   2682  N   THR A1358      55.042 -51.812 347.789  1.00 88.81           N  
ANISOU 2682  N   THR A1358    15562  10047   8134   1200    847   -529       N  
ATOM   2683  CA  THR A1358      54.914 -53.137 347.190  1.00 92.21           C  
ANISOU 2683  CA  THR A1358    16194  10254   8586   1288   1051   -527       C  
ATOM   2684  C   THR A1358      55.250 -53.092 345.704  1.00 94.29           C  
ANISOU 2684  C   THR A1358    16086  10727   9014   1240    868   -588       C  
ATOM   2685  O   THR A1358      54.830 -52.179 344.993  1.00 96.81           O  
ANISOU 2685  O   THR A1358    16043  11185   9555    999    738   -689       O  
ATOM   2686  CB  THR A1358      53.493 -53.707 347.369  1.00 90.71           C  
ANISOU 2686  CB  THR A1358    16226   9635   8605   1035   1466   -648       C  
ATOM   2687  OG1 THR A1358      53.114 -53.626 348.747  1.00 97.01           O  
ANISOU 2687  OG1 THR A1358    17382  10220   9258   1043   1675   -600       O  
ATOM   2688  CG2 THR A1358      53.432 -55.159 346.914  1.00 86.48           C  
ANISOU 2688  CG2 THR A1358    15974   8827   8056   1134   1725   -653       C  
ATOM   2689  N   TRP A1359      56.005 -54.082 345.239  1.00 97.37           N  
ANISOU 2689  N   TRP A1359    16599  11122   9274   1489    870   -521       N  
ATOM   2690  CA  TRP A1359      56.429 -54.134 343.844  1.00 94.74           C  
ANISOU 2690  CA  TRP A1359    15970  10976   9052   1473    724   -572       C  
ATOM   2691  C   TRP A1359      55.394 -54.818 342.957  1.00 91.02           C  
ANISOU 2691  C   TRP A1359    15526  10247   8810   1252    947   -720       C  
ATOM   2692  O   TRP A1359      54.873 -55.880 343.299  1.00 88.87           O  
ANISOU 2692  O   TRP A1359    15601   9633   8533   1265   1259   -742       O  
ATOM   2693  CB  TRP A1359      57.774 -54.855 343.724  1.00 96.55           C  
ANISOU 2693  CB  TRP A1359    16286  11348   9052   1853    623   -454       C  
ATOM   2694  CG  TRP A1359      58.336 -54.853 342.336  1.00106.44           C  
ANISOU 2694  CG  TRP A1359    17244  12804  10395   1846    491   -504       C  
ATOM   2695  CD1 TRP A1359      58.306 -55.879 341.436  1.00111.36           C  
ANISOU 2695  CD1 TRP A1359    17971  13281  11059   1891    636   -542       C  
ATOM   2696  CD2 TRP A1359      59.010 -53.769 341.685  1.00111.04           C  
ANISOU 2696  CD2 TRP A1359    17413  13747  11030   1779    224   -529       C  
ATOM   2697  NE1 TRP A1359      58.923 -55.502 340.267  1.00102.12           N  
ANISOU 2697  NE1 TRP A1359    16487  12369   9946   1868    466   -583       N  
ATOM   2698  CE2 TRP A1359      59.364 -54.210 340.394  1.00106.38           C  
ANISOU 2698  CE2 TRP A1359    16714  13211  10494   1797    227   -572       C  
ATOM   2699  CE3 TRP A1359      59.350 -52.468 342.069  1.00110.65           C  
ANISOU 2699  CE3 TRP A1359    17101  13957  10982   1692     16   -531       C  
ATOM   2700  CZ2 TRP A1359      60.040 -53.398 339.486  1.00110.66           C  
ANISOU 2700  CZ2 TRP A1359    16918  14044  11084   1735     49   -604       C  
ATOM   2701  CZ3 TRP A1359      60.021 -51.663 341.167  1.00111.70           C  
ANISOU 2701  CZ3 TRP A1359    16887  14372  11182   1619   -152   -571       C  
ATOM   2702  CH2 TRP A1359      60.359 -52.130 339.891  1.00111.60           C  
ANISOU 2702  CH2 TRP A1359    16795  14394  11214   1643   -126   -601       C  
ATOM   2703  N   ASP A1360      55.102 -54.199 341.818  1.00 92.59           N  
ANISOU 2703  N   ASP A1360    15375  10606   9200   1052    792   -834       N  
ATOM   2704  CA  ASP A1360      54.186 -54.773 340.839  1.00 97.55           C  
ANISOU 2704  CA  ASP A1360    15968  11061  10035    854    925  -1014       C  
ATOM   2705  C   ASP A1360      54.956 -55.220 339.600  1.00 89.80           C  
ANISOU 2705  C   ASP A1360    14901  10227   8992    974    814  -1012       C  
ATOM   2706  O   ASP A1360      55.496 -54.394 338.864  1.00 86.20           O  
ANISOU 2706  O   ASP A1360    14173  10057   8523    975    564   -989       O  
ATOM   2707  CB  ASP A1360      53.100 -53.766 340.457  1.00105.62           C  
ANISOU 2707  CB  ASP A1360    16689  12131  11311    555    825  -1175       C  
ATOM   2708  CG  ASP A1360      52.101 -54.334 339.469  1.00108.92           C  
ANISOU 2708  CG  ASP A1360    17032  12405  11947    359    916  -1410       C  
ATOM   2709  OD1 ASP A1360      51.837 -55.554 339.522  1.00109.26           O  
ANISOU 2709  OD1 ASP A1360    17324  12182  12008    355   1192  -1487       O  
ATOM   2710  OD2 ASP A1360      51.579 -53.561 338.638  1.00105.22           O  
ANISOU 2710  OD2 ASP A1360    16269  12085  11624    218    711  -1530       O  
ATOM   2711  N   ALA A1361      55.004 -56.529 339.379  1.00 86.80           N  
ANISOU 2711  N   ALA A1361    14785   9623   8571   1070   1038  -1039       N  
ATOM   2712  CA  ALA A1361      55.789 -57.098 338.290  1.00 91.55           C  
ANISOU 2712  CA  ALA A1361    15362  10327   9095   1211    984  -1034       C  
ATOM   2713  C   ALA A1361      55.211 -56.754 336.920  1.00 91.74           C  
ANISOU 2713  C   ALA A1361    15135  10448   9275    982    859  -1216       C  
ATOM   2714  O   ALA A1361      54.022 -56.948 336.667  1.00 93.69           O  
ANISOU 2714  O   ALA A1361    15365  10521   9711    740    959  -1418       O  
ATOM   2715  CB  ALA A1361      55.894 -58.607 338.452  1.00 95.86           C  
ANISOU 2715  CB  ALA A1361    16298  10561   9564   1366   1293  -1026       C  
ATOM   2716  N   TYR A1362      56.066 -56.244 336.039  1.00 87.26           N  
ANISOU 2716  N   TYR A1362    14377  10158   8619   1068    645  -1161       N  
ATOM   2717  CA  TYR A1362      55.664 -55.920 334.676  1.00 85.02           C  
ANISOU 2717  CA  TYR A1362    13920   9976   8407    911    510  -1307       C  
ATOM   2718  C   TYR A1362      55.563 -57.183 333.826  1.00 79.46           C  
ANISOU 2718  C   TYR A1362    13393   9104   7695    921    677  -1439       C  
ATOM   2719  O   TYR A1362      54.717 -57.275 332.936  1.00 85.98           O  
ANISOU 2719  O   TYR A1362    14157   9890   8622    736    638  -1646       O  
ATOM   2720  CB  TYR A1362      56.649 -54.930 334.045  1.00 88.92           C  
ANISOU 2720  CB  TYR A1362    14211  10787   8789    991    286  -1197       C  
ATOM   2721  CG  TYR A1362      56.323 -54.551 332.615  1.00 96.75           C  
ANISOU 2721  CG  TYR A1362    15099  11876   9787    873    149  -1315       C  
ATOM   2722  CD1 TYR A1362      55.395 -53.557 332.333  1.00 94.62           C  
ANISOU 2722  CD1 TYR A1362    14674  11661   9618    698    -25  -1398       C  
ATOM   2723  CD2 TYR A1362      56.950 -55.183 331.547  1.00101.38           C  
ANISOU 2723  CD2 TYR A1362    15766  12494  10258    965    192  -1342       C  
ATOM   2724  CE1 TYR A1362      55.096 -53.206 331.028  1.00 99.78           C  
ANISOU 2724  CE1 TYR A1362    15281  12402  10228    641   -177  -1498       C  
ATOM   2725  CE2 TYR A1362      56.657 -54.838 330.239  1.00 95.45           C  
ANISOU 2725  CE2 TYR A1362    14977  11825   9464    876     63  -1448       C  
ATOM   2726  CZ  TYR A1362      55.730 -53.850 329.986  1.00 97.03           C  
ANISOU 2726  CZ  TYR A1362    15048  12083   9736    727   -133  -1520       C  
ATOM   2727  OH  TYR A1362      55.436 -53.504 328.688  1.00 85.81           O  
ANISOU 2727  OH  TYR A1362    13635  10743   8225    687   -287  -1617       O  
ATOM   2728  N   ARG A2238      56.421 -58.160 334.110  1.00 76.86           N  
ANISOU 2728  N   ARG A2238    13288   8675   7239   1153    853  -1333       N  
ATOM   2729  CA  ARG A2238      56.438 -59.411 333.356  1.00 84.65           C  
ANISOU 2729  CA  ARG A2238    14481   9476   8206   1184   1051  -1447       C  
ATOM   2730  C   ARG A2238      55.337 -60.361 333.825  1.00 99.92           C  
ANISOU 2730  C   ARG A2238    16646  11037  10281   1023   1343  -1610       C  
ATOM   2731  O   ARG A2238      55.254 -61.504 333.375  1.00105.20           O  
ANISOU 2731  O   ARG A2238    17537  11483  10954   1025   1574  -1725       O  
ATOM   2732  CB  ARG A2238      57.808 -60.085 333.464  1.00 80.57           C  
ANISOU 2732  CB  ARG A2238    14117   8986   7510   1528   1141  -1272       C  
ATOM   2733  CG  ARG A2238      58.201 -60.503 334.871  1.00 91.43           C  
ANISOU 2733  CG  ARG A2238    15712  10226   8801   1766   1274  -1098       C  
ATOM   2734  CD  ARG A2238      59.649 -60.967 334.912  1.00 90.46           C  
ANISOU 2734  CD  ARG A2238    15650  10218   8503   2157   1271   -937       C  
ATOM   2735  NE  ARG A2238      60.588 -59.848 334.861  1.00 77.64           N  
ANISOU 2735  NE  ARG A2238    13684   8987   6827   2246    987   -844       N  
ATOM   2736  CZ  ARG A2238      61.882 -59.968 334.576  1.00 76.52           C  
ANISOU 2736  CZ  ARG A2238    13438   9045   6590   2521    930   -770       C  
ATOM   2737  NH1 ARG A2238      62.396 -61.160 334.300  1.00 73.88           N  
ANISOU 2737  NH1 ARG A2238    13328   8556   6187   2767   1120   -758       N  
ATOM   2738  NH2 ARG A2238      62.660 -58.895 334.557  1.00 74.61           N  
ANISOU 2738  NH2 ARG A2238    12860   9148   6339   2543    707   -729       N  
ATOM   2739  N   ARG A2239      54.499 -59.876 334.735  1.00101.80           N  
ANISOU 2739  N   ARG A2239    16838  11193  10647    869   1366  -1637       N  
ATOM   2740  CA  ARG A2239      53.318 -60.609 335.173  1.00108.09           C  
ANISOU 2740  CA  ARG A2239    17801  11638  11630    647   1668  -1839       C  
ATOM   2741  C   ARG A2239      52.167 -60.366 334.200  1.00107.30           C  
ANISOU 2741  C   ARG A2239    17439  11578  11750    328   1558  -2165       C  
ATOM   2742  O   ARG A2239      51.382 -61.270 333.905  1.00108.29           O  
ANISOU 2742  O   ARG A2239    17664  11454  12026    137   1794  -2428       O  
ATOM   2743  CB  ARG A2239      52.926 -60.188 336.592  1.00118.23           C  
ANISOU 2743  CB  ARG A2239    19157  12808  12957    620   1771  -1740       C  
ATOM   2744  CG  ARG A2239      51.520 -60.590 337.004  1.00128.75           C  
ANISOU 2744  CG  ARG A2239    20552  13819  14548    308   2066  -1997       C  
ATOM   2745  CD  ARG A2239      51.149 -59.986 338.348  1.00127.94           C  
ANISOU 2745  CD  ARG A2239    20497  13638  14477    273   2148  -1896       C  
ATOM   2746  NE  ARG A2239      49.704 -59.972 338.554  1.00134.08           N  
ANISOU 2746  NE  ARG A2239    21165  14209  15571    -81   2350  -2192       N  
ATOM   2747  CZ  ARG A2239      48.902 -59.001 338.128  1.00140.32           C  
ANISOU 2747  CZ  ARG A2239    21535  15201  16581   -292   2102  -2376       C  
ATOM   2748  NH1 ARG A2239      49.405 -57.965 337.471  1.00141.02           N  
ANISOU 2748  NH1 ARG A2239    21332  15670  16578   -186   1667  -2271       N  
ATOM   2749  NH2 ARG A2239      47.598 -59.065 338.356  1.00141.18           N  
ANISOU 2749  NH2 ARG A2239    21519  15118  17004   -599   2305  -2677       N  
ATOM   2750  N   ARG A2240      52.086 -59.137 333.700  1.00104.83           N  
ANISOU 2750  N   ARG A2240    16798  11582  11449    285   1194  -2158       N  
ATOM   2751  CA  ARG A2240      51.056 -58.738 332.745  1.00101.26           C  
ANISOU 2751  CA  ARG A2240    16079  11231  11162     57    997  -2448       C  
ATOM   2752  C   ARG A2240      51.192 -59.474 331.414  1.00 96.20           C  
ANISOU 2752  C   ARG A2240    15496  10608  10448     50    970  -2619       C  
ATOM   2753  O   ARG A2240      52.197 -59.325 330.719  1.00100.71           O  
ANISOU 2753  O   ARG A2240    16106  11359  10801    235    834  -2461       O  
ATOM   2754  CB  ARG A2240      51.119 -57.228 332.504  1.00107.55           C  
ANISOU 2754  CB  ARG A2240    16593  12348  11924     88    620  -2343       C  
ATOM   2755  CG  ARG A2240      50.797 -56.380 333.723  1.00119.25           C  
ANISOU 2755  CG  ARG A2240    17979  13821  13508     50    623  -2232       C  
ATOM   2756  CD  ARG A2240      49.298 -56.201 333.884  1.00132.60           C  
ANISOU 2756  CD  ARG A2240    19473  15408  15502   -206    643  -2528       C  
ATOM   2757  NE  ARG A2240      48.697 -55.585 332.703  1.00143.24           N  
ANISOU 2757  NE  ARG A2240    20554  16964  16906   -267    310  -2722       N  
ATOM   2758  CZ  ARG A2240      47.428 -55.197 332.625  1.00147.54           C  
ANISOU 2758  CZ  ARG A2240    20836  17513  17711   -440    209  -2999       C  
ATOM   2759  NH1 ARG A2240      46.968 -54.646 331.510  1.00145.20           N  
ANISOU 2759  NH1 ARG A2240    20330  17427  17414   -426   -138  -3160       N  
ATOM   2760  NH2 ARG A2240      46.620 -55.356 333.664  1.00151.21           N  
ANISOU 2760  NH2 ARG A2240    21255  17769  18430   -609    459  -3123       N  
ATOM   2761  N   PRO A2241      50.175 -60.269 331.053  1.00 92.90           N  
ANISOU 2761  N   PRO A2241    15078  10000  10220   -180   1118  -2969       N  
ATOM   2762  CA  PRO A2241      50.177 -60.977 329.769  1.00 93.97           C  
ANISOU 2762  CA  PRO A2241    15266  10148  10289   -220   1085  -3188       C  
ATOM   2763  C   PRO A2241      49.896 -60.036 328.602  1.00 97.66           C  
ANISOU 2763  C   PRO A2241    15472  10945  10689   -229    641  -3298       C  
ATOM   2764  O   PRO A2241      49.324 -58.963 328.801  1.00 90.15           O  
ANISOU 2764  O   PRO A2241    14266  10153   9832   -271    394  -3304       O  
ATOM   2765  CB  PRO A2241      49.052 -61.997 329.933  1.00 87.79           C  
ANISOU 2765  CB  PRO A2241    14523   9057   9776   -505   1389  -3569       C  
ATOM   2766  CG  PRO A2241      48.110 -61.343 330.885  1.00 93.07           C  
ANISOU 2766  CG  PRO A2241    14976   9688  10697   -666   1398  -3640       C  
ATOM   2767  CD  PRO A2241      48.966 -60.562 331.843  1.00 94.83           C  
ANISOU 2767  CD  PRO A2241    15270   9998  10764   -436   1353  -3209       C  
ATOM   2768  N   GLY A2242      50.297 -60.436 327.400  1.00 99.40           N  
ANISOU 2768  N   GLY A2242    15792  11248  10728   -172    553  -3380       N  
ATOM   2769  CA  GLY A2242      50.096 -59.615 326.221  1.00100.46           C  
ANISOU 2769  CA  GLY A2242    15772  11671  10728   -141    146  -3470       C  
ATOM   2770  C   GLY A2242      48.640 -59.517 325.809  1.00 98.51           C  
ANISOU 2770  C   GLY A2242    15270  11467  10692   -353    -58  -3891       C  
ATOM   2771  O   GLY A2242      47.843 -60.414 326.087  1.00 96.14           O  
ANISOU 2771  O   GLY A2242    14939  10954  10636   -574    166  -4205       O  
ATOM   2772  N   ARG A2243      48.294 -58.422 325.140  1.00 96.90           N  
ANISOU 2772  N   ARG A2243    14885  11533  10399   -279   -476  -3913       N  
ATOM   2773  CA  ARG A2243      46.932 -58.214 324.664  1.00102.79           C  
ANISOU 2773  CA  ARG A2243    15348  12381  11326   -416   -757  -4325       C  
ATOM   2774  C   ARG A2243      46.861 -58.277 323.141  1.00 92.07           C  
ANISOU 2774  C   ARG A2243    14058  11212   9712   -339  -1074  -4527       C  
ATOM   2775  O   ARG A2243      47.889 -58.252 322.464  1.00 90.46           O  
ANISOU 2775  O   ARG A2243    14123  11070   9177   -170  -1082  -4296       O  
ATOM   2776  CB  ARG A2243      46.390 -56.870 325.150  1.00112.75           C  
ANISOU 2776  CB  ARG A2243    16343  13796  12700   -357  -1021  -4230       C  
ATOM   2777  CG  ARG A2243      46.510 -56.641 326.645  1.00125.32           C  
ANISOU 2777  CG  ARG A2243    17895  15227  14495   -412   -740  -4006       C  
ATOM   2778  CD  ARG A2243      45.673 -55.447 327.058  1.00137.16           C  
ANISOU 2778  CD  ARG A2243    19089  16852  16174   -406   -987  -4036       C  
ATOM   2779  NE  ARG A2243      45.813 -54.343 326.112  1.00138.79           N  
ANISOU 2779  NE  ARG A2243    19276  17326  16133   -188  -1416  -3924       N  
ATOM   2780  CZ  ARG A2243      45.067 -53.244 326.129  1.00143.21           C  
ANISOU 2780  CZ  ARG A2243    19599  18025  16789   -118  -1714  -3971       C  
ATOM   2781  NH1 ARG A2243      44.120 -53.096 327.045  1.00150.13           N  
ANISOU 2781  NH1 ARG A2243    20193  18818  18030   -264  -1633  -4146       N  
ATOM   2782  NH2 ARG A2243      45.265 -52.293 325.227  1.00138.52           N  
ANISOU 2782  NH2 ARG A2243    19074  17634  15922    110  -2069  -3843       N  
ATOM   2783  N   PHE A2244      45.638 -58.353 322.618  1.00 87.82           N  
ANISOU 2783  N   PHE A2244    13269  10770   9330   -460  -1332  -4979       N  
ATOM   2784  CA  PHE A2244      45.378 -58.387 321.176  1.00 99.12           C  
ANISOU 2784  CA  PHE A2244    14746  12404  10509   -377  -1698  -5237       C  
ATOM   2785  C   PHE A2244      46.108 -59.523 320.463  1.00101.51           C  
ANISOU 2785  C   PHE A2244    15382  12590  10595   -411  -1470  -5288       C  
ATOM   2786  O   PHE A2244      46.484 -59.394 319.300  1.00106.82           O  
ANISOU 2786  O   PHE A2244    16261  13417  10911   -257  -1699  -5283       O  
ATOM   2787  CB  PHE A2244      45.759 -57.051 320.531  1.00 98.01           C  
ANISOU 2787  CB  PHE A2244    14694  12517  10030    -74  -2094  -4944       C  
ATOM   2788  CG  PHE A2244      44.927 -55.892 321.000  1.00102.55           C  
ANISOU 2788  CG  PHE A2244    14953  13225  10787     -5  -2384  -4947       C  
ATOM   2789  CD1 PHE A2244      43.809 -55.493 320.287  1.00104.26           C  
ANISOU 2789  CD1 PHE A2244    14933  13655  11027     63  -2850  -5310       C  
ATOM   2790  CD2 PHE A2244      45.260 -55.203 322.155  1.00 85.03           C  
ANISOU 2790  CD2 PHE A2244    12673  10924   8712     10  -2203  -4602       C  
ATOM   2791  CE1 PHE A2244      43.039 -54.428 320.715  1.00101.44           C  
ANISOU 2791  CE1 PHE A2244    14281  13413  10849    158  -3113  -5316       C  
ATOM   2792  CE2 PHE A2244      44.494 -54.137 322.588  1.00107.47           C  
ANISOU 2792  CE2 PHE A2244    15238  13868  11726     74  -2445  -4609       C  
ATOM   2793  CZ  PHE A2244      43.382 -53.750 321.867  1.00102.81           C  
ANISOU 2793  CZ  PHE A2244    14411  13477  11175    155  -2891  -4960       C  
ATOM   2794  N   VAL A2245      46.301 -60.635 321.163  1.00 65.11           N  
ANISOU 2794  N   VAL A2245     9927   8181   6631   1572  -1316    997       N  
ATOM   2795  CA  VAL A2245      46.993 -61.786 320.598  1.00 67.88           C  
ANISOU 2795  CA  VAL A2245    10318   8298   7175   1477  -1320   1031       C  
ATOM   2796  C   VAL A2245      46.127 -62.484 319.552  1.00 74.12           C  
ANISOU 2796  C   VAL A2245    11016   9054   8094   1139  -1067   1126       C  
ATOM   2797  O   VAL A2245      46.617 -62.887 318.497  1.00 82.17           O  
ANISOU 2797  O   VAL A2245    11926   9943   9350    998  -1077   1028       O  
ATOM   2798  CB  VAL A2245      47.392 -62.791 321.696  1.00 71.59           C  
ANISOU 2798  CB  VAL A2245    11095   8637   7470   1680  -1373   1193       C  
ATOM   2799  CG1 VAL A2245      48.100 -63.994 321.092  1.00 68.26           C  
ANISOU 2799  CG1 VAL A2245    10713   7939   7283   1601  -1389   1213       C  
