HEADER    MEMBRANE PROTEIN                        12-MAR-13   4BEY              
TITLE     NIGHT BLINDNESS CAUSING G90D RHODOPSIN IN COMPLEX WITH GACT2 PEPTIDE  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHODOPSIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(T) SUBUNIT ALPHA-1;   
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: RESIDUES 340-350;                                          
COMPND  10 SYNONYM: TRANSDUCIN ALPHA-1 CHAIN;                                   
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 ORGAN: EYE;                                                          
SOURCE   6 TISSUE: RETINA;                                                      
SOURCE   7 CELL: ROD PHOTORECEPTOR;                                             
SOURCE   8 GENE: RHO;                                                           
SOURCE   9 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  10 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  12 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  16 ORGANISM_COMMON: BOVINE;                                             
SOURCE  17 ORGANISM_TAXID: 9913                                                 
KEYWDS    MEMBRANE PROTEIN, GPCR, DISEASE MUTANT, CONGENTIAL STATIONARY NIGHT   
KEYWDS   2 BLINDNESS, ACTIVE STATE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SINGHAL,M.K.OSTERMAIER,S.A.VISHNIVETSKIY,V.PANNEELS,K.T.HOMAN,      
AUTHOR   2 J.J.G.TESMER,D.VEPRINTSEV,X.DEUPI,V.V.GUREVICH,G.F.X.SCHERTLER,      
AUTHOR   3 J.STANDFUSS                                                          
REVDAT   4   29-JUL-20 4BEY    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   04-SEP-19 4BEY    1       COMPND SOURCE DBREF  LINK                
REVDAT   2   19-JUN-13 4BEY    1       JRNL   REMARK                            
REVDAT   1   08-MAY-13 4BEY    0                                                
JRNL        AUTH   A.SINGHAL,M.K.OSTERMAIER,S.A.VISHNIVETSKIY,V.PANNEELS,       
JRNL        AUTH 2 K.T.HOMAN,J.J.TESMER,D.VEPRINTSEV,X.DEUPI,V.V.GUREVICH,      
JRNL        AUTH 3 G.F.SCHERTLER,J.STANDFUSS                                    
JRNL        TITL   INSIGHTS INTO CONGENITAL STATIONARY NIGHT BLINDNESS BASED ON 
JRNL        TITL 2 THE STRUCTURE OF G90D RHODOPSIN.                             
JRNL        REF    EMBO REP.                     V.  14   520 2013              
JRNL        REFN                   ISSN 1469-221X                               
JRNL        PMID   23579341                                                     
JRNL        DOI    10.1038/EMBOR.2013.44                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.010                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 27501                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1376                            
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 29.2648 -  6.2298    1.00     2687   142  0.2286 0.2744        
REMARK   3     2  6.2298 -  4.9525    1.00     2634   139  0.2225 0.2508        
REMARK   3     3  4.9525 -  4.3288    1.00     2621   138  0.1895 0.1847        
REMARK   3     4  4.3288 -  3.9340    1.00     2608   137  0.1906 0.2226        
REMARK   3     5  3.9340 -  3.6526    1.00     2613   138  0.2221 0.2153        
REMARK   3     6  3.6526 -  3.4376    1.00     2588   136  0.2325 0.2827        
REMARK   3     7  3.4376 -  3.2657    1.00     2607   137  0.2593 0.2988        
REMARK   3     8  3.2657 -  3.1237    1.00     2590   136  0.3012 0.3208        
REMARK   3     9  3.1237 -  3.0036    1.00     2590   137  0.3334 0.3668        
REMARK   3    10  3.0036 -  2.9000    1.00     2587   136  0.3686 0.4164        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.120           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 60.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.08                          
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      :  0.011           2879                                  
REMARK   3   ANGLE     :  1.657           3914                                  
REMARK   3   CHIRALITY :  0.129            445                                  
REMARK   3   PLANARITY :  0.007            474                                  
REMARK   3   DIHEDRAL  : 20.509           1025                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4BEY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290056118.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 27.90                              
REMARK 200  R MERGE                    (I) : 0.27000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 27.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER MR                                             
REMARK 200 STARTING MODEL: PDB ENTRY 4A4M                                       
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED USING A LOW DOSE, HIGH REDUNDANCY        
REMARK 200  STRATEGY AS SUGGESTED BY KARPLUS & DIEDERICHS, SCIENCE, 2012        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 84.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 7.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000      121.22000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.98640            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       36.78667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000      121.22000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       69.98640            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       36.78667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000      121.22000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       69.98640            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       36.78667            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000      121.22000            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       69.98640            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       36.78667            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000      121.22000            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       69.98640            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       36.78667            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000      121.22000            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       69.98640            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       36.78667            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      139.97280            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       73.57333            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000      139.97280            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       73.57333            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000      139.97280            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       73.57333            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000      139.97280            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       73.57333            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000      139.97280            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000       73.57333            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000      139.97280            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000       73.57333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.9 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     PRO A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     ALA A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     THR A   336                                                      
REMARK 465     VAL A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     LYS A   339                                                      
REMARK 465     THR A   340                                                      
REMARK 465     GLU A   341                                                      
REMARK 465     THR A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     GLN A   344                                                      
REMARK 465     VAL A   345                                                      
REMARK 465     ALA A   346                                                      
REMARK 465     PRO A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A   176     O    HOH A  2013              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O3   NAG C     1     O3   NAG C     1    16545     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A   1   C   -  N   -  CA  ANGL. DEV. =  23.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  25      -59.97   -121.35                                   
REMARK 500    ASP A  90      -67.56   -130.82                                   
REMARK 500    CYS A 167      -61.75   -102.14                                   
REMARK 500    SER A 176     -148.74     50.26                                   
REMARK 500    PHE A 212      -62.47   -127.04                                   
REMARK 500    SER A 281      161.61    170.77                                   
REMARK 500    VAL A 300      -60.35   -101.48                                   
REMARK 500    ILE A 307      -63.46   -128.57                                   
REMARK 500    CYS A 323       38.02     71.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 TRP A  175     SER A  176                 -149.94                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BEZ   RELATED DB: PDB                                   
REMARK 900 NIGHT BLINDNESS CAUSING G90D RHODOPSIN IN THE ACTIVE CONFORMATION    
DBREF  4BEY A    1   348  UNP    P02699   OPSD_BOVIN       1    348             
DBREF  4BEY B  340   350  UNP    P04695   GNAT1_BOVIN    340    350             
SEQADV 4BEY ACE A    0  UNP  P02699              EXPRESSION TAG                 
SEQADV 4BEY CYS A    2  UNP  P02699    ASN     2 ENGINEERED MUTATION            
SEQADV 4BEY ASP A   90  UNP  P02699    GLY    90 ENGINEERED MUTATION            
SEQADV 4BEY CYS A  282  UNP  P02699    ASP   282 ENGINEERED MUTATION            
SEQADV 4BEY LEU B  341  UNP  P04695    LYS   341 ENGINEERED MUTATION            
SEQRES   1 A  349  ACE MET CYS GLY THR GLU GLY PRO ASN PHE TYR VAL PRO          
SEQRES   2 A  349  PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU          
SEQRES   3 A  349  ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER          
SEQRES   4 A  349  MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY          
SEQRES   5 A  349  PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN          
SEQRES   6 A  349  HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU          
SEQRES   7 A  349  ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY ASP          
SEQRES   8 A  349  PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE          
SEQRES   9 A  349  VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE          
SEQRES  10 A  349  ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL          
SEQRES  11 A  349  VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO          
SEQRES  12 A  349  MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET          
SEQRES  13 A  349  GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA          
SEQRES  14 A  349  ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU          
SEQRES  15 A  349  GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO          
SEQRES  16 A  349  HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET          
SEQRES  17 A  349  PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE          
SEQRES  18 A  349  PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA          
SEQRES  19 A  349  ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA          
SEQRES  20 A  349  GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE          
SEQRES  21 A  349  ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA          
SEQRES  22 A  349  PHE TYR ILE PHE THR HIS GLN GLY SER CYS PHE GLY PRO          
SEQRES  23 A  349  ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER          
SEQRES  24 A  349  ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS          
SEQRES  25 A  349  GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY          
SEQRES  26 A  349  LYS ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL          
SEQRES  27 A  349  SER LYS THR GLU THR SER GLN VAL ALA PRO ALA                  
SEQRES   1 B   11  ILE LEU GLU ASN LEU LYS ASP CYS GLY LEU PHE                  
MODRES 4BEY ASN A   15  ASN  GLYCOSYLATION SITE                                 
HET    ACE  A   0       3                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET    MAN  C   4      11                                                       
HET    SO4  A1327       5                                                       
HET    ACT  A1328       4                                                       
HET    PLM  A1329      17                                                       
HET    BOG  A1334      20                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   3  MAN    C6 H12 O6                                                    
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  ACT    C2 H3 O2 1-                                                  
FORMUL   6  PLM    C16 H32 O2                                                   
FORMUL   7  BOG    C14 H28 O6                                                   
FORMUL   8  HOH   *20(H2 O)                                                     
HELIX    1   1 SER A   14  GLY A   18  5                                   5    
HELIX    2   2 GLU A   33  HIS A   65  1                                  33    
HELIX    3   3 LYS A   66  ARG A   69  5                                   4    
HELIX    4   4 THR A   70  LEU A   72  5                                   3    
HELIX    5   5 ASN A   73  ASP A   90  1                                  18    
HELIX    6   6 ASP A   90  LEU A   99  1                                  10    
HELIX    7   7 PHE A  105  LYS A  141  1                                  37    
HELIX    8   8 GLY A  149  VAL A  173  1                                  25    
HELIX    9   9 ASN A  199  HIS A  211  1                                  13    
HELIX   10  10 PHE A  212  GLN A  237  1                                  26    
HELIX   11  11 SER A  240  HIS A  278  1                                  39    
HELIX   12  12 GLY A  284  ILE A  307  1                                  24    
HELIX   13  13 ASN A  310  CYS A  322  1                                  13    
HELIX   14  14 ILE B  340  CYS B  347  1                                   8    
SHEET    1  AA 2 THR A   4  GLU A   5  0                                        
SHEET    2  AA 2 TYR A  10  VAL A  11 -1  N  VAL A  11   O  THR A   4           
SHEET    1  AB 2 TYR A 178  GLU A 181  0                                        
SHEET    2  AB 2 SER A 186  ILE A 189 -1  O  SER A 186   N  GLU A 181           
SSBOND   1 CYS A    2    CYS A  282                          1555   1555  2.07  
SSBOND   2 CYS A  110    CYS A  187                          1555   1555  2.05  
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.32  
LINK         ND2 ASN A  15                 C1  NAG C   1     1555   1555  1.45  
LINK         SG  CYS A 323                 C1  PLM A1329     1555   1555  1.68  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.46  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.42  
LINK         O3  BMA C   3                 C1  MAN C   4     1555   1555  1.45  
CRYST1  242.440  242.440  110.360  90.00  90.00 120.00 H 3 2        18          
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      0.004125  0.002381  0.000000        0.00000                         
SCALE2      0.000000  0.004763  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009061        0.00000                         
HETATM    1  C   ACE A   0      56.861 -44.967  39.967  1.00 83.92           C  
HETATM    2  O   ACE A   0      56.711 -43.889  39.375  1.00 91.65           O  
HETATM    3  CH3 ACE A   0      58.196 -45.396  40.464  1.00 80.33           C  
ATOM      4  N   MET A   1      55.934 -45.896  39.837  1.00 79.67           N  
ATOM      5  CA  MET A   1      54.685 -46.249  39.171  1.00 72.69           C  
ATOM      6  C   MET A   1      53.546 -46.588  40.128  1.00 69.40           C  
ATOM      7  O   MET A   1      53.595 -47.533  40.928  1.00 63.38           O  
ATOM      8  CB  MET A   1      54.888 -47.354  38.171  1.00 73.55           C  
ATOM      9  CG  MET A   1      55.291 -48.666  38.800  1.00 61.70           C  
ATOM     10  SD  MET A   1      55.379 -49.794  37.406  1.00 72.35           S  
ATOM     11  CE  MET A   1      53.700 -50.310  37.221  1.00 53.22           C  
ATOM     12  N   CYS A   2      52.524 -45.748  40.042  1.00 65.10           N  
ATOM     13  CA  CYS A   2      51.643 -45.495  41.169  1.00 56.66           C  
ATOM     14  C   CYS A   2      50.366 -46.332  41.334  1.00 59.23           C  
ATOM     15  O   CYS A   2      49.838 -46.398  42.441  1.00 59.30           O  
ATOM     16  CB  CYS A   2      51.296 -43.993  41.143  1.00 55.75           C  
ATOM     17  SG  CYS A   2      52.496 -42.959  40.286  1.00 61.68           S  
ATOM     18  N   GLY A   3      49.975 -47.088  40.315  1.00 52.83           N  
ATOM     19  CA  GLY A   3      48.661 -47.694  40.329  1.00 49.67           C  
ATOM     20  C   GLY A   3      48.738 -48.945  39.478  1.00 51.34           C  
ATOM     21  O   GLY A   3      49.837 -49.335  39.108  1.00 56.74           O  
ATOM     22  N   THR A   4      47.639 -49.667  39.274  1.00 41.18           N  
ATOM     23  CA  THR A   4      47.686 -50.731  38.303  1.00 34.91           C  
ATOM     24  C   THR A   4      46.642 -50.532  37.242  1.00 41.19           C  
ATOM     25  O   THR A   4      45.574 -50.070  37.544  1.00 43.09           O  
ATOM     26  CB  THR A   4      47.504 -52.100  38.932  1.00 36.06           C  
ATOM     27  OG1 THR A   4      46.437 -52.795  38.277  1.00 37.12           O  
ATOM     28  CG2 THR A   4      47.254 -52.006  40.381  1.00 32.22           C  
ATOM     29  N   GLU A   5      46.933 -50.895  36.003  1.00 44.24           N  
ATOM     30  CA  GLU A   5      46.016 -50.574  34.931  1.00 41.70           C  
ATOM     31  C   GLU A   5      45.515 -51.759  34.144  1.00 49.23           C  
ATOM     32  O   GLU A   5      46.077 -52.841  34.209  1.00 56.57           O  
ATOM     33  CB  GLU A   5      46.610 -49.527  34.004  1.00 46.13           C  
ATOM     34  CG  GLU A   5      47.664 -50.009  33.073  1.00 49.64           C  
ATOM     35  CD  GLU A   5      48.719 -48.933  32.781  1.00 55.68           C  
ATOM     36  OE1 GLU A   5      48.349 -47.815  32.388  1.00 49.61           O  
ATOM     37  OE2 GLU A   5      49.928 -49.203  32.962  1.00 65.46           O  
ATOM     38  N   GLY A   6      44.439 -51.531  33.395  1.00 51.35           N  
ATOM     39  CA  GLY A   6      43.687 -52.579  32.729  1.00 50.38           C  
ATOM     40  C   GLY A   6      43.120 -52.032  31.446  1.00 47.14           C  
ATOM     41  O   GLY A   6      43.336 -50.878  31.120  1.00 50.18           O  
ATOM     42  N   PRO A   7      42.446 -52.881  30.677  1.00 45.80           N  
ATOM     43  CA  PRO A   7      41.865 -52.390  29.433  1.00 50.09           C  
ATOM     44  C   PRO A   7      40.846 -51.239  29.621  1.00 55.39           C  
ATOM     45  O   PRO A   7      40.918 -50.229  28.903  1.00 53.92           O  
ATOM     46  CB  PRO A   7      41.231 -53.652  28.834  1.00 48.14           C  
ATOM     47  CG  PRO A   7      42.074 -54.767  29.383  1.00 46.23           C  
ATOM     48  CD  PRO A   7      42.408 -54.347  30.774  1.00 46.52           C  
ATOM     49  N   ASN A   8      39.899 -51.388  30.545  1.00 49.44           N  
ATOM     50  CA  ASN A   8      38.992 -50.277  30.892  1.00 48.01           C  
ATOM     51  C   ASN A   8      39.162 -49.386  32.121  1.00 47.91           C  
ATOM     52  O   ASN A   8      38.248 -48.648  32.429  1.00 49.73           O  
ATOM     53  CB  ASN A   8      37.545 -50.687  30.688  1.00 43.96           C  
ATOM     54  CG  ASN A   8      37.301 -51.095  29.277  1.00 46.48           C  
ATOM     55  OD1 ASN A   8      37.736 -50.419  28.342  1.00 40.54           O  
ATOM     56  ND2 ASN A   8      36.654 -52.236  29.099  1.00 50.32           N  
ATOM     57  N   PHE A   9      40.237 -49.540  32.887  1.00 48.13           N  
ATOM     58  CA  PHE A   9      40.343 -48.812  34.158  1.00 46.08           C  
ATOM     59  C   PHE A   9      41.780 -48.412  34.559  1.00 52.50           C  
ATOM     60  O   PHE A   9      42.762 -48.697  33.846  1.00 51.21           O  
ATOM     61  CB  PHE A   9      39.790 -49.667  35.286  1.00 48.30           C  
ATOM     62  CG  PHE A   9      40.509 -50.988  35.434  1.00 51.43           C  
ATOM     63  CD1 PHE A   9      40.098 -52.091  34.705  1.00 47.62           C  
ATOM     64  CD2 PHE A   9      41.602 -51.119  36.278  1.00 49.45           C  
ATOM     65  CE1 PHE A   9      40.738 -53.287  34.816  1.00 48.85           C  
ATOM     66  CE2 PHE A   9      42.255 -52.322  36.388  1.00 52.78           C  
ATOM     67  CZ  PHE A   9      41.815 -53.417  35.653  1.00 50.80           C  
ATOM     68  N   TYR A  10      41.869 -47.665  35.657  1.00 46.98           N  
ATOM     69  CA  TYR A  10      43.102 -47.459  36.361  1.00 42.37           C  
ATOM     70  C   TYR A  10      42.829 -47.516  37.856  1.00 40.43           C  
ATOM     71  O   TYR A  10      42.193 -46.615  38.398  1.00 42.43           O  
ATOM     72  CB  TYR A  10      43.664 -46.080  35.970  1.00 49.21           C  
ATOM     73  CG  TYR A  10      44.910 -45.643  36.727  1.00 50.44           C  
ATOM     74  CD1 TYR A  10      46.174 -46.129  36.375  1.00 44.80           C  
ATOM     75  CD2 TYR A  10      44.817 -44.744  37.789  1.00 45.51           C  
ATOM     76  CE1 TYR A  10      47.292 -45.750  37.065  1.00 46.27           C  
ATOM     77  CE2 TYR A  10      45.929 -44.364  38.491  1.00 50.02           C  
ATOM     78  CZ  TYR A  10      47.172 -44.862  38.129  1.00 53.91           C  
ATOM     79  OH  TYR A  10      48.292 -44.439  38.843  1.00 55.91           O  
ATOM     80  N   VAL A  11      43.391 -48.488  38.556  1.00 39.55           N  
ATOM     81  CA  VAL A  11      43.226 -48.528  40.005  1.00 40.17           C  
ATOM     82  C   VAL A  11      44.370 -47.771  40.670  1.00 48.04           C  
ATOM     83  O   VAL A  11      45.551 -48.035  40.415  1.00 47.25           O  
ATOM     84  CB  VAL A  11      43.129 -49.970  40.563  1.00 41.88           C  
ATOM     85  CG1 VAL A  11      43.112 -49.951  42.091  1.00 39.82           C  
ATOM     86  CG2 VAL A  11      41.897 -50.670  40.012  1.00 40.00           C  
ATOM     87  N   PRO A  12      44.029 -46.799  41.520  1.00 51.53           N  
ATOM     88  CA  PRO A  12      45.059 -45.987  42.187  1.00 47.01           C  
ATOM     89  C   PRO A  12      45.790 -46.732  43.300  1.00 45.46           C  
ATOM     90  O   PRO A  12      45.823 -46.246  44.425  1.00 49.19           O  
ATOM     91  CB  PRO A  12      44.247 -44.870  42.835  1.00 45.03           C  
ATOM     92  CG  PRO A  12      42.934 -44.886  42.156  1.00 48.20           C  
ATOM     93  CD  PRO A  12      42.673 -46.277  41.736  1.00 44.53           C  
ATOM     94  N   PHE A  13      46.342 -47.897  43.017  1.00 40.47           N  
ATOM     95  CA  PHE A  13      47.027 -48.648  44.053  1.00 44.51           C  
ATOM     96  C   PHE A  13      48.081 -49.541  43.411  1.00 51.03           C  
ATOM     97  O   PHE A  13      47.862 -49.996  42.297  1.00 49.22           O  
ATOM     98  CB  PHE A  13      46.011 -49.503  44.783  1.00 42.98           C  
ATOM     99  CG  PHE A  13      46.504 -50.080  46.060  1.00 42.30           C  
ATOM    100  CD1 PHE A  13      46.391 -49.368  47.235  1.00 38.65           C  
ATOM    101  CD2 PHE A  13      47.045 -51.353  46.094  1.00 41.67           C  
ATOM    102  CE1 PHE A  13      46.822 -49.903  48.427  1.00 41.20           C  
ATOM    103  CE2 PHE A  13      47.472 -51.895  47.277  1.00 40.27           C  
ATOM    104  CZ  PHE A  13      47.361 -51.168  48.450  1.00 42.36           C  
ATOM    105  N   SER A  14      49.197 -49.831  44.085  1.00 52.02           N  
ATOM    106  CA  SER A  14      50.213 -50.690  43.455  1.00 52.09           C  
ATOM    107  C   SER A  14      49.947 -52.206  43.570  1.00 50.27           C  
ATOM    108  O   SER A  14      49.550 -52.697  44.626  1.00 49.13           O  
ATOM    109  CB  SER A  14      51.602 -50.369  43.981  1.00 51.67           C  
ATOM    110  OG  SER A  14      52.557 -51.189  43.346  1.00 52.32           O  
ATOM    111  N   ASN A  15      50.179 -52.943  42.481  1.00 47.83           N  
ATOM    112  CA  ASN A  15      49.981 -54.401  42.462  1.00 40.95           C  
ATOM    113  C   ASN A  15      51.217 -55.202  42.846  1.00 48.00           C  
ATOM    114  O   ASN A  15      51.261 -56.425  42.686  1.00 47.79           O  
ATOM    115  CB  ASN A  15      49.401 -54.901  41.138  1.00 37.75           C  
ATOM    116  CG  ASN A  15      48.425 -56.033  41.345  1.00 38.85           C  
ATOM    117  OD1 ASN A  15      48.156 -56.421  42.488  1.00 33.44           O  
ATOM    118  ND2 ASN A  15      47.869 -56.558  40.250  1.00 39.98           N  
ATOM    119  N   LYS A  16      52.243 -54.496  43.292  1.00 48.30           N  
ATOM    120  CA  LYS A  16      53.439 -55.143  43.777  1.00 49.55           C  
ATOM    121  C   LYS A  16      53.112 -56.223  44.823  1.00 51.04           C  
ATOM    122  O   LYS A  16      53.848 -57.203  44.941  1.00 51.56           O  
ATOM    123  CB  LYS A  16      54.420 -54.109  44.337  1.00 51.25           C  
ATOM    124  CG  LYS A  16      54.145 -53.702  45.770  1.00 57.24           C  
ATOM    125  CD  LYS A  16      55.068 -52.578  46.183  1.00 67.63           C  
ATOM    126  CE  LYS A  16      54.402 -51.669  47.219  1.00 81.08           C  
ATOM    127  NZ  LYS A  16      54.856 -50.239  47.082  1.00 80.95           N  
ATOM    128  N   THR A  17      52.014 -56.073  45.558  1.00 44.96           N  
ATOM    129  CA  THR A  17      51.588 -57.137  46.467  1.00 45.74           C  
ATOM    130  C   THR A  17      50.631 -58.163  45.843  1.00 45.68           C  
ATOM    131  O   THR A  17      50.189 -59.091  46.515  1.00 46.55           O  
ATOM    132  CB  THR A  17      50.970 -56.597  47.773  1.00 49.00           C  
ATOM    133  OG1 THR A  17      49.956 -55.625  47.472  1.00 52.42           O  
ATOM    134  CG2 THR A  17      52.045 -55.984  48.654  1.00 41.92           C  
ATOM    135  N   GLY A  18      50.320 -57.996  44.563  1.00 45.48           N  
ATOM    136  CA  GLY A  18      49.417 -58.899  43.871  1.00 43.09           C  
ATOM    137  C   GLY A  18      47.944 -58.866  44.262  1.00 45.18           C  
ATOM    138  O   GLY A  18      47.185 -59.675  43.745  1.00 45.59           O  
ATOM    139  N   VAL A  19      47.533 -57.944  45.145  1.00 47.38           N  
ATOM    140  CA  VAL A  19      46.138 -57.870  45.667  1.00 48.02           C  
ATOM    141  C   VAL A  19      45.080 -57.157  44.793  1.00 40.86           C  
ATOM    142  O   VAL A  19      43.887 -57.349  44.958  1.00 40.45           O  
ATOM    143  CB  VAL A  19      46.079 -57.221  47.082  1.00 41.81           C  
ATOM    144  CG1 VAL A  19      47.065 -57.893  48.020  1.00 37.45           C  
ATOM    145  CG2 VAL A  19      46.313 -55.724  46.992  1.00 38.57           C  
ATOM    146  N   VAL A  20      45.537 -56.318  43.883  1.00 42.36           N  
ATOM    147  CA  VAL A  20      44.652 -55.487  43.096  1.00 41.82           C  
ATOM    148  C   VAL A  20      43.794 -56.273  42.116  1.00 40.30           C  
ATOM    149  O   VAL A  20      44.302 -57.115  41.375  1.00 36.10           O  
ATOM    150  CB  VAL A  20      45.426 -54.376  42.357  1.00 36.76           C  
ATOM    151  CG1 VAL A  20      44.502 -53.655  41.375  1.00 37.11           C  
ATOM    152  CG2 VAL A  20      46.035 -53.428  43.376  1.00 35.27           C  
ATOM    153  N   ARG A  21      42.493 -55.954  42.117  1.00 41.18           N  
ATOM    154  CA  ARG A  21      41.523 -56.550  41.204  1.00 43.78           C  
ATOM    155  C   ARG A  21      40.831 -55.503  40.328  1.00 41.86           C  
ATOM    156  O   ARG A  21      40.859 -54.317  40.628  1.00 41.11           O  
ATOM    157  CB  ARG A  21      40.474 -57.331  41.994  1.00 44.45           C  
ATOM    158  CG  ARG A  21      41.055 -58.269  43.023  1.00 45.38           C  
ATOM    159  CD  ARG A  21      41.647 -59.525  42.404  1.00 39.91           C  
ATOM    160  NE  ARG A  21      42.258 -60.347  43.442  1.00 44.63           N  
ATOM    161  CZ  ARG A  21      43.562 -60.568  43.561  1.00 48.19           C  
ATOM    162  NH1 ARG A  21      44.409 -60.048  42.685  1.00 46.11           N  
ATOM    163  NH2 ARG A  21      44.018 -61.316  44.554  1.00 47.16           N  
ATOM    164  N   SER A  22      40.245 -55.963  39.224  1.00 41.87           N  
ATOM    165  CA  SER A  22      39.370 -55.165  38.373  1.00 40.28           C  
ATOM    166  C   SER A  22      38.283 -54.543  39.234  1.00 42.77           C  
ATOM    167  O   SER A  22      37.637 -55.242  40.019  1.00 40.25           O  
ATOM    168  CB  SER A  22      38.723 -56.075  37.327  1.00 40.09           C  
ATOM    169  OG  SER A  22      38.068 -55.399  36.272  1.00 37.40           O  
ATOM    170  N   PRO A  23      38.075 -53.217  39.095  1.00 45.73           N  
ATOM    171  CA  PRO A  23      36.982 -52.515  39.790  1.00 46.46           C  
ATOM    172  C   PRO A  23      35.590 -52.958  39.271  1.00 43.37           C  
ATOM    173  O   PRO A  23      34.575 -52.682  39.899  1.00 38.71           O  
ATOM    174  CB  PRO A  23      37.241 -51.032  39.473  1.00 43.80           C  
ATOM    175  CG  PRO A  23      38.561 -50.980  38.771  1.00 48.03           C  
ATOM    176  CD  PRO A  23      38.799 -52.327  38.174  1.00 45.28           C  
ATOM    177  N   PHE A  24      35.571 -53.614  38.116  1.00 40.29           N  
ATOM    178  CA  PHE A  24      34.383 -54.237  37.570  1.00 42.18           C  
ATOM    179  C   PHE A  24      34.141 -55.671  38.072  1.00 44.05           C  
ATOM    180  O   PHE A  24      33.151 -56.299  37.695  1.00 44.29           O  
ATOM    181  CB  PHE A  24      34.484 -54.278  36.045  1.00 41.95           C  
ATOM    182  CG  PHE A  24      34.650 -52.941  35.419  1.00 46.71           C  
ATOM    183  CD1 PHE A  24      33.957 -51.843  35.909  1.00 50.48           C  
ATOM    184  CD2 PHE A  24      35.514 -52.761  34.346  1.00 48.46           C  
ATOM    185  CE1 PHE A  24      34.109 -50.584  35.323  1.00 48.67           C  
ATOM    186  CE2 PHE A  24      35.678 -51.515  33.758  1.00 48.27           C  
ATOM    187  CZ  PHE A  24      34.972 -50.427  34.248  1.00 51.19           C  
ATOM    188  N   GLU A  25      35.043 -56.182  38.913  1.00 43.00           N  
ATOM    189  CA  GLU A  25      35.039 -57.591  39.332  1.00 41.12           C  
ATOM    190  C   GLU A  25      34.922 -57.861  40.843  1.00 42.26           C  
ATOM    191  O   GLU A  25      34.061 -58.604  41.272  1.00 49.48           O  
ATOM    192  CB  GLU A  25      36.162 -58.389  38.678  1.00 43.97           C  
ATOM    193  CG  GLU A  25      36.141 -58.454  37.152  1.00 46.76           C  
ATOM    194  CD  GLU A  25      34.782 -58.803  36.535  1.00 55.69           C  
ATOM    195  OE1 GLU A  25      33.942 -59.486  37.185  1.00 55.63           O  
ATOM    196  OE2 GLU A  25      34.560 -58.388  35.368  1.00 59.44           O  
ATOM    197  N   ALA A  26      35.859 -57.374  41.629  1.00 42.97           N  
ATOM    198  CA  ALA A  26      35.815 -57.616  43.073  1.00 41.66           C  
ATOM    199  C   ALA A  26      36.054 -56.338  43.888  1.00 44.31           C  
ATOM    200  O   ALA A  26      36.587 -55.350  43.363  1.00 42.47           O  
ATOM    201  CB  ALA A  26      36.887 -58.689  43.458  1.00 49.59           C  
ATOM    202  N   PRO A  27      35.675 -56.356  45.181  1.00 44.14           N  
ATOM    203  CA  PRO A  27      35.899 -55.242  46.112  1.00 42.38           C  
ATOM    204  C   PRO A  27      37.315 -54.668  46.165  1.00 43.70           C  
ATOM    205  O   PRO A  27      38.337 -55.362  46.048  1.00 47.95           O  
ATOM    206  CB  PRO A  27      35.551 -55.855  47.462  1.00 41.25           C  
ATOM    207  CG  PRO A  27      34.510 -56.825  47.150  1.00 44.28           C  
ATOM    208  CD  PRO A  27      34.789 -57.372  45.773  1.00 42.01           C  
ATOM    209  N   GLN A  28      37.315 -53.354  46.359  1.00 40.65           N  
ATOM    210  CA  GLN A  28      38.472 -52.473  46.434  1.00 38.24           C  
ATOM    211  C   GLN A  28      39.029 -52.199  47.836  1.00 42.81           C  
ATOM    212  O   GLN A  28      39.697 -51.209  48.026  1.00 43.35           O  
ATOM    213  CB  GLN A  28      38.271 -51.229  45.576  1.00 38.26           C  
ATOM    214  CG  GLN A  28      37.837 -51.581  44.157  1.00 44.92           C  
ATOM    215  CD  GLN A  28      38.937 -52.240  43.332  1.00 45.16           C  
ATOM    216  OE1 GLN A  28      40.041 -51.694  43.217  1.00 46.55           O  
ATOM    217  NE2 GLN A  28      38.637 -53.405  42.740  1.00 40.60           N  
ATOM    218  N   TYR A  29      38.618 -52.981  48.834  1.00 39.65           N  
ATOM    219  CA  TYR A  29      38.905 -52.692  50.243  1.00 38.59           C  
ATOM    220  C   TYR A  29      40.382 -52.514  50.563  1.00 39.70           C  
ATOM    221  O   TYR A  29      40.743 -52.146  51.677  1.00 45.83           O  
ATOM    222  CB  TYR A  29      38.310 -53.772  51.148  1.00 36.91           C  
ATOM    223  CG  TYR A  29      36.804 -53.890  50.996  1.00 39.55           C  
ATOM    224  CD1 TYR A  29      36.000 -52.753  51.058  1.00 41.40           C  
ATOM    225  CD2 TYR A  29      36.189 -55.116  50.774  1.00 30.91           C  
ATOM    226  CE1 TYR A  29      34.639 -52.832  50.913  1.00 39.93           C  
ATOM    227  CE2 TYR A  29      34.826 -55.205  50.630  1.00 33.61           C  
ATOM    228  CZ  TYR A  29      34.049 -54.061  50.702  1.00 40.70           C  
ATOM    229  OH  TYR A  29      32.678 -54.118  50.558  1.00 37.91           O  
ATOM    230  N   TYR A  30      41.250 -52.835  49.620  1.00 37.61           N  
ATOM    231  CA  TYR A  30      42.641 -52.379  49.720  1.00 41.98           C  
ATOM    232  C   TYR A  30      42.876 -50.871  49.402  1.00 44.77           C  
ATOM    233  O   TYR A  30      43.831 -50.275  49.898  1.00 46.08           O  
ATOM    234  CB  TYR A  30      43.551 -53.223  48.855  1.00 37.02           C  
ATOM    235  CG  TYR A  30      43.109 -53.294  47.429  1.00 37.45           C  
ATOM    236  CD1 TYR A  30      42.244 -54.282  47.013  1.00 32.20           C  
ATOM    237  CD2 TYR A  30      43.557 -52.371  46.497  1.00 38.56           C  
ATOM    238  CE1 TYR A  30      41.848 -54.366  45.715  1.00 34.32           C  
ATOM    239  CE2 TYR A  30      43.157 -52.444  45.188  1.00 37.92           C  
ATOM    240  CZ  TYR A  30      42.306 -53.450  44.802  1.00 37.85           C  
ATOM    241  OH  TYR A  30      41.914 -53.537  43.490  1.00 39.43           O  
ATOM    242  N   LEU A  31      42.034 -50.276  48.556  1.00 43.64           N  
ATOM    243  CA  LEU A  31      42.057 -48.835  48.315  1.00 43.51           C  
ATOM    244  C   LEU A  31      41.655 -48.093  49.567  1.00 44.86           C  
ATOM    245  O   LEU A  31      42.254 -47.079  49.899  1.00 52.18           O  
ATOM    246  CB  LEU A  31      41.064 -48.437  47.228  1.00 45.04           C  
ATOM    247  CG  LEU A  31      41.381 -48.723  45.771  1.00 47.90           C  
ATOM    248  CD1 LEU A  31      40.268 -48.160  44.913  1.00 46.70           C  
ATOM    249  CD2 LEU A  31      42.699 -48.085  45.416  1.00 50.11           C  
ATOM    250  N   ALA A  32      40.597 -48.565  50.224  1.00 46.02           N  
ATOM    251  CA  ALA A  32      40.112 -47.949  51.460  1.00 45.27           C  
ATOM    252  C   ALA A  32      39.346 -48.959  52.310  1.00 41.40           C  
ATOM    253  O   ALA A  32      38.721 -49.861  51.765  1.00 38.11           O  
ATOM    254  CB  ALA A  32      39.227 -46.707  51.132  1.00 39.24           C  
ATOM    255  N   GLU A  33      39.344 -48.756  53.627  1.00 38.43           N  
ATOM    256  CA  GLU A  33      38.656 -49.628  54.566  1.00 39.25           C  
ATOM    257  C   GLU A  33      37.192 -49.747  54.168  1.00 44.38           C  
ATOM    258  O   GLU A  33      36.690 -48.913  53.433  1.00 46.80           O  
ATOM    259  CB  GLU A  33      38.750 -49.057  55.973  1.00 42.22           C  
ATOM    260  CG  GLU A  33      40.120 -49.158  56.595  1.00 45.25           C  
ATOM    261  CD  GLU A  33      40.507 -50.593  56.912  1.00 66.70           C  
ATOM    262  OE1 GLU A  33      39.695 -51.297  57.567  1.00 72.46           O  
ATOM    263  OE2 GLU A  33      41.616 -51.027  56.508  1.00 74.38           O  
ATOM    264  N   PRO A  34      36.506 -50.822  54.585  1.00 43.79           N  
ATOM    265  CA  PRO A  34      35.098 -50.855  54.202  1.00 42.18           C  
ATOM    266  C   PRO A  34      34.241 -49.727  54.816  1.00 42.57           C  
ATOM    267  O   PRO A  34      33.359 -49.242  54.116  1.00 44.25           O  