ATOM   2800  CG2 VAL A2245      48.275 -62.115 322.733  1.00 74.04           C  
ANISOU 2800  CG2 VAL A2245    11507   8990   7637   2031  -1670   1075       C  
ATOM   2801  N   ARG A2246      44.837 -62.613 319.846  1.00 71.46           N  
ANISOU 2801  N   ARG A2246    10710   8845   7598   1017   -844   1305       N  
ATOM   2802  CA  ARG A2246      43.894 -63.243 318.926  1.00 68.01           C  
ANISOU 2802  CA  ARG A2246    10170   8380   7290    685   -631   1394       C  
ATOM   2803  C   ARG A2246      43.667 -62.384 317.686  1.00 67.93           C  
ANISOU 2803  C   ARG A2246     9877   8488   7443    509   -640   1218       C  
ATOM   2804  O   ARG A2246      43.310 -62.891 316.622  1.00 59.77           O  
ANISOU 2804  O   ARG A2246     8746   7397   6567    254   -555   1199       O  
ATOM   2805  CB  ARG A2246      42.561 -63.507 319.627  1.00 60.71           C  
ANISOU 2805  CB  ARG A2246     9304   7587   6177    605   -393   1648       C  
ATOM   2806  CG  ARG A2246      42.625 -64.570 320.709  1.00 82.33           C  
ANISOU 2806  CG  ARG A2246    12327  10193   8761    712   -328   1901       C  
ATOM   2807  CD  ARG A2246      41.362 -64.561 321.551  1.00 87.34           C  
ANISOU 2807  CD  ARG A2246    12990  11034   9161    686    -73   2165       C  
ATOM   2808  NE  ARG A2246      41.220 -63.320 322.307  1.00 92.60           N  
ANISOU 2808  NE  ARG A2246    13633  11990   9561    948   -105   2077       N  
ATOM   2809  CZ  ARG A2246      40.182 -63.035 323.087  1.00 93.75           C  
ANISOU 2809  CZ  ARG A2246    13776  12388   9457   1003    116   2250       C  
ATOM   2810  NH1 ARG A2246      39.189 -63.903 323.215  1.00 89.15           N  
ANISOU 2810  NH1 ARG A2246    13186  11809   8877    787    397   2555       N  
ATOM   2811  NH2 ARG A2246      40.135 -61.883 323.741  1.00 91.97           N  
ANISOU 2811  NH2 ARG A2246    13544  12407   8994   1278     56   2113       N  
ATOM   2812  N   LEU A2247      43.872 -61.081 317.836  1.00 61.86           N  
ANISOU 2812  N   LEU A2247     8992   7877   6635    653   -760   1092       N  
ATOM   2813  CA  LEU A2247      43.681 -60.140 316.743  1.00 60.68           C  
ANISOU 2813  CA  LEU A2247     8585   7841   6631    513   -784    963       C  
ATOM   2814  C   LEU A2247      44.805 -60.238 315.719  1.00 77.38           C  
ANISOU 2814  C   LEU A2247    10606   9831   8963    465   -900    813       C  
ATOM   2815  O   LEU A2247      44.556 -60.392 314.523  1.00 64.15           O  
ANISOU 2815  O   LEU A2247     8798   8175   7402    246   -826    776       O  
ATOM   2816  CB  LEU A2247      43.587 -58.712 317.281  1.00 59.01           C  
ANISOU 2816  CB  LEU A2247     8289   7789   6343    696   -897    882       C  
ATOM   2817  CG  LEU A2247      43.478 -57.621 316.217  1.00 68.52           C  
ANISOU 2817  CG  LEU A2247     9234   9084   7718    578   -954    776       C  
ATOM   2818  CD1 LEU A2247      42.267 -57.876 315.349  1.00 88.46           C  
ANISOU 2818  CD1 LEU A2247    11630  11717  10264    304   -764    868       C  
ATOM   2819  CD2 LEU A2247      43.402 -56.246 316.854  1.00 75.75           C  
ANISOU 2819  CD2 LEU A2247    10091  10099   8590    781  -1093    688       C  
ATOM   2820  N   VAL A2248      46.041 -60.149 316.199  1.00 79.52           N  
ANISOU 2820  N   VAL A2248    10940   9992   9279    684  -1082    726       N  
ATOM   2821  CA  VAL A2248      47.213 -60.187 315.332  1.00 69.36           C  
ANISOU 2821  CA  VAL A2248     9533   8609   8209    677  -1180    590       C  
ATOM   2822  C   VAL A2248      47.313 -61.508 314.571  1.00 63.85           C  
ANISOU 2822  C   VAL A2248     8899   7774   7589    534  -1060    593       C  
ATOM   2823  O   VAL A2248      47.609 -61.523 313.377  1.00 81.59           O  
ANISOU 2823  O   VAL A2248    10998  10038   9963    406  -1020    497       O  
ATOM   2824  CB  VAL A2248      48.509 -59.964 316.140  1.00 71.46           C  
ANISOU 2824  CB  VAL A2248     9848   8772   8532    952  -1414    507       C  
ATOM   2825  CG1 VAL A2248      49.732 -60.109 315.248  1.00 71.67           C  
ANISOU 2825  CG1 VAL A2248     9716   8709   8807    946  -1480    386       C  
ATOM   2826  CG2 VAL A2248      48.488 -58.594 316.802  1.00 67.03           C  
ANISOU 2826  CG2 VAL A2248     9218   8320   7931   1095  -1579    450       C  
ATOM   2827  N   ALA A2249      47.051 -62.612 315.263  1.00 57.17           N  
ANISOU 2827  N   ALA A2249     8280   6785   6657    564  -1004    706       N  
ATOM   2828  CA  ALA A2249      47.134 -63.937 314.655  1.00 64.11           C  
ANISOU 2828  CA  ALA A2249     9250   7472   7635    446   -921    698       C  
ATOM   2829  C   ALA A2249      46.086 -64.125 313.562  1.00 79.50           C  
ANISOU 2829  C   ALA A2249    11100   9497   9609    145   -765    690       C  
ATOM   2830  O   ALA A2249      46.266 -64.931 312.648  1.00 82.14           O  
ANISOU 2830  O   ALA A2249    11441   9714  10055     33   -727    588       O  
ATOM   2831  CB  ALA A2249      46.984 -65.016 315.715  1.00 52.68           C  
ANISOU 2831  CB  ALA A2249     8074   5833   6108    532   -904    868       C  
ATOM   2832  N   ALA A2250      44.991 -63.379 313.661  1.00 75.52           N  
ANISOU 2832  N   ALA A2250    10501   9191   9001     31   -692    778       N  
ATOM   2833  CA  ALA A2250      43.913 -63.470 312.686  1.00 74.41           C  
ANISOU 2833  CA  ALA A2250    10244   9145   8882   -249   -578    779       C  
ATOM   2834  C   ALA A2250      44.198 -62.600 311.462  1.00 76.61           C  
ANISOU 2834  C   ALA A2250    10307   9586   9215   -314   -619    630       C  
ATOM   2835  O   ALA A2250      43.959 -63.010 310.325  1.00 72.01           O  
ANISOU 2835  O   ALA A2250     9670   9014   8676   -493   -578    541       O  
ATOM   2836  CB  ALA A2250      42.591 -63.074 313.326  1.00 66.11           C  
ANISOU 2836  CB  ALA A2250     9158   8247   7715   -329   -476    952       C  
ATOM   2837  N   VAL A2251      44.710 -61.397 311.704  1.00 65.93           N  
ANISOU 2837  N   VAL A2251     8841   8354   7856   -166   -712    608       N  
ATOM   2838  CA  VAL A2251      45.035 -60.471 310.628  1.00 70.55           C  
ANISOU 2838  CA  VAL A2251     9216   9086   8503   -220   -748    523       C  
ATOM   2839  C   VAL A2251      46.195 -61.011 309.796  1.00 78.18           C  
ANISOU 2839  C   VAL A2251    10169   9969   9568   -190   -755    387       C  
ATOM   2840  O   VAL A2251      46.178 -60.931 308.565  1.00 72.19           O  
ANISOU 2840  O   VAL A2251     9298   9318   8811   -318   -703    319       O  
ATOM   2841  CB  VAL A2251      45.390 -59.074 311.173  1.00 71.57           C  
ANISOU 2841  CB  VAL A2251     9231   9305   8658    -64   -870    539       C  
ATOM   2842  CG1 VAL A2251      45.874 -58.167 310.054  1.00 81.70           C  
ANISOU 2842  CG1 VAL A2251    10298  10703  10044   -126   -906    494       C  
ATOM   2843  CG2 VAL A2251      44.187 -58.462 311.874  1.00 71.64           C  
ANISOU 2843  CG2 VAL A2251     9234   9428   8557    -71   -847    641       C  
ATOM   2844  N   VAL A2252      47.193 -61.569 310.476  1.00 74.81           N  
ANISOU 2844  N   VAL A2252     9853   9364   9206     -1   -819    347       N  
ATOM   2845  CA  VAL A2252      48.329 -62.193 309.805  1.00 71.79           C  
ANISOU 2845  CA  VAL A2252     9452   8891   8934     69   -814    209       C  
ATOM   2846  C   VAL A2252      47.858 -63.332 308.905  1.00 81.23           C  
ANISOU 2846  C   VAL A2252    10741  10023  10100    -89   -702    123       C  
ATOM   2847  O   VAL A2252      48.317 -63.471 307.769  1.00 87.94           O  
ANISOU 2847  O   VAL A2252    11503  10941  10968   -122   -645    -11       O  
ATOM   2848  CB  VAL A2252      49.364 -62.727 310.822  1.00 57.37           C  
ANISOU 2848  CB  VAL A2252     7746   6859   7193    315   -924    193       C  
ATOM   2849  CG1 VAL A2252      50.306 -63.729 310.167  1.00 52.12           C  
ANISOU 2849  CG1 VAL A2252     7101   6059   6645    388   -890     45       C  
ATOM   2850  CG2 VAL A2252      50.146 -61.576 311.437  1.00 48.87           C  
ANISOU 2850  CG2 VAL A2252     6531   5843   6193    483  -1078    205       C  
ATOM   2851  N   ALA A2253      46.928 -64.132 309.417  1.00 74.48           N  
ANISOU 2851  N   ALA A2253    10060   9040   9200   -186   -671    201       N  
ATOM   2852  CA  ALA A2253      46.354 -65.235 308.657  1.00 71.38           C  
ANISOU 2852  CA  ALA A2253     9764   8540   8816   -361   -605    115       C  
ATOM   2853  C   ALA A2253      45.693 -64.737 307.373  1.00 70.73           C  
ANISOU 2853  C   ALA A2253     9530   8690   8653   -561   -558     41       C  
ATOM   2854  O   ALA A2253      45.835 -65.349 306.315  1.00 73.36           O  
ANISOU 2854  O   ALA A2253     9883   9011   8981   -624   -532   -135       O  
ATOM   2855  CB  ALA A2253      45.350 -65.998 309.509  1.00 57.14           C  
ANISOU 2855  CB  ALA A2253     8128   6572   7011   -469   -581    270       C  
ATOM   2856  N   ALA A2254      44.980 -63.619 307.472  1.00 64.07           N  
ANISOU 2856  N   ALA A2254     8545   8062   7736   -638   -561    167       N  
ATOM   2857  CA  ALA A2254      44.294 -63.046 306.319  1.00 68.70           C  
ANISOU 2857  CA  ALA A2254     8986   8881   8237   -814   -542    136       C  
ATOM   2858  C   ALA A2254      45.283 -62.358 305.384  1.00 73.39           C  
ANISOU 2858  C   ALA A2254     9441   9638   8805   -729   -534     52       C  
ATOM   2859  O   ALA A2254      45.071 -62.297 304.175  1.00 67.05           O  
ANISOU 2859  O   ALA A2254     8576   8997   7904   -838   -505    -30       O  
ATOM   2860  CB  ALA A2254      43.221 -62.068 306.772  1.00 56.54           C  
ANISOU 2860  CB  ALA A2254     7330   7499   6653   -896   -555    308       C  
ATOM   2861  N   PHE A2255      46.363 -61.842 305.959  1.00 68.43           N  
ANISOU 2861  N   PHE A2255     8759   8976   8266   -535   -562     82       N  
ATOM   2862  CA  PHE A2255      47.403 -61.162 305.199  1.00 65.57           C  
ANISOU 2862  CA  PHE A2255     8228   8754   7929   -454   -538     45       C  
ATOM   2863  C   PHE A2255      48.138 -62.135 304.282  1.00 79.16           C  
ANISOU 2863  C   PHE A2255     9999  10449   9628   -408   -450   -147       C  
ATOM   2864  O   PHE A2255      48.412 -61.827 303.123  1.00 89.71           O  
ANISOU 2864  O   PHE A2255    11224  11990  10872   -442   -370   -196       O  
ATOM   2865  CB  PHE A2255      48.381 -60.477 306.158  1.00 54.85           C  
ANISOU 2865  CB  PHE A2255     6791   7323   6726   -263   -622    113       C  
ATOM   2866  CG  PHE A2255      49.576 -59.858 305.487  1.00 51.28           C  
ANISOU 2866  CG  PHE A2255     6133   6980   6370   -183   -591     97       C  
ATOM   2867  CD1 PHE A2255      49.491 -58.602 304.911  1.00 52.90           C  
ANISOU 2867  CD1 PHE A2255     6140   7378   6581   -265   -591    221       C  
ATOM   2868  CD2 PHE A2255      50.795 -60.520 305.462  1.00 54.52           C  
ANISOU 2868  CD2 PHE A2255     6533   7292   6891    -21   -560    -19       C  
ATOM   2869  CE1 PHE A2255      50.594 -58.025 304.305  1.00 65.24           C  
ANISOU 2869  CE1 PHE A2255     7491   9039   8256   -213   -542    252       C  
ATOM   2870  CE2 PHE A2255      51.901 -59.951 304.857  1.00 51.20           C  
ANISOU 2870  CE2 PHE A2255     5882   6991   6583     46   -506    -12       C  
ATOM   2871  CZ  PHE A2255      51.801 -58.702 304.278  1.00 61.77           C  
ANISOU 2871  CZ  PHE A2255     7017   8526   7926    -61   -488    137       C  
ATOM   2872  N   ALA A2256      48.450 -63.315 304.809  1.00 75.64           N  
ANISOU 2872  N   ALA A2256     9729   9753   9257   -315   -463   -253       N  
ATOM   2873  CA  ALA A2256      49.185 -64.322 304.054  1.00 73.03           C  
ANISOU 2873  CA  ALA A2256     9462   9353   8931   -226   -393   -471       C  
ATOM   2874  C   ALA A2256      48.305 -65.010 303.013  1.00 77.07           C  
ANISOU 2874  C   ALA A2256    10079   9911   9292   -399   -358   -619       C  
ATOM   2875  O   ALA A2256      48.810 -65.571 302.039  1.00 82.03           O  
ANISOU 2875  O   ALA A2256    10730  10586   9853   -337   -286   -828       O  
ATOM   2876  CB  ALA A2256      49.787 -65.352 304.997  1.00 69.58           C  
ANISOU 2876  CB  ALA A2256     9188   8596   8653    -56   -449   -527       C  
ATOM   2877  N   LEU A2257      46.992 -64.966 303.221  1.00 69.86           N  
ANISOU 2877  N   LEU A2257     9221   8993   8330   -605   -415   -524       N  
ATOM   2878  CA  LEU A2257      46.056 -65.624 302.315  1.00 74.25           C  
ANISOU 2878  CA  LEU A2257     9866   9570   8776   -793   -432   -667       C  
ATOM   2879  C   LEU A2257      45.579 -64.702 301.196  1.00 74.30           C  
ANISOU 2879  C   LEU A2257     9725   9927   8580   -910   -415   -646       C  
ATOM   2880  O   LEU A2257      45.021 -65.166 300.204  1.00 83.70           O  
ANISOU 2880  O   LEU A2257    10974  11195   9633  -1027   -443   -808       O  
ATOM   2881  CB  LEU A2257      44.847 -66.159 303.087  1.00 70.84           C  
ANISOU 2881  CB  LEU A2257     9541   8942   8432   -972   -506   -566       C  
ATOM   2882  CG  LEU A2257      45.077 -67.420 303.921  1.00 82.84           C  
ANISOU 2882  CG  LEU A2257    11267  10079  10131   -911   -532   -603       C  
ATOM   2883  CD1 LEU A2257      43.776 -67.877 304.560  1.00 87.33           C  
ANISOU 2883  CD1 LEU A2257    11904  10496  10783  -1132   -574   -457       C  
ATOM   2884  CD2 LEU A2257      45.676 -68.526 303.067  1.00 85.58           C  
ANISOU 2884  CD2 LEU A2257    11746  10271  10498   -837   -538   -906       C  
ATOM   2885  N   CYS A2258      45.800 -63.401 301.353  1.00 64.76           N  
ANISOU 2885  N   CYS A2258     8333   8915   7356   -875   -393   -448       N  
ATOM   2886  CA  CYS A2258      45.346 -62.434 300.361  1.00 68.98           C  
ANISOU 2886  CA  CYS A2258     8728   9769   7713   -979   -388   -370       C  
ATOM   2887  C   CYS A2258      46.490 -61.931 299.485  1.00 82.58           C  
ANISOU 2887  C   CYS A2258    10333  11703   9339   -848   -271   -389       C  
ATOM   2888  O   CYS A2258      46.319 -61.728 298.282  1.00 99.62           O  
ANISOU 2888  O   CYS A2258    12464  14115  11274   -902   -232   -432       O  
ATOM   2889  CB  CYS A2258      44.651 -61.253 301.044  1.00 72.92           C  
ANISOU 2889  CB  CYS A2258     9093  10338   8276  -1049   -454   -115       C  
ATOM   2890  SG  CYS A2258      43.069 -61.669 301.818  1.00 77.93           S  
ANISOU 2890  SG  CYS A2258     9796  10842   8970  -1231   -548    -55       S  
ATOM   2891  N   TRP A2259      47.656 -61.733 300.091  1.00 77.58           N  
ANISOU 2891  N   TRP A2259     9625  10979   8872   -674   -215   -347       N  
ATOM   2892  CA  TRP A2259      48.821 -61.255 299.357  1.00 81.84           C  
ANISOU 2892  CA  TRP A2259    10007  11712   9376   -552    -79   -333       C  
ATOM   2893  C   TRP A2259      49.705 -62.414 298.910  1.00 82.19           C  
ANISOU 2893  C   TRP A2259    10142  11694   9391   -390     31   -598       C  
ATOM   2894  O   TRP A2259      50.624 -62.234 298.110  1.00 77.79           O  
ANISOU 2894  O   TRP A2259     9462  11337   8757   -279    187   -629       O  
ATOM   2895  CB  TRP A2259      49.623 -60.272 300.211  1.00 83.91           C  
ANISOU 2895  CB  TRP A2259    10081  11922   9878   -460   -100   -134       C  
ATOM   2896  CG  TRP A2259      48.881 -59.004 300.489  1.00 86.41           C  
ANISOU 2896  CG  TRP A2259    10291  12318  10224   -585   -200    106       C  
ATOM   2897  CD1 TRP A2259      48.135 -58.716 301.592  1.00 88.48           C  
ANISOU 2897  CD1 TRP A2259    10602  12424  10593   -624   -340    189       C  
ATOM   2898  CD2 TRP A2259      48.805 -57.854 299.640  1.00 95.59           C  
ANISOU 2898  CD2 TRP A2259    11281  13734  11305   -669   -162    298       C  
ATOM   2899  NE1 TRP A2259      47.601 -57.454 301.486  1.00 94.38           N  
ANISOU 2899  NE1 TRP A2259    11215  13299  11347   -713   -403    389       N  
ATOM   2900  CE2 TRP A2259      47.998 -56.904 300.296  1.00 96.58           C  
ANISOU 2900  CE2 TRP A2259    11359  13812  11525   -750   -307    473       C  
ATOM   2901  CE3 TRP A2259      49.342 -57.533 298.389  1.00 93.54           C  
ANISOU 2901  CE3 TRP A2259    10907  13742  10892   -671    -11    354       C  
ATOM   2902  CZ2 TRP A2259      47.716 -55.656 299.745  1.00102.03           C  
ANISOU 2902  CZ2 TRP A2259    11895  14673  12198   -836   -333    697       C  
ATOM   2903  CZ3 TRP A2259      49.061 -56.295 297.843  1.00 89.44           C  
ANISOU 2903  CZ3 TRP A2259    10238  13411  10333   -771    -23    611       C  
ATOM   2904  CH2 TRP A2259      48.255 -55.371 298.520  1.00 96.58           C  
ANISOU 2904  CH2 TRP A2259    11102  14223  11370   -854   -196    780       C  
ATOM   2905  N   GLY A2260      49.417 -63.600 299.434  1.00 84.09           N  
ANISOU 2905  N   GLY A2260    10591  11653   9705   -371    -44   -777       N  
ATOM   2906  CA  GLY A2260      50.137 -64.805 299.062  1.00 85.65           C  
ANISOU 2906  CA  GLY A2260    10908  11731   9903   -207     25  -1061       C  
ATOM   2907  C   GLY A2260      50.036 -65.131 297.584  1.00 90.10           C  
ANISOU 2907  C   GLY A2260    11519  12543  10172   -212    123  -1272       C  
ATOM   2908  O   GLY A2260      51.034 -65.052 296.866  1.00 90.57           O  
ANISOU 2908  O   GLY A2260    11471  12800  10142    -45    294  -1350       O  
ATOM   2909  N   PRO A2261      48.831 -65.507 297.122  1.00 90.20           N  
ANISOU 2909  N   PRO A2261    11686  12560  10025   -397     12  -1369       N  
ATOM   2910  CA  PRO A2261      48.578 -65.826 295.712  1.00 86.70           C  
ANISOU 2910  CA  PRO A2261    11324  12361   9257   -408     52  -1596       C  
ATOM   2911  C   PRO A2261      49.001 -64.710 294.762  1.00 81.81           C  
ANISOU 2911  C   PRO A2261    10516  12185   8385   -375    210  -1437       C  
ATOM   2912  O   PRO A2261      49.440 -64.993 293.649  1.00 81.54           O  
ANISOU 2912  O   PRO A2261    10515  12389   8078   -254    339  -1629       O  
ATOM   2913  CB  PRO A2261      47.062 -66.025 295.668  1.00 80.72           C  
ANISOU 2913  CB  PRO A2261    10686  11536   8446   -668   -151  -1609       C  
ATOM   2914  CG  PRO A2261      46.711 -66.479 297.035  1.00 74.49           C  
ANISOU 2914  CG  PRO A2261     9961  10356   7984   -734   -259  -1521       C  
ATOM   2915  CD  PRO A2261      47.635 -65.733 297.954  1.00 85.07           C  
ANISOU 2915  CD  PRO A2261    11141  11675   9506   -597   -166  -1284       C  
ATOM   2916  N   TYR A2262      48.872 -63.463 295.202  1.00 73.76           N  
ANISOU 2916  N   TYR A2262     9305  11267   7453   -470    203  -1087       N  
ATOM   2917  CA  TYR A2262      49.234 -62.322 294.370  1.00 68.89           C  
ANISOU 2917  CA  TYR A2262     8498  11031   6645   -466    342   -868       C  
ATOM   2918  C   TYR A2262      50.700 -62.356 293.945  1.00 75.85           C  
ANISOU 2918  C   TYR A2262     9245  12059   7515   -240    591   -908       C  
ATOM   2919  O   TYR A2262      51.006 -62.340 292.753  1.00 84.77           O  
ANISOU 2919  O   TYR A2262    10364  13517   8326   -166    755   -975       O  
ATOM   2920  CB  TYR A2262      48.945 -61.009 295.096  1.00 65.87           C  
ANISOU 2920  CB  TYR A2262     7933  10640   6455   -588    266   -496       C  
ATOM   2921  CG  TYR A2262      49.505 -59.809 294.371  1.00 60.04           C  
ANISOU 2921  CG  TYR A2262     6975  10224   5612   -579    412   -223       C  
ATOM   2922  CD1 TYR A2262      50.611 -59.128 294.862  1.00 62.90           C  
ANISOU 2922  CD1 TYR A2262     7111  10553   6236   -491    515    -32       C  
ATOM   2923  CD2 TYR A2262      48.943 -59.373 293.180  1.00 71.89           C  
ANISOU 2923  CD2 TYR A2262     8493  12059   6763   -662    435   -144       C  
ATOM   2924  CE1 TYR A2262      51.132 -58.034 294.196  1.00 76.51           C  
ANISOU 2924  CE1 TYR A2262     8616  12546   7909   -508    654    253       C  
ATOM   2925  CE2 TYR A2262      49.458 -58.280 292.504  1.00 80.05           C  
ANISOU 2925  CE2 TYR A2262     9333  13382   7701   -660    581    154       C  
ATOM   2926  CZ  TYR A2262      50.551 -57.616 293.016  1.00 80.86           C  
ANISOU 2926  CZ  TYR A2262     9199  13424   8101   -594    699    362       C  
ATOM   2927  OH  TYR A2262      51.066 -56.529 292.347  1.00 69.24           O  
ANISOU 2927  OH  TYR A2262     7516  12214   6579   -618    848    692       O  
ATOM   2928  N   HIS A2263      51.600 -62.405 294.923  1.00 76.22           N  
ANISOU 2928  N   HIS A2263     9180  11880   7902   -121    620   -866       N  
ATOM   2929  CA  HIS A2263      53.035 -62.381 294.648  1.00 73.96           C  
ANISOU 2929  CA  HIS A2263     8701  11716   7683     92    850   -878       C  
ATOM   2930  C   HIS A2263      53.495 -63.593 293.843  1.00 80.03           C  
ANISOU 2930  C   HIS A2263     9612  12548   8250    295    988  -1256       C  
ATOM   2931  O   HIS A2263      54.527 -63.545 293.175  1.00 84.50           O  
ANISOU 2931  O   HIS A2263    10019  13356   8731    474   1238  -1284       O  
ATOM   2932  CB  HIS A2263      53.833 -62.300 295.951  1.00 65.32           C  
ANISOU 2932  CB  HIS A2263     7472  10326   7019    185    787   -793       C  
ATOM   2933  CG  HIS A2263      53.744 -60.972 296.633  1.00 70.93           C  
ANISOU 2933  CG  HIS A2263     7988  11023   7939     50    690   -440       C  
ATOM   2934  ND1 HIS A2263      52.846 -60.713 297.647  1.00 70.09           N  
ANISOU 2934  ND1 HIS A2263     7983  10683   7966    -83    458   -347       N  
ATOM   2935  CD2 HIS A2263      54.440 -59.824 296.447  1.00 67.68           C  
ANISOU 2935  CD2 HIS A2263     7283  10790   7643     32    792   -164       C  
ATOM   2936  CE1 HIS A2263      52.994 -59.466 298.057  1.00 69.61           C  
ANISOU 2936  CE1 HIS A2263     7717  10652   8080   -156    405    -64       C  
ATOM   2937  NE2 HIS A2263      53.955 -58.905 297.343  1.00 64.95           N  
ANISOU 2937  NE2 HIS A2263     6885  10290   7505   -102    592     58       N  
ATOM   2938  N   VAL A2264      52.732 -64.679 293.913  1.00 77.00           N  
ANISOU 2938  N   VAL A2264     9516  11937   7805    270    829  -1549       N  
ATOM   2939  CA  VAL A2264      53.054 -65.876 293.148  1.00 83.61           C  
ANISOU 2939  CA  VAL A2264    10526  12784   8457    465    913  -1958       C  
ATOM   2940  C   VAL A2264      52.921 -65.594 291.655  1.00 99.78           C  
ANISOU 2940  C   VAL A2264    12588  15299  10026    483   1071  -2022       C  
ATOM   2941  O   VAL A2264      53.771 -65.990 290.858  1.00 94.32           O  
ANISOU 2941  O   VAL A2264    11869  14824   9145    722   1298  -2224       O  
ATOM   2942  CB  VAL A2264      52.146 -67.060 293.534  1.00 82.54           C  
ANISOU 2942  CB  VAL A2264    10701  12264   8395    390    667  -2240       C  
ATOM   2943  CG1 VAL A2264      52.476 -68.283 292.695  1.00 83.90           C  
ANISOU 2943  CG1 VAL A2264    11068  12420   8391    604    724  -2701       C  
ATOM   2944  CG2 VAL A2264      52.289 -67.375 295.013  1.00 86.82           C  
ANISOU 2944  CG2 VAL A2264    11252  12365   9370    389    529  -2146       C  
ATOM   2945  N   PHE A2265      51.855 -64.892 291.288  1.00100.40           N  
ANISOU 2945  N   PHE A2265    12703  15548   9895    249    952  -1841       N  
ATOM   2946  CA  PHE A2265      51.606 -64.547 289.894  1.00 92.03           C  
ANISOU 2946  CA  PHE A2265    11680  14946   8342    252   1060  -1857       C  
ATOM   2947  C   PHE A2265      52.471 -63.378 289.431  1.00 87.34           C  
ANISOU 2947  C   PHE A2265    10794  14737   7656    306   1342  -1495       C  
ATOM   2948  O   PHE A2265      52.881 -63.323 288.272  1.00 90.16           O  
ANISOU 2948  O   PHE A2265    11142  15500   7616    441   1567  -1546       O  
ATOM   2949  CB  PHE A2265      50.125 -64.222 289.686  1.00 89.02           C  
ANISOU 2949  CB  PHE A2265    11432  14596   7797    -14    797  -1780       C  
ATOM   2950  CG  PHE A2265      49.236 -65.433 289.670  1.00 97.02           C  
ANISOU 2950  CG  PHE A2265    12735  15345   8785    -70    548  -2178       C  
ATOM   2951  CD1 PHE A2265      48.894 -66.041 288.474  1.00109.06           C  
ANISOU 2951  CD1 PHE A2265    14466  17086   9886     -4    510  -2515       C  
ATOM   2952  CD2 PHE A2265      48.748 -65.968 290.850  1.00100.56           C  
ANISOU 2952  CD2 PHE A2265    13249  15325   9634   -190    347  -2210       C  
ATOM   2953  CE1 PHE A2265      48.079 -67.157 288.454  1.00110.73           C  
ANISOU 2953  CE1 PHE A2265    14931  17016  10124    -74    248  -2894       C  
ATOM   2954  CE2 PHE A2265      47.933 -67.084 290.838  1.00103.95           C  
ANISOU 2954  CE2 PHE A2265    13923  15483  10091   -270    119  -2542       C  
ATOM   2955  CZ  PHE A2265      47.598 -67.679 289.639  1.00105.61           C  
ANISOU 2955  CZ  PHE A2265    14324  15877   9928   -221     56  -2893       C  
ATOM   2956  N   SER A2266      52.745 -62.448 290.341  1.00 85.70           N  
ANISOU 2956  N   SER A2266    10349  14399   7813    202   1327  -1128       N  
ATOM   2957  CA  SER A2266      53.571 -61.286 290.028  1.00 83.64           C  
ANISOU 2957  CA  SER A2266     9780  14431   7570    213   1565   -744       C  
ATOM   2958  C   SER A2266      54.998 -61.692 289.669  1.00 85.83           C  
ANISOU 2958  C   SER A2266     9890  14862   7859    485   1888   -861       C  
ATOM   2959  O   SER A2266      55.616 -61.101 288.784  1.00 94.14           O  
ANISOU 2959  O   SER A2266    10760  16315   8692    547   2171   -663       O  
ATOM   2960  CB  SER A2266      53.586 -60.307 291.204  1.00 86.83           C  
ANISOU 2960  CB  SER A2266     9979  14582   8430     58   1427   -394       C  
ATOM   2961  OG  SER A2266      54.364 -59.161 290.906  1.00 83.28           O  
ANISOU 2961  OG  SER A2266     9219  14369   8055     40   1626    -12       O  
ATOM   2962  N   LEU A2267      55.517 -62.701 290.360  1.00 87.37           N  
ANISOU 2962  N   LEU A2267    10136  14742   8318    652   1852  -1163       N  
ATOM   2963  CA  LEU A2267      56.846 -63.223 290.063  1.00 92.73           C  
ANISOU 2963  CA  LEU A2267    10656  15540   9039    945   2140  -1328       C  
ATOM   2964  C   LEU A2267      56.852 -63.982 288.740  1.00100.28           C  
ANISOU 2964  C   LEU A2267    11798  16826   9475   1140   2330  -1668       C  
ATOM   2965  O   LEU A2267      57.862 -64.013 288.036  1.00 82.22           O  
ANISOU 2965  O   LEU A2267     9333  14865   7043   1365   2670  -1696       O  
ATOM   2966  CB  LEU A2267      57.335 -64.133 291.192  1.00 90.38           C  
ANISOU 2966  CB  LEU A2267    10386  14783   9172   1088   2006  -1565       C  
ATOM   2967  CG  LEU A2267      57.821 -63.450 292.472  1.00 89.11           C  
ANISOU 2967  CG  LEU A2267     9976  14356   9528   1010   1890  -1270       C  
ATOM   2968  CD1 LEU A2267      58.109 -64.484 293.548  1.00 87.66           C  
ANISOU 2968  CD1 LEU A2267     9904  13716   9686   1158   1710  -1524       C  
ATOM   2969  CD2 LEU A2267      59.056 -62.611 292.190  1.00 70.94           C  
ANISOU 2969  CD2 LEU A2267     7253  12334   7369   1091   2175   -996       C  
ATOM   2970  N   LEU A2268      55.718 -64.592 288.409  1.00 95.73           N  
ANISOU 2970  N   LEU A2268    11574  16175   8625   1059   2104  -1935       N  
ATOM   2971  CA  LEU A2268      55.586 -65.343 287.166  1.00 98.03           C  
ANISOU 2971  CA  LEU A2268    12095  16755   8397   1239   2212  -2314       C  
ATOM   2972  C   LEU A2268      55.535 -64.412 285.961  1.00106.83           C  
ANISOU 2972  C   LEU A2268    13127  18450   9013   1208   2436  -2047       C  
ATOM   2973  O   LEU A2268      56.002 -64.758 284.876  1.00 90.63           O  
ANISOU 2973  O   LEU A2268    11125  16786   6525   1446   2696  -2251       O  
ATOM   2974  CB  LEU A2268      54.337 -66.225 287.204  1.00 91.05           C  
ANISOU 2974  CB  LEU A2268    11593  15586   7415   1126   1852  -2666       C  
ATOM   2975  CG  LEU A2268      54.419 -67.455 288.107  1.00 90.75           C  
ANISOU 2975  CG  LEU A2268    11711  15005   7767   1218   1666  -3020       C  
ATOM   2976  CD1 LEU A2268      53.114 -68.237 288.080  1.00 93.33           C  
ANISOU 2976  CD1 LEU A2268    12384  15060   8018   1054   1311  -3313       C  
ATOM   2977  CD2 LEU A2268      55.588 -68.338 287.698  1.00 88.70           C  
ANISOU 2977  CD2 LEU A2268    11437  14799   7468   1605   1913  -3384       C  
ATOM   2978  N   GLU A2269      54.964 -63.229 286.164  1.00 97.43           N  
ANISOU 2978  N   GLU A2269    11819  17317   7881    929   2335  -1586       N  
ATOM   2979  CA  GLU A2269      54.879 -62.217 285.118  1.00 92.94           C  
ANISOU 2979  CA  GLU A2269    11162  17261   6891    868   2521  -1238       C  
ATOM   2980  C   GLU A2269      56.269 -61.725 284.722  1.00 88.19           C  
ANISOU 2980  C   GLU A2269    10220  16996   6294   1043   2970   -991       C  
ATOM   2981  O   GLU A2269      56.518 -61.402 283.561  1.00117.22           O  
ANISOU 2981  O   GLU A2269    13882  21140   9516   1135   3232   -869       O  
ATOM   2982  CB  GLU A2269      54.013 -61.046 285.583  1.00 94.60           C  
ANISOU 2982  CB  GLU A2269    11298  17373   7275    541   2288   -786       C  
ATOM   2983  CG  GLU A2269      53.784 -59.973 284.533  1.00100.31           C  
ANISOU 2983  CG  GLU A2269    11959  18577   7579    456   2422   -387       C  
ATOM   2984  CD  GLU A2269      53.004 -58.792 285.077  1.00107.34           C  
ANISOU 2984  CD  GLU A2269    12751  19316   8719    159   2183     58       C  
ATOM   2985  OE1 GLU A2269      52.282 -58.143 284.292  1.00119.33           O  
ANISOU 2985  OE1 GLU A2269    14348  21118   9872     54   2119    284       O  
ATOM   2986  OE2 GLU A2269      53.114 -58.512 286.289  1.00 99.08           O  
ANISOU 2986  OE2 GLU A2269    11554  17868   8224     50   2049    172       O  
ATOM   2987  N   ALA A2270      57.172 -61.669 285.695  1.00 86.29           N  
ANISOU 2987  N   ALA A2270     9704  16477   6603   1081   3036   -901       N  
ATOM   2988  CA  ALA A2270      58.552 -61.283 285.435  1.00 96.37           C  
ANISOU 2988  CA  ALA A2270    10603  18025   7987   1243   3449   -685       C  
ATOM   2989  C   ALA A2270      59.293 -62.425 284.750  1.00106.38           C  
ANISOU 2989  C   ALA A2270    11942  19503   8976   1618   3724  -1146       C  
ATOM   2990  O   ALA A2270      60.191 -62.205 283.933  1.00104.68           O  
ANISOU 2990  O   ALA A2270    11552  19586   8634   1757   4072  -1007       O  
ATOM   2991  CB  ALA A2270      59.249 -60.890 286.727  1.00 86.98           C  
ANISOU 2991  CB  ALA A2270     9097  16453   7500   1168   3372   -479       C  
ATOM   2992  N   ARG A2271      58.898 -63.648 285.091  1.00108.34           N  
ANISOU 2992  N   ARG A2271    12497  19414   9253   1738   3487  -1668       N  
ATOM   2993  CA  ARG A2271      59.477 -64.851 284.507  1.00113.09           C  
ANISOU 2993  CA  ARG A2271    13226  20126   9618   2113   3676  -2188       C  
ATOM   2994  C   ARG A2271      58.963 -65.061 283.085  1.00119.43           C  
ANISOU 2994  C   ARG A2271    14349  21214   9817   2154   3706  -2329       C  
ATOM   2995  O   ARG A2271      59.589 -65.751 282.279  1.00117.89           O  
ANISOU 2995  O   ARG A2271    14237  21129   9428   2420   3907  -2602       O  
ATOM   2996  CB  ARG A2271      59.148 -66.069 285.376  1.00108.79           C  
ANISOU 2996  CB  ARG A2271    12940  19001   9394   2177   3336  -2655       C  
ATOM   2997  CG  ARG A2271      59.949 -67.323 285.062  1.00111.58           C  
ANISOU 2997  CG  ARG A2271    13365  19333   9696   2592   3504  -3185       C  
ATOM   2998  CD  ARG A2271      61.339 -67.262 285.674  1.00119.74           C  
ANISOU 2998  CD  ARG A2271    13987  20305  11206   2785   3747  -3062       C  
ATOM   2999  NE  ARG A2271      62.008 -68.559 285.631  1.00123.47           N  
ANISOU 2999  NE  ARG A2271    14545  20616  11750   3181   3817  -3595       N  
ATOM   3000  CZ  ARG A2271      62.805 -68.956 284.645  1.00130.78           C  
ANISOU 3000  CZ  ARG A2271    15454  21751  12486   3424   4105  -3726       C  
ATOM   3001  NH1 ARG A2271      63.040 -68.154 283.616  1.00137.66           N  
ANISOU 3001  NH1 ARG A2271    16206  23081  13016   3352   4396  -3402       N  
ATOM   3002  NH2 ARG A2271      63.370 -70.154 284.690  1.00137.12           N  
ANISOU 3002  NH2 ARG A2271    16363  22287  13447   3739   4100  -4172       N  
ATOM   3003  N   ALA A2272      57.823 -64.446 282.783  1.00121.61           N  
ANISOU 3003  N   ALA A2272    14800  21577   9830   1887   3484  -2129       N  
ATOM   3004  CA  ALA A2272      57.142 -64.648 281.509  1.00124.21           C  
ANISOU 3004  CA  ALA A2272    15467  22107   9622   1897   3408  -2268       C  
ATOM   3005  C   ALA A2272      57.783 -63.870 280.359  1.00131.46           C  
ANISOU 3005  C   ALA A2272    16249  23443  10255   1946   3754  -1902       C  
ATOM   3006  O   ALA A2272      57.291 -63.903 279.230  1.00114.15           O  
ANISOU 3006  O   ALA A2272    14313  21469   7589   1966   3722  -1961       O  
ATOM   3007  CB  ALA A2272      55.675 -64.270 281.640  1.00101.70           C  
ANISOU 3007  CB  ALA A2272    12828  19173   6642   1599   3013  -2181       C  
ATOM   3008  N   HIS A2273      58.876 -63.169 280.645  1.00123.43           N  
ANISOU 3008  N   HIS A2273    14827  22527   9545   1958   4070  -1522       N  
ATOM   3009  CA  HIS A2273      59.593 -62.435 279.608  1.00126.35           C  
ANISOU 3009  CA  HIS A2273    15036  23265   9705   1993   4424  -1159       C  
ATOM   3010  C   HIS A2273      60.500 -63.370 278.814  1.00126.63           C  
ANISOU 3010  C   HIS A2273    15127  23463   9523   2340   4725  -1530       C  
ATOM   3011  O   HIS A2273      60.759 -63.144 277.633  1.00128.44           O  
ANISOU 3011  O   HIS A2273    15414  24034   9353   2421   4958  -1424       O  
ATOM   3012  CB  HIS A2273      60.413 -61.296 280.216  1.00127.36           C  
ANISOU 3012  CB  HIS A2273    14691  23394  10307   1835   4620   -597       C  
ATOM   3013  CG  HIS A2273      61.109 -60.443 279.201  1.00134.54           C  
ANISOU 3013  CG  HIS A2273    15422  24644  11053   1822   4963   -175       C  
ATOM   3014  ND1 HIS A2273      62.343 -60.764 278.678  1.00141.04           N  
ANISOU 3014  ND1 HIS A2273    16056  25660  11872   2054   5363   -240       N  
ATOM   3015  CD2 HIS A2273      60.741 -59.281 278.610  1.00136.76           C  
ANISOU 3015  CD2 HIS A2273    15683  25099  11180   1605   4964    320       C  
ATOM   3016  CE1 HIS A2273      62.707 -59.837 277.810  1.00139.28           C  
ANISOU 3016  CE1 HIS A2273    15704  25731  11485   1968   5609    203       C  
ATOM   3017  NE2 HIS A2273      61.753 -58.926 277.750  1.00141.98           N  
ANISOU 3017  NE2 HIS A2273    16153  26055  11737   1701   5367    550       N  
ATOM   3018  N   ALA A2274      60.976 -64.422 279.472  1.00135.69           N  
ANISOU 3018  N   ALA A2274    16262  24356  10939   2555   4714  -1967       N  
ATOM   3019  CA  ALA A2274      61.850 -65.397 278.834  1.00127.37           C  
ANISOU 3019  CA  ALA A2274    15255  23396   9744   2908   4975  -2363       C  
ATOM   3020  C   ALA A2274      61.063 -66.625 278.386  1.00134.09           C  
ANISOU 3020  C   ALA A2274    16591  24104  10252   3059   4708  -2976       C  
ATOM   3021  O   ALA A2274      61.423 -67.284 277.410  1.00150.63           O  
ANISOU 3021  O   ALA A2274    18851  26375  12007   3309   4878  -3280       O  
ATOM   3022  CB  ALA A2274      62.970 -65.800 279.778  1.00126.37           C  
ANISOU 3022  CB  ALA A2274    14792  23052  10172   3080   5129  -2457       C  
ATOM   3023  N   ASN A2275      59.988 -66.926 279.106  1.00124.16           N  
ANISOU 3023  N   ASN A2275    15555  22515   9105   2896   4282  -3158       N  
ATOM   3024  CA  ASN A2275      59.128 -68.054 278.772  1.00134.97           C  
ANISOU 3024  CA  ASN A2275    17378  23673  10233   2974   3959  -3718       C  
ATOM   3025  C   ASN A2275      57.749 -67.590 278.317  1.00134.47           C  
ANISOU 3025  C   ASN A2275    17584  23687   9823   2703   3639  -3604       C  
ATOM   3026  O   ASN A2275      56.968 -67.073 279.116  1.00124.19           O  
ANISOU 3026  O   ASN A2275    16245  22215   8727   2429   3377  -3393       O  
ATOM   3027  CB  ASN A2275      59.000 -69.000 279.968  1.00136.47           C  
ANISOU 3027  CB  ASN A2275    17631  23339  10881   3019   3692  -4097       C  
ATOM   3028  CG  ASN A2275      60.316 -69.661 280.331  1.00143.56           C  
ANISOU 3028  CG  ASN A2275    18317  24113  12115   3337   3954  -4295       C  
ATOM   3029  OD1 ASN A2275      61.151 -69.924 279.465  1.00148.25           O  
ANISOU 3029  OD1 ASN A2275    18867  24954  12506   3588   4270  -4396       O  
ATOM   3030  ND2 ASN A2275      60.507 -69.933 281.616  1.00136.56           N  
ANISOU 3030  ND2 ASN A2275    17293  22844  11751   3336   3821  -4352       N  
ATOM   3031  N   PRO A2276      57.445 -67.775 277.023  1.00130.02           N  
ANISOU 3031  N   PRO A2276    17285  23384   8731   2788   3653  -3748       N  
ATOM   3032  CA  PRO A2276      56.192 -67.308 276.422  1.00129.84           C  
ANISOU 3032  CA  PRO A2276    17509  23478   8347   2562   3359  -3629       C  
ATOM   3033  C   PRO A2276      54.983 -68.154 276.814  1.00127.45           C  
ANISOU 3033  C   PRO A2276    17532  22775   8119   2439   2853  -4054       C  
ATOM   3034  O   PRO A2276      53.849 -67.690 276.695  1.00125.49           O  
ANISOU 3034  O   PRO A2276    17413  22531   7735   2191   2547  -3908       O  
ATOM   3035  CB  PRO A2276      56.468 -67.421 274.921  1.00148.08           C  