ATOM    268  CB  PRO A  34      34.652 -52.233  54.692  1.00 32.37           C  
ATOM    269  CG  PRO A  34      35.836 -53.015  54.625  1.00 31.69           C  
ATOM    270  CD  PRO A  34      36.913 -52.122  55.128  1.00 37.28           C  
ATOM    271  N   TRP A  35      34.494 -49.311  56.058  1.00 43.33           N  
ATOM    272  CA  TRP A  35      33.681 -48.261  56.676  1.00 41.16           C  
ATOM    273  C   TRP A  35      33.706 -46.987  55.855  1.00 42.40           C  
ATOM    274  O   TRP A  35      32.722 -46.271  55.784  1.00 43.53           O  
ATOM    275  CB  TRP A  35      34.074 -47.979  58.133  1.00 39.61           C  
ATOM    276  CG  TRP A  35      35.422 -47.334  58.335  1.00 48.27           C  
ATOM    277  CD1 TRP A  35      36.591 -47.960  58.679  1.00 46.86           C  
ATOM    278  CD2 TRP A  35      35.736 -45.934  58.235  1.00 52.49           C  
ATOM    279  NE1 TRP A  35      37.602 -47.041  58.794  1.00 49.98           N  
ATOM    280  CE2 TRP A  35      37.107 -45.791  58.525  1.00 49.62           C  
ATOM    281  CE3 TRP A  35      34.990 -44.786  57.927  1.00 49.36           C  
ATOM    282  CZ2 TRP A  35      37.744 -44.559  58.511  1.00 45.25           C  
ATOM    283  CZ3 TRP A  35      35.629 -43.566  57.928  1.00 46.21           C  
ATOM    284  CH2 TRP A  35      36.987 -43.464  58.215  1.00 45.12           C  
ATOM    285  N   GLN A  36      34.840 -46.711  55.233  1.00 44.47           N  
ATOM    286  CA  GLN A  36      34.949 -45.603  54.316  1.00 41.16           C  
ATOM    287  C   GLN A  36      34.086 -45.828  53.084  1.00 41.59           C  
ATOM    288  O   GLN A  36      33.678 -44.880  52.436  1.00 43.43           O  
ATOM    289  CB  GLN A  36      36.392 -45.431  53.904  1.00 39.85           C  
ATOM    290  CG  GLN A  36      37.309 -45.233  55.079  1.00 42.81           C  
ATOM    291  CD  GLN A  36      38.747 -45.037  54.647  1.00 44.13           C  
ATOM    292  OE1 GLN A  36      39.344 -45.897  54.010  1.00 39.47           O  
ATOM    293  NE2 GLN A  36      39.299 -43.886  54.969  1.00 48.76           N  
ATOM    294  N   PHE A  37      33.794 -47.076  52.742  1.00 42.37           N  
ATOM    295  CA  PHE A  37      32.875 -47.316  51.628  1.00 42.47           C  
ATOM    296  C   PHE A  37      31.427 -47.037  52.056  1.00 41.66           C  
ATOM    297  O   PHE A  37      30.601 -46.553  51.268  1.00 39.57           O  
ATOM    298  CB  PHE A  37      33.043 -48.722  51.054  1.00 34.62           C  
ATOM    299  CG  PHE A  37      34.076 -48.804  49.983  1.00 43.03           C  
ATOM    300  CD1 PHE A  37      33.729 -48.598  48.655  1.00 41.64           C  
ATOM    301  CD2 PHE A  37      35.412 -49.074  50.296  1.00 44.65           C  
ATOM    302  CE1 PHE A  37      34.708 -48.672  47.652  1.00 43.92           C  
ATOM    303  CE2 PHE A  37      36.392 -49.142  49.294  1.00 43.95           C  
ATOM    304  CZ  PHE A  37      36.036 -48.939  47.973  1.00 42.94           C  
ATOM    305  N   SER A  38      31.156 -47.336  53.321  1.00 36.51           N  
ATOM    306  CA  SER A  38      29.888 -47.060  53.960  1.00 38.77           C  
ATOM    307  C   SER A  38      29.603 -45.559  54.087  1.00 40.28           C  
ATOM    308  O   SER A  38      28.446 -45.115  53.929  1.00 35.05           O  
ATOM    309  CB  SER A  38      29.913 -47.642  55.358  1.00 35.95           C  
ATOM    310  OG  SER A  38      29.915 -49.025  55.291  1.00 34.00           O  
ATOM    311  N   MET A  39      30.659 -44.815  54.425  1.00 38.72           N  
ATOM    312  CA  MET A  39      30.619 -43.384  54.594  1.00 33.77           C  
ATOM    313  C   MET A  39      30.349 -42.748  53.276  1.00 35.21           C  
ATOM    314  O   MET A  39      29.572 -41.799  53.184  1.00 32.10           O  
ATOM    315  CB  MET A  39      31.949 -42.881  55.094  1.00 34.93           C  
ATOM    316  CG  MET A  39      32.065 -42.891  56.580  1.00 43.32           C  
ATOM    317  SD  MET A  39      30.442 -42.860  57.352  1.00 46.87           S  
ATOM    318  CE  MET A  39      29.893 -41.160  57.111  1.00 35.54           C  
ATOM    319  N   LEU A  40      30.995 -43.270  52.246  1.00 34.68           N  
ATOM    320  CA  LEU A  40      30.753 -42.766  50.919  1.00 35.30           C  
ATOM    321  C   LEU A  40      29.287 -42.983  50.619  1.00 39.42           C  
ATOM    322  O   LEU A  40      28.625 -42.085  50.107  1.00 40.51           O  
ATOM    323  CB  LEU A  40      31.617 -43.481  49.904  1.00 36.78           C  
ATOM    324  CG  LEU A  40      31.117 -43.438  48.461  1.00 37.91           C  
ATOM    325  CD1 LEU A  40      31.142 -42.059  47.884  1.00 31.14           C  
ATOM    326  CD2 LEU A  40      31.949 -44.391  47.603  1.00 46.21           C  
ATOM    327  N   ALA A  41      28.778 -44.169  50.972  1.00 40.40           N  
ATOM    328  CA  ALA A  41      27.368 -44.522  50.791  1.00 35.65           C  
ATOM    329  C   ALA A  41      26.491 -43.630  51.647  1.00 34.90           C  
ATOM    330  O   ALA A  41      25.515 -43.085  51.155  1.00 37.53           O  
ATOM    331  CB  ALA A  41      27.122 -45.990  51.130  1.00 31.27           C  
ATOM    332  N   ALA A  42      26.833 -43.482  52.922  1.00 30.21           N  
ATOM    333  CA  ALA A  42      26.171 -42.493  53.750  1.00 31.74           C  
ATOM    334  C   ALA A  42      26.131 -41.111  53.054  1.00 39.06           C  
ATOM    335  O   ALA A  42      25.066 -40.452  53.004  1.00 37.24           O  
ATOM    336  CB  ALA A  42      26.820 -42.390  55.118  1.00 29.74           C  
ATOM    337  N   TYR A  43      27.254 -40.663  52.499  1.00 38.48           N  
ATOM    338  CA  TYR A  43      27.190 -39.388  51.810  1.00 38.17           C  
ATOM    339  C   TYR A  43      26.195 -39.437  50.642  1.00 37.45           C  
ATOM    340  O   TYR A  43      25.341 -38.562  50.521  1.00 39.95           O  
ATOM    341  CB  TYR A  43      28.560 -38.867  51.368  1.00 34.53           C  
ATOM    342  CG  TYR A  43      28.523 -37.376  51.156  1.00 36.57           C  
ATOM    343  CD1 TYR A  43      28.400 -36.516  52.243  1.00 41.39           C  
ATOM    344  CD2 TYR A  43      28.555 -36.823  49.873  1.00 37.28           C  
ATOM    345  CE1 TYR A  43      28.338 -35.138  52.073  1.00 40.61           C  
ATOM    346  CE2 TYR A  43      28.493 -35.448  49.688  1.00 40.55           C  
ATOM    347  CZ  TYR A  43      28.387 -34.611  50.800  1.00 44.79           C  
ATOM    348  OH  TYR A  43      28.321 -33.240  50.666  1.00 47.60           O  
ATOM    349  N   MET A  44      26.284 -40.456  49.800  1.00 34.31           N  
ATOM    350  CA  MET A  44      25.306 -40.589  48.722  1.00 40.35           C  
ATOM    351  C   MET A  44      23.855 -40.594  49.249  1.00 42.32           C  
ATOM    352  O   MET A  44      22.934 -40.075  48.580  1.00 40.12           O  
ATOM    353  CB  MET A  44      25.567 -41.837  47.864  1.00 40.86           C  
ATOM    354  CG  MET A  44      26.852 -41.809  47.061  1.00 40.13           C  
ATOM    355  SD  MET A  44      27.062 -40.341  46.045  1.00 40.20           S  
ATOM    356  CE  MET A  44      28.118 -39.359  47.116  1.00 35.80           C  
ATOM    357  N   PHE A  45      23.663 -41.162  50.447  1.00 38.17           N  
ATOM    358  CA  PHE A  45      22.350 -41.160  51.084  1.00 40.06           C  
ATOM    359  C   PHE A  45      21.852 -39.713  51.356  1.00 39.96           C  
ATOM    360  O   PHE A  45      20.727 -39.333  50.975  1.00 37.47           O  
ATOM    361  CB  PHE A  45      22.319 -42.016  52.368  1.00 33.36           C  
ATOM    362  CG  PHE A  45      20.903 -42.328  52.844  1.00 38.41           C  
ATOM    363  CD1 PHE A  45      19.929 -42.744  51.934  1.00 33.52           C  
ATOM    364  CD2 PHE A  45      20.533 -42.183  54.183  1.00 36.97           C  
ATOM    365  CE1 PHE A  45      18.653 -43.010  52.344  1.00 25.29           C  
ATOM    366  CE2 PHE A  45      19.227 -42.464  54.588  1.00 29.69           C  
ATOM    367  CZ  PHE A  45      18.310 -42.871  53.663  1.00 26.10           C  
ATOM    368  N   LEU A  46      22.703 -38.932  52.018  1.00 36.05           N  
ATOM    369  CA  LEU A  46      22.439 -37.530  52.299  1.00 36.63           C  
ATOM    370  C   LEU A  46      21.982 -36.788  51.050  1.00 38.54           C  
ATOM    371  O   LEU A  46      20.998 -36.063  51.075  1.00 38.04           O  
ATOM    372  CB  LEU A  46      23.708 -36.849  52.833  1.00 39.06           C  
ATOM    373  CG  LEU A  46      23.518 -35.503  53.533  1.00 37.99           C  
ATOM    374  CD1 LEU A  46      22.381 -35.669  54.509  1.00 37.26           C  
ATOM    375  CD2 LEU A  46      24.763 -35.019  54.265  1.00 32.23           C  
ATOM    376  N   LEU A  47      22.712 -36.959  49.956  1.00 39.81           N  
ATOM    377  CA  LEU A  47      22.471 -36.149  48.773  1.00 40.35           C  
ATOM    378  C   LEU A  47      21.179 -36.530  48.104  1.00 36.48           C  
ATOM    379  O   LEU A  47      20.573 -35.704  47.472  1.00 37.98           O  
ATOM    380  CB  LEU A  47      23.639 -36.230  47.776  1.00 42.95           C  
ATOM    381  CG  LEU A  47      25.026 -35.703  48.203  1.00 42.56           C  
ATOM    382  CD1 LEU A  47      25.944 -35.735  47.015  1.00 45.32           C  
ATOM    383  CD2 LEU A  47      24.991 -34.294  48.790  1.00 41.57           C  
ATOM    384  N   ILE A  48      20.757 -37.784  48.241  1.00 41.74           N  
ATOM    385  CA  ILE A  48      19.475 -38.215  47.675  1.00 41.48           C  
ATOM    386  C   ILE A  48      18.346 -37.697  48.557  1.00 41.15           C  
ATOM    387  O   ILE A  48      17.359 -37.138  48.072  1.00 37.04           O  
ATOM    388  CB  ILE A  48      19.357 -39.758  47.590  1.00 39.42           C  
ATOM    389  CG1 ILE A  48      20.477 -40.354  46.719  1.00 38.70           C  
ATOM    390  CG2 ILE A  48      17.970 -40.149  47.057  1.00 32.26           C  
ATOM    391  CD1 ILE A  48      20.700 -41.879  46.881  1.00 35.87           C  
ATOM    392  N   MET A  49      18.520 -37.891  49.862  1.00 41.48           N  
ATOM    393  CA  MET A  49      17.538 -37.496  50.846  1.00 38.08           C  
ATOM    394  C   MET A  49      17.249 -36.009  50.800  1.00 40.72           C  
ATOM    395  O   MET A  49      16.100 -35.619  50.901  1.00 44.66           O  
ATOM    396  CB  MET A  49      17.960 -37.952  52.247  1.00 37.24           C  
ATOM    397  CG  MET A  49      17.797 -39.451  52.494  1.00 41.31           C  
ATOM    398  SD  MET A  49      16.100 -40.128  52.385  1.00 38.13           S  
ATOM    399  CE  MET A  49      15.979 -40.512  50.637  1.00 37.44           C  
ATOM    400  N   LEU A  50      18.286 -35.181  50.692  1.00 40.08           N  
ATOM    401  CA  LEU A  50      18.106 -33.760  50.415  1.00 34.77           C  
ATOM    402  C   LEU A  50      17.894 -33.452  48.922  1.00 39.67           C  
ATOM    403  O   LEU A  50      17.027 -32.691  48.565  1.00 43.47           O  
ATOM    404  CB  LEU A  50      19.272 -32.943  50.972  1.00 31.88           C  
ATOM    405  CG  LEU A  50      19.614 -33.210  52.442  1.00 36.86           C  
ATOM    406  CD1 LEU A  50      20.734 -32.304  52.992  1.00 31.14           C  
ATOM    407  CD2 LEU A  50      18.372 -33.158  53.305  1.00 30.76           C  
ATOM    408  N   GLY A  51      18.668 -34.052  48.039  1.00 39.76           N  
ATOM    409  CA  GLY A  51      18.644 -33.629  46.655  1.00 33.21           C  
ATOM    410  C   GLY A  51      17.334 -33.848  45.951  1.00 37.07           C  
ATOM    411  O   GLY A  51      16.944 -33.027  45.137  1.00 42.31           O  
ATOM    412  N   PHE A  52      16.683 -34.978  46.227  1.00 40.80           N  
ATOM    413  CA  PHE A  52      15.416 -35.330  45.579  1.00 38.52           C  
ATOM    414  C   PHE A  52      14.223 -34.481  45.994  1.00 39.13           C  
ATOM    415  O   PHE A  52      13.541 -33.951  45.127  1.00 40.83           O  
ATOM    416  CB  PHE A  52      15.072 -36.820  45.735  1.00 38.58           C  
ATOM    417  CG  PHE A  52      13.730 -37.178  45.165  1.00 37.18           C  
ATOM    418  CD1 PHE A  52      13.578 -37.362  43.801  1.00 38.44           C  
ATOM    419  CD2 PHE A  52      12.608 -37.284  45.980  1.00 35.09           C  
ATOM    420  CE1 PHE A  52      12.330 -37.671  43.259  1.00 38.66           C  
ATOM    421  CE2 PHE A  52      11.367 -37.587  45.439  1.00 35.20           C  
ATOM    422  CZ  PHE A  52      11.233 -37.785  44.081  1.00 34.56           C  
ATOM    423  N   PRO A  53      13.951 -34.365  47.312  1.00 41.10           N  
ATOM    424  CA  PRO A  53      12.763 -33.582  47.641  1.00 42.10           C  
ATOM    425  C   PRO A  53      12.883 -32.184  47.092  1.00 43.75           C  
ATOM    426  O   PRO A  53      11.976 -31.693  46.430  1.00 45.72           O  
ATOM    427  CB  PRO A  53      12.827 -33.479  49.160  1.00 38.21           C  
ATOM    428  CG  PRO A  53      13.577 -34.638  49.580  1.00 40.58           C  
ATOM    429  CD  PRO A  53      14.600 -34.890  48.520  1.00 38.62           C  
ATOM    430  N   ILE A  54      14.021 -31.553  47.314  1.00 41.41           N  
ATOM    431  CA  ILE A  54      14.070 -30.140  47.027  1.00 44.34           C  
ATOM    432  C   ILE A  54      14.099 -29.885  45.531  1.00 44.43           C  
ATOM    433  O   ILE A  54      13.621 -28.860  45.060  1.00 52.61           O  
ATOM    434  CB  ILE A  54      15.172 -29.390  47.807  1.00 45.67           C  
ATOM    435  CG1 ILE A  54      16.321 -28.985  46.898  1.00 44.76           C  
ATOM    436  CG2 ILE A  54      15.562 -30.157  49.073  1.00 48.75           C  
ATOM    437  CD1 ILE A  54      16.429 -27.508  46.781  1.00 52.36           C  
ATOM    438  N   ASN A  55      14.636 -30.810  44.764  1.00 39.68           N  
ATOM    439  CA  ASN A  55      14.621 -30.612  43.322  1.00 42.95           C  
ATOM    440  C   ASN A  55      13.337 -30.996  42.668  1.00 42.14           C  
ATOM    441  O   ASN A  55      12.958 -30.433  41.651  1.00 44.87           O  
ATOM    442  CB  ASN A  55      15.771 -31.342  42.640  1.00 44.17           C  
ATOM    443  CG  ASN A  55      17.029 -30.537  42.656  1.00 49.22           C  
ATOM    444  OD1 ASN A  55      17.119 -29.511  41.966  1.00 52.68           O  
ATOM    445  ND2 ASN A  55      18.006 -30.959  43.465  1.00 40.90           N  
ATOM    446  N   PHE A  56      12.704 -32.012  43.233  1.00 43.55           N  
ATOM    447  CA  PHE A  56      11.469 -32.528  42.689  1.00 45.56           C  
ATOM    448  C   PHE A  56      10.362 -31.541  43.052  1.00 46.11           C  
ATOM    449  O   PHE A  56       9.537 -31.191  42.212  1.00 40.88           O  
ATOM    450  CB  PHE A  56      11.181 -33.931  43.236  1.00 40.65           C  
ATOM    451  CG  PHE A  56       9.800 -34.410  42.945  1.00 43.98           C  
ATOM    452  CD1 PHE A  56       9.475 -34.912  41.693  1.00 42.76           C  
ATOM    453  CD2 PHE A  56       8.817 -34.325  43.906  1.00 46.05           C  
ATOM    454  CE1 PHE A  56       8.201 -35.329  41.411  1.00 41.97           C  
ATOM    455  CE2 PHE A  56       7.526 -34.731  43.626  1.00 50.57           C  
ATOM    456  CZ  PHE A  56       7.220 -35.240  42.378  1.00 48.14           C  
ATOM    457  N   LEU A  57      10.374 -31.088  44.302  1.00 44.07           N  
ATOM    458  CA  LEU A  57       9.415 -30.104  44.776  1.00 50.39           C  
ATOM    459  C   LEU A  57       9.351 -28.905  43.834  1.00 50.61           C  
ATOM    460  O   LEU A  57       8.278 -28.429  43.494  1.00 52.43           O  
ATOM    461  CB  LEU A  57       9.763 -29.648  46.190  1.00 49.29           C  
ATOM    462  CG  LEU A  57       8.744 -28.696  46.813  1.00 57.29           C  
ATOM    463  CD1 LEU A  57       7.432 -29.411  47.160  1.00 53.83           C  
ATOM    464  CD2 LEU A  57       9.326 -27.990  48.027  1.00 54.86           C  
ATOM    465  N   THR A  58      10.513 -28.441  43.399  1.00 48.74           N  
ATOM    466  CA  THR A  58      10.608 -27.423  42.361  1.00 50.00           C  
ATOM    467  C   THR A  58       9.770 -27.718  41.112  1.00 48.57           C  
ATOM    468  O   THR A  58       9.058 -26.842  40.635  1.00 51.30           O  
ATOM    469  CB  THR A  58      12.067 -27.188  41.935  1.00 46.76           C  
ATOM    470  OG1 THR A  58      12.835 -26.805  43.081  1.00 42.26           O  
ATOM    471  CG2 THR A  58      12.136 -26.106  40.855  1.00 40.88           C  
ATOM    472  N   LEU A  59       9.852 -28.927  40.572  1.00 47.02           N  
ATOM    473  CA  LEU A  59       9.063 -29.253  39.392  1.00 49.59           C  
ATOM    474  C   LEU A  59       7.598 -29.266  39.767  1.00 48.95           C  
ATOM    475  O   LEU A  59       6.741 -28.815  39.016  1.00 46.45           O  
ATOM    476  CB  LEU A  59       9.450 -30.619  38.834  1.00 46.21           C  
ATOM    477  CG  LEU A  59      10.916 -30.795  38.440  1.00 51.72           C  
ATOM    478  CD1 LEU A  59      11.131 -32.151  37.787  1.00 53.14           C  
ATOM    479  CD2 LEU A  59      11.376 -29.664  37.522  1.00 52.28           C  
ATOM    480  N   TYR A  60       7.325 -29.788  40.950  1.00 51.20           N  
ATOM    481  CA  TYR A  60       5.962 -30.017  41.378  1.00 55.35           C  
ATOM    482  C   TYR A  60       5.228 -28.703  41.576  1.00 54.81           C  
ATOM    483  O   TYR A  60       4.171 -28.459  40.999  1.00 53.66           O  
ATOM    484  CB  TYR A  60       5.973 -30.820  42.670  1.00 54.54           C  
ATOM    485  CG  TYR A  60       4.604 -31.110  43.187  1.00 58.03           C  
ATOM    486  CD1 TYR A  60       3.801 -32.063  42.579  1.00 57.64           C  
ATOM    487  CD2 TYR A  60       4.104 -30.428  44.282  1.00 59.53           C  
ATOM    488  CE1 TYR A  60       2.542 -32.330  43.053  1.00 60.41           C  
ATOM    489  CE2 TYR A  60       2.848 -30.695  44.761  1.00 60.51           C  
ATOM    490  CZ  TYR A  60       2.073 -31.641  44.143  1.00 61.98           C  
ATOM    491  OH  TYR A  60       0.817 -31.893  44.624  1.00 73.12           O  
ATOM    492  N   VAL A  61       5.824 -27.859  42.401  1.00 54.98           N  
ATOM    493  CA  VAL A  61       5.333 -26.518  42.685  1.00 50.52           C  
ATOM    494  C   VAL A  61       5.139 -25.664  41.423  1.00 48.19           C  
ATOM    495  O   VAL A  61       4.246 -24.841  41.377  1.00 51.62           O  
ATOM    496  CB  VAL A  61       6.268 -25.831  43.700  1.00 49.92           C  
ATOM    497  CG1 VAL A  61       6.815 -24.564  43.158  1.00 52.37           C  
ATOM    498  CG2 VAL A  61       5.567 -25.610  45.017  1.00 51.34           C  
ATOM    499  N   THR A  62       5.951 -25.870  40.395  1.00 47.80           N  