ANISOU 3035  CB  PRO A2276    19992  26186  10084   2764   3572  -3724       C  
ATOM   3036  CG  PRO A2276      57.440 -68.540 274.816  1.00149.95           C  
ANISOU 3036  CG  PRO A2276    20250  26339  10385   3105   3784  -4188       C  
ATOM   3037  CD  PRO A2276      58.316 -68.437 276.036  1.00143.01           C  
ANISOU 3037  CD  PRO A2276    19001  25247  10089   3125   3958  -4038       C  
ATOM   3038  N   GLY A2277      55.225 -69.376 277.278  1.00127.92           N  
ANISOU 3038  N   GLY A2277    17708  22470   8427   2604   2758  -4558       N  
ATOM   3039  CA  GLY A2277      54.149 -70.287 277.623  1.00137.22           C  
ANISOU 3039  CA  GLY A2277    19193  23216   9729   2484   2283  -4978       C  
ATOM   3040  C   GLY A2277      53.381 -69.899 278.873  1.00134.61           C  
ANISOU 3040  C   GLY A2277    18761  22583   9801   2174   1998  -4778       C  
ATOM   3041  O   GLY A2277      52.234 -70.305 279.054  1.00137.73           O  
ANISOU 3041  O   GLY A2277    19380  22701  10252   1973   1581  -4974       O  
ATOM   3042  N   LEU A2278      54.011 -69.112 279.739  1.00132.86           N  
ANISOU 3042  N   LEU A2278    18190  22416   9876   2127   2219  -4386       N  
ATOM   3043  CA  LEU A2278      53.394 -68.715 281.001  1.00135.59           C  
ANISOU 3043  CA  LEU A2278    18415  22498  10606   1854   1988  -4194       C  
ATOM   3044  C   LEU A2278      52.447 -67.530 280.830  1.00132.00           C  
ANISOU 3044  C   LEU A2278    17909  22271   9974   1546   1844  -3741       C  
ATOM   3045  O   LEU A2278      51.655 -67.225 281.723  1.00113.66           O  
ANISOU 3045  O   LEU A2278    15543  19743   7901   1283   1586  -3613       O  
ATOM   3046  CB  LEU A2278      54.471 -68.371 282.035  1.00130.28           C  
ANISOU 3046  CB  LEU A2278    17384  21776  10339   1939   2263  -3978       C  
ATOM   3047  CG  LEU A2278      55.496 -69.456 282.373  1.00125.65           C  
ANISOU 3047  CG  LEU A2278    16787  20930  10024   2259   2405  -4370       C  
ATOM   3048  CD1 LEU A2278      56.513 -68.932 283.376  1.00115.71           C  
ANISOU 3048  CD1 LEU A2278    15128  19664   9173   2323   2658  -4087       C  
ATOM   3049  CD2 LEU A2278      54.809 -70.705 282.904  1.00124.85           C  
ANISOU 3049  CD2 LEU A2278    16994  20285  10159   2238   2017  -4868       C  
ATOM   3050  N   ARG A2279      52.530 -66.872 279.678  1.00137.74           N  
ANISOU 3050  N   ARG A2279    18644  23409  10281   1584   2010  -3498       N  
ATOM   3051  CA  ARG A2279      51.774 -65.646 279.429  1.00130.30           C  
ANISOU 3051  CA  ARG A2279    17628  22691   9187   1330   1909  -3010       C  
ATOM   3052  C   ARG A2279      50.247 -65.815 279.445  1.00133.09           C  
ANISOU 3052  C   ARG A2279    18218  22856   9496   1087   1423  -3142       C  
ATOM   3053  O   ARG A2279      49.557 -65.007 280.069  1.00129.62           O  
ANISOU 3053  O   ARG A2279    17643  22366   9239    825   1253  -2804       O  
ATOM   3054  CB  ARG A2279      52.221 -65.022 278.103  1.00122.56           C  
ANISOU 3054  CB  ARG A2279    16645  22162   7758   1454   2186  -2758       C  
ATOM   3055  CG  ARG A2279      53.637 -64.476 278.159  1.00121.44           C  
ANISOU 3055  CG  ARG A2279    16174  22235   7734   1600   2669  -2443       C  
ATOM   3056  CD  ARG A2279      54.123 -63.978 276.812  1.00125.86           C  
ANISOU 3056  CD  ARG A2279    16746  23229   7847   1729   2962  -2227       C  
ATOM   3057  NE  ARG A2279      55.482 -63.452 276.908  1.00123.56           N  
ANISOU 3057  NE  ARG A2279    16101  23113   7734   1838   3419  -1907       N  
ATOM   3058  CZ  ARG A2279      56.215 -63.070 275.869  1.00131.77           C  
ANISOU 3058  CZ  ARG A2279    17078  24521   8469   1975   3770  -1707       C  
ATOM   3059  NH1 ARG A2279      55.726 -63.157 274.640  1.00142.56           N  
ANISOU 3059  NH1 ARG A2279    18734  26141   9293   2040   3719  -1803       N  
ATOM   3060  NH2 ARG A2279      57.442 -62.605 276.058  1.00127.51           N  
ANISOU 3060  NH2 ARG A2279    16178  24096   8172   2042   4166  -1411       N  
ATOM   3061  N   PRO A2280      49.704 -66.849 278.769  1.00137.86           N  
ANISOU 3061  N   PRO A2280    19154  23341   9886   1163   1187  -3625       N  
ATOM   3062  CA  PRO A2280      48.244 -66.979 278.874  1.00132.63           C  
ANISOU 3062  CA  PRO A2280    18660  22471   9263    902    710  -3719       C  
ATOM   3063  C   PRO A2280      47.780 -67.334 280.288  1.00115.73           C  
ANISOU 3063  C   PRO A2280    16439  19892   7639    699    478  -3810       C  
ATOM   3064  O   PRO A2280      46.656 -67.004 280.666  1.00108.60           O  
ANISOU 3064  O   PRO A2280    15526  18867   6870    423    158  -3679       O  
ATOM   3065  CB  PRO A2280      47.919 -68.111 277.890  1.00133.84           C  
ANISOU 3065  CB  PRO A2280    19170  22552   9130   1039    523  -4248       C  
ATOM   3066  CG  PRO A2280      49.185 -68.873 277.750  1.00137.31           C  
ANISOU 3066  CG  PRO A2280    19626  22985   9558   1357    852  -4540       C  
ATOM   3067  CD  PRO A2280      50.273 -67.850 277.848  1.00141.07           C  
ANISOU 3067  CD  PRO A2280    19786  23800  10014   1457   1309  -4071       C  
ATOM   3068  N   LEU A2281      48.643 -67.989 281.057  1.00110.16           N  
ANISOU 3068  N   LEU A2281    15670  18956   7231    841    642  -4023       N  
ATOM   3069  CA  LEU A2281      48.314 -68.373 282.425  1.00113.30           C  
ANISOU 3069  CA  LEU A2281    16005  18926   8117    670    451  -4117       C  
ATOM   3070  C   LEU A2281      48.234 -67.155 283.341  1.00109.75           C  
ANISOU 3070  C   LEU A2281    15251  18572   7877    454    520  -3594       C  
ATOM   3071  O   LEU A2281      47.410 -67.104 284.256  1.00100.91           O  
ANISOU 3071  O   LEU A2281    14095  17077   7168    184    258  -3460       O  
ATOM   3072  CB  LEU A2281      49.346 -69.368 282.960  1.00121.72           C  
ANISOU 3072  CB  LEU A2281    17089  19710   9449    920    617  -4465       C  
ATOM   3073  CG  LEU A2281      49.164 -69.839 284.404  1.00126.06           C  
ANISOU 3073  CG  LEU A2281    17591  19703  10605    768    444  -4495       C  
ATOM   3074  CD1 LEU A2281      47.788 -70.457 284.600  1.00133.72           C  
ANISOU 3074  CD1 LEU A2281    18766  20316  11727    492     -9  -4707       C  
ATOM   3075  CD2 LEU A2281      50.258 -70.825 284.785  1.00124.36           C  
ANISOU 3075  CD2 LEU A2281    17407  19197  10648   1063    607  -4812       C  
ATOM   3076  N   VAL A2282      49.095 -66.176 283.085  1.00107.94           N  
ANISOU 3076  N   VAL A2282    14796  18721   7496    559    873  -3207       N  
ATOM   3077  CA  VAL A2282      49.134 -64.953 283.878  1.00 93.86           C  
ANISOU 3077  CA  VAL A2282    12718  16898   6045    360    939  -2619       C  
ATOM   3078  C   VAL A2282      47.879 -64.110 283.657  1.00 94.67           C  
ANISOU 3078  C   VAL A2282    12829  17133   6010     88    671  -2335       C  
ATOM   3079  O   VAL A2282      47.321 -63.549 284.603  1.00 92.90           O  
ANISOU 3079  O   VAL A2282    12468  16639   6189   -144    512  -2041       O  
ATOM   3080  CB  VAL A2282      50.391 -64.117 283.546  1.00 90.62           C  
ANISOU 3080  CB  VAL A2282    12051  16864   5518    530   1378  -2274       C  
ATOM   3081  CG1 VAL A2282      50.317 -62.741 284.191  1.00 88.12           C  
ANISOU 3081  CG1 VAL A2282    11451  16530   5501    307   1396  -1667       C  
ATOM   3082  CG2 VAL A2282      51.647 -64.851 283.991  1.00 88.00           C  
ANISOU 3082  CG2 VAL A2282    11633  16352   5451    784   1629  -2498       C  
ATOM   3083  N   TRP A2283      47.426 -64.045 282.408  1.00102.68           N  
ANISOU 3083  N   TRP A2283    14010  18447   6558    137    601  -2394       N  
ATOM   3084  CA  TRP A2283      46.265 -63.235 282.043  1.00103.38           C  
ANISOU 3084  CA  TRP A2283    14105  18628   6548    -76    338  -2104       C  
ATOM   3085  C   TRP A2283      44.970 -63.736 282.683  1.00 99.84           C  
ANISOU 3085  C   TRP A2283    13744  17844   6345   -321    -88  -2308       C  
ATOM   3086  O   TRP A2283      43.965 -63.027 282.698  1.00 92.30           O  
ANISOU 3086  O   TRP A2283    12726  16905   5439   -521   -319  -2042       O  
ATOM   3087  CB  TRP A2283      46.109 -63.198 280.520  1.00118.39           C  
ANISOU 3087  CB  TRP A2283    16200  20817   7967     65    339  -2145       C  
ATOM   3088  CG  TRP A2283      47.274 -62.573 279.808  1.00124.49           C  
ANISOU 3088  CG  TRP A2283    16866  21939   8497    267    761  -1869       C  
ATOM   3089  CD1 TRP A2283      48.238 -61.776 280.353  1.00123.90           C  
ANISOU 3089  CD1 TRP A2283    16496  21951   8631    278   1084  -1479       C  
ATOM   3090  CD2 TRP A2283      47.601 -62.704 278.419  1.00129.52           C  
ANISOU 3090  CD2 TRP A2283    17681  22876   8656    474    904  -1952       C  
ATOM   3091  NE1 TRP A2283      49.142 -61.398 279.389  1.00131.73           N  
ANISOU 3091  NE1 TRP A2283    17448  23265   9339    466   1426  -1299       N  
ATOM   3092  CE2 TRP A2283      48.773 -61.956 278.193  1.00128.88           C  
ANISOU 3092  CE2 TRP A2283    17383  23055   8532    594   1334  -1584       C  
ATOM   3093  CE3 TRP A2283      47.015 -63.380 277.344  1.00130.35           C  
ANISOU 3093  CE3 TRP A2283    18107  23050   8370    562    704  -2301       C  
ATOM   3094  CZ2 TRP A2283      49.370 -61.864 276.938  1.00120.54           C  
ANISOU 3094  CZ2 TRP A2283    16418  22338   7045    796   1591  -1544       C  
ATOM   3095  CZ3 TRP A2283      47.608 -63.288 276.100  1.00127.23           C  
ANISOU 3095  CZ3 TRP A2283    17823  23003   7516    776    950  -2279       C  
ATOM   3096  CH2 TRP A2283      48.773 -62.537 275.907  1.00128.16           C  
ANISOU 3096  CH2 TRP A2283    17718  23390   7588    891   1400  -1899       C  
ATOM   3097  N   ARG A2284      44.999 -64.956 283.211  1.00112.91           N  
ANISOU 3097  N   ARG A2284    15530  19175   8196   -303   -190  -2766       N  
ATOM   3098  CA  ARG A2284      43.824 -65.547 283.841  1.00115.10           C  
ANISOU 3098  CA  ARG A2284    15879  19085   8770   -552   -576  -2963       C  
ATOM   3099  C   ARG A2284      43.794 -65.296 285.346  1.00110.36           C  
ANISOU 3099  C   ARG A2284    15078  18054   8800   -716   -560  -2674       C  
ATOM   3100  O   ARG A2284      42.787 -64.840 285.888  1.00115.15           O  
ANISOU 3100  O   ARG A2284    15582  18530   9640   -960   -776  -2451       O  
ATOM   3101  CB  ARG A2284      43.779 -67.052 283.571  1.00118.27           C  
ANISOU 3101  CB  ARG A2284    16550  19193   9193   -452   -729  -3550       C  
ATOM   3102  CG  ARG A2284      43.789 -67.415 282.102  1.00127.16           C  
ANISOU 3102  CG  ARG A2284    17916  20524   9875   -254   -757  -3778       C  
ATOM   3103  CD  ARG A2284      43.985 -68.907 281.905  1.00139.43           C  
ANISOU 3103  CD  ARG A2284    19734  21751  11490   -120   -859  -4351       C  
ATOM   3104  NE  ARG A2284      44.004 -69.264 280.490  1.00155.42           N  
ANISOU 3104  NE  ARG A2284    22006  23982  13065     63   -886  -4585       N  
ATOM   3105  CZ  ARG A2284      44.221 -70.492 280.031  1.00160.63           C  
ANISOU 3105  CZ  ARG A2284    22922  24424  13685    211   -957  -5081       C  
ATOM   3106  NH1 ARG A2284      44.442 -71.490 280.877  1.00161.30           N  
ANISOU 3106  NH1 ARG A2284    23050  24047  14189    207  -1014  -5377       N  
ATOM   3107  NH2 ARG A2284      44.218 -70.723 278.726  1.00162.49           N  
ANISOU 3107  NH2 ARG A2284    23376  24893  13472    365   -974  -5274       N  
ATOM   3108  N   GLY A2285      44.904 -65.593 286.013  1.00 99.31           N  
ANISOU 3108  N   GLY A2285    13621  16452   7661   -561   -306  -2686       N  
ATOM   3109  CA  GLY A2285      44.958 -65.547 287.462  1.00 89.42           C  
ANISOU 3109  CA  GLY A2285    12230  14773   6973   -674   -306  -2485       C  
ATOM   3110  C   GLY A2285      45.196 -64.177 288.066  1.00 91.88           C  
ANISOU 3110  C   GLY A2285    12272  15186   7454   -739   -168  -1956       C  
ATOM   3111  O   GLY A2285      44.618 -63.844 289.100  1.00101.91           O  
ANISOU 3111  O   GLY A2285    13438  16196   9088   -915   -291  -1742       O  
ATOM   3112  N   LEU A2286      46.048 -63.382 287.426  1.00 88.94           N  
ANISOU 3112  N   LEU A2286    11784  15186   6825   -595     91  -1745       N  
ATOM   3113  CA  LEU A2286      46.442 -62.082 287.972  1.00 84.91           C  
ANISOU 3113  CA  LEU A2286    11008  14737   6516   -644    227  -1254       C  
ATOM   3114  C   LEU A2286      45.281 -61.105 288.235  1.00 87.56           C  
ANISOU 3114  C   LEU A2286    11249  15084   6935   -879      3   -931       C  
ATOM   3115  O   LEU A2286      45.287 -60.420 289.259  1.00 90.01           O  
ANISOU 3115  O   LEU A2286    11390  15191   7618   -960     -7   -651       O  
ATOM   3116  CB  LEU A2286      47.472 -61.416 287.052  1.00 83.37           C  
ANISOU 3116  CB  LEU A2286    10701  14971   6004   -474    539  -1067       C  
ATOM   3117  CG  LEU A2286      48.137 -60.165 287.631  1.00 79.69           C  
ANISOU 3117  CG  LEU A2286     9942  14516   5821   -507    702   -584       C  
ATOM   3118  CD1 LEU A2286      48.770 -60.475 288.979  1.00 83.21           C  
ANISOU 3118  CD1 LEU A2286    10286  14542   6787   -474    728   -619       C  
ATOM   3119  CD2 LEU A2286      49.171 -59.602 286.670  1.00 70.53           C  
ANISOU 3119  CD2 LEU A2286     8655  13780   4365   -356   1035   -386       C  
ATOM   3120  N   PRO A2287      44.288 -61.022 287.325  1.00 93.94           N  
ANISOU 3120  N   PRO A2287    12162  16131   7400   -969   -192   -979       N  
ATOM   3121  CA  PRO A2287      43.183 -60.108 287.647  1.00 91.23           C  
ANISOU 3121  CA  PRO A2287    11701  15775   7189  -1172   -412   -676       C  
ATOM   3122  C   PRO A2287      42.369 -60.529 288.875  1.00 93.59           C  
ANISOU 3122  C   PRO A2287    11979  15650   7932  -1334   -609   -745       C  
ATOM   3123  O   PRO A2287      41.753 -59.679 289.522  1.00 75.73           O  
ANISOU 3123  O   PRO A2287     9560  13312   5902  -1455   -707   -454       O  
ATOM   3124  CB  PRO A2287      42.312 -60.157 286.387  1.00 81.56           C  
ANISOU 3124  CB  PRO A2287    10611  14881   5496  -1213   -610   -785       C  
ATOM   3125  CG  PRO A2287      43.236 -60.572 285.305  1.00101.31           C  
ANISOU 3125  CG  PRO A2287    13252  17696   7547   -997   -395   -977       C  
ATOM   3126  CD  PRO A2287      44.180 -61.535 285.947  1.00100.26           C  
ANISOU 3126  CD  PRO A2287    13162  17271   7663   -870   -216  -1256       C  
ATOM   3127  N   PHE A2288      42.368 -61.821 289.188  1.00 96.71           N  
ANISOU 3127  N   PHE A2288    12529  15774   8443  -1325   -659  -1117       N  
ATOM   3128  CA  PHE A2288      41.610 -62.334 290.325  1.00 92.04           C  
ANISOU 3128  CA  PHE A2288    11928  14787   8256  -1482   -820  -1167       C  
ATOM   3129  C   PHE A2288      42.345 -62.108 291.641  1.00 80.53           C  
ANISOU 3129  C   PHE A2288    10360  13054   7182  -1422   -658   -986       C  
ATOM   3130  O   PHE A2288      41.788 -61.534 292.578  1.00 73.34           O  
ANISOU 3130  O   PHE A2288     9320  12004   6540  -1530   -725   -752       O  
ATOM   3131  CB  PHE A2288      41.314 -63.825 290.142  1.00102.40           C  
ANISOU 3131  CB  PHE A2288    13456  15877   9574  -1511   -955  -1612       C  
ATOM   3132  CG  PHE A2288      40.644 -64.461 291.327  1.00120.40           C  
ANISOU 3132  CG  PHE A2288    15729  17731  12285  -1674  -1079  -1636       C  
ATOM   3133  CD1 PHE A2288      39.293 -64.261 291.568  1.00125.74           C  
ANISOU 3133  CD1 PHE A2288    16312  18370  13094  -1906  -1301  -1530       C  
ATOM   3134  CD2 PHE A2288      41.363 -65.267 292.196  1.00124.16           C  
ANISOU 3134  CD2 PHE A2288    16283  17856  13035  -1587   -966  -1746       C  
ATOM   3135  CE1 PHE A2288      38.675 -64.847 292.657  1.00121.21           C  
ANISOU 3135  CE1 PHE A2288    15715  17433  12908  -2059  -1376  -1516       C  
ATOM   3136  CE2 PHE A2288      40.750 -65.855 293.284  1.00119.65           C  
ANISOU 3136  CE2 PHE A2288    15717  16908  12836  -1735  -1062  -1723       C  
ATOM   3137  CZ  PHE A2288      39.405 -65.645 293.514  1.00118.00           C  
ANISOU 3137  CZ  PHE A2288    15408  16682  12745  -1977  -1251  -1601       C  
ATOM   3138  N   VAL A2289      43.594 -62.561 291.707  1.00 78.92           N  
ANISOU 3138  N   VAL A2289    10205  12787   6994  -1231   -454  -1110       N  
ATOM   3139  CA  VAL A2289      44.381 -62.466 292.933  1.00 66.92           C  
ANISOU 3139  CA  VAL A2289     8597  11001   5830  -1150   -332   -981       C  
ATOM   3140  C   VAL A2289      44.706 -61.018 293.295  1.00 69.82           C  
ANISOU 3140  C   VAL A2289     8736  11497   6293  -1144   -251   -584       C  
ATOM   3141  O   VAL A2289      45.046 -60.722 294.439  1.00 78.39           O  
ANISOU 3141  O   VAL A2289     9732  12361   7691  -1118   -228   -441       O  
ATOM   3142  CB  VAL A2289      45.695 -63.266 292.825  1.00 64.84           C  
ANISOU 3142  CB  VAL A2289     8408  10662   5565   -924   -145  -1212       C  
ATOM   3143  CG1 VAL A2289      45.400 -64.739 292.585  1.00 60.86           C  
ANISOU 3143  CG1 VAL A2289     8144   9948   5032   -916   -251  -1625       C  
ATOM   3144  CG2 VAL A2289      46.579 -62.703 291.722  1.00 60.49           C  
ANISOU 3144  CG2 VAL A2289     7777  10505   4701   -775     66  -1157       C  
ATOM   3145  N   THR A2290      44.604 -60.119 292.319  1.00 70.41           N  
ANISOU 3145  N   THR A2290     8730  11921   6101  -1161   -224   -406       N  
ATOM   3146  CA  THR A2290      44.761 -58.694 292.584  1.00 69.22           C  
ANISOU 3146  CA  THR A2290     8368  11865   6067  -1184   -190    -14       C  
ATOM   3147  C   THR A2290      43.549 -58.185 293.348  1.00 72.76           C  
ANISOU 3147  C   THR A2290     8759  12172   6713  -1340   -401    134       C  
ATOM   3148  O   THR A2290      43.682 -57.451 294.329  1.00 76.03           O  
ANISOU 3148  O   THR A2290     9044  12428   7415  -1334   -409    337       O  
ATOM   3149  CB  THR A2290      44.931 -57.880 291.288  1.00 68.78           C  
ANISOU 3149  CB  THR A2290     8252  12215   5666  -1166   -107    178       C  
ATOM   3150  OG1 THR A2290      46.110 -58.313 290.600  1.00 73.62           O  
ANISOU 3150  OG1 THR A2290     8890  12996   6085   -999    137     58       O  
ATOM   3151  CG2 THR A2290      45.054 -56.396 291.601  1.00 51.98           C  
ANISOU 3151  CG2 THR A2290     5906  10121   3724  -1207   -100    602       C  
ATOM   3152  N   SER A2291      42.366 -58.589 292.893  1.00 63.26           N  
ANISOU 3152  N   SER A2291     7645  11031   5359  -1468   -580     13       N  
ATOM   3153  CA  SER A2291      41.121 -58.236 293.565  1.00 74.06           C  
ANISOU 3153  CA  SER A2291     8938  12287   6915  -1613   -769    125       C  
ATOM   3154  C   SER A2291      41.017 -58.935 294.919  1.00 79.18           C  
ANISOU 3154  C   SER A2291     9623  12577   7887  -1629   -772     26       C  
ATOM   3155  O   SER A2291      40.293 -58.482 295.804  1.00 69.24           O  
ANISOU 3155  O   SER A2291     8266  11203   6839  -1694   -851    171       O  
ATOM   3156  CB  SER A2291      39.918 -58.591 292.689  1.00 75.30           C  
ANISOU 3156  CB  SER A2291     9156  12606   6849  -1750   -972      1       C  
ATOM   3157  OG  SER A2291      39.898 -57.810 291.505  1.00 89.59           O  
ANISOU 3157  OG  SER A2291    10935  14767   8340  -1728   -996    148       O  
ATOM   3158  N   LEU A2292      41.742 -60.040 295.072  1.00 80.46           N  
ANISOU 3158  N   LEU A2292     9927  12569   8072  -1552   -680   -216       N  
ATOM   3159  CA  LEU A2292      41.795 -60.755 296.341  1.00 85.53           C  
ANISOU 3159  CA  LEU A2292    10629  12866   9001  -1545   -669   -282       C  
ATOM   3160  C   LEU A2292      42.533 -59.928 297.390  1.00 85.32           C  
ANISOU 3160  C   LEU A2292    10487  12740   9190  -1425   -582    -66       C  
ATOM   3161  O   LEU A2292      42.100 -59.834 298.539  1.00 79.90           O  
ANISOU 3161  O   LEU A2292     9776  11869   8713  -1448   -625     27       O  
ATOM   3162  CB  LEU A2292      42.468 -62.118 296.169  1.00 89.00           C  
ANISOU 3162  CB  LEU A2292    11257  13136   9422  -1466   -610   -589       C  
ATOM   3163  CG  LEU A2292      42.679 -62.942 297.444  1.00 87.54           C  
ANISOU 3163  CG  LEU A2292    11160  12576   9524  -1432   -594   -637       C  
ATOM   3164  CD1 LEU A2292      41.350 -63.295 298.095  1.00 77.36           C  
ANISOU 3164  CD1 LEU A2292     9882  11127   8385  -1631   -725   -591       C  
ATOM   3165  CD2 LEU A2292      43.485 -64.198 297.151  1.00 91.95           C  
ANISOU 3165  CD2 LEU A2292    11899  12967  10070  -1315   -539   -936       C  
ATOM   3166  N   ALA A2293      43.647 -59.326 296.986  1.00 77.92           N  
ANISOU 3166  N   ALA A2293     9473  11934   8200  -1295   -461     13       N  
ATOM   3167  CA  ALA A2293      44.399 -58.446 297.870  1.00 68.90           C  
ANISOU 3167  CA  ALA A2293     8198  10701   7281  -1190   -416    208       C  
ATOM   3168  C   ALA A2293      43.600 -57.178 298.151  1.00 70.81           C  
ANISOU 3168  C   ALA A2293     8297  11014   7595  -1266   -525    460       C  
ATOM   3169  O   ALA A2293      43.733 -56.565 299.210  1.00 76.28           O  
ANISOU 3169  O   ALA A2293     8918  11558   8508  -1207   -563    577       O  
ATOM   3170  CB  ALA A2293      45.749 -58.105 297.264  1.00 61.40           C  
ANISOU 3170  CB  ALA A2293     7158   9883   6288  -1062   -262    246       C  
ATOM   3171  N   PHE A2294      42.771 -56.789 297.187  1.00 74.05           N  
ANISOU 3171  N   PHE A2294     8673  11650   7810  -1377   -594    527       N  
ATOM   3172  CA  PHE A2294      41.878 -55.648 297.351  1.00 82.94           C  
ANISOU 3172  CA  PHE A2294     9666  12844   9004  -1440   -719    751       C  
ATOM   3173  C   PHE A2294      40.875 -55.902 298.470  1.00 80.63           C  
ANISOU 3173  C   PHE A2294     9384  12371   8881  -1488   -810    718       C  
ATOM   3174  O   PHE A2294      40.562 -55.004 299.251  1.00 85.19           O  
ANISOU 3174  O   PHE A2294     9855  12885   9628  -1449   -867    870       O  
ATOM   3175  CB  PHE A2294      41.136 -55.352 296.044  1.00 84.75           C  
ANISOU 3175  CB  PHE A2294     9875  13357   8970  -1541   -799    811       C  
ATOM   3176  CG  PHE A2294      41.836 -54.364 295.155  1.00 90.61           C  
ANISOU 3176  CG  PHE A2294    10524  14309   9595  -1495   -735   1030       C  
ATOM   3177  CD1 PHE A2294      41.749 -54.472 293.775  1.00 98.88           C  
ANISOU 3177  CD1 PHE A2294    11624  15649  10298  -1528   -723   1028       C  
ATOM   3178  CD2 PHE A2294      42.565 -53.321 295.697  1.00 87.40           C  
ANISOU 3178  CD2 PHE A2294     9979  13807   9422  -1420   -696   1249       C  
ATOM   3179  CE1 PHE A2294      42.387 -53.563 292.953  1.00 92.60           C  
ANISOU 3179  CE1 PHE A2294    10742  15064   9377  -1489   -637   1280       C  
ATOM   3180  CE2 PHE A2294      43.203 -52.408 294.880  1.00 97.15           C  
ANISOU 3180  CE2 PHE A2294    11109  15213  10589  -1404   -629   1495       C  
ATOM   3181  CZ  PHE A2294      43.114 -52.529 293.506  1.00 92.70           C  
ANISOU 3181  CZ  PHE A2294    10598  14960   9666  -1439   -582   1531       C  
ATOM   3182  N   PHE A2295      40.385 -57.135 298.547  1.00 68.12           N  
ANISOU 3182  N   PHE A2295     7926  10700   7256  -1569   -816    520       N  
ATOM   3183  CA  PHE A2295      39.345 -57.493 299.504  1.00 77.16           C  
ANISOU 3183  CA  PHE A2295     9068  11705   8546  -1644   -873    514       C  
ATOM   3184  C   PHE A2295      39.909 -57.746 300.900  1.00 81.72           C  
ANISOU 3184  C   PHE A2295     9707  12035   9310  -1524   -795    515       C  
ATOM   3185  O   PHE A2295      39.162 -58.023 301.839  1.00 75.03           O  
ANISOU 3185  O   PHE A2295     8863  11075   8570  -1558   -801    543       O  
ATOM   3186  CB  PHE A2295      38.577 -58.727 299.020  1.00 83.40           C  
ANISOU 3186  CB  PHE A2295     9956  12472   9260  -1806   -927    325       C  
ATOM   3187  CG  PHE A2295      37.744 -58.483 297.788  1.00 96.08           C  
ANISOU 3187  CG  PHE A2295    11497  14327  10684  -1931  -1061    316       C  
ATOM   3188  CD1 PHE A2295      37.431 -57.193 297.386  1.00102.86           C  
ANISOU 3188  CD1 PHE A2295    12200  15393  11490  -1909  -1130    522       C  
ATOM   3189  CD2 PHE A2295      37.268 -59.546 297.035  1.00 95.25           C  
ANISOU 3189  CD2 PHE A2295    11492  14231  10469  -2064  -1148     97       C  
ATOM   3190  CE1 PHE A2295      36.663 -56.968 296.255  1.00101.25           C  
ANISOU 3190  CE1 PHE A2295    11945  15426  11100  -2008  -1278    531       C  
ATOM   3191  CE2 PHE A2295      36.499 -59.327 295.903  1.00 96.53           C  
ANISOU 3191  CE2 PHE A2295    11602  14633  10440  -2167  -1309     72       C  
ATOM   3192  CZ  PHE A2295      36.196 -58.036 295.513  1.00 96.63           C  
ANISOU 3192  CZ  PHE A2295    11462  14877  10377  -2134  -1372    300       C  
ATOM   3193  N   ASN A2296      41.229 -57.653 301.031  1.00 80.64           N  
ANISOU 3193  N   ASN A2296     9607  11829   9204  -1379   -720    495       N  
ATOM   3194  CA  ASN A2296      41.880 -57.795 302.327  1.00 84.61           C  
ANISOU 3194  CA  ASN A2296    10167  12113   9868  -1237   -683    498       C  
ATOM   3195  C   ASN A2296      41.536 -56.623 303.240  1.00 90.68           C  
ANISOU 3195  C   ASN A2296    10822  12877  10755  -1162   -746    661       C  
ATOM   3196  O   ASN A2296      41.520 -56.757 304.464  1.00 91.39           O  
ANISOU 3196  O   ASN A2296    10972  12818  10935  -1068   -743    668       O  
ATOM   3197  CB  ASN A2296      43.398 -57.908 302.153  1.00 85.14           C  
ANISOU 3197  CB  ASN A2296    10257  12128   9965  -1097   -614    434       C  
ATOM   3198  CG  ASN A2296      44.134 -58.054 303.475  1.00 74.24           C  
ANISOU 3198  CG  ASN A2296     8934  10525   8749   -934   -618    428       C  
ATOM   3199  OD1 ASN A2296      44.611 -57.071 304.046  1.00 66.03           O  
ANISOU 3199  OD1 ASN A2296     7795   9466   7827   -827   -671    528       O  
ATOM   3200  ND2 ASN A2296      44.238 -59.286 303.962  1.00 66.35           N  
ANISOU 3200  ND2 ASN A2296     8103   9342   7764   -910   -585    308       N  
ATOM   3201  N   SER A2297      41.252 -55.475 302.631  1.00 90.71           N  
ANISOU 3201  N   SER A2297    10676  13044  10747  -1188   -809    788       N  
ATOM   3202  CA  SER A2297      40.907 -54.264 303.369  1.00 88.16           C  
ANISOU 3202  CA  SER A2297    10238  12706  10551  -1102   -893    920       C  
ATOM   3203  C   SER A2297      39.473 -54.310 303.890  1.00 84.73           C  
ANISOU 3203  C   SER A2297     9773  12308  10114  -1158   -918    948       C  
ATOM   3204  O   SER A2297      39.084 -53.507 304.738  1.00 79.23           O  
ANISOU 3204  O   SER A2297     9010  11583   9512  -1050   -966   1013       O  
ATOM   3205  CB  SER A2297      41.098 -53.029 302.484  1.00 79.19           C  
ANISOU 3205  CB  SER A2297     8951  11700   9436  -1113   -962   1070       C  
ATOM   3206  OG  SER A2297      42.440 -52.918 302.043  1.00 83.07           O  
ANISOU 3206  OG  SER A2297     9430  12174   9958  -1065   -911   1081       O  
ATOM   3207  N   VAL A2298      38.691 -55.252 303.374  1.00 74.33           N  
ANISOU 3207  N   VAL A2298     8490  11053   8698  -1320   -889    886       N  
ATOM   3208  CA  VAL A2298      37.302 -55.410 303.785  1.00 72.21           C  
ANISOU 3208  CA  VAL A2298     8150  10833   8455  -1406   -898    924       C  
ATOM   3209  C   VAL A2298      37.186 -56.519 304.829  1.00 70.99           C  
ANISOU 3209  C   VAL A2298     8126  10515   8335  -1409   -792    869       C  
ATOM   3210  O   VAL A2298      36.245 -56.551 305.624  1.00 67.57           O  
ANISOU 3210  O   VAL A2298     7632  10092   7949  -1417   -749    937       O  
ATOM   3211  CB  VAL A2298      36.395 -55.729 302.576  1.00 81.92           C  
ANISOU 3211  CB  VAL A2298     9305  12227   9594  -1608   -969    905       C  
ATOM   3212  CG1 VAL A2298      34.924 -55.639 302.960  1.00 78.24           C  
ANISOU 3212  CG1 VAL A2298     8685  11839   9205  -1690   -996    974       C  
ATOM   3213  CG2 VAL A2298      36.700 -54.781 301.427  1.00 77.18           C  
ANISOU 3213  CG2 VAL A2298     8624  11793   8906  -1598  -1063    977       C  
ATOM   3214  N   ALA A2299      38.163 -57.419 304.828  1.00 72.72           N  
ANISOU 3214  N   ALA A2299     8515  10584   8530  -1389   -741    764       N  
ATOM   3215  CA  ALA A2299      38.159 -58.558 305.737  1.00 73.63           C  
ANISOU 3215  CA  ALA A2299     8782  10512   8683  -1393   -654    734       C  
ATOM   3216  C   ALA A2299      38.612 -58.171 307.143  1.00 77.49           C  
ANISOU 3216  C   ALA A2299     9333  10906   9206  -1177   -616    801       C  
ATOM   3217  O   ALA A2299      38.007 -58.588 308.131  1.00 74.15           O  
ANISOU 3217  O   ALA A2299     8955  10431   8789  -1167   -537    875       O  
ATOM   3218  CB  ALA A2299      39.041 -59.670 305.188  1.00 71.79           C  
ANISOU 3218  CB  ALA A2299     8712  10136   8427  -1425   -636    583       C  
ATOM   3219  N   ASN A2300      39.672 -57.371 307.223  1.00 78.29           N  
ANISOU 3219  N   ASN A2300     9429  10991   9325  -1006   -676    779       N  
ATOM   3220  CA  ASN A2300      40.282 -57.006 308.504  1.00 78.10           C  
ANISOU 3220  CA  ASN A2300     9483  10864   9327   -781   -692    797       C  
ATOM   3221  C   ASN A2300      39.345 -56.366 309.544  1.00 86.06           C  
ANISOU 3221  C   ASN A2300    10442  11945  10310   -686   -674    885       C  
ATOM   3222  O   ASN A2300      39.354 -56.785 310.702  1.00 72.38           O  
ANISOU 3222  O   ASN A2300     8841  10137   8524   -567   -617    911       O  
ATOM   3223  CB  ASN A2300      41.478 -56.076 308.267  1.00 65.94           C  
ANISOU 3223  CB  ASN A2300     7885   9305   7863   -648   -798    760       C  
ATOM   3224  CG  ASN A2300      42.643 -56.783 307.604  1.00 71.36           C  
ANISOU 3224  CG  ASN A2300     8633   9907   8572   -660   -779    668       C  
ATOM   3225  OD1 ASN A2300      42.761 -58.007 307.670  1.00 67.65           O  
ANISOU 3225  OD1 ASN A2300     8306   9331   8069   -697   -711    606       O  
ATOM   3226  ND2 ASN A2300      43.516 -56.012 306.965  1.00 72.95           N  
ANISOU 3226  ND2 ASN A2300     8718  10151   8848   -624   -834    668       N  
ATOM   3227  N   PRO A2301      38.544 -55.351 309.155  1.00 87.83           N  
ANISOU 3227  N   PRO A2301    10482  12326  10561   -715   -720    934       N  
ATOM   3228  CA  PRO A2301      37.687 -54.744 310.184  1.00 79.04           C  
ANISOU 3228  CA  PRO A2301     9318  11291   9423   -582   -688    990       C  
ATOM   3229  C   PRO A2301      36.677 -55.718 310.792  1.00 80.37           C  
ANISOU 3229  C   PRO A2301     9519  11496   9522   -669   -518   1071       C  
ATOM   3230  O   PRO A2301      36.325 -55.575 311.963  1.00 88.19           O  
ANISOU 3230  O   PRO A2301    10552  12519  10436   -507   -438   1115       O  
ATOM   3231  CB  PRO A2301      36.970 -53.618 309.429  1.00 75.13           C  
ANISOU 3231  CB  PRO A2301     8603  10944   9000   -622   -775   1029       C  
ATOM   3232  CG  PRO A2301      37.088 -53.972 307.997  1.00 89.63           C  
ANISOU 3232  CG  PRO A2301    10388  12819  10848   -840   -810   1029       C  
ATOM   3233  CD  PRO A2301      38.399 -54.666 307.859  1.00 88.45           C  
ANISOU 3233  CD  PRO A2301    10402  12523  10683   -831   -803    949       C  
ATOM   3234  N   VAL A2302      36.223 -56.691 310.010  1.00 71.40           N  
ANISOU 3234  N   VAL A2302     8362  10355   8413   -920   -465   1091       N  
ATOM   3235  CA  VAL A2302      35.349 -57.732 310.533  1.00 67.81           C  
ANISOU 3235  CA  VAL A2302     7929   9887   7948  -1047   -309   1190       C  
ATOM   3236  C   VAL A2302      36.110 -58.578 311.545  1.00 79.27           C  
ANISOU 3236  C   VAL A2302     9630  11157   9333   -934   -234   1213       C  
ATOM   3237  O   VAL A2302      35.573 -58.967 312.582  1.00 92.39           O  
ANISOU 3237  O   VAL A2302    11341  12832  10932   -888    -89   1342       O  
ATOM   3238  CB  VAL A2302      34.805 -58.639 309.415  1.00 74.14           C  
ANISOU 3238  CB  VAL A2302     8667  10670   8832  -1353   -321   1172       C  
ATOM   3239  CG1 VAL A2302      33.844 -59.670 309.989  1.00 72.04           C  
ANISOU 3239  CG1 VAL A2302     8388  10364   8620  -1514   -169   1302       C  
ATOM   3240  CG2 VAL A2302      34.122 -57.807 308.341  1.00 84.61           C  
ANISOU 3240  CG2 VAL A2302     9763  12186  10198  -1451   -433   1150       C  
ATOM   3241  N   LEU A2303      37.374 -58.849 311.237  1.00 79.43           N  
ANISOU 3241  N   LEU A2303     9798  11020   9361   -877   -328   1103       N  
ATOM   3242  CA  LEU A2303      38.219 -59.664 312.098  1.00 72.71           C  
ANISOU 3242  CA  LEU A2303     9184   9977   8463   -753   -299   1115       C  
ATOM   3243  C   LEU A2303      38.599 -58.921 313.376  1.00 72.68           C  
ANISOU 3243  C   LEU A2303     9261  10011   8342   -455   -319   1138       C  
ATOM   3244  O   LEU A2303      38.883 -59.543 314.399  1.00 69.33           O  
ANISOU 3244  O   LEU A2303     9028   9491   7823   -333   -265   1211       O  
ATOM   3245  CB  LEU A2303      39.480 -60.102 311.348  1.00 68.99           C  
ANISOU 3245  CB  LEU A2303     8808   9347   8057   -752   -402    972       C  
ATOM   3246  CG  LEU A2303      39.268 -60.923 310.072  1.00 71.82           C  
ANISOU 3246  CG  LEU A2303     9138   9657   8495  -1004   -400    895       C  
ATOM   3247  CD1 LEU A2303      40.597 -61.233 309.396  1.00 74.26           C  
ANISOU 3247  CD1 LEU A2303     9529   9847   8839   -939   -477    736       C  
ATOM   3248  CD2 LEU A2303      38.506 -62.205 310.373  1.00 67.82           C  
ANISOU 3248  CD2 LEU A2303     8721   9014   8034  -1178   -298    987       C  
ATOM   3249  N   TYR A2304      38.605 -57.592 313.312  1.00 69.24           N  
ANISOU 3249  N   TYR A2304     8693   9705   7911   -330   -417   1071       N  
ATOM   3250  CA  TYR A2304      38.909 -56.771 314.480  1.00 67.27           C  
ANISOU 3250  CA  TYR A2304     8514   9489   7555    -34   -477   1043       C  
ATOM   3251  C   TYR A2304      37.893 -57.013 315.593  1.00 87.98           C  
ANISOU 3251  C   TYR A2304    11184  12234  10011     43   -294   1178       C  
ATOM   3252  O   TYR A2304      38.251 -57.125 316.766  1.00101.74           O  
ANISOU 3252  O   TYR A2304    13113  13957  11587    269   -283   1198       O  
ATOM   3253  CB  TYR A2304      38.933 -55.282 314.115  1.00 63.77           C  
ANISOU 3253  CB  TYR A2304     7899   9135   7197     58   -624    947       C  
ATOM   3254  CG  TYR A2304      40.068 -54.866 313.201  1.00 70.02           C  
ANISOU 3254  CG  TYR A2304     8640   9820   8146     25   -796    847       C  
ATOM   3255  CD1 TYR A2304      41.168 -55.689 313.002  1.00 69.26           C  
ANISOU 3255  CD1 TYR A2304     8663   9568   8084      3   -825    805       C  
ATOM   3256  CD2 TYR A2304      40.041 -53.643 312.543  1.00 69.39           C  
ANISOU 3256  CD2 TYR A2304     8380   9794   8191     23   -919    814       C  
ATOM   3257  CE1 TYR A2304      42.206 -55.310 312.171  1.00 75.69           C  
ANISOU 3257  CE1 TYR A2304     9399  10317   9043    -21   -944    731       C  
ATOM   3258  CE2 TYR A2304      41.073 -53.256 311.708  1.00 81.32           C  
ANISOU 3258  CE2 TYR A2304     9826  11223   9849    -20  -1043    769       C  
ATOM   3259  CZ  TYR A2304      42.153 -54.093 311.527  1.00 86.05           C  
ANISOU 3259  CZ  TYR A2304    10526  11700  10470    -42  -1042    727       C  
ATOM   3260  OH  TYR A2304      43.183 -53.713 310.699  1.00 97.10           O  
ANISOU 3260  OH  TYR A2304    11828  13048  12016    -79  -1130    698       O  
ATOM   3261  N   VAL A2305      36.623 -57.099 315.209  1.00 80.00           N  
ANISOU 3261  N   VAL A2305     9994  11366   9038   -141   -150   1280       N  
ATOM   3262  CA  VAL A2305      35.529 -57.260 316.158  1.00 72.58           C  
ANISOU 3262  CA  VAL A2305     9027  10586   7964    -89     65   1434       C  
ATOM   3263  C   VAL A2305      35.436 -58.686 316.699  1.00 81.03           C  
ANISOU 3263  C   VAL A2305    10264  11551   8971   -199    237   1618       C  
ATOM   3264  O   VAL A2305      35.245 -58.894 317.897  1.00 94.20           O  
ANISOU 3264  O   VAL A2305    12063  13288  10441    -29    380   1744       O  
ATOM   3265  CB  VAL A2305      34.180 -56.872 315.513  1.00 73.27           C  
ANISOU 3265  CB  VAL A2305     8812  10863   8163   -262    153   1490       C  
ATOM   3266  CG1 VAL A2305      33.016 -57.336 316.371  1.00 95.21           C  
ANISOU 3266  CG1 VAL A2305    11524  13804  10849   -278    427   1691       C  
ATOM   3267  CG2 VAL A2305      34.116 -55.371 315.282  1.00 64.09           C  
ANISOU 3267  CG2 VAL A2305     7499   9814   7039    -88      4   1350       C  
ATOM   3268  N   LEU A2306      35.582 -59.664 315.812  1.00 77.45           N  
ANISOU 3268  N   LEU A2306     9820  10926   8682   -472    218   1634       N  
ATOM   3269  CA  LEU A2306      35.428 -61.067 316.187  1.00 72.53           C  
ANISOU 3269  CA  LEU A2306     9339  10147   8071   -619    359   1817       C  
ATOM   3270  C   LEU A2306      36.502 -61.564 317.155  1.00 75.35           C  
ANISOU 3270  C   LEU A2306    10008  10342   8279   -394    324   1851       C  