ATOM    500  CA  THR A  62       5.761 -25.155  39.139  1.00 48.97           C  
ATOM    501  C   THR A  62       4.452 -25.586  38.521  1.00 51.19           C  
ATOM    502  O   THR A  62       3.693 -24.762  37.997  1.00 51.60           O  
ATOM    503  CB  THR A  62       6.882 -25.453  38.142  1.00 49.36           C  
ATOM    504  OG1 THR A  62       8.116 -24.982  38.677  1.00 52.98           O  
ATOM    505  CG2 THR A  62       6.640 -24.751  36.822  1.00 49.21           C  
ATOM    506  N   VAL A  63       4.194 -26.892  38.581  1.00 51.69           N  
ATOM    507  CA  VAL A  63       2.934 -27.457  38.097  1.00 54.16           C  
ATOM    508  C   VAL A  63       1.700 -26.859  38.835  1.00 52.03           C  
ATOM    509  O   VAL A  63       0.676 -26.614  38.214  1.00 47.64           O  
ATOM    510  CB  VAL A  63       2.981 -29.030  38.097  1.00 48.12           C  
ATOM    511  CG1 VAL A  63       1.592 -29.647  37.973  1.00 44.39           C  
ATOM    512  CG2 VAL A  63       3.865 -29.519  36.980  1.00 44.14           C  
ATOM    513  N   GLN A  64       1.833 -26.589  40.135  1.00 53.16           N  
ATOM    514  CA  GLN A  64       0.743 -26.033  40.941  1.00 52.90           C  
ATOM    515  C   GLN A  64       0.521 -24.516  40.888  1.00 54.46           C  
ATOM    516  O   GLN A  64      -0.559 -24.058  41.242  1.00 52.24           O  
ATOM    517  CB  GLN A  64       0.910 -26.438  42.405  1.00 52.15           C  
ATOM    518  CG  GLN A  64       1.129 -27.909  42.618  1.00 57.98           C  
ATOM    519  CD  GLN A  64      -0.134 -28.724  42.449  1.00 68.90           C  
ATOM    520  OE1 GLN A  64      -0.576 -29.002  41.324  1.00 67.20           O  
ATOM    521  NE2 GLN A  64      -0.730 -29.119  43.575  1.00 83.12           N  
ATOM    522  N   HIS A  65       1.538 -23.748  40.492  1.00 53.43           N  
ATOM    523  CA  HIS A  65       1.457 -22.277  40.503  1.00 50.51           C  
ATOM    524  C   HIS A  65       1.678 -21.632  39.146  1.00 53.74           C  
ATOM    525  O   HIS A  65       2.780 -21.655  38.620  1.00 53.71           O  
ATOM    526  CB  HIS A  65       2.431 -21.693  41.509  1.00 40.65           C  
ATOM    527  CG  HIS A  65       2.215 -22.195  42.894  1.00 45.18           C  
ATOM    528  ND1 HIS A  65       1.539 -21.473  43.853  1.00 48.39           N  
ATOM    529  CD2 HIS A  65       2.553 -23.368  43.476  1.00 49.16           C  
ATOM    530  CE1 HIS A  65       1.493 -22.167  44.976  1.00 50.43           C  
ATOM    531  NE2 HIS A  65       2.101 -23.323  44.774  1.00 53.90           N  
ATOM    532  N   LYS A  66       0.628 -21.028  38.606  1.00 58.70           N  
ATOM    533  CA  LYS A  66       0.629 -20.479  37.256  1.00 58.99           C  
ATOM    534  C   LYS A  66       1.640 -19.359  37.072  1.00 60.75           C  
ATOM    535  O   LYS A  66       2.198 -19.175  35.990  1.00 60.87           O  
ATOM    536  CB  LYS A  66      -0.770 -19.953  36.951  1.00 59.67           C  
ATOM    537  CG  LYS A  66      -0.931 -19.217  35.635  1.00 66.53           C  
ATOM    538  CD  LYS A  66      -2.148 -18.295  35.691  1.00 78.88           C  
ATOM    539  CE  LYS A  66      -1.753 -16.877  36.073  1.00 78.94           C  
ATOM    540  NZ  LYS A  66      -0.947 -16.222  35.002  1.00 79.49           N  
ATOM    541  N   LYS A  67       1.860 -18.604  38.139  1.00 56.34           N  
ATOM    542  CA  LYS A  67       2.727 -17.445  38.086  1.00 55.54           C  
ATOM    543  C   LYS A  67       4.172 -17.852  37.896  1.00 55.75           C  
ATOM    544  O   LYS A  67       5.007 -17.045  37.501  1.00 58.56           O  
ATOM    545  CB  LYS A  67       2.565 -16.616  39.359  1.00 57.15           C  
ATOM    546  CG  LYS A  67       1.258 -15.845  39.419  1.00 61.04           C  
ATOM    547  CD  LYS A  67       0.938 -15.230  38.057  1.00 72.89           C  
ATOM    548  CE  LYS A  67      -0.189 -14.217  38.141  1.00 82.37           C  
ATOM    549  NZ  LYS A  67      -0.892 -13.991  36.850  1.00 81.59           N  
ATOM    550  N   LEU A  68       4.450 -19.119  38.180  1.00 51.46           N  
ATOM    551  CA  LEU A  68       5.790 -19.668  38.006  1.00 49.35           C  
ATOM    552  C   LEU A  68       6.161 -20.058  36.590  1.00 46.27           C  
ATOM    553  O   LEU A  68       7.343 -20.084  36.298  1.00 47.69           O  
ATOM    554  CB  LEU A  68       6.018 -20.869  38.905  1.00 47.65           C  
ATOM    555  CG  LEU A  68       6.118 -20.563  40.385  1.00 49.97           C  
ATOM    556  CD1 LEU A  68       6.322 -21.869  41.126  1.00 44.94           C  
ATOM    557  CD2 LEU A  68       7.246 -19.583  40.686  1.00 49.32           C  
ATOM    558  N   ARG A  69       5.209 -20.291  35.692  1.00 48.25           N  
ATOM    559  CA  ARG A  69       5.669 -20.785  34.429  1.00 49.37           C  
ATOM    560  C   ARG A  69       5.759 -19.611  33.527  1.00 44.86           C  
ATOM    561  O   ARG A  69       4.781 -19.196  32.935  1.00 52.61           O  
ATOM    562  CB  ARG A  69       4.682 -21.782  33.852  1.00 47.43           C  
ATOM    563  CG  ARG A  69       4.116 -22.734  34.874  1.00 49.71           C  
ATOM    564  CD  ARG A  69       2.945 -23.478  34.313  1.00 55.70           C  
ATOM    565  NE  ARG A  69       2.111 -23.937  35.409  1.00 62.15           N  
ATOM    566  CZ  ARG A  69       0.879 -23.503  35.644  1.00 64.14           C  
ATOM    567  NH1 ARG A  69       0.306 -22.624  34.830  1.00 65.85           N  
ATOM    568  NH2 ARG A  69       0.219 -23.961  36.694  1.00 59.07           N  
ATOM    569  N   THR A  70       6.992 -19.158  33.353  1.00 51.31           N  
ATOM    570  CA  THR A  70       7.313 -17.933  32.648  1.00 53.33           C  
ATOM    571  C   THR A  70       8.654 -18.257  32.012  1.00 60.98           C  
ATOM    572  O   THR A  70       9.428 -19.063  32.563  1.00 58.56           O  
ATOM    573  CB  THR A  70       7.479 -16.730  33.606  1.00 47.98           C  
ATOM    574  OG1 THR A  70       8.634 -16.921  34.424  1.00 56.37           O  
ATOM    575  CG2 THR A  70       6.291 -16.554  34.522  1.00 49.07           C  
ATOM    576  N   PRO A  71       8.942 -17.645  30.856  1.00 58.45           N  
ATOM    577  CA  PRO A  71      10.182 -17.836  30.101  1.00 59.09           C  
ATOM    578  C   PRO A  71      11.468 -17.706  30.930  1.00 57.51           C  
ATOM    579  O   PRO A  71      12.399 -18.485  30.717  1.00 60.35           O  
ATOM    580  CB  PRO A  71      10.080 -16.738  29.046  1.00 58.67           C  
ATOM    581  CG  PRO A  71       8.643 -16.744  28.741  1.00 57.44           C  
ATOM    582  CD  PRO A  71       7.985 -16.840  30.088  1.00 49.19           C  
ATOM    583  N   LEU A  72      11.516 -16.766  31.870  1.00 53.65           N  
ATOM    584  CA  LEU A  72      12.716 -16.571  32.691  1.00 56.17           C  
ATOM    585  C   LEU A  72      12.930 -17.686  33.711  1.00 61.06           C  
ATOM    586  O   LEU A  72      14.046 -17.876  34.205  1.00 59.94           O  
ATOM    587  CB  LEU A  72      12.690 -15.222  33.408  1.00 54.81           C  
ATOM    588  CG  LEU A  72      12.946 -13.961  32.566  1.00 58.72           C  
ATOM    589  CD1 LEU A  72      12.893 -12.681  33.407  1.00 51.74           C  
ATOM    590  CD2 LEU A  72      14.267 -14.043  31.841  1.00 64.77           C  
ATOM    591  N   ASN A  73      11.855 -18.404  34.030  1.00 55.58           N  
ATOM    592  CA  ASN A  73      11.944 -19.536  34.937  1.00 51.70           C  
ATOM    593  C   ASN A  73      12.285 -20.856  34.252  1.00 52.90           C  
ATOM    594  O   ASN A  73      12.647 -21.823  34.920  1.00 52.83           O  
ATOM    595  CB  ASN A  73      10.655 -19.667  35.738  1.00 49.75           C  
ATOM    596  CG  ASN A  73      10.566 -18.658  36.853  1.00 51.40           C  
ATOM    597  OD1 ASN A  73      11.574 -18.143  37.311  1.00 58.05           O  
ATOM    598  ND2 ASN A  73       9.357 -18.376  37.304  1.00 59.87           N  
ATOM    599  N   TYR A  74      12.181 -20.895  32.926  1.00 52.58           N  
ATOM    600  CA  TYR A  74      12.444 -22.123  32.172  1.00 53.69           C  
ATOM    601  C   TYR A  74      13.812 -22.749  32.521  1.00 53.45           C  
ATOM    602  O   TYR A  74      13.923 -23.948  32.794  1.00 48.62           O  
ATOM    603  CB  TYR A  74      12.392 -21.867  30.665  1.00 54.19           C  
ATOM    604  CG  TYR A  74      11.029 -21.693  30.039  1.00 57.19           C  
ATOM    605  CD1 TYR A  74       9.885 -21.555  30.805  1.00 57.17           C  
ATOM    606  CD2 TYR A  74      10.902 -21.676  28.655  1.00 61.93           C  
ATOM    607  CE1 TYR A  74       8.655 -21.386  30.198  1.00 58.71           C  
ATOM    608  CE2 TYR A  74       9.693 -21.511  28.045  1.00 63.05           C  
ATOM    609  CZ  TYR A  74       8.570 -21.365  28.809  1.00 62.16           C  
ATOM    610  OH  TYR A  74       7.364 -21.208  28.156  1.00 68.59           O  
ATOM    611  N   ILE A  75      14.847 -21.917  32.515  1.00 53.39           N  
ATOM    612  CA  ILE A  75      16.200 -22.367  32.828  1.00 51.71           C  
ATOM    613  C   ILE A  75      16.359 -22.839  34.277  1.00 50.77           C  
ATOM    614  O   ILE A  75      17.169 -23.723  34.557  1.00 49.33           O  
ATOM    615  CB  ILE A  75      17.254 -21.263  32.550  1.00 54.27           C  
ATOM    616  CG1 ILE A  75      18.678 -21.830  32.627  1.00 50.20           C  
ATOM    617  CG2 ILE A  75      17.104 -20.106  33.514  1.00 50.20           C  
ATOM    618  CD1 ILE A  75      19.110 -22.595  31.399  1.00 51.20           C  
ATOM    619  N   LEU A  76      15.605 -22.236  35.196  1.00 50.21           N  
ATOM    620  CA  LEU A  76      15.609 -22.669  36.596  1.00 48.81           C  
ATOM    621  C   LEU A  76      15.022 -24.075  36.720  1.00 51.44           C  
ATOM    622  O   LEU A  76      15.412 -24.873  37.584  1.00 47.15           O  
ATOM    623  CB  LEU A  76      14.791 -21.714  37.459  1.00 44.72           C  
ATOM    624  CG  LEU A  76      15.443 -20.368  37.685  1.00 48.65           C  
ATOM    625  CD1 LEU A  76      14.739 -19.690  38.829  1.00 53.09           C  
ATOM    626  CD2 LEU A  76      16.906 -20.562  37.991  1.00 44.92           C  
ATOM    627  N   LEU A  77      14.060 -24.361  35.853  1.00 50.21           N  
ATOM    628  CA  LEU A  77      13.424 -25.655  35.847  1.00 51.22           C  
ATOM    629  C   LEU A  77      14.425 -26.669  35.314  1.00 48.67           C  
ATOM    630  O   LEU A  77      14.592 -27.759  35.864  1.00 46.98           O  
ATOM    631  CB  LEU A  77      12.137 -25.603  35.010  1.00 54.81           C  
ATOM    632  CG  LEU A  77      10.971 -25.007  35.801  1.00 51.92           C  
ATOM    633  CD1 LEU A  77       9.854 -24.516  34.895  1.00 62.08           C  
ATOM    634  CD2 LEU A  77      10.451 -26.033  36.797  1.00 49.18           C  
ATOM    635  N   ASN A  78      15.094 -26.277  34.239  1.00 50.74           N  
ATOM    636  CA  ASN A  78      16.176 -27.050  33.635  1.00 49.89           C  
ATOM    637  C   ASN A  78      17.262 -27.456  34.627  1.00 45.87           C  
ATOM    638  O   ASN A  78      17.745 -28.576  34.593  1.00 50.43           O  
ATOM    639  CB  ASN A  78      16.805 -26.224  32.528  1.00 49.81           C  
ATOM    640  CG  ASN A  78      17.586 -27.054  31.575  1.00 50.06           C  
ATOM    641  OD1 ASN A  78      17.114 -28.081  31.109  1.00 49.65           O  
ATOM    642  ND2 ASN A  78      18.794 -26.620  31.270  1.00 49.80           N  
ATOM    643  N   LEU A  79      17.644 -26.524  35.492  1.00 43.16           N  
ATOM    644  CA  LEU A  79      18.542 -26.782  36.624  1.00 45.81           C  
ATOM    645  C   LEU A  79      18.034 -27.905  37.552  1.00 44.58           C  
ATOM    646  O   LEU A  79      18.797 -28.760  38.001  1.00 45.40           O  
ATOM    647  CB  LEU A  79      18.734 -25.491  37.446  1.00 45.40           C  
ATOM    648  CG  LEU A  79      19.625 -25.660  38.672  1.00 42.01           C  
ATOM    649  CD1 LEU A  79      21.046 -25.837  38.183  1.00 41.98           C  
ATOM    650  CD2 LEU A  79      19.498 -24.524  39.682  1.00 39.86           C  
ATOM    651  N   ALA A  80      16.740 -27.877  37.842  1.00 45.42           N  
ATOM    652  CA  ALA A  80      16.087 -28.900  38.659  1.00 44.90           C  
ATOM    653  C   ALA A  80      16.107 -30.312  38.044  1.00 45.30           C  
ATOM    654  O   ALA A  80      16.281 -31.289  38.767  1.00 41.72           O  
ATOM    655  CB  ALA A  80      14.643 -28.474  38.961  1.00 44.88           C  
ATOM    656  N   VAL A  81      15.889 -30.401  36.727  1.00 43.92           N  
ATOM    657  CA  VAL A  81      15.886 -31.670  35.986  1.00 45.65           C  
ATOM    658  C   VAL A  81      17.318 -32.224  35.888  1.00 46.55           C  
ATOM    659  O   VAL A  81      17.570 -33.422  36.085  1.00 40.40           O  
ATOM    660  CB  VAL A  81      15.288 -31.501  34.548  1.00 48.21           C  
ATOM    661  CG1 VAL A  81      15.274 -32.834  33.800  1.00 46.13           C  
ATOM    662  CG2 VAL A  81      13.895 -30.916  34.595  1.00 42.35           C  
ATOM    663  N   ALA A  82      18.243 -31.316  35.589  1.00 44.66           N  
ATOM    664  CA  ALA A  82      19.670 -31.581  35.628  1.00 44.28           C  
ATOM    665  C   ALA A  82      20.061 -32.164  36.976  1.00 44.81           C  
ATOM    666  O   ALA A  82      20.667 -33.220  37.039  1.00 44.92           O  
ATOM    667  CB  ALA A  82      20.439 -30.307  35.356  1.00 42.08           C  
ATOM    668  N   ASP A  83      19.709 -31.487  38.058  1.00 41.87           N  
ATOM    669  CA  ASP A  83      19.986 -32.028  39.380  1.00 41.07           C  
ATOM    670  C   ASP A  83      19.394 -33.409  39.603  1.00 42.65           C  
ATOM    671  O   ASP A  83      19.928 -34.189  40.382  1.00 43.32           O  
ATOM    672  CB  ASP A  83      19.465 -31.108  40.469  1.00 40.12           C  
ATOM    673  CG  ASP A  83      20.245 -29.840  40.566  1.00 45.15           C  
ATOM    674  OD1 ASP A  83      21.421 -29.859  40.154  1.00 45.86           O  
ATOM    675  OD2 ASP A  83      19.685 -28.826  41.044  1.00 46.19           O  
ATOM    676  N   LEU A  84      18.275 -33.705  38.947  1.00 41.60           N  
ATOM    677  CA  LEU A  84      17.594 -34.969  39.174  1.00 37.96           C  
ATOM    678  C   LEU A  84      18.378 -36.096  38.514  1.00 42.91           C  
ATOM    679  O   LEU A  84      18.605 -37.128  39.143  1.00 36.46           O  
ATOM    680  CB  LEU A  84      16.128 -34.903  38.745  1.00 35.35           C  
ATOM    681  CG  LEU A  84      15.240 -34.207  39.788  1.00 37.71           C  
ATOM    682  CD1 LEU A  84      13.767 -34.133  39.357  1.00 41.45           C  
ATOM    683  CD2 LEU A  84      15.375 -34.815  41.195  1.00 36.00           C  
ATOM    684  N   PHE A  85      18.835 -35.854  37.282  1.00 41.19           N  
ATOM    685  CA  PHE A  85      19.771 -36.734  36.588  1.00 41.98           C  
ATOM    686  C   PHE A  85      20.957 -37.064  37.498  1.00 44.90           C  
ATOM    687  O   PHE A  85      21.297 -38.227  37.697  1.00 45.63           O  
ATOM    688  CB  PHE A  85      20.297 -36.054  35.324  1.00 46.55           C  
ATOM    689  CG  PHE A  85      19.372 -36.144  34.136  1.00 52.68           C  
ATOM    690  CD1 PHE A  85      18.077 -35.653  34.202  1.00 51.45           C  
ATOM    691  CD2 PHE A  85      19.808 -36.692  32.939  1.00 56.34           C  
ATOM    692  CE1 PHE A  85      17.224 -35.724  33.103  1.00 50.83           C  
ATOM    693  CE2 PHE A  85      18.962 -36.765  31.839  1.00 54.79           C  
ATOM    694  CZ  PHE A  85      17.672 -36.278  31.922  1.00 53.79           C  
ATOM    695  N   MET A  86      21.564 -36.033  38.081  1.00 43.82           N  
ATOM    696  CA  MET A  86      22.623 -36.227  39.073  1.00 43.72           C  
ATOM    697  C   MET A  86      22.142 -37.128  40.225  1.00 45.16           C  
ATOM    698  O   MET A  86      22.849 -38.013  40.686  1.00 45.88           O  
ATOM    699  CB  MET A  86      23.115 -34.885  39.622  1.00 39.36           C  
ATOM    700  CG  MET A  86      23.616 -33.892  38.564  1.00 42.43           C  
ATOM    701  SD  MET A  86      24.271 -32.390  39.318  1.00 40.68           S  
ATOM    702  CE  MET A  86      25.779 -33.017  40.047  1.00 49.73           C  
ATOM    703  N   VAL A  87      20.922 -36.914  40.685  1.00 44.69           N  
ATOM    704  CA  VAL A  87      20.413 -37.690  41.815  1.00 46.06           C  
ATOM    705  C   VAL A  87      20.224 -39.194  41.465  1.00 48.40           C  
ATOM    706  O   VAL A  87      20.695 -40.082  42.185  1.00 46.57           O  
ATOM    707  CB  VAL A  87      19.123 -37.034  42.424  1.00 42.48           C  
ATOM    708  CG1 VAL A  87      18.402 -37.993  43.354  1.00 41.37           C  
ATOM    709  CG2 VAL A  87      19.477 -35.753  43.179  1.00 41.94           C  
ATOM    710  N   PHE A  88      19.512 -39.467  40.375  1.00 47.29           N  
ATOM    711  CA  PHE A  88      19.268 -40.842  39.943  1.00 43.86           C  
ATOM    712  C   PHE A  88      20.391 -41.544  39.171  1.00 47.23           C  
ATOM    713  O   PHE A  88      20.809 -42.638  39.531  1.00 49.57           O  
ATOM    714  CB  PHE A  88      17.944 -40.921  39.187  1.00 40.87           C  
ATOM    715  CG  PHE A  88      16.758 -40.604  40.050  1.00 49.30           C  
ATOM    716  CD1 PHE A  88      16.273 -41.550  40.945  1.00 46.33           C  
ATOM    717  CD2 PHE A  88      16.139 -39.346  39.987  1.00 47.41           C  
ATOM    718  CE1 PHE A  88      15.188 -41.270  41.754  1.00 46.63           C  
ATOM    719  CE2 PHE A  88      15.050 -39.050  40.794  1.00 43.48           C  
ATOM    720  CZ  PHE A  88      14.573 -40.017  41.681  1.00 48.39           C  
ATOM    721  N   GLY A  89      20.921 -40.901  38.144  1.00 43.92           N  
ATOM    722  CA  GLY A  89      21.919 -41.551  37.311  1.00 44.19           C  
ATOM    723  C   GLY A  89      23.286 -41.652  37.985  1.00 50.33           C  
ATOM    724  O   GLY A  89      24.215 -42.283  37.483  1.00 51.84           O  
ATOM    725  N   ASP A  90      23.423 -40.999  39.128  1.00 49.17           N  
ATOM    726  CA  ASP A  90      24.717 -40.853  39.740  1.00 42.71           C  
ATOM    727  C   ASP A  90      24.657 -41.240  41.212  1.00 46.11           C  
ATOM    728  O   ASP A  90      25.192 -42.267  41.595  1.00 48.05           O  
ATOM    729  CB  ASP A  90      25.225 -39.426  39.499  1.00 42.39           C  
ATOM    730  CG  ASP A  90      26.560 -39.121  40.202  1.00 53.13           C  
ATOM    731  OD1 ASP A  90      27.206 -40.066  40.697  1.00 54.51           O  
ATOM    732  OD2 ASP A  90      26.944 -37.931  40.237  1.00 54.37           O  