ATOM   3271  O   LEU A2306      36.296 -62.551 317.861  1.00 67.55           O  
ANISOU 3271  O   LEU A2306     9167   9262   7237   -432    469   2064       O  
ATOM   3272  CB  LEU A2306      35.426 -61.944 314.934  1.00 68.73           C  
ANISOU 3272  CB  LEU A2306     8811   9484   7819   -938    292   1762       C  
ATOM   3273  CG  LEU A2306      34.225 -61.781 314.004  1.00 73.41           C  
ANISOU 3273  CG  LEU A2306     9112  10216   8566  -1208    320   1767       C  
ATOM   3274  CD1 LEU A2306      34.408 -62.624 312.754  1.00 84.66           C  
ANISOU 3274  CD1 LEU A2306    10541  11452  10173  -1477    202   1651       C  
ATOM   3275  CD2 LEU A2306      32.941 -62.158 314.725  1.00 65.36           C  
ANISOU 3275  CD2 LEU A2306     7965   9312   7557  -1319    557   2020       C  
ATOM   3276  N   THR A2307      37.644 -60.882 317.188  1.00 76.36           N  
ANISOU 3276  N   THR A2307    10226  10429   8359   -166    122   1659       N  
ATOM   3277  CA  THR A2307      38.750 -61.304 318.043  1.00 79.85           C  
ANISOU 3277  CA  THR A2307    10943  10715   8679     63     34   1663       C  
ATOM   3278  C   THR A2307      38.983 -60.345 319.212  1.00 81.45           C  
ANISOU 3278  C   THR A2307    11236  11079   8634    415    -20   1622       C  
ATOM   3279  O   THR A2307      39.832 -60.596 320.070  1.00 73.28           O  
ANISOU 3279  O   THR A2307    10434   9953   7454    644   -114   1627       O  
ATOM   3280  CB  THR A2307      40.057 -61.436 317.246  1.00 71.61           C  
ANISOU 3280  CB  THR A2307     9944   9468   7799     68   -183   1466       C  
ATOM   3281  OG1 THR A2307      40.489 -60.140 316.812  1.00 62.19           O  
ANISOU 3281  OG1 THR A2307     8601   8380   6650    173   -344   1269       O  
ATOM   3282  CG2 THR A2307      39.848 -62.336 316.036  1.00 64.74           C  
ANISOU 3282  CG2 THR A2307     9001   8454   7143   -246   -146   1452       C  
HETATM 3283  N   YCM A2308      38.234 -59.246 319.244  1.00 79.49           N  
ANISOU 3283  N   YCM A2308    10807  11060   8337    477     17   1563       N  
HETATM 3284  CA  YCM A2308      38.335 -58.302 320.337  1.00 72.46           C  
ANISOU 3284  CA  YCM A2308    10000  10325   7208    823    -38   1485       C  
HETATM 3285  CB  YCM A2308      39.175 -57.067 319.999  1.00 70.71           C  
ANISOU 3285  CB  YCM A2308     9709  10066   7092    979   -328   1209       C  
HETATM 3286  SG  YCM A2308      39.667 -56.045 321.361  1.00 80.04           S  
ANISOU 3286  SG  YCM A2308    11059  11337   8013   1429   -504   1040       S  
HETATM 3287  CD  YCM A2308      40.722 -57.044 322.360  1.00 76.46           C  
ANISOU 3287  CD  YCM A2308    10949  10743   7358   1612   -589   1110       C  
HETATM 3288  CE  YCM A2308      39.995 -57.721 323.501  1.00 85.35           C  
ANISOU 3288  CE  YCM A2308    12266  12029   8133   1730   -338   1343       C  
HETATM 3289  OZ1 YCM A2308      38.875 -57.305 323.875  1.00 84.77           O  
ANISOU 3289  OZ1 YCM A2308    12107  12201   7901   1779   -123   1408       O  
HETATM 3290  NZ2 YCM A2308      40.584 -58.797 324.111  1.00 92.11           N  
ANISOU 3290  NZ2 YCM A2308    13382  12761   8853   1789   -339   1502       N  
HETATM 3291  C   YCM A2308      36.990 -57.885 320.940  1.00 77.33           C  
ANISOU 3291  C   YCM A2308    10504  11225   7654    885    203   1599       C  
HETATM 3292  O   YCM A2308      36.304 -56.978 320.466  1.00 67.23           O  
ANISOU 3292  O   YCM A2308     8988  10088   6469    858    210   1509       O  
ATOM   3293  N   PRO A2309      36.595 -58.572 322.023  1.00 84.76           N  
ANISOU 3293  N   PRO A2309    11612  12257   8335    983    418   1819       N  
ATOM   3294  CA  PRO A2309      35.362 -58.282 322.766  1.00 76.48           C  
ANISOU 3294  CA  PRO A2309    10469  11512   7078   1081    700   1960       C  
ATOM   3295  C   PRO A2309      35.239 -56.823 323.211  1.00 71.22           C  
ANISOU 3295  C   PRO A2309     9744  11047   6268   1412    600   1715       C  
ATOM   3296  O   PRO A2309      34.130 -56.285 323.206  1.00 70.89           O  
ANISOU 3296  O   PRO A2309     9478  11237   6221   1420    781   1739       O  
ATOM   3297  CB  PRO A2309      35.464 -59.217 323.973  1.00 71.30           C  
ANISOU 3297  CB  PRO A2309    10099  10880   6113   1213    871   2215       C  
ATOM   3298  CG  PRO A2309      36.220 -60.381 323.455  1.00 72.10           C  
ANISOU 3298  CG  PRO A2309    10330  10655   6409    984    774   2309       C  
ATOM   3299  CD  PRO A2309      37.246 -59.800 322.510  1.00 81.60           C  
ANISOU 3299  CD  PRO A2309    11483  11669   7852    971    434   1993       C  
ATOM   3300  N   ASP A2310      36.353 -56.193 323.575  1.00 68.48           N  
ANISOU 3300  N   ASP A2310     9581  10600   5840   1681    301   1474       N  
ATOM   3301  CA  ASP A2310      36.328 -54.802 324.024  1.00 79.08           C  
ANISOU 3301  CA  ASP A2310    10895  12076   7076   2008    153   1206       C  
ATOM   3302  C   ASP A2310      35.917 -53.872 322.886  1.00 85.14           C  
ANISOU 3302  C   ASP A2310    11346  12823   8180   1854     56   1062       C  
ATOM   3303  O   ASP A2310      35.236 -52.873 323.111  1.00 87.37           O  
ANISOU 3303  O   ASP A2310    11499  13277   8421   2039     79    939       O  
ATOM   3304  CB  ASP A2310      37.689 -54.383 324.592  1.00 85.91           C  
ANISOU 3304  CB  ASP A2310    12011  12787   7844   2290   -200    970       C  
ATOM   3305  CG  ASP A2310      37.999 -55.047 325.925  1.00100.81           C  
ANISOU 3305  CG  ASP A2310    14233  14757   9313   2549   -136   1082       C  
ATOM   3306  OD1 ASP A2310      37.580 -56.205 326.132  1.00107.46           O  
ANISOU 3306  OD1 ASP A2310    15147  15639  10042   2399    139   1398       O  
ATOM   3307  OD2 ASP A2310      38.663 -54.408 326.769  1.00106.05           O  
ANISOU 3307  OD2 ASP A2310    15093  15436   9763   2904   -378    858       O  
ATOM   3308  N   MET A2311      36.326 -54.210 321.665  1.00 84.55           N  
ANISOU 3308  N   MET A2311    11155  12545   8424   1535    -51   1081       N  
ATOM   3309  CA  MET A2311      35.935 -53.439 320.488  1.00 89.16           C  
ANISOU 3309  CA  MET A2311    11451  13115   9309   1361   -138    997       C  
ATOM   3310  C   MET A2311      34.442 -53.569 320.215  1.00 88.66           C  
ANISOU 3310  C   MET A2311    11140  13270   9276   1205    142   1161       C  
ATOM   3311  O   MET A2311      33.761 -52.579 319.943  1.00 90.52           O  
ANISOU 3311  O   MET A2311    11163  13623   9606   1274    118   1072       O  
ATOM   3312  CB  MET A2311      36.720 -53.885 319.250  1.00102.84           C  
ANISOU 3312  CB  MET A2311    13139  14618  11315   1066   -285    997       C  
ATOM   3313  CG  MET A2311      38.149 -53.375 319.178  1.00109.89           C  
ANISOU 3313  CG  MET A2311    14143  15305  12305   1192   -600    804       C  
ATOM   3314  SD  MET A2311      38.856 -53.609 317.534  1.00 90.79           S  
ANISOU 3314  SD  MET A2311    11582  12699  10214    861   -723    801       S  
ATOM   3315  CE  MET A2311      40.527 -53.021 317.793  1.00122.45           C  
ANISOU 3315  CE  MET A2311    15705  16498  14321   1060  -1051    604       C  
ATOM   3316  N   LEU A2312      33.943 -54.798 320.285  1.00 84.24           N  
ANISOU 3316  N   LEU A2312    10593  12746   8667    992    391   1407       N  
ATOM   3317  CA  LEU A2312      32.536 -55.070 320.019  1.00 80.80           C  
ANISOU 3317  CA  LEU A2312     9891  12504   8305    799    657   1589       C  
ATOM   3318  C   LEU A2312      31.642 -54.415 321.066  1.00 87.56           C  
ANISOU 3318  C   LEU A2312    10677  13658   8934   1099    860   1598       C  
ATOM   3319  O   LEU A2312      30.611 -53.834 320.727  1.00 94.62           O  
ANISOU 3319  O   LEU A2312    11277  14728   9946   1077    949   1597       O  
ATOM   3320  CB  LEU A2312      32.279 -56.578 319.968  1.00 82.38           C  
ANISOU 3320  CB  LEU A2312    10138  12632   8531    502    862   1859       C  
ATOM   3321  CG  LEU A2312      30.837 -57.024 319.709  1.00 85.22           C  
ANISOU 3321  CG  LEU A2312    10199  13165   9016    251   1133   2078       C  
ATOM   3322  CD1 LEU A2312      30.265 -56.330 318.482  1.00 83.78           C  
ANISOU 3322  CD1 LEU A2312     9698  13023   9111     84    998   1961       C  
ATOM   3323  CD2 LEU A2312      30.760 -58.537 319.555  1.00 79.95           C  
ANISOU 3323  CD2 LEU A2312     9599  12333   8445    -76   1265   2321       C  
ATOM   3324  N   ARG A2313      32.039 -54.511 322.333  1.00 92.00           N  
ANISOU 3324  N   ARG A2313    11509  14289   9156   1401    930   1601       N  
ATOM   3325  CA  ARG A2313      31.299 -53.869 323.415  1.00 96.89           C  
ANISOU 3325  CA  ARG A2313    12108  15216   9490   1750   1126   1574       C  
ATOM   3326  C   ARG A2313      31.215 -52.364 323.194  1.00 88.78           C  
ANISOU 3326  C   ARG A2313    10946  14226   8562   1991    910   1263       C  
ATOM   3327  O   ARG A2313      30.145 -51.768 323.309  1.00 89.08           O  
ANISOU 3327  O   ARG A2313    10744  14500   8604   2105   1076   1251       O  
ATOM   3328  CB  ARG A2313      31.947 -54.151 324.773  1.00110.29           C  
ANISOU 3328  CB  ARG A2313    14177  16966  10762   2072   1163   1583       C  
ATOM   3329  CG  ARG A2313      31.815 -55.581 325.268  1.00117.53           C  
ANISOU 3329  CG  ARG A2313    15235  17901  11521   1906   1442   1948       C  
ATOM   3330  CD  ARG A2313      32.344 -55.710 326.690  1.00117.54           C  
ANISOU 3330  CD  ARG A2313    15605  18015  11040   2287   1481   1965       C  
ATOM   3331  NE  ARG A2313      32.518 -57.104 327.085  1.00119.73           N  
ANISOU 3331  NE  ARG A2313    16078  18216  11200   2122   1661   2320       N  
ATOM   3332  CZ  ARG A2313      33.680 -57.749 327.053  1.00118.77           C  
ANISOU 3332  CZ  ARG A2313    16225  17805  11097   2078   1427   2323       C  
ATOM   3333  NH1 ARG A2313      34.778 -57.122 326.650  1.00108.65           N  
ANISOU 3333  NH1 ARG A2313    15029  16309   9945   2176   1021   1995       N  
ATOM   3334  NH2 ARG A2313      33.747 -59.019 327.429  1.00124.10           N  
ANISOU 3334  NH2 ARG A2313    17071  18397  11684   1937   1598   2669       N  
ATOM   3335  N   LYS A2314      32.352 -51.759 322.869  1.00 78.73           N  
ANISOU 3335  N   LYS A2314     9811  12702   7400   2067    536   1021       N  
ATOM   3336  CA  LYS A2314      32.427 -50.316 322.693  1.00 81.63           C  
ANISOU 3336  CA  LYS A2314    10086  13033   7896   2295    282    728       C  
ATOM   3337  C   LYS A2314      31.658 -49.874 321.453  1.00 86.57           C  
ANISOU 3337  C   LYS A2314    10356  13657   8880   2051    264    765       C  
ATOM   3338  O   LYS A2314      31.264 -48.713 321.339  1.00 87.50           O  
ANISOU 3338  O   LYS A2314    10323  13810   9112   2239    147    592       O  
ATOM   3339  CB  LYS A2314      33.885 -49.865 322.599  1.00 85.80           C  
ANISOU 3339  CB  LYS A2314    10824  13265   8510   2380   -116    504       C  
ATOM   3340  CG  LYS A2314      34.109 -48.414 322.984  1.00102.96           C  
ANISOU 3340  CG  LYS A2314    13019  15391  10712   2735   -387    177       C  
ATOM   3341  CD  LYS A2314      33.781 -48.178 324.451  1.00116.97           C  
ANISOU 3341  CD  LYS A2314    14982  17399  12064   3172   -265     52       C  
ATOM   3342  CE  LYS A2314      34.705 -48.970 325.366  1.00107.08           C  
ANISOU 3342  CE  LYS A2314    14081  16115  10488   3288   -300     77       C  
ATOM   3343  NZ  LYS A2314      36.129 -48.559 325.211  1.00 98.97           N  
ANISOU 3343  NZ  LYS A2314    13206  14767   9631   3322   -741   -143       N  
ATOM   3344  N   LEU A2315      31.447 -50.806 320.528  1.00 86.13           N  
ANISOU 3344  N   LEU A2315    10174  13549   9001   1645    357    983       N  
ATOM   3345  CA  LEU A2315      30.690 -50.524 319.314  1.00 86.65           C  
ANISOU 3345  CA  LEU A2315     9912  13634   9375   1393    329   1039       C  
ATOM   3346  C   LEU A2315      29.183 -50.532 319.570  1.00 90.85           C  
ANISOU 3346  C   LEU A2315    10162  14470   9888   1414    630   1169       C  
ATOM   3347  O   LEU A2315      28.474 -49.616 319.153  1.00 93.02           O  
ANISOU 3347  O   LEU A2315    10182  14831  10329   1490    569   1092       O  
ATOM   3348  CB  LEU A2315      31.039 -51.535 318.218  1.00 85.93           C  
ANISOU 3348  CB  LEU A2315     9807  13380   9461    969    290   1184       C  
ATOM   3349  CG  LEU A2315      30.271 -51.380 316.902  1.00 91.48           C  
ANISOU 3349  CG  LEU A2315    10196  14117  10445    689    240   1249       C  
ATOM   3350  CD1 LEU A2315      30.483 -49.992 316.312  1.00 88.89           C  
ANISOU 3350  CD1 LEU A2315     9769  13716  10288    825    -38   1078       C  
ATOM   3351  CD2 LEU A2315      30.676 -52.458 315.907  1.00 88.48           C  
ANISOU 3351  CD2 LEU A2315     9853  13584  10183    306    199   1352       C  
ATOM   3352  N   ARG A2316      28.697 -51.567 320.251  1.00 88.92           N  
ANISOU 3352  N   ARG A2316     9945  14380   9459   1345    954   1385       N  
ATOM   3353  CA  ARG A2316      27.274 -51.678 320.563  1.00 81.50           C  
ANISOU 3353  CA  ARG A2316     8707  13749   8510   1347   1285   1547       C  
ATOM   3354  C   ARG A2316      26.815 -50.528 321.452  1.00 82.43           C  
ANISOU 3354  C   ARG A2316     8777  14090   8453   1813   1350   1364       C  
ATOM   3355  O   ARG A2316      25.675 -50.072 321.357  1.00 91.54           O  
ANISOU 3355  O   ARG A2316     9598  15469   9716   1873   1499   1390       O  
ATOM   3356  CB  ARG A2316      26.967 -53.010 321.245  1.00 82.28           C  
ANISOU 3356  CB  ARG A2316     8877  13951   8435   1196   1631   1845       C  
ATOM   3357  CG  ARG A2316      26.990 -54.219 320.329  1.00 85.28           C  
ANISOU 3357  CG  ARG A2316     9203  14145   9054    708   1623   2049       C  
ATOM   3358  CD  ARG A2316      26.475 -55.443 321.069  1.00106.24           C  
ANISOU 3358  CD  ARG A2316    11874  16904  11587    565   1990   2378       C  
ATOM   3359  NE  ARG A2316      26.482 -56.647 320.244  1.00116.43           N  
ANISOU 3359  NE  ARG A2316    13127  17977  13133    102   1965   2555       N  
ATOM   3360  CZ  ARG A2316      26.058 -57.836 320.661  1.00121.98           C  
ANISOU 3360  CZ  ARG A2316    13826  18682  13838   -118   2236   2868       C  
ATOM   3361  NH1 ARG A2316      25.589 -57.983 321.893  1.00115.84           N  
ANISOU 3361  NH1 ARG A2316    13075  18149  12792     81   2585   3074       N  
ATOM   3362  NH2 ARG A2316      26.101 -58.879 319.844  1.00123.41           N  
ANISOU 3362  NH2 ARG A2316    13983  18617  14290   -533   2159   2978       N  
ATOM   3363  N   ARG A2317      27.713 -50.075 322.321  1.00 82.54           N  
ANISOU 3363  N   ARG A2317     9122  14039   8201   2157   1225   1162       N  
ATOM   3364  CA  ARG A2317      27.450 -48.929 323.184  1.00 97.95           C  
ANISOU 3364  CA  ARG A2317    11093  16156   9967   2643   1222    913       C  
ATOM   3365  C   ARG A2317      27.209 -47.670 322.358  1.00 87.37           C  
ANISOU 3365  C   ARG A2317     9524  14712   8959   2713    945    700       C  
ATOM   3366  O   ARG A2317      26.238 -46.945 322.580  1.00 85.08           O  
ANISOU 3366  O   ARG A2317     8997  14634   8695   2949   1064    622       O  
ATOM   3367  CB  ARG A2317      28.617 -48.709 324.152  1.00111.00           C  
ANISOU 3367  CB  ARG A2317    13173  17698  11304   2965   1044    702       C  
ATOM   3368  CG  ARG A2317      28.520 -49.485 325.461  1.00122.08           C  
ANISOU 3368  CG  ARG A2317    14802  19349  12236   3154   1371    848       C  
ATOM   3369  CD  ARG A2317      29.909 -49.842 325.977  1.00127.85           C  
ANISOU 3369  CD  ARG A2317    15960  19866  12752   3237   1138    765       C  
ATOM   3370  NE  ARG A2317      29.969 -49.919 327.434  1.00134.22           N  
ANISOU 3370  NE  ARG A2317    17050  20913  13036   3644   1304    728       N  
ATOM   3371  CZ  ARG A2317      30.927 -49.363 328.168  1.00134.09           C  
ANISOU 3371  CZ  ARG A2317    17364  20804  12782   3997   1011    431       C  
ATOM   3372  NH1 ARG A2317      31.909 -48.692 327.581  1.00124.78           N  
ANISOU 3372  NH1 ARG A2317    16243  19280  11890   3969    551    164       N  
ATOM   3373  NH2 ARG A2317      30.907 -49.477 329.490  1.00133.24           N  
ANISOU 3373  NH2 ARG A2317    17522  20955  12150   4378   1172    407       N  
ATOM   3374  N   SER A2318      28.105 -47.419 321.409  1.00 88.66           N  
ANISOU 3374  N   SER A2318     9757  14551   9380   2517    585    621       N  
ATOM   3375  CA  SER A2318      27.979 -46.278 320.512  1.00 95.01           C  
ANISOU 3375  CA  SER A2318    10366  15213  10521   2536    299    477       C  
ATOM   3376  C   SER A2318      26.737 -46.413 319.638  1.00 94.18           C  
ANISOU 3376  C   SER A2318     9855  15272  10658   2298    441    668       C  
ATOM   3377  O   SER A2318      26.014 -45.441 319.425  1.00 93.34           O  
ANISOU 3377  O   SER A2318     9512  15233  10721   2477    375    569       O  
ATOM   3378  CB  SER A2318      29.230 -46.139 319.644  1.00102.54           C  
ANISOU 3378  CB  SER A2318    11471  15810  11680   2329    -66    423       C  
ATOM   3379  OG  SER A2318      29.535 -47.360 318.995  1.00120.24           O  
ANISOU 3379  OG  SER A2318    13740  17997  13948   1921     14    649       O  
ATOM   3380  N   LEU A2319      26.493 -47.623 319.139  1.00 93.94           N  
ANISOU 3380  N   LEU A2319     9744  15290  10661   1903    611    929       N  
ATOM   3381  CA  LEU A2319      25.323 -47.897 318.308  1.00 97.27           C  
ANISOU 3381  CA  LEU A2319     9775  15865  11319   1638    725   1114       C  
ATOM   3382  C   LEU A2319      24.025 -47.644 319.071  1.00 97.35           C  
ANISOU 3382  C   LEU A2319     9507  16220  11260   1880   1040   1148       C  
ATOM   3383  O   LEU A2319      23.087 -47.048 318.542  1.00100.04           O  
ANISOU 3383  O   LEU A2319     9500  16676  11836   1902   1010   1148       O  
ATOM   3384  CB  LEU A2319      25.354 -49.339 317.794  1.00101.12           C  
ANISOU 3384  CB  LEU A2319    10266  16316  11838   1185    846   1360       C  
ATOM   3385  CG  LEU A2319      24.113 -49.792 317.021  1.00104.30           C  
ANISOU 3385  CG  LEU A2319    10264  16882  12485    882    961   1552       C  
ATOM   3386  CD1 LEU A2319      23.980 -49.026 315.712  1.00109.35           C  
ANISOU 3386  CD1 LEU A2319    10714  17423  13410    776    632   1479       C  
ATOM   3387  CD2 LEU A2319      24.144 -51.292 316.774  1.00 98.38           C  
ANISOU 3387  CD2 LEU A2319     9556  16077  11747    471   1101   1772       C  
ATOM   3388  N   ARG A2320      23.981 -48.100 320.319  1.00 94.87           N  
ANISOU 3388  N   ARG A2320     9344  16087  10616   2077   1346   1188       N  
ATOM   3389  CA  ARG A2320      22.812 -47.902 321.166  1.00 96.77           C  
ANISOU 3389  CA  ARG A2320     9337  16698  10734   2343   1705   1229       C  
ATOM   3390  C   ARG A2320      22.593 -46.421 321.457  1.00 99.19           C  
ANISOU 3390  C   ARG A2320     9580  17047  11060   2816   1558    919       C  
ATOM   3391  O   ARG A2320      21.467 -45.930 321.397  1.00 96.19           O  
ANISOU 3391  O   ARG A2320     8829  16895  10825   2949   1693    922       O  
ATOM   3392  CB  ARG A2320      22.961 -48.685 322.473  1.00 96.34           C  
ANISOU 3392  CB  ARG A2320     9521  16826  10258   2480   2058   1349       C  
ATOM   3393  CG  ARG A2320      21.897 -48.380 323.517  1.00103.30           C  
ANISOU 3393  CG  ARG A2320    10201  18126  10921   2843   2460   1365       C  
ATOM   3394  CD  ARG A2320      22.078 -49.251 324.750  1.00109.31           C  
ANISOU 3394  CD  ARG A2320    11222  19078  11232   2945   2820   1544       C  
ATOM   3395  NE  ARG A2320      21.399 -48.700 325.918  1.00121.83           N  
ANISOU 3395  NE  ARG A2320    12749  21055  12484   3438   3149   1456       N  
ATOM   3396  CZ  ARG A2320      21.964 -47.855 326.776  1.00121.34           C  
ANISOU 3396  CZ  ARG A2320    13003  21017  12085   3943   3029   1121       C  
ATOM   3397  NH1 ARG A2320      23.218 -47.466 326.594  1.00124.24           N  
ANISOU 3397  NH1 ARG A2320    13737  21021  12445   3992   2581    866       N  
ATOM   3398  NH2 ARG A2320      21.276 -47.398 327.813  1.00108.42           N  
ANISOU 3398  NH2 ARG A2320    11356  19650  10191   4322   3263   1025       N  
ATOM   3399  N   THR A2321      23.678 -45.714 321.762  1.00108.92           N  
ANISOU 3399  N   THR A2321    11163  18042  12180   3068   1262    645       N  
ATOM   3400  CA  THR A2321      23.619 -44.284 322.050  1.00115.00           C  
ANISOU 3400  CA  THR A2321    11928  18771  12997   3521   1059    313       C  
ATOM   3401  C   THR A2321      23.105 -43.495 320.848  1.00115.33           C  
ANISOU 3401  C   THR A2321    11644  18688  13488   3412    805    300       C  
ATOM   3402  O   THR A2321      22.303 -42.570 320.994  1.00114.84           O  
ANISOU 3402  O   THR A2321    11351  18747  13538   3730    813    156       O  
ATOM   3403  CB  THR A2321      25.002 -43.739 322.463  1.00115.20           C  
ANISOU 3403  CB  THR A2321    12388  18489  12892   3730    717     33       C  
ATOM   3404  OG1 THR A2321      25.462 -44.433 323.630  1.00121.69           O  
ANISOU 3404  OG1 THR A2321    13525  19446  13267   3876    927     38       O  
ATOM   3405  CG2 THR A2321      24.929 -42.249 322.762  1.00111.39           C  
ANISOU 3405  CG2 THR A2321    11904  17916  12503   4194    474   -329       C  
ATOM   3406  N   VAL A2322      23.568 -43.871 319.661  1.00116.83           N  
ANISOU 3406  N   VAL A2322    11823  18646  13921   2980    580    451       N  
ATOM   3407  CA  VAL A2322      23.144 -43.222 318.424  1.00118.10           C  
ANISOU 3407  CA  VAL A2322    11705  18693  14475   2838    321    487       C  
ATOM   3408  C   VAL A2322      21.654 -43.439 318.166  1.00122.94           C  
ANISOU 3408  C   VAL A2322    11854  19625  15234   2770    567    657       C  
ATOM   3409  O   VAL A2322      20.925 -42.497 317.852  1.00127.68           O  
ANISOU 3409  O   VAL A2322    12183  20265  16066   2970    454    576       O  
ATOM   3410  CB  VAL A2322      23.957 -43.738 317.217  1.00117.57           C  
ANISOU 3410  CB  VAL A2322    11741  18366  14563   2380     76    635       C  
ATOM   3411  CG1 VAL A2322      23.277 -43.371 315.907  1.00113.47           C  
ANISOU 3411  CG1 VAL A2322    10895  17832  14385   2176   -110    755       C  
ATOM   3412  CG2 VAL A2322      25.376 -43.188 317.260  1.00118.63           C  
ANISOU 3412  CG2 VAL A2322    12238  18158  14679   2472   -239    456       C  
ATOM   3413  N   LEU A2323      21.205 -44.681 318.312  1.00123.66           N  
ANISOU 3413  N   LEU A2323    11841  19927  15217   2489    892    898       N  
ATOM   3414  CA  LEU A2323      19.805 -45.021 318.077  1.00119.56           C  
ANISOU 3414  CA  LEU A2323    10847  19711  14868   2369   1134   1087       C  
ATOM   3415  C   LEU A2323      18.881 -44.405 319.126  1.00122.63           C  
ANISOU 3415  C   LEU A2323    11022  20418  15153   2836   1427    978       C  
ATOM   3416  O   LEU A2323      17.732 -44.080 318.833  1.00128.76           O  
ANISOU 3416  O   LEU A2323    11356  21402  16166   2889   1504   1031       O  
ATOM   3417  CB  LEU A2323      19.625 -46.539 318.045  1.00117.43           C  
ANISOU 3417  CB  LEU A2323    10537  19546  14535   1938   1405   1378       C  
ATOM   3418  CG  LEU A2323      20.284 -47.267 316.872  1.00118.59           C  
ANISOU 3418  CG  LEU A2323    10808  19426  14824   1455   1145   1490       C  
ATOM   3419  CD1 LEU A2323      20.063 -48.769 316.972  1.00122.30           C  
ANISOU 3419  CD1 LEU A2323    11247  19973  15249   1067   1415   1752       C  
ATOM   3420  CD2 LEU A2323      19.760 -46.732 315.549  1.00117.46           C  
ANISOU 3420  CD2 LEU A2323    10365  19234  15031   1299    839   1500       C  
ATOM   3421  N   GLU A2324      19.384 -44.247 320.346  1.00126.97           N  
ANISOU 3421  N   GLU A2324    11882  21021  15340   3191   1583    815       N  
ATOM   3422  CA  GLU A2324      18.600 -43.645 321.420  1.00142.57           C  
ANISOU 3422  CA  GLU A2324    13709  23317  17144   3692   1875    670       C  
ATOM   3423  C   GLU A2324      18.408 -42.147 321.202  1.00157.40           C  
ANISOU 3423  C   GLU A2324    15488  25076  19241   4092   1573    362       C  
ATOM   3424  O   GLU A2324      17.431 -41.564 321.672  1.00153.34           O  
ANISOU 3424  O   GLU A2324    14791  24712  18758   4356   1728    259       O  
ATOM   3425  CB  GLU A2324      19.264 -43.888 322.777  1.00140.45           C  
ANISOU 3425  CB  GLU A2324    13852  23138  16373   3983   2089    561       C  
ATOM   3426  CG  GLU A2324      19.002 -45.262 323.373  1.00138.71           C  
ANISOU 3426  CG  GLU A2324    13628  23181  15892   3747   2547    893       C  
ATOM   3427  CD  GLU A2324      19.753 -45.481 324.672  1.00143.58           C  
ANISOU 3427  CD  GLU A2324    14701  23871  15982   4045   2706    797       C  
ATOM   3428  OE1 GLU A2324      20.883 -44.964 324.799  1.00143.85           O  
ANISOU 3428  OE1 GLU A2324    15139  23613  15905   4210   2353    528       O  
ATOM   3429  OE2 GLU A2324      19.213 -46.164 325.568  1.00144.65           O  
ANISOU 3429  OE2 GLU A2324    14842  24273  15846   4057   3119    995       O  
ATOM   3430  N   SER A2325      19.345 -41.531 320.489  1.00171.73           N  
ANISOU 3430  N   SER A2325    17539  26479  21231   4025   1100    223       N  
ATOM   3431  CA  SER A2325      19.304 -40.093 320.244  1.00175.03           C  
ANISOU 3431  CA  SER A2325    17912  26697  21894   4378    759    -51       C  
ATOM   3432  C   SER A2325      18.125 -39.707 319.356  1.00172.18           C  
ANISOU 3432  C   SER A2325    17152  26339  21931   4223    695     67       C  
ATOM   3433  O   SER A2325      17.561 -38.622 319.497  1.00175.93           O  
ANISOU 3433  O   SER A2325    17557  26715  22572   4517    590   -130       O  
ATOM   3434  CB  SER A2325      20.615 -39.623 319.608  1.00179.81           C  
ANISOU 3434  CB  SER A2325    18865  26824  22631   4245    278   -153       C  
ATOM   3435  OG  SER A2325      20.839 -40.265 318.366  1.00179.89           O  
ANISOU 3435  OG  SER A2325    18804  26704  22841   3713    132    126       O  
ATOM   3436  N   VAL A2326      17.757 -40.599 318.443  1.00153.52           N  
ANISOU 3436  N   VAL A2326    14543  24063  19724   3755    738    377       N  
ATOM   3437  CA  VAL A2326      16.634 -40.355 317.546  1.00137.56           C  
ANISOU 3437  CA  VAL A2326    12157  22037  18072   3570    652    495       C  
ATOM   3438  C   VAL A2326      15.309 -40.525 318.287  1.00131.67           C  
ANISOU 3438  C   VAL A2326    11105  21622  17300   3713   1058    521       C  
ATOM   3439  O   VAL A2326      14.344 -39.802 318.035  1.00133.97           O  
ANISOU 3439  O   VAL A2326    11136  21902  17866   3840    994    460       O  
ATOM   3440  CB  VAL A2326      16.669 -41.301 316.328  1.00129.31           C  
ANISOU 3440  CB  VAL A2326    10997  20951  17183   3005    533    782       C  
ATOM   3441  CG1 VAL A2326      15.613 -40.900 315.308  1.00125.74           C  
ANISOU 3441  CG1 VAL A2326    10234  20431  17112   2849    343    850       C  
ATOM   3442  CG2 VAL A2326      18.051 -41.291 315.693  1.00124.06           C  
ANISOU 3442  CG2 VAL A2326    10657  20000  16482   2844    199    781       C  
ATOM   3443  N   LEU A2327      15.273 -41.482 319.209  1.00126.05           N  
ANISOU 3443  N   LEU A2327    10435  21191  16268   3686   1477    627       N  
ATOM   3444  CA  LEU A2327      14.076 -41.738 320.000  1.00127.80           C  
ANISOU 3444  CA  LEU A2327    10397  21728  16432   3790   1903    687       C  
ATOM   3445  C   LEU A2327      14.052 -40.879 321.262  1.00126.67           C  
ANISOU 3445  C   LEU A2327    10431  21680  16017   4361   2059    391       C  
ATOM   3446  O   LEU A2327      13.874 -39.662 321.194  1.00122.39           O  
ANISOU 3446  O   LEU A2327     9877  20980  15644   4688   1827    134       O  
ATOM   3447  CB  LEU A2327      13.988 -43.220 320.371  1.00126.75           C  
ANISOU 3447  CB  LEU A2327    10248  21808  16102   3435   2281    988       C  
TER    3448      LEU A2327                                                      
HETATM 3449  S   SO4 A2401      60.407 -29.774 356.688  1.00 82.49           S  
HETATM 3450  O1  SO4 A2401      60.925 -30.895 355.908  1.00 86.20           O  
HETATM 3451  O2  SO4 A2401      60.956 -28.525 356.170  1.00 82.84           O  
HETATM 3452  O3  SO4 A2401      58.952 -29.746 356.585  1.00 71.07           O  
HETATM 3453  O4  SO4 A2401      60.795 -29.935 358.085  1.00 98.32           O  
HETATM 3454  S   SO4 A2402      59.766 -56.762 336.667  1.00 85.22           S  
HETATM 3455  O1  SO4 A2402      58.481 -57.357 336.322  1.00 78.79           O  
HETATM 3456  O2  SO4 A2402      60.751 -57.096 335.643  1.00 80.49           O  
HETATM 3457  O3  SO4 A2402      60.209 -57.284 337.958  1.00101.35           O  
HETATM 3458  O4  SO4 A2402      59.627 -55.311 336.746  1.00 68.90           O  
HETATM 3459  S   SO4 A2403      52.236 -44.081 328.260  1.00108.69           S  
HETATM 3460  O1  SO4 A2403      52.318 -45.469 327.813  1.00110.40           O  
HETATM 3461  O2  SO4 A2403      52.699 -43.196 327.195  1.00113.03           O  
HETATM 3462  O3  SO4 A2403      53.075 -43.902 329.440  1.00104.15           O  
HETATM 3463  O4  SO4 A2403      50.851 -43.758 328.588  1.00104.23           O  
HETATM 3464  S   SO4 A2404      49.645 -52.618 325.918  0.80 86.21           S  
HETATM 3465  O1  SO4 A2404      48.323 -53.046 325.471  0.80 76.91           O  
HETATM 3466  O2  SO4 A2404      49.961 -51.322 325.328  0.80 86.97           O  
HETATM 3467  O3  SO4 A2404      50.643 -53.598 325.502  0.80 79.80           O  
HETATM 3468  O4  SO4 A2404      49.652 -52.505 327.374  0.80 98.73           O  
HETATM 3469  S   SO4 A2405      39.130 -49.721 326.962  1.00147.62           S  
HETATM 3470  O1  SO4 A2405      38.454 -48.473 326.626  1.00139.92           O  
HETATM 3471  O2  SO4 A2405      38.553 -50.813 326.183  1.00141.70           O  
HETATM 3472  O3  SO4 A2405      38.963 -49.999 328.386  1.00152.46           O  
HETATM 3473  O4  SO4 A2405      40.552 -49.602 326.655  1.00149.94           O  
HETATM 3474  S   SO4 A2406      70.146 -61.724 326.031  1.00150.95           S  
HETATM 3475  O1  SO4 A2406      70.647 -61.185 324.771  1.00153.87           O  
HETATM 3476  O2  SO4 A2406      68.710 -61.968 325.920  1.00145.31           O  
HETATM 3477  O3  SO4 A2406      70.832 -62.977 326.331  1.00148.94           O  
HETATM 3478  O4  SO4 A2406      70.396 -60.765 327.102  1.00151.04           O  
HETATM 3479  S   SO4 A2407      80.734 -46.635 335.150  1.00159.75           S  
HETATM 3480  O1  SO4 A2407      81.000 -47.740 334.233  1.00159.83           O  
HETATM 3481  O2  SO4 A2407      81.327 -45.411 334.619  1.00159.96           O  
HETATM 3482  O3  SO4 A2407      81.317 -46.930 336.455  1.00160.29           O  
HETATM 3483  O4  SO4 A2407      79.292 -46.457 335.293  1.00155.98           O  
HETATM 3484  C1  FT4 A2408      42.792 -55.530 284.953  1.00131.72           C  
HETATM 3485  N2  FT4 A2408      43.814 -54.526 284.662  1.00136.00           N  
HETATM 3486  C3  FT4 A2408      44.850 -54.559 285.650  1.00133.66           C  
HETATM 3487  C5  FT4 A2408      45.069 -56.011 286.217  1.00 64.31           C  
HETATM 3488  C6  FT4 A2408      46.240 -56.063 287.195  1.00 67.48           C  
HETATM 3489  C7  FT4 A2408      46.306 -54.878 288.140  1.00 71.75           C  
HETATM 3490  C8  FT4 A2408      45.529 -53.754 287.959  1.00 69.44           C  
HETATM 3491  C9  FT4 A2408      44.539 -53.591 286.764  1.00130.75           C  
HETATM 3492  C10 FT4 A2408      45.856 -52.844 289.047  1.00 67.76           C  
HETATM 3493  C11 FT4 A2408      45.433 -51.564 289.429  1.00 66.97           C  
HETATM 3494  C12 FT4 A2408      45.974 -50.957 290.582  1.00 71.52           C  
HETATM 3495  C13 FT4 A2408      46.915 -51.618 291.331  1.00 73.14           C  
HETATM 3496  C14 FT4 A2408      47.341 -52.906 290.945  1.00 71.92           C  
HETATM 3497  C15 FT4 A2408      46.802 -53.513 289.798  1.00 72.04           C  
HETATM 3498  N16 FT4 A2408      47.050 -54.705 289.245  1.00 71.46           N  
HETATM 3499  C17 FT4 A2408      47.996 -55.681 289.768  1.00 65.93           C  
HETATM 3500  C18 FT4 A2408      49.457 -55.193 289.595  1.00 75.16           C  
HETATM 3501  O19 FT4 A2408      50.464 -56.024 289.781  1.00 84.75           O  
HETATM 3502  O20 FT4 A2408      49.689 -54.025 289.288  1.00 75.58           O  
HETATM 3503  S21 FT4 A2408      44.443 -54.738 283.108  1.00122.00           S  
HETATM 3504  O22 FT4 A2408      43.313 -54.972 282.124  1.00127.89           O  
HETATM 3505  O23 FT4 A2408      45.233 -53.497 282.711  1.00105.84           O  
HETATM 3506  C24 FT4 A2408      45.543 -56.202 283.127  1.00 59.02           C  
HETATM 3507  C25 FT4 A2408      46.911 -56.050 283.365  1.00 61.04           C  
HETATM 3508  C26 FT4 A2408      47.735 -57.167 283.385  1.00 69.25           C  
HETATM 3509  C27 FT4 A2408      47.196 -58.431 283.169  1.00 72.01           C  
HETATM 3510  C29 FT4 A2408      45.840 -58.577 282.937  1.00 58.47           C  
HETATM 3511  C30 FT4 A2408      45.013 -57.452 282.918  1.00 62.30           C  
HETATM 3512  F28 FT4 A2408      48.008 -59.535 283.188  1.00 90.02           F  
HETATM 3513  O1  MES A2409      58.872 -30.065 336.075  1.00118.73           O  
HETATM 3514  C2  MES A2409      57.635 -30.274 336.752  1.00119.51           C  
HETATM 3515  C3  MES A2409      57.572 -29.478 338.052  1.00129.43           C  
HETATM 3516  N4  MES A2409      58.790 -29.751 338.804  1.00139.58           N  
HETATM 3517  C5  MES A2409      60.067 -29.569 338.127  1.00131.97           C  
HETATM 3518  C6  MES A2409      60.001 -30.424 336.869  1.00123.69           C  
HETATM 3519  C7  MES A2409      58.748 -29.465 340.234  1.00147.26           C  
HETATM 3520  C8  MES A2409      59.600 -30.531 340.914  1.00149.32           C  
HETATM 3521  S   MES A2409      59.537 -30.358 342.570  1.00108.87           S  
HETATM 3522  O1S MES A2409      58.128 -30.400 343.022  1.00121.05           O  
HETATM 3523  O2S MES A2409      60.141 -29.064 342.959  1.00 93.40           O  
HETATM 3524  O3S MES A2409      60.287 -31.461 343.209  1.00 96.42           O  
HETATM 3525  C1  OLA A2410      40.243 -69.562 316.377  1.00148.87           C  
HETATM 3526  O1  OLA A2410      40.756 -69.402 317.506  1.00146.78           O  
HETATM 3527  O2  OLA A2410      39.781 -70.682 316.070  1.00150.21           O  
HETATM 3528  C2  OLA A2410      40.175 -68.410 315.406  1.00142.33           C  
HETATM 3529  C3  OLA A2410      40.665 -68.862 314.038  1.00131.92           C  
HETATM 3530  C4  OLA A2410      41.932 -68.096 313.670  1.00128.09           C  
HETATM 3531  C5  OLA A2410      42.168 -68.154 312.169  1.00131.19           C  
HETATM 3532  C6  OLA A2410      41.261 -67.163 311.456  1.00130.57           C  
HETATM 3533  C7  OLA A2410      40.944 -67.635 310.041  1.00124.21           C  
HETATM 3534  C8  OLA A2410      40.732 -66.441 309.115  1.00119.39           C  
HETATM 3535  C9  OLA A2410      41.221 -66.768 307.721  1.00115.74           C  
HETATM 3536  C10 OLA A2410      41.118 -65.730 306.685  1.00113.61           C  
HETATM 3537  C11 OLA A2410      39.861 -64.888 306.648  1.00106.84           C  
HETATM 3538  C12 OLA A2410      39.879 -63.928 305.459  1.00101.58           C  
HETATM 3539  C13 OLA A2410      39.789 -64.674 304.130  1.00103.49           C  
HETATM 3540  C14 OLA A2410      39.733 -63.703 302.958  1.00108.43           C  
HETATM 3541  C15 OLA A2410      38.379 -63.004 302.865  1.00109.87           C  
HETATM 3542  C16 OLA A2410      38.411 -61.890 301.817  1.00105.86           C  
HETATM 3543  C17 OLA A2410      37.079 -61.775 301.083  1.00103.86           C  
HETATM 3544  C18 OLA A2410      36.364 -60.477 301.428  1.00100.56           C  
HETATM 3545  C1  OLA A2411      47.833 -41.498 316.049  1.00127.38           C  
HETATM 3546  O1  OLA A2411      47.399 -41.351 314.884  1.00120.09           O  
HETATM 3547  O2  OLA A2411      49.067 -41.579 316.236  1.00130.86           O  
HETATM 3548  C2  OLA A2411      46.879 -41.590 317.218  1.00128.34           C  
HETATM 3549  C3  OLA A2411      46.041 -40.316 317.360  1.00128.01           C  
HETATM 3550  C4  OLA A2411      44.751 -40.616 318.132  1.00122.85           C  
HETATM 3551  C5  OLA A2411      43.707 -39.515 317.994  1.00117.48           C  
HETATM 3552  C6  OLA A2411      42.871 -39.739 316.742  1.00117.78           C  
HETATM 3553  C7  OLA A2411      41.773 -38.688 316.620  1.00120.17           C  
HETATM 3554  C8  OLA A2411      40.973 -38.850 315.328  1.00118.11           C  
HETATM 3555  C9  OLA A2411      40.362 -40.229 315.217  1.00112.17           C  
HETATM 3556  C10 OLA A2411      39.560 -40.525 314.019  1.00108.61           C  
HETATM 3557  C11 OLA A2411      38.653 -39.436 313.483  1.00111.03           C  
HETATM 3558  C12 OLA A2411      38.134 -39.789 312.088  1.00110.64           C  
HETATM 3559  C13 OLA A2411      36.789 -40.509 312.144  1.00108.58           C  
HETATM 3560  C14 OLA A2411      36.448 -41.138 310.800  1.00107.80           C  
HETATM 3561  C15 OLA A2411      36.700 -40.173 309.647  1.00106.09           C  
HETATM 3562  C16 OLA A2411      36.521 -40.874 308.302  1.00106.16           C  
HETATM 3563  C17 OLA A2411      35.810 -39.976 307.296  1.00105.15           C  
HETATM 3564  C18 OLA A2411      36.743 -38.905 306.749  1.00100.81           C  