ATOM    733  N   PHE A  91      23.956 -40.458  42.020  1.00 44.08           N  
ATOM    734  CA  PHE A  91      23.983 -40.629  43.472  1.00 41.56           C  
ATOM    735  C   PHE A  91      23.522 -42.015  43.930  1.00 43.95           C  
ATOM    736  O   PHE A  91      24.142 -42.587  44.828  1.00 43.48           O  
ATOM    737  CB  PHE A  91      23.130 -39.561  44.184  1.00 40.18           C  
ATOM    738  CG  PHE A  91      23.574 -38.129  43.949  1.00 46.47           C  
ATOM    739  CD1 PHE A  91      24.789 -37.838  43.320  1.00 50.82           C  
ATOM    740  CD2 PHE A  91      22.786 -37.071  44.375  1.00 41.30           C  
ATOM    741  CE1 PHE A  91      25.195 -36.531  43.106  1.00 44.73           C  
ATOM    742  CE2 PHE A  91      23.193 -35.768  44.168  1.00 42.21           C  
ATOM    743  CZ  PHE A  91      24.400 -35.500  43.531  1.00 41.41           C  
ATOM    744  N   THR A  92      22.436 -42.528  43.329  1.00 42.08           N  
ATOM    745  CA  THR A  92      21.833 -43.818  43.710  1.00 44.34           C  
ATOM    746  C   THR A  92      22.646 -45.024  43.242  1.00 42.58           C  
ATOM    747  O   THR A  92      22.925 -45.938  44.026  1.00 38.96           O  
ATOM    748  CB  THR A  92      20.376 -44.006  43.153  1.00 44.94           C  
ATOM    749  OG1 THR A  92      20.367 -43.902  41.719  1.00 49.57           O  
ATOM    750  CG2 THR A  92      19.430 -42.994  43.740  1.00 44.30           C  
ATOM    751  N   THR A  93      23.010 -44.998  41.958  1.00 41.37           N  
ATOM    752  CA  THR A  93      23.994 -45.908  41.401  1.00 41.01           C  
ATOM    753  C   THR A  93      25.229 -45.974  42.288  1.00 39.96           C  
ATOM    754  O   THR A  93      25.690 -47.056  42.624  1.00 42.75           O  
ATOM    755  CB  THR A  93      24.483 -45.476  40.013  1.00 39.99           C  
ATOM    756  OG1 THR A  93      23.373 -45.140  39.180  1.00 36.55           O  
ATOM    757  CG2 THR A  93      25.266 -46.620  39.376  1.00 41.91           C  
ATOM    758  N   THR A  94      25.766 -44.829  42.671  1.00 37.39           N  
ATOM    759  CA  THR A  94      26.917 -44.840  43.546  1.00 40.48           C  
ATOM    760  C   THR A  94      26.588 -45.398  44.936  1.00 41.46           C  
ATOM    761  O   THR A  94      27.432 -46.041  45.551  1.00 47.71           O  
ATOM    762  CB  THR A  94      27.635 -43.468  43.634  1.00 40.62           C  
ATOM    763  OG1 THR A  94      28.127 -43.095  42.338  1.00 44.51           O  
ATOM    764  CG2 THR A  94      28.817 -43.545  44.593  1.00 37.97           C  
ATOM    765  N   LEU A  95      25.367 -45.199  45.419  1.00 40.27           N  
ATOM    766  CA  LEU A  95      24.973 -45.707  46.743  1.00 43.31           C  
ATOM    767  C   LEU A  95      25.026 -47.224  46.705  1.00 43.63           C  
ATOM    768  O   LEU A  95      25.427 -47.926  47.650  1.00 41.34           O  
ATOM    769  CB  LEU A  95      23.526 -45.302  47.083  1.00 42.01           C  
ATOM    770  CG  LEU A  95      23.016 -45.849  48.420  1.00 37.41           C  
ATOM    771  CD1 LEU A  95      23.893 -45.330  49.542  1.00 39.31           C  
ATOM    772  CD2 LEU A  95      21.598 -45.473  48.654  1.00 36.77           C  
ATOM    773  N   TYR A  96      24.547 -47.714  45.584  1.00 40.21           N  
ATOM    774  CA  TYR A  96      24.414 -49.118  45.368  1.00 40.76           C  
ATOM    775  C   TYR A  96      25.769 -49.839  45.230  1.00 44.43           C  
ATOM    776  O   TYR A  96      26.099 -50.751  46.004  1.00 43.44           O  
ATOM    777  CB  TYR A  96      23.598 -49.284  44.115  1.00 42.15           C  
ATOM    778  CG  TYR A  96      23.318 -50.701  43.850  1.00 47.47           C  
ATOM    779  CD1 TYR A  96      22.635 -51.475  44.793  1.00 44.65           C  
ATOM    780  CD2 TYR A  96      23.762 -51.290  42.677  1.00 46.73           C  
ATOM    781  CE1 TYR A  96      22.394 -52.782  44.569  1.00 44.01           C  
ATOM    782  CE2 TYR A  96      23.521 -52.598  42.435  1.00 46.06           C  
ATOM    783  CZ  TYR A  96      22.833 -53.342  43.387  1.00 46.55           C  
ATOM    784  OH  TYR A  96      22.599 -54.663  43.147  1.00 47.12           O  
ATOM    785  N   THR A  97      26.562 -49.380  44.257  1.00 43.95           N  
ATOM    786  CA  THR A  97      27.900 -49.904  43.989  1.00 39.69           C  
ATOM    787  C   THR A  97      28.858 -49.656  45.127  1.00 39.12           C  
ATOM    788  O   THR A  97      29.724 -50.477  45.375  1.00 42.17           O  
ATOM    789  CB  THR A  97      28.549 -49.285  42.745  1.00 39.10           C  
ATOM    790  OG1 THR A  97      28.744 -47.874  42.950  1.00 42.40           O  
ATOM    791  CG2 THR A  97      27.722 -49.547  41.501  1.00 37.25           C  
ATOM    792  N   SER A  98      28.746 -48.536  45.823  1.00 37.10           N  
ATOM    793  CA  SER A  98      29.609 -48.385  46.992  1.00 44.41           C  
ATOM    794  C   SER A  98      29.427 -49.548  47.986  1.00 39.21           C  
ATOM    795  O   SER A  98      30.390 -50.041  48.568  1.00 40.40           O  
ATOM    796  CB  SER A  98      29.476 -47.013  47.665  1.00 39.52           C  
ATOM    797  OG  SER A  98      28.127 -46.696  47.919  1.00 45.94           O  
ATOM    798  N   LEU A  99      28.199 -50.024  48.116  1.00 38.43           N  
ATOM    799  CA  LEU A  99      27.876 -51.093  49.065  1.00 42.45           C  
ATOM    800  C   LEU A  99      28.410 -52.511  48.684  1.00 46.45           C  
ATOM    801  O   LEU A  99      28.426 -53.443  49.518  1.00 38.45           O  
ATOM    802  CB  LEU A  99      26.361 -51.090  49.323  1.00 40.94           C  
ATOM    803  CG  LEU A  99      25.979 -49.935  50.267  1.00 36.55           C  
ATOM    804  CD1 LEU A  99      24.470 -49.892  50.557  1.00 40.27           C  
ATOM    805  CD2 LEU A  99      26.803 -49.985  51.575  1.00 32.42           C  
ATOM    806  N   HIS A 100      28.807 -52.647  47.418  1.00 45.39           N  
ATOM    807  CA  HIS A 100      29.593 -53.763  46.929  1.00 44.28           C  
ATOM    808  C   HIS A 100      31.131 -53.583  47.046  1.00 48.32           C  
ATOM    809  O   HIS A 100      31.883 -54.559  46.984  1.00 50.87           O  
ATOM    810  CB  HIS A 100      29.223 -53.998  45.478  1.00 39.93           C  
ATOM    811  CG  HIS A 100      27.779 -54.336  45.267  1.00 48.65           C  
ATOM    812  ND1 HIS A 100      26.807 -53.373  45.112  1.00 53.20           N  
ATOM    813  CD2 HIS A 100      27.139 -55.528  45.210  1.00 47.52           C  
ATOM    814  CE1 HIS A 100      25.631 -53.958  44.952  1.00 51.08           C  
ATOM    815  NE2 HIS A 100      25.805 -55.264  45.009  1.00 48.21           N  
ATOM    816  N   GLY A 101      31.592 -52.351  47.249  1.00 43.03           N  
ATOM    817  CA  GLY A 101      33.005 -52.045  47.218  1.00 40.92           C  
ATOM    818  C   GLY A 101      33.619 -52.000  45.834  1.00 42.45           C  
ATOM    819  O   GLY A 101      34.839 -51.989  45.715  1.00 43.77           O  
ATOM    820  N   TYR A 102      32.796 -51.988  44.787  1.00 40.41           N  
ATOM    821  CA  TYR A 102      33.302 -51.831  43.402  1.00 42.03           C  
ATOM    822  C   TYR A 102      32.185 -51.549  42.378  1.00 40.98           C  
ATOM    823  O   TYR A 102      31.010 -51.615  42.718  1.00 41.72           O  
ATOM    824  CB  TYR A 102      34.088 -53.063  42.949  1.00 39.42           C  
ATOM    825  CG  TYR A 102      33.261 -54.332  42.806  1.00 42.59           C  
ATOM    826  CD1 TYR A 102      32.856 -55.059  43.934  1.00 36.74           C  
ATOM    827  CD2 TYR A 102      32.917 -54.819  41.539  1.00 38.36           C  
ATOM    828  CE1 TYR A 102      32.131 -56.208  43.802  1.00 39.00           C  
ATOM    829  CE2 TYR A 102      32.186 -55.963  41.392  1.00 35.18           C  
ATOM    830  CZ  TYR A 102      31.790 -56.661  42.525  1.00 39.48           C  
ATOM    831  OH  TYR A 102      31.051 -57.817  42.386  1.00 29.99           O  
ATOM    832  N   PHE A 103      32.529 -51.309  41.114  1.00 41.83           N  
ATOM    833  CA  PHE A 103      31.497 -50.913  40.186  1.00 42.85           C  
ATOM    834  C   PHE A 103      30.974 -52.164  39.526  1.00 40.85           C  
ATOM    835  O   PHE A 103      31.554 -52.673  38.566  1.00 46.23           O  
ATOM    836  CB  PHE A 103      32.062 -49.940  39.140  1.00 43.99           C  
ATOM    837  CG  PHE A 103      31.009 -49.297  38.292  1.00 51.02           C  
ATOM    838  CD1 PHE A 103      30.291 -48.182  38.759  1.00 50.22           C  
ATOM    839  CD2 PHE A 103      30.714 -49.808  37.037  1.00 50.09           C  
ATOM    840  CE1 PHE A 103      29.304 -47.600  37.986  1.00 46.85           C  
ATOM    841  CE2 PHE A 103      29.726 -49.237  36.254  1.00 49.87           C  
ATOM    842  CZ  PHE A 103      29.023 -48.130  36.721  1.00 49.62           C  
ATOM    843  N   VAL A 104      29.779 -52.554  39.943  1.00 42.43           N  
ATOM    844  CA  VAL A 104      29.298 -53.904  39.704  1.00 41.48           C  
ATOM    845  C   VAL A 104      28.587 -53.964  38.384  1.00 40.88           C  
ATOM    846  O   VAL A 104      28.099 -54.996  37.985  1.00 45.45           O  
ATOM    847  CB  VAL A 104      28.304 -54.333  40.811  1.00 37.01           C  
ATOM    848  CG1 VAL A 104      29.043 -54.517  42.101  1.00 33.82           C  
ATOM    849  CG2 VAL A 104      27.215 -53.289  40.956  1.00 41.60           C  
ATOM    850  N   PHE A 105      28.515 -52.842  37.702  1.00 43.09           N  
ATOM    851  CA  PHE A 105      27.760 -52.786  36.471  1.00 45.43           C  
ATOM    852  C   PHE A 105      28.651 -52.999  35.257  1.00 46.80           C  
ATOM    853  O   PHE A 105      28.168 -53.053  34.127  1.00 42.71           O  
ATOM    854  CB  PHE A 105      26.975 -51.463  36.397  1.00 48.69           C  
ATOM    855  CG  PHE A 105      25.869 -51.365  37.422  1.00 48.32           C  
ATOM    856  CD1 PHE A 105      24.929 -52.379  37.539  1.00 46.81           C  
ATOM    857  CD2 PHE A 105      25.781 -50.286  38.285  1.00 48.82           C  
ATOM    858  CE1 PHE A 105      23.921 -52.311  38.478  1.00 43.60           C  
ATOM    859  CE2 PHE A 105      24.757 -50.221  39.229  1.00 49.57           C  
ATOM    860  CZ  PHE A 105      23.837 -51.239  39.320  1.00 43.04           C  
ATOM    861  N   GLY A 106      29.955 -53.132  35.492  1.00 53.22           N  
ATOM    862  CA  GLY A 106      30.904 -53.367  34.413  1.00 51.49           C  
ATOM    863  C   GLY A 106      31.187 -52.174  33.514  1.00 54.41           C  
ATOM    864  O   GLY A 106      30.684 -51.077  33.751  1.00 54.08           O  
ATOM    865  N   PRO A 107      32.003 -52.385  32.468  1.00 55.89           N  
ATOM    866  CA  PRO A 107      32.451 -51.351  31.523  1.00 53.77           C  
ATOM    867  C   PRO A 107      31.322 -50.602  30.792  1.00 51.51           C  
ATOM    868  O   PRO A 107      31.449 -49.407  30.543  1.00 55.33           O  
ATOM    869  CB  PRO A 107      33.298 -52.145  30.519  1.00 49.17           C  
ATOM    870  CG  PRO A 107      33.747 -53.325  31.265  1.00 50.88           C  
ATOM    871  CD  PRO A 107      32.631 -53.683  32.186  1.00 47.90           C  
ATOM    872  N   THR A 108      30.248 -51.293  30.435  1.00 53.24           N  
ATOM    873  CA  THR A 108      29.111 -50.651  29.776  1.00 58.75           C  
ATOM    874  C   THR A 108      28.222 -49.930  30.790  1.00 56.51           C  
ATOM    875  O   THR A 108      27.602 -48.913  30.482  1.00 55.45           O  
ATOM    876  CB  THR A 108      28.293 -51.669  28.983  1.00 59.56           C  
ATOM    877  OG1 THR A 108      28.172 -52.863  29.763  1.00 69.61           O  
ATOM    878  CG2 THR A 108      28.997 -52.004  27.672  1.00 60.04           C  
ATOM    879  N   GLY A 109      28.187 -50.459  32.008  1.00 53.21           N  
ATOM    880  CA  GLY A 109      27.516 -49.800  33.107  1.00 49.67           C  
ATOM    881  C   GLY A 109      28.262 -48.537  33.445  1.00 53.03           C  
ATOM    882  O   GLY A 109      27.673 -47.537  33.841  1.00 56.63           O  
ATOM    883  N   CYS A 110      29.577 -48.591  33.269  1.00 53.55           N  
ATOM    884  CA  CYS A 110      30.453 -47.447  33.510  1.00 52.72           C  
ATOM    885  C   CYS A 110      30.184 -46.305  32.535  1.00 54.42           C  
ATOM    886  O   CYS A 110      30.057 -45.147  32.943  1.00 54.24           O  
ATOM    887  CB  CYS A 110      31.915 -47.876  33.406  1.00 50.07           C  
ATOM    888  SG  CYS A 110      33.048 -46.703  34.122  1.00 51.53           S  
ATOM    889  N   ASN A 111      30.100 -46.640  31.250  1.00 53.01           N  
ATOM    890  CA  ASN A 111      29.787 -45.665  30.210  1.00 55.84           C  
ATOM    891  C   ASN A 111      28.467 -44.929  30.419  1.00 55.67           C  
ATOM    892  O   ASN A 111      28.407 -43.701  30.344  1.00 53.79           O  
ATOM    893  CB  ASN A 111      29.749 -46.351  28.859  1.00 55.22           C  
ATOM    894  CG  ASN A 111      31.097 -46.462  28.244  1.00 55.09           C  
ATOM    895  OD1 ASN A 111      31.985 -45.667  28.526  1.00 55.60           O  
ATOM    896  ND2 ASN A 111      31.268 -47.446  27.387  1.00 62.77           N  
ATOM    897  N   LEU A 112      27.415 -45.707  30.670  1.00 54.28           N  
ATOM    898  CA  LEU A 112      26.085 -45.194  30.937  1.00 49.67           C  
ATOM    899  C   LEU A 112      26.082 -44.327  32.173  1.00 47.70           C  
ATOM    900  O   LEU A 112      25.742 -43.152  32.109  1.00 45.17           O  
ATOM    901  CB  LEU A 112      25.148 -46.371  31.192  1.00 51.44           C  
ATOM    902  CG  LEU A 112      24.399 -47.019  30.039  1.00 50.94           C  
ATOM    903  CD1 LEU A 112      23.956 -48.387  30.481  1.00 55.73           C  
ATOM    904  CD2 LEU A 112      23.196 -46.172  29.677  1.00 53.89           C  
ATOM    905  N   GLU A 113      26.477 -44.913  33.298  1.00 44.81           N  
ATOM    906  CA  GLU A 113      26.418 -44.204  34.561  1.00 45.57           C  
ATOM    907  C   GLU A 113      27.294 -42.973  34.484  1.00 51.88           C  
ATOM    908  O   GLU A 113      26.967 -41.949  35.060  1.00 54.41           O  
ATOM    909  CB  GLU A 113      26.838 -45.092  35.732  1.00 41.59           C  
ATOM    910  CG  GLU A 113      26.677 -44.435  37.090  1.00 39.75           C  
ATOM    911  CD  GLU A 113      27.828 -43.518  37.449  1.00 47.93           C  
ATOM    912  OE1 GLU A 113      28.923 -43.675  36.882  1.00 52.67           O  
ATOM    913  OE2 GLU A 113      27.656 -42.621  38.291  1.00 52.86           O  
ATOM    914  N   GLY A 114      28.409 -43.075  33.768  1.00 49.40           N  
ATOM    915  CA  GLY A 114      29.301 -41.947  33.600  1.00 49.28           C  
ATOM    916  C   GLY A 114      28.706 -40.889  32.693  1.00 52.74           C  
ATOM    917  O   GLY A 114      28.817 -39.695  32.978  1.00 53.26           O  
ATOM    918  N   PHE A 115      28.076 -41.320  31.602  1.00 52.29           N  
ATOM    919  CA  PHE A 115      27.446 -40.388  30.671  1.00 53.31           C  
ATOM    920  C   PHE A 115      26.346 -39.575  31.355  1.00 54.13           C  
ATOM    921  O   PHE A 115      26.318 -38.345  31.248  1.00 52.98           O  
ATOM    922  CB  PHE A 115      26.885 -41.117  29.445  1.00 50.63           C  
ATOM    923  CG  PHE A 115      26.112 -40.228  28.509  1.00 52.28           C  
ATOM    924  CD1 PHE A 115      26.764 -39.495  27.535  1.00 51.96           C  
ATOM    925  CD2 PHE A 115      24.732 -40.120  28.604  1.00 51.59           C  
ATOM    926  CE1 PHE A 115      26.052 -38.670  26.673  1.00 51.30           C  
ATOM    927  CE2 PHE A 115      24.024 -39.300  27.748  1.00 48.82           C  
ATOM    928  CZ  PHE A 115      24.683 -38.578  26.782  1.00 50.34           C  
ATOM    929  N   PHE A 116      25.446 -40.254  32.064  1.00 51.93           N  
ATOM    930  CA  PHE A 116      24.338 -39.551  32.714  1.00 53.94           C  
ATOM    931  C   PHE A 116      24.790 -38.655  33.854  1.00 54.01           C  
ATOM    932  O   PHE A 116      24.331 -37.513  33.964  1.00 52.15           O  
ATOM    933  CB  PHE A 116      23.210 -40.502  33.143  1.00 49.23           C  
ATOM    934  CG  PHE A 116      22.370 -40.945  31.999  1.00 48.92           C  
ATOM    935  CD1 PHE A 116      21.638 -40.022  31.277  1.00 51.20           C  
ATOM    936  CD2 PHE A 116      22.356 -42.263  31.602  1.00 51.81           C  
ATOM    937  CE1 PHE A 116      20.883 -40.410  30.189  1.00 54.01           C  
ATOM    938  CE2 PHE A 116      21.608 -42.660  30.518  1.00 53.98           C  
ATOM    939  CZ  PHE A 116      20.866 -41.729  29.809  1.00 53.11           C  
ATOM    940  N   ALA A 117      25.699 -39.166  34.680  1.00 50.53           N  
ATOM    941  CA  ALA A 117      26.284 -38.371  35.755  1.00 52.09           C  
ATOM    942  C   ALA A 117      26.954 -37.096  35.209  1.00 51.39           C  
ATOM    943  O   ALA A 117      26.849 -36.012  35.796  1.00 42.40           O  
ATOM    944  CB  ALA A 117      27.274 -39.205  36.552  1.00 47.80           C  
ATOM    945  N   THR A 118      27.630 -37.243  34.073  1.00 51.75           N  
ATOM    946  CA  THR A 118      28.285 -36.115  33.432  1.00 52.42           C  
ATOM    947  C   THR A 118      27.260 -35.205  32.753  1.00 52.11           C  
ATOM    948  O   THR A 118      27.315 -33.986  32.901  1.00 52.26           O  
ATOM    949  CB  THR A 118      29.398 -36.562  32.433  1.00 56.03           C  
ATOM    950  OG1 THR A 118      30.400 -37.328  33.126  1.00 52.74           O  
ATOM    951  CG2 THR A 118      30.055 -35.337  31.757  1.00 49.16           C  
ATOM    952  N   LEU A 119      26.321 -35.792  32.017  1.00 54.15           N  
ATOM    953  CA  LEU A 119      25.285 -34.999  31.352  1.00 55.23           C  
ATOM    954  C   LEU A 119      24.523 -34.129  32.346  1.00 51.90           C  
ATOM    955  O   LEU A 119      24.184 -32.994  32.045  1.00 51.22           O  
ATOM    956  CB  LEU A 119      24.297 -35.895  30.615  1.00 54.02           C  
ATOM    957  CG  LEU A 119      23.347 -35.193  29.652  1.00 50.34           C  
ATOM    958  CD1 LEU A 119      24.123 -34.661  28.456  1.00 48.20           C  
ATOM    959  CD2 LEU A 119      22.238 -36.150  29.221  1.00 52.12           C  
ATOM    960  N   GLY A 120      24.258 -34.672  33.531  1.00 54.85           N  
ATOM    961  CA  GLY A 120      23.454 -33.990  34.532  1.00 53.00           C  
ATOM    962  C   GLY A 120      24.102 -32.743  35.096  1.00 49.41           C  
ATOM    963  O   GLY A 120      23.524 -31.660  35.045  1.00 50.86           O  
ATOM    964  N   GLY A 121      25.309 -32.898  35.622  1.00 45.26           N  
ATOM    965  CA  GLY A 121      26.053 -31.788  36.190  1.00 46.94           C  
ATOM    966  C   GLY A 121      26.543 -30.765  35.174  1.00 50.74           C  
ATOM    967  O   GLY A 121      26.877 -29.622  35.522  1.00 45.99           O  
ATOM    968  N   GLU A 122      26.613 -31.185  33.915  1.00 50.33           N  
ATOM    969  CA  GLU A 122      26.996 -30.279  32.847  1.00 50.12           C  
ATOM    970  C   GLU A 122      25.834 -29.417  32.384  1.00 49.03           C  
ATOM    971  O   GLU A 122      26.015 -28.232  32.105  1.00 52.43           O  
ATOM    972  CB  GLU A 122      27.675 -31.035  31.703  1.00 49.45           C  
ATOM    973  CG  GLU A 122      29.115 -31.402  32.054  1.00 51.18           C  
ATOM    974  CD  GLU A 122      30.036 -30.187  32.125  1.00 53.62           C  
ATOM    975  OE1 GLU A 122      30.033 -29.415  31.150  1.00 56.82           O  
ATOM    976  OE2 GLU A 122      30.761 -30.000  33.134  1.00 53.50           O  
ATOM    977  N   ILE A 123      24.644 -30.010  32.313  1.00 52.04           N  
ATOM    978  CA  ILE A 123      23.412 -29.255  32.047  1.00 50.20           C  
ATOM    979  C   ILE A 123      23.208 -28.235  33.158  1.00 48.83           C  
ATOM    980  O   ILE A 123      22.925 -27.074  32.893  1.00 46.01           O  
ATOM    981  CB  ILE A 123      22.175 -30.171  31.958  1.00 46.59           C  
ATOM    982  CG1 ILE A 123      22.215 -30.983  30.672  1.00 49.79           C  
ATOM    983  CG2 ILE A 123      20.911 -29.355  31.961  1.00 48.02           C  
ATOM    984  CD1 ILE A 123      21.317 -32.194  30.692  1.00 50.49           C  
ATOM    985  N   ALA A 124      23.383 -28.690  34.399  1.00 47.31           N  
ATOM    986  CA  ALA A 124      23.333 -27.828  35.564  1.00 44.51           C  
ATOM    987  C   ALA A 124      24.329 -26.673  35.419  1.00 49.83           C  
ATOM    988  O   ALA A 124      23.965 -25.515  35.615  1.00 52.93           O  
ATOM    989  CB  ALA A 124      23.594 -28.630  36.828  1.00 40.51           C  
ATOM    990  N   LEU A 125      25.572 -26.981  35.049  1.00 51.81           N  
ATOM    991  CA  LEU A 125      26.600 -25.964  34.851  1.00 50.21           C  
ATOM    992  C   LEU A 125      26.182 -24.925  33.823  1.00 50.11           C  
ATOM    993  O   LEU A 125      26.169 -23.731  34.109  1.00 49.03           O  
ATOM    994  CB  LEU A 125      27.925 -26.603  34.403  1.00 54.29           C  
ATOM    995  CG  LEU A 125      29.058 -25.650  33.979  1.00 53.01           C  
ATOM    996  CD1 LEU A 125      29.484 -24.740  35.111  1.00 48.37           C  
ATOM    997  CD2 LEU A 125      30.226 -26.431  33.483  1.00 55.12           C  
ATOM    998  N   TRP A 126      25.846 -25.379  32.623  1.00 49.97           N  
ATOM    999  CA  TRP A 126      25.506 -24.444  31.559  1.00 52.70           C  
ATOM   1000  C   TRP A 126      24.205 -23.698  31.849  1.00 54.76           C  
ATOM   1001  O   TRP A 126      24.006 -22.564  31.392  1.00 54.56           O  
ATOM   1002  CB  TRP A 126      25.527 -25.128  30.188  1.00 51.46           C  
ATOM   1003  CG  TRP A 126      26.946 -25.304  29.729  1.00 54.93           C  
ATOM   1004  CD1 TRP A 126      27.688 -26.453  29.742  1.00 53.32           C  
ATOM   1005  CD2 TRP A 126      27.818 -24.272  29.254  1.00 54.13           C  
ATOM   1006  NE1 TRP A 126      28.956 -26.204  29.276  1.00 49.67           N  
ATOM   1007  CE2 TRP A 126      29.063 -24.873  28.969  1.00 54.45           C  
ATOM   1008  CE3 TRP A 126      27.663 -22.896  29.031  1.00 49.34           C  
ATOM   1009  CZ2 TRP A 126      30.147 -24.145  28.473  1.00 56.64           C  
ATOM   1010  CZ3 TRP A 126      28.730 -22.181  28.535  1.00 50.94           C  
ATOM   1011  CH2 TRP A 126      29.961 -22.801  28.267  1.00 54.96           C  
ATOM   1012  N   SER A 127      23.341 -24.322  32.644  1.00 53.28           N  
ATOM   1013  CA  SER A 127      22.160 -23.645  33.144  1.00 48.52           C  
ATOM   1014  C   SER A 127      22.573 -22.412  33.932  1.00 49.19           C  
ATOM   1015  O   SER A 127      22.078 -21.316  33.678  1.00 49.52           O  
ATOM   1016  CB  SER A 127      21.313 -24.578  33.997  1.00 46.63           C  
ATOM   1017  OG  SER A 127      20.542 -25.417  33.162  1.00 49.37           O  
ATOM   1018  N   LEU A 128      23.490 -22.587  34.873  1.00 45.73           N  
ATOM   1019  CA  LEU A 128      24.017 -21.452  35.620  1.00 51.29           C  
ATOM   1020  C   LEU A 128      24.633 -20.366  34.705  1.00 52.34           C  
ATOM   1021  O   LEU A 128      24.549 -19.154  34.978  1.00 45.96           O  
ATOM   1022  CB  LEU A 128      25.033 -21.931  36.662  1.00 48.54           C  
ATOM   1023  CG  LEU A 128      24.420 -22.710  37.822  1.00 45.78           C  
ATOM   1024  CD1 LEU A 128      25.332 -22.630  39.041  1.00 44.93           C  
ATOM   1025  CD2 LEU A 128      23.025 -22.189  38.132  1.00 44.92           C  
ATOM   1026  N   VAL A 129      25.259 -20.805  33.620  1.00 52.62           N  
ATOM   1027  CA  VAL A 129      25.773 -19.851  32.649  1.00 54.63           C  
ATOM   1028  C   VAL A 129      24.626 -19.128  31.932  1.00 48.42           C  
ATOM   1029  O   VAL A 129      24.538 -17.899  31.991  1.00 46.88           O  
ATOM   1030  CB  VAL A 129      26.772 -20.502  31.659  1.00 51.92           C  
ATOM   1031  CG1 VAL A 129      27.021 -19.597  30.471  1.00 47.69           C  
ATOM   1032  CG2 VAL A 129      28.052 -20.804  32.372  1.00 47.23           C  
ATOM   1033  N   VAL A 130      23.731 -19.891  31.304  1.00 47.77           N  
ATOM   1034  CA  VAL A 130      22.612 -19.298  30.547  1.00 53.99           C  
ATOM   1035  C   VAL A 130      21.747 -18.321  31.362  1.00 50.56           C  
ATOM   1036  O   VAL A 130      21.408 -17.234  30.895  1.00 44.29           O  
ATOM   1037  CB  VAL A 130      21.740 -20.380  29.871  1.00 49.29           C  
ATOM   1038  CG1 VAL A 130      20.426 -19.791  29.368  1.00 45.62           C  
ATOM   1039  CG2 VAL A 130      22.524 -21.010  28.737  1.00 50.34           C  
ATOM   1040  N   LEU A 131      21.434 -18.716  32.590  1.00 50.49           N  
ATOM   1041  CA  LEU A 131      20.706 -17.871  33.512  1.00 48.43           C  
ATOM   1042  C   LEU A 131      21.366 -16.507  33.581  1.00 48.32           C  
ATOM   1043  O   LEU A 131      20.726 -15.488  33.360  1.00 53.14           O  
ATOM   1044  CB  LEU A 131      20.697 -18.510  34.898  1.00 51.13           C  
ATOM   1045  CG  LEU A 131      19.854 -17.814  35.966  1.00 52.55           C  
ATOM   1046  CD1 LEU A 131      18.429 -17.631  35.496  1.00 50.53           C  
ATOM   1047  CD2 LEU A 131      19.878 -18.594  37.253  1.00 50.73           C  
ATOM   1048  N   ALA A 132      22.662 -16.499  33.857  1.00 51.28           N  
ATOM   1049  CA  ALA A 132      23.428 -15.262  33.971  1.00 46.86           C  
ATOM   1050  C   ALA A 132      23.351 -14.415  32.702  1.00 49.20           C  
ATOM   1051  O   ALA A 132      23.141 -13.209  32.786  1.00 48.56           O  
ATOM   1052  CB  ALA A 132      24.887 -15.572  34.324  1.00 48.36           C  
ATOM   1053  N   ILE A 133      23.523 -15.042  31.538  1.00 48.84           N  
ATOM   1054  CA  ILE A 133      23.439 -14.330  30.262  1.00 49.44           C  
ATOM   1055  C   ILE A 133      22.100 -13.615  30.127  1.00 53.36           C  
ATOM   1056  O   ILE A 133      22.047 -12.427  29.795  1.00 54.51           O  
ATOM   1057  CB  ILE A 133      23.584 -15.273  29.053  1.00 48.53           C  
ATOM   1058  CG1 ILE A 133      24.942 -15.972  29.063  1.00 48.17           C  
ATOM   1059  CG2 ILE A 133      23.398 -14.510  27.747  1.00 42.08           C  
ATOM   1060  CD1 ILE A 133      25.059 -17.073  28.010  1.00 45.76           C  
ATOM   1061  N   GLU A 134      21.020 -14.349  30.393  1.00 52.86           N  
ATOM   1062  CA  GLU A 134      19.668 -13.807  30.335  1.00 49.89           C  
ATOM   1063  C   GLU A 134      19.470 -12.644  31.286  1.00 52.90           C  
ATOM   1064  O   GLU A 134      19.009 -11.585  30.878  1.00 53.31           O  
ATOM   1065  CB  GLU A 134      18.659 -14.891  30.656  1.00 47.75           C  
ATOM   1066  CG  GLU A 134      18.632 -15.977  29.634  1.00 50.16           C  
ATOM   1067  CD  GLU A 134      17.761 -17.120  30.055  1.00 56.92           C  
ATOM   1068  OE1 GLU A 134      17.259 -17.086  31.207  1.00 59.03           O  
ATOM   1069  OE2 GLU A 134      17.583 -18.046  29.232  1.00 58.67           O  
ATOM   1070  N   ARG A 135      19.811 -12.844  32.553  1.00 49.28           N  
ATOM   1071  CA  ARG A 135      19.701 -11.779  33.538  1.00 51.26           C  
ATOM   1072  C   ARG A 135      20.510 -10.554  33.126  1.00 55.37           C  
ATOM   1073  O   ARG A 135      20.094  -9.413  33.333  1.00 55.06           O  
ATOM   1074  CB  ARG A 135      20.155 -12.260  34.904  1.00 48.17           C  
ATOM   1075  CG  ARG A 135      19.360 -13.419  35.423  1.00 45.09           C  
ATOM   1076  CD  ARG A 135      19.774 -13.757  36.836  1.00 49.71           C  
ATOM   1077  NE  ARG A 135      18.796 -14.631  37.465  1.00 54.99           N  
ATOM   1078  CZ  ARG A 135      18.967 -15.265  38.622  1.00 55.82           C  
ATOM   1079  NH1 ARG A 135      20.091 -15.147  39.316  1.00 49.60           N  
ATOM   1080  NH2 ARG A 135      17.993 -16.037  39.081  1.00 61.83           N  
ATOM   1081  N   TYR A 136      21.670 -10.790  32.530  1.00 57.73           N  
ATOM   1082  CA  TYR A 136      22.448  -9.695  31.970  1.00 57.89           C  
ATOM   1083  C   TYR A 136      21.638  -9.007  30.863  1.00 57.15           C  
ATOM   1084  O   TYR A 136      21.359  -7.821  30.953  1.00 57.11           O  
ATOM   1085  CB  TYR A 136      23.792 -10.213  31.463  1.00 53.51           C  
ATOM   1086  CG  TYR A 136      24.491  -9.289  30.520  1.00 53.07           C  
ATOM   1087  CD1 TYR A 136      25.121  -8.149  30.985  1.00 55.97           C  
ATOM   1088  CD2 TYR A 136      24.522  -9.554  29.155  1.00 53.31           C  
ATOM   1089  CE1 TYR A 136      25.756  -7.286  30.113  1.00 60.41           C  
ATOM   1090  CE2 TYR A 136      25.157  -8.708  28.277  1.00 55.52           C  
ATOM   1091  CZ  TYR A 136      25.772  -7.575  28.758  1.00 60.13           C  
ATOM   1092  OH  TYR A 136      26.407  -6.728  27.881  1.00 62.71           O  
ATOM   1093  N   VAL A 137      21.224  -9.767  29.854  1.00 54.47           N  
ATOM   1094  CA  VAL A 137      20.391  -9.239  28.773  1.00 58.14           C  
ATOM   1095  C   VAL A 137      19.149  -8.446  29.249  1.00 61.88           C  
ATOM   1096  O   VAL A 137      18.893  -7.327  28.786  1.00 58.46           O  
ATOM   1097  CB  VAL A 137      19.949 -10.371  27.817  1.00 54.58           C  
ATOM   1098  CG1 VAL A 137      18.683  -9.996  27.070  1.00 58.22           C  
ATOM   1099  CG2 VAL A 137      21.059 -10.702  26.856  1.00 54.05           C  
ATOM   1100  N   VAL A 138      18.388  -9.028  30.172  1.00 62.76           N  
ATOM   1101  CA  VAL A 138      17.122  -8.449  30.613  1.00 59.26           C  
ATOM   1102  C   VAL A 138      17.324  -7.218  31.496  1.00 57.81           C  
ATOM   1103  O   VAL A 138      16.704  -6.186  31.269  1.00 62.13           O  
ATOM   1104  CB  VAL A 138      16.264  -9.495  31.360  1.00 59.70           C  
ATOM   1105  CG1 VAL A 138      15.052  -8.850  31.978  1.00 58.67           C  
ATOM   1106  CG2 VAL A 138      15.862 -10.626  30.422  1.00 59.96           C  
ATOM   1107  N   VAL A 139      18.193  -7.324  32.495  1.00 55.97           N  
ATOM   1108  CA  VAL A 139      18.429  -6.202  33.399  1.00 56.48           C  
ATOM   1109  C   VAL A 139      19.362  -5.129  32.823  1.00 57.31           C  
ATOM   1110  O   VAL A 139      19.117  -3.950  33.000  1.00 65.58           O  
ATOM   1111  CB  VAL A 139      18.922  -6.648  34.805  1.00 54.11           C  
ATOM   1112  CG1 VAL A 139      19.302  -5.447  35.656  1.00 50.71           C  
ATOM   1113  CG2 VAL A 139      17.868  -7.473  35.516  1.00 53.60           C  
ATOM   1114  N   CYS A 140      20.422  -5.512  32.128  1.00 62.48           N  
ATOM   1115  CA  CYS A 140      21.373  -4.510  31.662  1.00 63.23           C  
ATOM   1116  C   CYS A 140      20.985  -3.871  30.332  1.00 64.64           C  
ATOM   1117  O   CYS A 140      21.628  -2.919  29.903  1.00 66.55           O  
ATOM   1118  CB  CYS A 140      22.787  -5.091  31.589  1.00 61.39           C  
ATOM   1119  SG  CYS A 140      23.495  -5.459  33.207  1.00 64.11           S  
ATOM   1120  N   LYS A 141      19.941  -4.390  29.693  1.00 66.55           N  
ATOM   1121  CA  LYS A 141      19.476  -3.880  28.399  1.00 70.19           C  
ATOM   1122  C   LYS A 141      20.592  -3.553  27.383  1.00 74.97           C  
ATOM   1123  O   LYS A 141      20.645  -2.449  26.850  1.00 83.82           O  
ATOM   1124  CB  LYS A 141      18.582  -2.643  28.616  1.00 71.81           C  
ATOM   1125  CG  LYS A 141      17.235  -2.921  29.294  1.00 66.00           C  
ATOM   1126  CD  LYS A 141      16.614  -1.652  29.879  1.00 76.47           C  
ATOM   1127  CE  LYS A 141      15.134  -1.844  30.221  1.00 81.56           C  
ATOM   1128  NZ  LYS A 141      14.542  -0.636  30.867  1.00 89.20           N  
ATOM   1129  N   PRO A 142      21.498  -4.512  27.113  1.00 86.79           N  
ATOM   1130  CA  PRO A 142      22.643  -4.252  26.222  1.00 86.79           C  
ATOM   1131  C   PRO A 142      22.242  -4.109  24.758  1.00 87.24           C  
ATOM   1132  O   PRO A 142      22.951  -3.504  23.955  1.00 89.37           O  
ATOM   1133  CB  PRO A 142      23.517  -5.490  26.410  1.00 86.79           C  
ATOM   1134  CG  PRO A 142      22.567  -6.559  26.772  1.00 86.79           C  
ATOM   1135  CD  PRO A 142      21.446  -5.924  27.527  1.00 86.79           C  
ATOM   1136  N   MET A 143      21.106  -4.707  24.424  1.00 92.34           N  
ATOM   1137  CA  MET A 143      20.515  -4.600  23.101  1.00 99.99           C  
ATOM   1138  C   MET A 143      19.400  -3.575  23.208  1.00113.72           C  
ATOM   1139  O   MET A 143      18.735  -3.476  24.241  1.00115.41           O  
ATOM   1140  CB  MET A 143      19.918  -5.940  22.662  1.00103.12           C  
ATOM   1141  CG  MET A 143      20.775  -7.154  22.992  1.00 97.28           C  
ATOM   1142  SD  MET A 143      20.424  -8.548  21.914  1.00 82.40           S  
ATOM   1143  CE  MET A 143      21.994  -9.405  21.950  1.00 98.72           C  
ATOM   1144  N   SER A 144      19.186  -2.798  22.154  1.00115.69           N  
ATOM   1145  CA  SER A 144      18.089  -1.834  22.178  1.00117.54           C  
ATOM   1146  C   SER A 144      16.785  -2.496  21.751  1.00118.99           C  
ATOM   1147  O   SER A 144      16.778  -3.362  20.873  1.00119.50           O  
ATOM   1148  CB  SER A 144      18.378  -0.629  21.275  1.00123.43           C  
ATOM   1149  OG  SER A 144      18.049  -0.910  19.924  1.00123.10           O  
ATOM   1150  N   ASN A 145      15.690  -2.096  22.390  1.00115.92           N  
ATOM   1151  CA  ASN A 145      14.342  -2.457  21.954  1.00123.41           C  
ATOM   1152  C   ASN A 145      14.107  -3.964  21.883  1.00119.94           C  
ATOM   1153  O   ASN A 145      13.298  -4.436  21.086  1.00118.47           O  
ATOM   1154  CB  ASN A 145      14.033  -1.801  20.600  1.00130.20           C  
ATOM   1155  CG  ASN A 145      13.964  -0.286  20.684  1.00131.09           C  
ATOM   1156  OD1 ASN A 145      13.243   0.267  21.513  1.00139.11           O  
ATOM   1157  ND2 ASN A 145      14.718   0.392  19.827  1.00125.92           N  
ATOM   1158  N   PHE A 146      14.827  -4.708  22.719  1.00127.35           N  
ATOM   1159  CA  PHE A 146      14.752  -6.171  22.741  1.00116.52           C  
ATOM   1160  C   PHE A 146      14.031  -6.697  23.981  1.00107.42           C  
ATOM   1161  O   PHE A 146      14.389  -6.356  25.107  1.00103.54           O  
ATOM   1162  CB  PHE A 146      16.164  -6.760  22.673  1.00111.51           C  
ATOM   1163  CG  PHE A 146      16.223  -8.237  22.954  1.00108.81           C  
ATOM   1164  CD1 PHE A 146      16.040  -9.157  21.940  1.00106.39           C  
ATOM   1165  CD2 PHE A 146      16.473  -8.708  24.235  1.00102.92           C  
ATOM   1166  CE1 PHE A 146      16.096 -10.509  22.203  1.00 94.14           C  
ATOM   1167  CE2 PHE A 146      16.521 -10.060  24.496  1.00 88.68           C  
ATOM   1168  CZ  PHE A 146      16.335 -10.956  23.483  1.00 87.14           C  
ATOM   1169  N   ARG A 147      13.027  -7.540  23.772  1.00113.86           N  
ATOM   1170  CA  ARG A 147      12.295  -8.121  24.889  1.00113.86           C  
ATOM   1171  C   ARG A 147      12.396  -9.639  24.891  1.00113.86           C  
ATOM   1172  O   ARG A 147      12.095 -10.301  23.895  1.00113.86           O  
ATOM   1173  CB  ARG A 147      10.829  -7.681  24.874  1.00114.21           C  
ATOM   1174  CG  ARG A 147      10.030  -8.164  26.079  1.00118.02           C  
ATOM   1175  CD  ARG A 147      10.422  -7.416  27.345  1.00124.98           C  
ATOM   1176  NE  ARG A 147       9.954  -8.081  28.559  1.00128.41           N  
ATOM   1177  CZ  ARG A 147      10.728  -8.815  29.355  1.00119.93           C  
ATOM   1178  NH1 ARG A 147      12.011  -8.981  29.067  1.00113.86           N  
ATOM   1179  NH2 ARG A 147      10.222  -9.381  30.441  1.00116.35           N  
ATOM   1180  N   PHE A 148      12.819 -10.170  26.032  1.00104.95           N  
ATOM   1181  CA  PHE A 148      13.048 -11.598  26.214  1.00 96.53           C  
ATOM   1182  C   PHE A 148      11.718 -12.325  26.383  1.00 93.09           C  
ATOM   1183  O   PHE A 148      10.852 -11.883  27.139  1.00 97.86           O  
ATOM   1184  CB  PHE A 148      13.985 -11.836  27.419  1.00 89.06           C  
ATOM   1185  CG  PHE A 148      14.304 -13.282  27.676  1.00 81.17           C  
ATOM   1186  CD1 PHE A 148      13.468 -14.058  28.464  1.00 79.47           C  
ATOM   1187  CD2 PHE A 148      15.441 -13.865  27.146  1.00 78.25           C  
ATOM   1188  CE1 PHE A 148      13.748 -15.382  28.702  1.00 70.89           C  
ATOM   1189  CE2 PHE A 148      15.725 -15.198  27.388  1.00 73.59           C  
ATOM   1190  CZ  PHE A 148      14.877 -15.951  28.164  1.00 69.74           C  
ATOM   1191  N   GLY A 149      11.577 -13.459  25.706  1.00 83.79           N  
ATOM   1192  CA  GLY A 149      10.298 -14.127  25.619  1.00 80.05           C  
ATOM   1193  C   GLY A 149      10.429 -15.620  25.435  1.00 74.49           C  
ATOM   1194  O   GLY A 149      11.522 -16.163  25.479  1.00 75.76           O  
ATOM   1195  N   GLU A 150       9.299 -16.286  25.253  1.00 76.65           N  
ATOM   1196  CA  GLU A 150       9.263 -17.737  25.218  1.00 71.05           C  
ATOM   1197  C   GLU A 150      10.284 -18.370  24.282  1.00 74.49           C  