HETATM 3565  C1  PGE A2412      58.516 -49.087 320.352  1.00 78.72           C  
HETATM 3566  O1  PGE A2412      57.638 -49.023 321.468  1.00 78.30           O  
HETATM 3567  C2  PGE A2412      58.689 -50.535 319.940  1.00 88.44           C  
HETATM 3568  O2  PGE A2412      59.467 -50.588 318.760  1.00102.13           O  
HETATM 3569  C3  PGE A2412      59.433 -51.843 318.109  1.00106.63           C  
HETATM 3570  C4  PGE A2412      59.974 -51.689 316.700  1.00108.67           C  
HETATM 3571  O4  PGE A2412      63.711 -50.280 316.796  1.00104.42           O  
HETATM 3572  C6  PGE A2412      63.462 -51.106 315.666  1.00105.74           C  
HETATM 3573  C5  PGE A2412      61.965 -51.269 315.498  1.00107.91           C  
HETATM 3574  O3  PGE A2412      61.383 -51.574 316.750  1.00111.30           O  
HETATM 3575  C1  PGE A2413      70.116 -54.096 344.108  1.00121.11           C  
HETATM 3576  O1  PGE A2413      71.436 -53.616 344.336  1.00116.99           O  
HETATM 3577  C2  PGE A2413      69.810 -54.028 342.625  1.00118.44           C  
HETATM 3578  O2  PGE A2413      68.884 -55.044 342.298  1.00118.87           O  
HETATM 3579  C3  PGE A2413      69.510 -56.174 341.721  1.00125.08           C  
HETATM 3580  C4  PGE A2413      68.442 -57.172 341.304  1.00132.10           C  
HETATM 3581  O4  PGE A2413      68.788 -61.625 339.634  1.00135.71           O  
HETATM 3582  C6  PGE A2413      69.088 -60.252 339.392  1.00137.98           C  
HETATM 3583  C5  PGE A2413      68.601 -59.409 340.560  1.00139.03           C  
HETATM 3584  O3  PGE A2413      68.990 -58.062 340.347  1.00137.49           O  
HETATM 3585  C1  PGO A2414      37.015 -60.759 327.121  1.00 67.91           C  
HETATM 3586  C2  PGO A2414      38.136 -59.799 326.733  1.00 71.74           C  
HETATM 3587  C3  PGO A2414      39.500 -60.398 327.042  1.00 73.48           C  
HETATM 3588  O1  PGO A2414      37.209 -62.021 326.467  1.00 69.73           O  
HETATM 3589  O2  PGO A2414      38.012 -58.568 327.452  1.00 82.62           O  
HETATM 3590  C1  PGO A2415      60.921 -54.234 309.273  1.00 95.55           C  
HETATM 3591  C2  PGO A2415      60.696 -53.884 307.805  1.00 96.32           C  
HETATM 3592  C3  PGO A2415      60.792 -55.121 306.919  1.00 89.24           C  
HETATM 3593  O1  PGO A2415      60.869 -53.046 310.071  1.00 88.01           O  
HETATM 3594  O2  PGO A2415      61.676 -52.930 307.383  1.00101.75           O  
HETATM 3595  C1  PGO A2416      41.268 -57.605 278.145  1.00 97.79           C  
HETATM 3596  C2  PGO A2416      42.309 -56.834 278.953  1.00 93.33           C  
HETATM 3597  C3  PGO A2416      42.081 -55.330 278.845  1.00 82.41           C  
HETATM 3598  O1  PGO A2416      40.046 -57.678 278.896  1.00 95.54           O  
HETATM 3599  O2  PGO A2416      43.627 -57.152 278.488  1.00 90.01           O  
HETATM 3600  C1  PGO A2417      31.099 -46.647 293.919  1.00 98.86           C  
HETATM 3601  C2  PGO A2417      30.059 -46.502 295.027  1.00 97.25           C  
HETATM 3602  C3  PGO A2417      30.621 -45.784 296.250  1.00 82.13           C  
HETATM 3603  O1  PGO A2417      30.490 -47.187 292.740  1.00101.30           O  
HETATM 3604  O2  PGO A2417      29.600 -47.799 295.420  1.00102.06           O  
HETATM 3605  C1  PEG A2418      51.308 -42.357 296.966  1.00 86.63           C  
HETATM 3606  O1  PEG A2418      50.328 -41.317 297.080  1.00 84.85           O  
HETATM 3607  C2  PEG A2418      52.708 -41.778 297.151  1.00 94.24           C  
HETATM 3608  O2  PEG A2418      53.471 -42.024 295.971  1.00103.38           O  
HETATM 3609  C3  PEG A2418      54.541 -41.088 295.826  1.00108.71           C  
HETATM 3610  C4  PEG A2418      54.701 -40.754 294.343  1.00109.50           C  
HETATM 3611  O4  PEG A2418      55.712 -39.745 294.202  1.00108.62           O  
HETATM 3612  O   HOH A2501      28.935 -43.939 323.600  1.00 60.79           O  
HETATM 3613  O   HOH A2502      50.587 -48.996 326.399  1.00 55.27           O  
HETATM 3614  O   HOH A2503      42.928 -50.911 324.984  1.00 77.55           O  
HETATM 3615  O   HOH A2504      79.507 -48.426 332.053  1.00 68.16           O  
HETATM 3616  O   HOH A2505      57.358 -51.185 278.083  1.00 79.48           O  
HETATM 3617  O   HOH A2506      52.978 -30.542 329.617  1.00 64.06           O  
HETATM 3618  O   HOH A2507      79.541 -52.568 333.561  1.00 69.36           O  
HETATM 3619  O   HOH A2508      47.802 -45.534 344.800  1.00 85.53           O  
CONECT   50 1478                                                                
CONECT  731 1350                                                                
CONECT 1350  731                                                                
CONECT 1478   50                                                                
CONECT 3278 3283                                                                
CONECT 3283 3278 3284                                                           
CONECT 3284 3283 3285 3291                                                      
CONECT 3285 3284 3286                                                           
CONECT 3286 3285 3287                                                           
CONECT 3287 3286 3288                                                           
CONECT 3288 3287 3289 3290                                                      
CONECT 3289 3288                                                                
CONECT 3290 3288                                                                
CONECT 3291 3284 3292 3293                                                      
CONECT 3292 3291                                                                
CONECT 3293 3291                                                                
CONECT 3449 3450 3451 3452 3453                                                 
CONECT 3450 3449                                                                
CONECT 3451 3449                                                                
CONECT 3452 3449                                                                
CONECT 3453 3449                                                                
CONECT 3454 3455 3456 3457 3458                                                 
CONECT 3455 3454                                                                
CONECT 3456 3454                                                                
CONECT 3457 3454                                                                
CONECT 3458 3454                                                                
CONECT 3459 3460 3461 3462 3463                                                 
CONECT 3460 3459                                                                
CONECT 3461 3459                                                                
CONECT 3462 3459                                                                
CONECT 3463 3459                                                                
CONECT 3464 3465 3466 3467 3468                                                 
CONECT 3465 3464                                                                
CONECT 3466 3464                                                                
CONECT 3467 3464                                                                
CONECT 3468 3464                                                                
CONECT 3469 3470 3471 3472 3473                                                 
CONECT 3470 3469                                                                
CONECT 3471 3469                                                                
CONECT 3472 3469                                                                
CONECT 3473 3469                                                                
CONECT 3474 3475 3476 3477 3478                                                 
CONECT 3475 3474                                                                
CONECT 3476 3474                                                                
CONECT 3477 3474                                                                
CONECT 3478 3474                                                                
CONECT 3479 3480 3481 3482 3483                                                 
CONECT 3480 3479                                                                
CONECT 3481 3479                                                                
CONECT 3482 3479                                                                
CONECT 3483 3479                                                                
CONECT 3484 3485                                                                
CONECT 3485 3484 3486 3503                                                      
CONECT 3486 3485 3487 3491                                                      
CONECT 3487 3486 3488                                                           
CONECT 3488 3487 3489                                                           
CONECT 3489 3488 3490 3498                                                      
CONECT 3490 3489 3491 3492                                                      
CONECT 3491 3486 3490                                                           
CONECT 3492 3490 3493 3497                                                      
CONECT 3493 3492 3494                                                           
CONECT 3494 3493 3495                                                           
CONECT 3495 3494 3496                                                           
CONECT 3496 3495 3497                                                           
CONECT 3497 3492 3496 3498                                                      
CONECT 3498 3489 3497 3499                                                      
CONECT 3499 3498 3500                                                           
CONECT 3500 3499 3501 3502                                                      
CONECT 3501 3500                                                                
CONECT 3502 3500                                                                
CONECT 3503 3485 3504 3505 3506                                                 
CONECT 3504 3503                                                                
CONECT 3505 3503                                                                
CONECT 3506 3503 3507 3511                                                      
CONECT 3507 3506 3508                                                           
CONECT 3508 3507 3509                                                           
CONECT 3509 3508 3510 3512                                                      
CONECT 3510 3509 3511                                                           
CONECT 3511 3506 3510                                                           
CONECT 3512 3509                                                                
CONECT 3513 3514 3518                                                           
CONECT 3514 3513 3515                                                           
CONECT 3515 3514 3516                                                           
CONECT 3516 3515 3517 3519                                                      
CONECT 3517 3516 3518                                                           
CONECT 3518 3513 3517                                                           
CONECT 3519 3516 3520                                                           
CONECT 3520 3519 3521                                                           
CONECT 3521 3520 3522 3523 3524                                                 
CONECT 3522 3521                                                                
CONECT 3523 3521                                                                
CONECT 3524 3521                                                                
CONECT 3525 3526 3527 3528                                                      
CONECT 3526 3525                                                                
CONECT 3527 3525                                                                
CONECT 3528 3525 3529                                                           
CONECT 3529 3528 3530                                                           
CONECT 3530 3529 3531                                                           
CONECT 3531 3530 3532                                                           
CONECT 3532 3531 3533                                                           
CONECT 3533 3532 3534                                                           
CONECT 3534 3533 3535                                                           
CONECT 3535 3534 3536                                                           
CONECT 3536 3535 3537                                                           
CONECT 3537 3536 3538                                                           
CONECT 3538 3537 3539                                                           
CONECT 3539 3538 3540                                                           
CONECT 3540 3539 3541                                                           
CONECT 3541 3540 3542                                                           
CONECT 3542 3541 3543                                                           
CONECT 3543 3542 3544                                                           
CONECT 3544 3543                                                                
CONECT 3545 3546 3547 3548                                                      
CONECT 3546 3545                                                                
CONECT 3547 3545                                                                
CONECT 3548 3545 3549                                                           
CONECT 3549 3548 3550                                                           
CONECT 3550 3549 3551                                                           
CONECT 3551 3550 3552                                                           
CONECT 3552 3551 3553                                                           
CONECT 3553 3552 3554                                                           
CONECT 3554 3553 3555                                                           
CONECT 3555 3554 3556                                                           
CONECT 3556 3555 3557                                                           
CONECT 3557 3556 3558                                                           
CONECT 3558 3557 3559                                                           
CONECT 3559 3558 3560                                                           
CONECT 3560 3559 3561                                                           
CONECT 3561 3560 3562                                                           
CONECT 3562 3561 3563                                                           
CONECT 3563 3562 3564                                                           
CONECT 3564 3563                                                                
CONECT 3565 3566 3567                                                           
CONECT 3566 3565                                                                
CONECT 3567 3565 3568                                                           
CONECT 3568 3567 3569                                                           
CONECT 3569 3568 3570                                                           
CONECT 3570 3569 3574                                                           
CONECT 3571 3572                                                                
CONECT 3572 3571 3573                                                           
CONECT 3573 3572 3574                                                           
CONECT 3574 3570 3573                                                           
CONECT 3575 3576 3577                                                           
CONECT 3576 3575                                                                
CONECT 3577 3575 3578                                                           
CONECT 3578 3577 3579                                                           
CONECT 3579 3578 3580                                                           
CONECT 3580 3579 3584                                                           
CONECT 3581 3582                                                                
CONECT 3582 3581 3583                                                           
CONECT 3583 3582 3584                                                           
CONECT 3584 3580 3583                                                           
CONECT 3585 3586 3588                                                           
CONECT 3586 3585 3587 3589                                                      
CONECT 3587 3586                                                                
CONECT 3588 3585                                                                
CONECT 3589 3586                                                                
CONECT 3590 3591 3593                                                           
CONECT 3591 3590 3592 3594                                                      
CONECT 3592 3591                                                                
CONECT 3593 3590                                                                
CONECT 3594 3591                                                                
CONECT 3595 3596 3598                                                           
CONECT 3596 3595 3597 3599                                                      
CONECT 3597 3596                                                                
CONECT 3598 3595                                                                
CONECT 3599 3596                                                                
CONECT 3600 3601 3603                                                           
CONECT 3601 3600 3602 3604                                                      
CONECT 3602 3601                                                                
CONECT 3603 3600                                                                
CONECT 3604 3601                                                                
CONECT 3605 3606 3607                                                           
CONECT 3606 3605                                                                
CONECT 3607 3605 3608                                                           
CONECT 3608 3607 3609                                                           
CONECT 3609 3608 3610                                                           
CONECT 3610 3609 3611                                                           
CONECT 3611 3610                                                                
MASTER      401    0   19   24    2    0   25    6 3618    1  179   37          
END