ATOM   1198  O   GLU A 150      10.919 -19.346  24.648  1.00 76.28           O  
ATOM   1199  CB  GLU A 150       7.870 -18.231  24.856  1.00 69.58           C  
ATOM   1200  CG  GLU A 150       7.580 -19.572  25.458  1.00 70.43           C  
ATOM   1201  CD  GLU A 150       6.761 -20.443  24.554  1.00 74.45           C  
ATOM   1202  OE1 GLU A 150       6.832 -20.273  23.322  1.00 80.26           O  
ATOM   1203  OE2 GLU A 150       6.045 -21.311  25.070  1.00 79.02           O  
ATOM   1204  N   ASN A 151      10.445 -17.819  23.084  1.00 77.81           N  
ATOM   1205  CA  ASN A 151      11.306 -18.442  22.083  1.00 75.93           C  
ATOM   1206  C   ASN A 151      12.799 -18.350  22.370  1.00 75.93           C  
ATOM   1207  O   ASN A 151      13.577 -19.151  21.867  1.00 75.93           O  
ATOM   1208  CB  ASN A 151      10.993 -17.909  20.685  1.00 78.70           C  
ATOM   1209  CG  ASN A 151       9.742 -18.536  20.094  1.00 96.78           C  
ATOM   1210  OD1 ASN A 151       9.358 -19.645  20.471  1.00 91.29           O  
ATOM   1211  ND2 ASN A 151       9.099 -17.831  19.163  1.00110.44           N  
ATOM   1212  N   HIS A 152      13.198 -17.370  23.169  1.00 73.81           N  
ATOM   1213  CA  HIS A 152      14.592 -17.236  23.586  1.00 75.73           C  
ATOM   1214  C   HIS A 152      14.838 -18.207  24.716  1.00 73.58           C  
ATOM   1215  O   HIS A 152      15.856 -18.872  24.753  1.00 77.63           O  
ATOM   1216  CB  HIS A 152      14.903 -15.815  24.061  1.00 76.69           C  
ATOM   1217  CG  HIS A 152      14.629 -14.753  23.039  1.00 78.95           C  
ATOM   1218  ND1 HIS A 152      13.368 -14.499  22.545  1.00 79.46           N  
ATOM   1219  CD2 HIS A 152      15.456 -13.886  22.415  1.00 81.35           C  
ATOM   1220  CE1 HIS A 152      13.432 -13.527  21.655  1.00 75.72           C  
ATOM   1221  NE2 HIS A 152      14.687 -13.134  21.560  1.00 78.45           N  
ATOM   1222  N   ALA A 153      13.876 -18.299  25.626  1.00 69.60           N  
ATOM   1223  CA  ALA A 153      13.984 -19.177  26.783  1.00 71.68           C  
ATOM   1224  C   ALA A 153      14.127 -20.652  26.393  1.00 72.46           C  
ATOM   1225  O   ALA A 153      14.821 -21.423  27.068  1.00 71.15           O  
ATOM   1226  CB  ALA A 153      12.801 -18.982  27.701  1.00 65.42           C  
ATOM   1227  N   ILE A 154      13.469 -21.046  25.306  1.00 70.15           N  
ATOM   1228  CA  ILE A 154      13.634 -22.400  24.790  1.00 70.21           C  
ATOM   1229  C   ILE A 154      15.089 -22.609  24.348  1.00 72.38           C  
ATOM   1230  O   ILE A 154      15.753 -23.533  24.808  1.00 69.03           O  
ATOM   1231  CB  ILE A 154      12.688 -22.720  23.607  1.00 69.13           C  
ATOM   1232  CG1 ILE A 154      11.237 -22.285  23.890  1.00 71.93           C  
ATOM   1233  CG2 ILE A 154      12.764 -24.190  23.262  1.00 60.82           C  
ATOM   1234  CD1 ILE A 154      10.480 -23.138  24.867  1.00 70.27           C  
ATOM   1235  N   MET A 155      15.585 -21.742  23.472  1.00 81.71           N  
ATOM   1236  CA  MET A 155      16.944 -21.872  22.961  1.00 81.71           C  
ATOM   1237  C   MET A 155      17.976 -21.948  24.081  1.00 81.71           C  
ATOM   1238  O   MET A 155      18.886 -22.766  24.035  1.00 81.71           O  
ATOM   1239  CB  MET A 155      17.280 -20.711  22.040  1.00 81.71           C  
ATOM   1240  CG  MET A 155      16.801 -20.869  20.617  1.00 81.71           C  
ATOM   1241  SD  MET A 155      16.543 -19.250  19.867  1.00115.90           S  
ATOM   1242  CE  MET A 155      17.933 -18.322  20.529  1.00111.16           C  
ATOM   1243  N   GLY A 156      17.824 -21.095  25.087  1.00 63.15           N  
ATOM   1244  CA  GLY A 156      18.697 -21.112  26.251  1.00 61.74           C  
ATOM   1245  C   GLY A 156      18.768 -22.500  26.875  1.00 63.80           C  
ATOM   1246  O   GLY A 156      19.851 -23.034  27.121  1.00 61.98           O  
ATOM   1247  N   VAL A 157      17.600 -23.087  27.123  1.00 65.49           N  
ATOM   1248  CA  VAL A 157      17.495 -24.480  27.559  1.00 62.20           C  
ATOM   1249  C   VAL A 157      18.192 -25.434  26.579  1.00 57.84           C  
ATOM   1250  O   VAL A 157      19.046 -26.215  26.983  1.00 54.38           O  
ATOM   1251  CB  VAL A 157      16.006 -24.900  27.734  1.00 60.87           C  
ATOM   1252  CG1 VAL A 157      15.896 -26.373  28.072  1.00 53.48           C  
ATOM   1253  CG2 VAL A 157      15.322 -24.033  28.794  1.00 56.50           C  
ATOM   1254  N   ALA A 158      17.831 -25.348  25.298  1.00 58.80           N  
ATOM   1255  CA  ALA A 158      18.374 -26.235  24.275  1.00 56.97           C  
ATOM   1256  C   ALA A 158      19.893 -26.090  24.181  1.00 59.26           C  
ATOM   1257  O   ALA A 158      20.625 -27.076  24.068  1.00 60.00           O  
ATOM   1258  CB  ALA A 158      17.723 -25.966  22.934  1.00 55.99           C  
ATOM   1259  N   PHE A 159      20.364 -24.853  24.258  1.00 60.45           N  
ATOM   1260  CA  PHE A 159      21.798 -24.561  24.224  1.00 55.49           C  
ATOM   1261  C   PHE A 159      22.601 -25.263  25.318  1.00 56.38           C  
ATOM   1262  O   PHE A 159      23.752 -25.623  25.097  1.00 57.68           O  
ATOM   1263  CB  PHE A 159      22.032 -23.058  24.295  1.00 48.58           C  
ATOM   1264  CG  PHE A 159      23.456 -22.679  24.488  1.00 45.51           C  
ATOM   1265  CD1 PHE A 159      24.341 -22.703  23.428  1.00 46.36           C  
ATOM   1266  CD2 PHE A 159      23.916 -22.278  25.729  1.00 49.12           C  
ATOM   1267  CE1 PHE A 159      25.669 -22.336  23.604  1.00 44.20           C  
ATOM   1268  CE2 PHE A 159      25.245 -21.906  25.915  1.00 47.17           C  
ATOM   1269  CZ  PHE A 159      26.118 -21.936  24.850  1.00 41.95           C  
ATOM   1270  N   THR A 160      21.995 -25.461  26.489  1.00 55.78           N  
ATOM   1271  CA  THR A 160      22.658 -26.168  27.588  1.00 55.64           C  
ATOM   1272  C   THR A 160      22.770 -27.683  27.309  1.00 57.41           C  
ATOM   1273  O   THR A 160      23.704 -28.334  27.794  1.00 56.93           O  
ATOM   1274  CB  THR A 160      21.984 -25.910  28.959  1.00 54.64           C  
ATOM   1275  OG1 THR A 160      20.653 -26.429  28.952  1.00 55.05           O  
ATOM   1276  CG2 THR A 160      21.905 -24.419  29.248  1.00 53.40           C  
ATOM   1277  N   TRP A 161      21.821 -28.222  26.540  1.00 55.60           N  
ATOM   1278  CA ATRP A 161      21.838 -29.629  26.168  0.42 56.09           C  
ATOM   1279  CA BTRP A 161      21.852 -29.626  26.156  0.58 54.77           C  
ATOM   1280  C   TRP A 161      22.900 -29.894  25.111  1.00 59.12           C  
ATOM   1281  O   TRP A 161      23.543 -30.912  25.155  1.00 57.34           O  
ATOM   1282  CB ATRP A 161      20.460 -30.071  25.687  0.42 51.64           C  
ATOM   1283  CB BTRP A 161      20.509 -30.036  25.602  0.58 56.48           C  
ATOM   1284  CG ATRP A 161      19.493 -30.198  26.846  0.42 54.69           C  
ATOM   1285  CG BTRP A 161      19.461 -29.980  26.619  0.58 54.62           C  
ATOM   1286  CD1ATRP A 161      18.882 -29.176  27.532  0.42 53.77           C  
ATOM   1287  CD1BTRP A 161      19.635 -29.873  27.970  0.58 53.15           C  
ATOM   1288  CD2ATRP A 161      19.055 -31.413  27.474  0.42 54.72           C  
ATOM   1289  CD2BTRP A 161      18.054 -30.028  26.395  0.58 52.80           C  
ATOM   1290  NE1ATRP A 161      18.087 -29.684  28.536  0.42 51.74           N  
ATOM   1291  NE1BTRP A 161      18.419 -29.857  28.601  0.58 51.58           N  
ATOM   1292  CE2ATRP A 161      18.174 -31.053  28.521  0.42 52.76           C  
ATOM   1293  CE2BTRP A 161      17.431 -29.951  27.655  0.58 51.98           C  
ATOM   1294  CE3ATRP A 161      19.316 -32.774  27.250  0.42 50.78           C  
ATOM   1295  CE3BTRP A 161      17.255 -30.133  25.252  0.58 50.72           C  
ATOM   1296  CZ2ATRP A 161      17.551 -32.006  29.338  0.42 50.86           C  
ATOM   1297  CZ2BTRP A 161      16.047 -29.973  27.805  0.58 51.43           C  
ATOM   1298  CZ3ATRP A 161      18.696 -33.715  28.066  0.42 49.66           C  
ATOM   1299  CZ3BTRP A 161      15.879 -30.156  25.404  0.58 48.89           C  
ATOM   1300  CH2ATRP A 161      17.825 -33.325  29.093  0.42 50.50           C  
ATOM   1301  CH2BTRP A 161      15.290 -30.077  26.671  0.58 50.32           C  
ATOM   1302  N   VAL A 162      23.034 -28.967  24.159  1.00 56.10           N  
ATOM   1303  CA  VAL A 162      24.056 -29.069  23.120  1.00 54.21           C  
ATOM   1304  C   VAL A 162      25.428 -28.929  23.777  1.00 56.88           C  
ATOM   1305  O   VAL A 162      26.323 -29.729  23.538  1.00 56.23           O  
ATOM   1306  CB  VAL A 162      23.817 -28.038  22.007  1.00 50.76           C  
ATOM   1307  CG1 VAL A 162      25.077 -27.791  21.221  1.00 46.77           C  
ATOM   1308  CG2 VAL A 162      22.705 -28.494  21.096  1.00 44.17           C  
ATOM   1309  N   MET A 163      25.563 -27.970  24.679  1.00 54.32           N  
ATOM   1310  CA  MET A 163      26.808 -27.843  25.421  1.00 56.55           C  
ATOM   1311  C   MET A 163      27.122 -29.076  26.273  1.00 58.88           C  
ATOM   1312  O   MET A 163      28.255 -29.562  26.288  1.00 59.09           O  
ATOM   1313  CB  MET A 163      26.823 -26.578  26.276  1.00 54.98           C  
ATOM   1314  CG  MET A 163      26.876 -25.331  25.452  1.00 53.69           C  
ATOM   1315  SD  MET A 163      28.161 -25.453  24.201  1.00 59.05           S  
ATOM   1316  CE  MET A 163      29.626 -25.302  25.223  1.00 50.53           C  
ATOM   1317  N   ALA A 164      26.119 -29.599  26.966  1.00 57.80           N  
ATOM   1318  CA  ALA A 164      26.342 -30.760  27.824  1.00 57.19           C  
ATOM   1319  C   ALA A 164      26.671 -32.030  27.032  1.00 57.41           C  
ATOM   1320  O   ALA A 164      27.456 -32.857  27.481  1.00 58.37           O  
ATOM   1321  CB  ALA A 164      25.151 -30.991  28.736  1.00 54.74           C  
ATOM   1322  N   LEU A 165      26.069 -32.193  25.859  1.00 55.23           N  
ATOM   1323  CA  LEU A 165      26.404 -33.328  25.003  1.00 51.66           C  
ATOM   1324  C   LEU A 165      27.804 -33.150  24.431  1.00 54.73           C  
ATOM   1325  O   LEU A 165      28.541 -34.107  24.269  1.00 51.39           O  
ATOM   1326  CB  LEU A 165      25.374 -33.496  23.884  1.00 50.66           C  
ATOM   1327  CG  LEU A 165      24.053 -34.113  24.347  1.00 55.67           C  
ATOM   1328  CD1 LEU A 165      22.990 -34.090  23.249  1.00 51.35           C  
ATOM   1329  CD2 LEU A 165      24.299 -35.532  24.848  1.00 51.90           C  
ATOM   1330  N   ALA A 166      28.170 -31.902  24.159  1.00 56.96           N  
ATOM   1331  CA  ALA A 166      29.483 -31.557  23.636  1.00 53.24           C  
ATOM   1332  C   ALA A 166      30.586 -31.915  24.628  1.00 57.51           C  
ATOM   1333  O   ALA A 166      31.772 -31.958  24.281  1.00 61.50           O  
ATOM   1334  CB  ALA A 166      29.535 -30.070  23.307  1.00 55.63           C  
ATOM   1335  N   CYS A 167      30.178 -32.166  25.865  1.00 56.80           N  
ATOM   1336  CA  CYS A 167      31.072 -32.593  26.934  1.00 59.63           C  
ATOM   1337  C   CYS A 167      30.975 -34.114  27.211  1.00 58.09           C  
ATOM   1338  O   CYS A 167      31.963 -34.840  27.072  1.00 54.80           O  
ATOM   1339  CB  CYS A 167      30.805 -31.767  28.192  1.00 56.58           C  
ATOM   1340  SG  CYS A 167      31.725 -32.337  29.617  1.00 68.82           S  
ATOM   1341  N   ALA A 168      29.788 -34.565  27.616  1.00 53.60           N  
ATOM   1342  CA  ALA A 168      29.495 -35.970  27.923  1.00 55.05           C  
ATOM   1343  C   ALA A 168      29.596 -36.980  26.759  1.00 57.53           C  
ATOM   1344  O   ALA A 168      30.091 -38.093  26.949  1.00 53.12           O  
ATOM   1345  CB  ALA A 168      28.118 -36.077  28.583  1.00 56.38           C  
ATOM   1346  N   ALA A 169      29.113 -36.607  25.574  1.00 54.63           N  
ATOM   1347  CA  ALA A 169      29.122 -37.517  24.418  1.00 53.22           C  
ATOM   1348  C   ALA A 169      30.491 -38.007  23.905  1.00 55.55           C  
ATOM   1349  O   ALA A 169      30.621 -39.187  23.600  1.00 52.55           O  
ATOM   1350  CB  ALA A 169      28.294 -36.963  23.265  1.00 43.35           C  
ATOM   1351  N   PRO A 170      31.503 -37.114  23.781  1.00 52.86           N  
ATOM   1352  CA  PRO A 170      32.808 -37.540  23.240  1.00 54.72           C  
ATOM   1353  C   PRO A 170      33.502 -38.770  23.884  1.00 54.14           C  
ATOM   1354  O   PRO A 170      34.009 -39.594  23.130  1.00 50.79           O  
ATOM   1355  CB  PRO A 170      33.675 -36.275  23.374  1.00 55.03           C  
ATOM   1356  CG  PRO A 170      32.702 -35.174  23.314  1.00 53.84           C  
ATOM   1357  CD  PRO A 170      31.472 -35.656  24.001  1.00 50.19           C  
ATOM   1358  N   PRO A 171      33.534 -38.892  25.229  1.00 55.05           N  
ATOM   1359  CA  PRO A 171      34.160 -40.100  25.778  1.00 50.31           C  
ATOM   1360  C   PRO A 171      33.471 -41.402  25.373  1.00 53.84           C  
ATOM   1361  O   PRO A 171      34.124 -42.440  25.365  1.00 61.75           O  
ATOM   1362  CB  PRO A 171      34.051 -39.898  27.290  1.00 51.16           C  
ATOM   1363  CG  PRO A 171      33.981 -38.442  27.472  1.00 54.87           C  
ATOM   1364  CD  PRO A 171      33.207 -37.927  26.295  1.00 54.09           C  
ATOM   1365  N   LEU A 172      32.179 -41.369  25.072  1.00 52.91           N  
ATOM   1366  CA  LEU A 172      31.501 -42.559  24.569  1.00 52.71           C  
ATOM   1367  C   LEU A 172      32.098 -42.942  23.223  1.00 54.55           C  
ATOM   1368  O   LEU A 172      32.141 -44.112  22.863  1.00 60.60           O  
ATOM   1369  CB  LEU A 172      29.988 -42.350  24.423  1.00 45.36           C  
ATOM   1370  CG  LEU A 172      29.203 -42.251  25.730  1.00 48.83           C  
ATOM   1371  CD1 LEU A 172      27.728 -42.349  25.485  1.00 45.38           C  
ATOM   1372  CD2 LEU A 172      29.643 -43.318  26.714  1.00 50.71           C  
ATOM   1373  N   VAL A 173      32.525 -41.934  22.470  1.00 57.87           N  
ATOM   1374  CA  VAL A 173      33.141 -42.161  21.156  1.00 57.77           C  
ATOM   1375  C   VAL A 173      34.677 -42.180  20.938  1.00 56.66           C  
ATOM   1376  O   VAL A 173      35.138 -42.230  19.809  1.00 58.93           O  
ATOM   1377  CB  VAL A 173      32.294 -41.571  19.963  1.00 57.91           C  
ATOM   1378  CG1 VAL A 173      30.996 -42.342  19.843  1.00 50.62           C  
ATOM   1379  CG2 VAL A 173      32.036 -40.088  20.137  1.00 52.69           C  
ATOM   1380  N   GLY A 174      35.465 -42.128  22.000  1.00 53.58           N  
ATOM   1381  CA  GLY A 174      36.900 -42.218  21.802  1.00 56.26           C  
ATOM   1382  C   GLY A 174      37.718 -40.976  22.076  1.00 62.33           C  
ATOM   1383  O   GLY A 174      38.950 -41.012  21.987  1.00 69.33           O  
ATOM   1384  N   TRP A 175      37.047 -39.866  22.370  1.00 62.07           N  
ATOM   1385  CA  TRP A 175      37.722 -38.687  22.906  1.00 59.74           C  
ATOM   1386  C   TRP A 175      37.507 -38.610  24.430  1.00 58.84           C  
ATOM   1387  O   TRP A 175      36.406 -38.364  24.922  1.00 57.92           O  
ATOM   1388  CB  TRP A 175      37.278 -37.417  22.181  1.00 59.97           C  
ATOM   1389  CG  TRP A 175      38.267 -36.292  22.319  1.00 62.11           C  
ATOM   1390  CD1 TRP A 175      39.587 -36.389  22.690  1.00 63.69           C  
ATOM   1391  CD2 TRP A 175      38.013 -34.896  22.105  1.00 63.46           C  
ATOM   1392  NE1 TRP A 175      40.165 -35.135  22.714  1.00 62.85           N  
ATOM   1393  CE2 TRP A 175      39.223 -34.204  22.361  1.00 62.93           C  
ATOM   1394  CE3 TRP A 175      36.879 -34.163  21.725  1.00 59.70           C  
ATOM   1395  CZ2 TRP A 175      39.329 -32.816  22.243  1.00 61.30           C  
ATOM   1396  CZ3 TRP A 175      36.988 -32.784  21.607  1.00 55.18           C  
ATOM   1397  CH2 TRP A 175      38.203 -32.127  21.868  1.00 61.72           C  
ATOM   1398  N   SER A 176      38.616 -38.803  25.130  1.00 57.99           N  
ATOM   1399  CA  SER A 176      38.728 -39.387  26.468  1.00 58.60           C  
ATOM   1400  C   SER A 176      37.986 -40.723  26.613  1.00 57.32           C  
ATOM   1401  O   SER A 176      37.845 -41.453  25.639  1.00 53.90           O  
ATOM   1402  CB  SER A 176      38.265 -38.424  27.543  1.00 56.09           C  
ATOM   1403  OG  SER A 176      38.766 -38.756  28.833  1.00 55.86           O  
ATOM   1404  N   ARG A 177      37.480 -41.010  27.814  1.00 54.69           N  
ATOM   1405  CA  ARG A 177      36.795 -42.275  28.118  1.00 53.12           C  
ATOM   1406  C   ARG A 177      36.047 -42.194  29.468  1.00 55.89           C  
ATOM   1407  O   ARG A 177      36.369 -41.328  30.292  1.00 55.55           O  
ATOM   1408  CB  ARG A 177      37.774 -43.457  28.058  1.00 53.08           C  
ATOM   1409  CG  ARG A 177      39.011 -43.255  28.890  1.00 55.99           C  
ATOM   1410  CD  ARG A 177      39.945 -44.449  28.839  1.00 61.60           C  
ATOM   1411  NE  ARG A 177      40.840 -44.431  29.997  1.00 61.07           N  
ATOM   1412  CZ  ARG A 177      41.619 -45.440  30.357  1.00 50.13           C  
ATOM   1413  NH1 ARG A 177      41.624 -46.545  29.642  1.00 53.38           N  
ATOM   1414  NH2 ARG A 177      42.384 -45.338  31.432  1.00 48.38           N  
ATOM   1415  N   TYR A 178      35.098 -43.093  29.736  1.00 50.51           N  
ATOM   1416  CA  TYR A 178      34.628 -43.210  31.126  1.00 51.06           C  
ATOM   1417  C   TYR A 178      35.293 -44.370  31.854  1.00 46.15           C  
ATOM   1418  O   TYR A 178      35.343 -45.481  31.348  1.00 59.04           O  
ATOM   1419  CB  TYR A 178      33.090 -43.296  31.244  1.00 56.54           C  
ATOM   1420  CG  TYR A 178      32.384 -42.078  30.720  1.00 52.77           C  
ATOM   1421  CD1 TYR A 178      32.332 -40.906  31.469  1.00 50.71           C  
ATOM   1422  CD2 TYR A 178      31.784 -42.099  29.461  1.00 51.80           C  
ATOM   1423  CE1 TYR A 178      31.692 -39.776  30.974  1.00 55.16           C  
ATOM   1424  CE2 TYR A 178      31.149 -40.995  28.952  1.00 53.53           C  
ATOM   1425  CZ  TYR A 178      31.098 -39.823  29.713  1.00 57.36           C  
ATOM   1426  OH  TYR A 178      30.460 -38.700  29.215  1.00 51.39           O  
ATOM   1427  N   ILE A 179      35.818 -44.119  33.042  1.00 38.73           N  
ATOM   1428  CA  ILE A 179      36.426 -45.199  33.821  1.00 46.87           C  
ATOM   1429  C   ILE A 179      36.048 -45.011  35.282  1.00 44.28           C  
ATOM   1430  O   ILE A 179      35.754 -43.896  35.687  1.00 39.47           O  
ATOM   1431  CB  ILE A 179      38.018 -45.291  33.657  1.00 45.67           C  
ATOM   1432  CG1 ILE A 179      38.713 -44.058  34.242  1.00 48.43           C  
ATOM   1433  CG2 ILE A 179      38.439 -45.473  32.196  1.00 41.72           C  
ATOM   1434  CD1 ILE A 179      40.234 -44.161  34.266  1.00 50.90           C  
ATOM   1435  N   PRO A 180      36.041 -46.100  36.075  1.00 45.56           N  
ATOM   1436  CA  PRO A 180      35.800 -45.908  37.510  1.00 47.00           C  
ATOM   1437  C   PRO A 180      36.788 -44.884  38.044  1.00 46.10           C  
ATOM   1438  O   PRO A 180      37.907 -44.833  37.551  1.00 48.16           O  
ATOM   1439  CB  PRO A 180      36.084 -47.293  38.107  1.00 43.23           C  
ATOM   1440  CG  PRO A 180      35.872 -48.238  36.999  1.00 45.23           C  
ATOM   1441  CD  PRO A 180      36.225 -47.519  35.729  1.00 44.50           C  
ATOM   1442  N   GLU A 181      36.387 -44.057  38.997  1.00 46.96           N  
ATOM   1443  CA  GLU A 181      37.309 -43.077  39.552  1.00 51.79           C  
ATOM   1444  C   GLU A 181      37.354 -43.177  41.064  1.00 51.41           C  
ATOM   1445  O   GLU A 181      36.433 -43.712  41.680  1.00 51.07           O  
ATOM   1446  CB  GLU A 181      36.910 -41.659  39.146  1.00 47.62           C  
ATOM   1447  CG  GLU A 181      35.638 -41.177  39.821  1.00 56.70           C  
ATOM   1448  CD  GLU A 181      35.315 -39.708  39.559  1.00 64.75           C  
ATOM   1449  OE1 GLU A 181      36.264 -38.922  39.324  1.00 64.78           O  
ATOM   1450  OE2 GLU A 181      34.106 -39.353  39.590  1.00 66.18           O  
ATOM   1451  N   GLY A 182      38.423 -42.652  41.661  1.00 46.27           N  
ATOM   1452  CA  GLY A 182      38.488 -42.556  43.109  1.00 46.22           C  
ATOM   1453  C   GLY A 182      38.523 -43.930  43.731  1.00 46.50           C  
ATOM   1454  O   GLY A 182      39.415 -44.736  43.489  1.00 46.53           O  
ATOM   1455  N   MET A 183      37.502 -44.195  44.531  1.00 49.86           N  
ATOM   1456  CA  MET A 183      37.325 -45.482  45.193  1.00 49.58           C  
ATOM   1457  C   MET A 183      36.705 -46.511  44.232  1.00 44.64           C  
ATOM   1458  O   MET A 183      36.382 -47.642  44.616  1.00 40.02           O  
ATOM   1459  CB  MET A 183      36.504 -45.303  46.460  1.00 47.87           C  
ATOM   1460  CG  MET A 183      37.222 -44.436  47.460  1.00 46.98           C  
ATOM   1461  SD  MET A 183      36.140 -43.982  48.812  1.00 49.10           S  
ATOM   1462  CE  MET A 183      35.842 -45.568  49.586  1.00 48.43           C  
ATOM   1463  N   GLN A 184      36.558 -46.068  42.980  1.00 43.56           N  
ATOM   1464  CA  GLN A 184      36.171 -46.886  41.831  1.00 45.22           C  
ATOM   1465  C   GLN A 184      34.742 -47.368  41.929  1.00 47.79           C  
ATOM   1466  O   GLN A 184      34.372 -48.364  41.307  1.00 50.32           O  
ATOM   1467  CB  GLN A 184      37.090 -48.134  41.742  1.00 49.23           C  
ATOM   1468  CG  GLN A 184      38.618 -47.885  41.819  1.00 41.77           C  
ATOM   1469  CD  GLN A 184      39.176 -47.242  40.562  1.00 41.67           C  
ATOM   1470  OE1 GLN A 184      39.099 -47.820  39.478  1.00 36.05           O  
ATOM   1471  NE2 GLN A 184      39.705 -46.029  40.694  1.00 40.07           N  
ATOM   1472  N   CYS A 185      33.934 -46.657  42.706  1.00 51.69           N  
ATOM   1473  CA  CYS A 185      32.521 -46.982  42.809  1.00 47.95           C  
ATOM   1474  C   CYS A 185      31.665 -46.195  41.843  1.00 53.31           C  
ATOM   1475  O   CYS A 185      30.483 -46.506  41.655  1.00 55.95           O  
ATOM   1476  CB  CYS A 185      32.024 -46.744  44.225  1.00 46.42           C  
ATOM   1477  SG  CYS A 185      32.617 -47.975  45.360  1.00 46.89           S  
ATOM   1478  N   SER A 186      32.255 -45.187  41.217  1.00 48.75           N  
ATOM   1479  CA  SER A 186      31.501 -44.329  40.325  1.00 48.77           C  
ATOM   1480  C   SER A 186      32.381 -43.991  39.146  1.00 49.80           C  
ATOM   1481  O   SER A 186      33.595 -43.967  39.289  1.00 50.67           O  
ATOM   1482  CB  SER A 186      31.087 -43.075  41.071  1.00 49.35           C  
ATOM   1483  OG  SER A 186      32.196 -42.576  41.796  1.00 58.97           O  
ATOM   1484  N   CYS A 187      31.778 -43.751  37.986  1.00 48.43           N  
ATOM   1485  CA  CYS A 187      32.543 -43.480  36.776  1.00 47.94           C  
ATOM   1486  C   CYS A 187      32.486 -42.015  36.322  1.00 50.50           C  
ATOM   1487  O   CYS A 187      31.448 -41.373  36.445  1.00 55.51           O  
ATOM   1488  CB  CYS A 187      32.092 -44.420  35.663  1.00 46.22           C  
ATOM   1489  SG  CYS A 187      32.465 -46.154  36.012  1.00 53.96           S  
ATOM   1490  N   GLY A 188      33.600 -41.511  35.787  1.00 48.42           N  
ATOM   1491  CA  GLY A 188      33.734 -40.132  35.363  1.00 45.66           C  
ATOM   1492  C   GLY A 188      34.721 -40.003  34.209  1.00 48.70           C  
ATOM   1493  O   GLY A 188      35.294 -40.970  33.741  1.00 50.83           O  
ATOM   1494  N   ILE A 189      34.930 -38.786  33.738  1.00 58.99           N  
ATOM   1495  CA  ILE A 189      35.815 -38.557  32.603  1.00 55.22           C  
ATOM   1496  C   ILE A 189      37.219 -38.868  33.059  1.00 55.83           C  
ATOM   1497  O   ILE A 189      37.553 -38.579  34.204  1.00 53.83           O  
ATOM   1498  CB  ILE A 189      35.700 -37.087  32.121  1.00 55.97           C  
ATOM   1499  CG1 ILE A 189      34.507 -36.930  31.166  1.00 53.95           C  
ATOM   1500  CG2 ILE A 189      36.991 -36.584  31.467  1.00 49.37           C  
ATOM   1501  CD1 ILE A 189      34.260 -35.512  30.708  1.00 48.84           C  
ATOM   1502  N   ASP A 190      38.056 -39.432  32.185  1.00 58.56           N  
ATOM   1503  CA  ASP A 190      39.425 -39.647  32.621  1.00 58.30           C  
ATOM   1504  C   ASP A 190      40.206 -38.410  32.208  1.00 56.73           C  
ATOM   1505  O   ASP A 190      40.571 -38.215  31.050  1.00 58.45           O  
ATOM   1506  CB  ASP A 190      39.980 -40.882  31.901  1.00 61.18           C  
ATOM   1507  CG  ASP A 190      41.438 -41.167  32.234  1.00 57.93           C  
ATOM   1508  OD1 ASP A 190      41.918 -40.681  33.280  1.00 53.03           O  
ATOM   1509  OD2 ASP A 190      42.084 -41.896  31.443  1.00 55.74           O  
ATOM   1510  N   TYR A 191      40.439 -37.558  33.198  1.00 58.03           N  
ATOM   1511  CA  TYR A 191      41.279 -36.392  33.023  1.00 59.84           C  
ATOM   1512  C   TYR A 191      42.653 -36.608  33.644  1.00 57.86           C  
ATOM   1513  O   TYR A 191      43.547 -35.794  33.447  1.00 64.62           O  
ATOM   1514  CB  TYR A 191      40.583 -35.160  33.645  1.00 52.80           C  
ATOM   1515  CG  TYR A 191      40.336 -35.300  35.134  1.00 52.07           C  
ATOM   1516  CD1 TYR A 191      39.330 -36.132  35.615  1.00 50.43           C  
ATOM   1517  CD2 TYR A 191      41.127 -34.620  36.062  1.00 54.24           C  
ATOM   1518  CE1 TYR A 191      39.112 -36.285  36.972  1.00 52.88           C  
ATOM   1519  CE2 TYR A 191      40.918 -34.761  37.425  1.00 55.72           C  
ATOM   1520  CZ  TYR A 191      39.908 -35.596  37.872  1.00 61.32           C  
ATOM   1521  OH  TYR A 191      39.693 -35.746  39.227  1.00 67.84           O  
ATOM   1522  N   TYR A 192      42.814 -37.694  34.397  1.00 54.17           N  
ATOM   1523  CA  TYR A 192      44.035 -37.872  35.188  1.00 57.28           C  
ATOM   1524  C   TYR A 192      45.071 -38.814  34.588  1.00 54.42           C  
ATOM   1525  O   TYR A 192      46.154 -38.970  35.125  1.00 59.41           O  
ATOM   1526  CB  TYR A 192      43.699 -38.264  36.631  1.00 55.63           C  
ATOM   1527  CG  TYR A 192      42.634 -39.317  36.682  1.00 58.36           C  
ATOM   1528  CD1 TYR A 192      41.292 -38.969  36.706  1.00 52.89           C  
ATOM   1529  CD2 TYR A 192      42.966 -40.672  36.636  1.00 58.36           C  
ATOM   1530  CE1 TYR A 192      40.311 -39.926  36.730  1.00 53.21           C  
ATOM   1531  CE2 TYR A 192      41.983 -41.646  36.654  1.00 55.28           C  
ATOM   1532  CZ  TYR A 192      40.658 -41.264  36.702  1.00 56.94           C  
ATOM   1533  OH  TYR A 192      39.678 -42.225  36.719  1.00 55.06           O  
ATOM   1534  N   THR A 193      44.743 -39.432  33.467  1.00 55.86           N  
ATOM   1535  CA  THR A 193      45.579 -40.493  32.914  1.00 56.91           C  
ATOM   1536  C   THR A 193      45.901 -40.127  31.479  1.00 60.75           C  
ATOM   1537  O   THR A 193      45.022 -39.637  30.741  1.00 62.85           O  
ATOM   1538  CB  THR A 193      44.828 -41.857  32.964  1.00 56.56           C  
ATOM   1539  OG1 THR A 193      45.200 -42.572  34.149  1.00 54.16           O  
ATOM   1540  CG2 THR A 193      45.073 -42.701  31.716  1.00 50.41           C  
ATOM   1541  N   PRO A 194      47.157 -40.368  31.065  1.00 66.18           N  
ATOM   1542  CA  PRO A 194      47.552 -39.871  29.749  1.00 64.04           C  
ATOM   1543  C   PRO A 194      47.294 -40.912  28.697  1.00 65.34           C  
ATOM   1544  O   PRO A 194      48.238 -41.323  28.047  1.00 70.74           O  
ATOM   1545  CB  PRO A 194      49.062 -39.667  29.894  1.00 62.22           C  
ATOM   1546  CG  PRO A 194      49.337 -39.766  31.352  1.00 62.39           C  
ATOM   1547  CD  PRO A 194      48.332 -40.716  31.873  1.00 62.70           C  
ATOM   1548  N   HIS A 195      46.044 -41.275  28.463  1.00 63.91           N  
ATOM   1549  CA  HIS A 195      45.796 -42.465  27.699  1.00 64.64           C  
ATOM   1550  C   HIS A 195      45.709 -42.015  26.251  1.00 66.67           C  
ATOM   1551  O   HIS A 195      44.712 -41.465  25.815  1.00 66.12           O  
ATOM   1552  CB  HIS A 195      44.484 -43.060  28.196  1.00 57.72           C  
ATOM   1553  CG  HIS A 195      44.102 -44.348  27.542  1.00 62.18           C  
ATOM   1554  ND1 HIS A 195      43.179 -44.411  26.523  1.00 65.12           N  
ATOM   1555  CD2 HIS A 195      44.474 -45.627  27.789  1.00 61.47           C  
ATOM   1556  CE1 HIS A 195      43.015 -45.668  26.153  1.00 64.12           C  
ATOM   1557  NE2 HIS A 195      43.792 -46.426  26.903  1.00 64.18           N  
ATOM   1558  N   GLU A 196      46.742 -42.332  25.483  1.00 73.64           N  
ATOM   1559  CA  GLU A 196      46.961 -41.646  24.218  1.00 71.92           C  
ATOM   1560  C   GLU A 196      46.054 -42.205  23.141  1.00 69.64           C  
ATOM   1561  O   GLU A 196      45.865 -41.601  22.089  1.00 69.64           O  
ATOM   1562  CB  GLU A 196      48.432 -41.747  23.787  1.00 69.83           C  
ATOM   1563  CG  GLU A 196      49.382 -40.769  24.489  1.00 77.75           C  
ATOM   1564  CD  GLU A 196      50.153 -41.409  25.631  1.00 88.84           C  
ATOM   1565  OE1 GLU A 196      49.832 -42.572  25.973  1.00 93.91           O  
ATOM   1566  OE2 GLU A 196      51.076 -40.757  26.181  1.00 84.71           O  
ATOM   1567  N   GLU A 197      45.490 -43.367  23.423  1.00 65.79           N  
ATOM   1568  CA  GLU A 197      44.675 -44.065  22.453  1.00 66.85           C  
ATOM   1569  C   GLU A 197      43.386 -43.272  22.253  1.00 69.43           C  
ATOM   1570  O   GLU A 197      42.872 -43.171  21.136  1.00 67.10           O  
ATOM   1571  CB  GLU A 197      44.403 -45.498  22.925  1.00 65.79           C  
ATOM   1572  CG  GLU A 197      45.610 -46.460  22.838  1.00 71.69           C  
ATOM   1573  CD  GLU A 197      46.784 -46.077  23.757  1.00 80.89           C  
ATOM   1574  OE1 GLU A 197      46.565 -45.883  24.976  1.00 72.60           O  
ATOM   1575  OE2 GLU A 197      47.932 -45.967  23.253  1.00 88.99           O  
ATOM   1576  N   THR A 198      42.880 -42.709  23.352  1.00 68.64           N  
ATOM   1577  CA  THR A 198      41.683 -41.854  23.347  1.00 68.34           C  
ATOM   1578  C   THR A 198      41.933 -40.320  23.323  1.00 67.36           C  
ATOM   1579  O   THR A 198      40.983 -39.530  23.317  1.00 64.57           O  
ATOM   1580  CB  THR A 198      40.688 -42.226  24.485  1.00 62.79           C  
ATOM   1581  OG1 THR A 198      41.401 -42.491  25.701  1.00 60.47           O  
ATOM   1582  CG2 THR A 198      39.857 -43.433  24.102  1.00 54.22           C  
ATOM   1583  N   ASN A 199      43.202 -39.917  23.306  1.00 63.71           N  
ATOM   1584  CA  ASN A 199      43.584 -38.500  23.309  1.00 67.93           C  
ATOM   1585  C   ASN A 199      43.108 -37.738  24.539  1.00 64.23           C  
ATOM   1586  O   ASN A 199      42.606 -36.620  24.435  1.00 61.56           O  
ATOM   1587  CB  ASN A 199      43.103 -37.779  22.049  1.00 68.01           C  
ATOM   1588  CG  ASN A 199      43.922 -38.115  20.842  1.00 67.91           C  
ATOM   1589  OD1 ASN A 199      45.090 -37.742  20.759  1.00 77.22           O  
ATOM   1590  ND2 ASN A 199      43.319 -38.814  19.889  1.00 63.35           N  
ATOM   1591  N   ASN A 200      43.279 -38.355  25.702  1.00 64.74           N  
ATOM   1592  CA  ASN A 200      42.849 -37.767  26.962  1.00 63.40           C  
ATOM   1593  C   ASN A 200      43.363 -36.364  27.233  1.00 65.21           C  
ATOM   1594  O   ASN A 200      42.709 -35.576  27.916  1.00 71.92           O  
ATOM   1595  CB  ASN A 200      43.178 -38.698  28.115  1.00 55.46           C  
ATOM   1596  CG  ASN A 200      42.351 -39.930  28.075  1.00 59.27           C  
ATOM   1597  OD1 ASN A 200      41.829 -40.305  27.023  1.00 57.37           O  
ATOM   1598  ND2 ASN A 200      42.204 -40.575  29.215  1.00 61.94           N  
ATOM   1599  N   GLU A 201      44.516 -36.036  26.679  1.00 76.94           N  
ATOM   1600  CA  GLU A 201      45.128 -34.756  26.980  1.00 76.94           C  
ATOM   1601  C   GLU A 201      44.474 -33.579  26.254  1.00 76.94           C  
ATOM   1602  O   GLU A 201      44.244 -32.526  26.845  1.00 76.94           O  
ATOM   1603  CB  GLU A 201      46.616 -34.816  26.671  1.00 76.94           C  
ATOM   1604  CG  GLU A 201      47.303 -33.482  26.752  1.00 76.94           C  
ATOM   1605  CD  GLU A 201      48.796 -33.627  26.738  1.00 88.84           C  
ATOM   1606  OE1 GLU A 201      49.333 -34.248  27.680  1.00 93.70           O  
ATOM   1607  OE2 GLU A 201      49.427 -33.135  25.780  1.00 91.40           O  
ATOM   1608  N   SER A 202      44.182 -33.752  24.972  1.00 62.65           N  
ATOM   1609  CA  SER A 202      43.576 -32.670  24.211  1.00 60.49           C  
ATOM   1610  C   SER A 202      42.163 -32.428  24.718  1.00 65.29           C  
ATOM   1611  O   SER A 202      41.638 -31.322  24.621  1.00 67.39           O  
ATOM   1612  CB  SER A 202      43.568 -32.965  22.706  1.00 60.86           C  
ATOM   1613  OG  SER A 202      42.769 -34.088  22.405  1.00 68.54           O  
ATOM   1614  N   PHE A 203      41.552 -33.474  25.270  1.00 65.84           N  
ATOM   1615  CA  PHE A 203      40.214 -33.371  25.845  1.00 61.74           C  
ATOM   1616  C   PHE A 203      40.193 -32.607  27.172  1.00 58.89           C  
ATOM   1617  O   PHE A 203      39.326 -31.766  27.388  1.00 56.80           O  
ATOM   1618  CB  PHE A 203      39.581 -34.747  26.020  1.00 56.98           C  
ATOM   1619  CG  PHE A 203      38.127 -34.690  26.384  1.00 57.21           C  
ATOM   1620  CD1 PHE A 203      37.160 -34.667  25.397  1.00 56.56           C  
ATOM   1621  CD2 PHE A 203      37.726 -34.650  27.711  1.00 53.66           C  
ATOM   1622  CE1 PHE A 203      35.817 -34.622  25.722  1.00 53.89           C  
ATOM   1623  CE2 PHE A 203      36.397 -34.609  28.040  1.00 50.03           C  
ATOM   1624  CZ  PHE A 203      35.438 -34.590  27.045  1.00 53.27           C  
ATOM   1625  N   VAL A 204      41.140 -32.892  28.056  1.00 58.38           N  
ATOM   1626  CA  VAL A 204      41.193 -32.180  29.324  1.00 59.63           C  
ATOM   1627  C   VAL A 204      41.486 -30.681  29.121  1.00 60.54           C  
ATOM   1628  O   VAL A 204      41.068 -29.851  29.925  1.00 57.00           O  
ATOM   1629  CB  VAL A 204      42.189 -32.834  30.325  1.00 61.77           C  
ATOM   1630  CG1 VAL A 204      43.621 -32.776  29.802  1.00 65.23           C  
ATOM   1631  CG2 VAL A 204      42.100 -32.171  31.689  1.00 63.51           C  
ATOM   1632  N   ILE A 205      42.186 -30.327  28.047  1.00 58.96           N  
ATOM   1633  CA  ILE A 205      42.397 -28.910  27.758  1.00 60.27           C  
ATOM   1634  C   ILE A 205      41.090 -28.310  27.269  1.00 56.98           C  
ATOM   1635  O   ILE A 205      40.626 -27.295  27.786  1.00 56.59           O  
ATOM   1636  CB  ILE A 205      43.551 -28.654  26.740  1.00 61.41           C  
ATOM   1637  CG1 ILE A 205      44.905 -28.698  27.447  1.00 59.09           C  
ATOM   1638  CG2 ILE A 205      43.410 -27.294  26.091  1.00 57.23           C  
ATOM   1639  CD1 ILE A 205      45.950 -29.484  26.685  1.00 65.33           C  
ATOM   1640  N   TYR A 206      40.487 -28.972  26.293  1.00 54.84           N  
ATOM   1641  CA  TYR A 206      39.191 -28.573  25.776  1.00 54.94           C  
ATOM   1642  C   TYR A 206      38.107 -28.521  26.859  1.00 57.47           C  
ATOM   1643  O   TYR A 206      37.227 -27.670  26.813  1.00 57.76           O  
ATOM   1644  CB  TYR A 206      38.779 -29.499  24.648  1.00 53.82           C  
ATOM   1645  CG  TYR A 206      37.303 -29.574  24.472  1.00 56.40           C  
ATOM   1646  CD1 TYR A 206      36.621 -28.603  23.759  1.00 54.35           C  
ATOM   1647  CD2 TYR A 206      36.577 -30.622  25.028  1.00 59.68           C  
ATOM   1648  CE1 TYR A 206      35.241 -28.674  23.601  1.00 60.12           C  
ATOM   1649  CE2 TYR A 206      35.197 -30.704  24.878  1.00 61.95           C  
ATOM   1650  CZ  TYR A 206      34.535 -29.730  24.165  1.00 60.95           C  
ATOM   1651  OH  TYR A 206      33.174 -29.829  24.018  1.00 58.08           O  
ATOM   1652  N   MET A 207      38.171 -29.428  27.827  1.00 59.60           N  
ATOM   1653  CA  MET A 207      37.305 -29.353  29.001  1.00 58.43           C  
ATOM   1654  C   MET A 207      37.615 -28.113  29.809  1.00 57.02           C  
ATOM   1655  O   MET A 207      36.718 -27.371  30.192  1.00 55.06           O  
ATOM   1656  CB  MET A 207      37.524 -30.560  29.902  1.00 54.19           C  
ATOM   1657  CG  MET A 207      36.589 -31.688  29.620  1.00 59.91           C  
ATOM   1658  SD  MET A 207      34.952 -31.434  30.313  1.00 70.17           S  
ATOM   1659  CE  MET A 207      35.249 -31.905  32.023  1.00 55.04           C  
ATOM   1660  N   PHE A 208      38.902 -27.910  30.073  1.00 53.85           N  
ATOM   1661  CA  PHE A 208      39.352 -26.859  30.968  1.00 52.16           C  
ATOM   1662  C   PHE A 208      38.977 -25.497  30.415  1.00 56.48           C  
ATOM   1663  O   PHE A 208      38.568 -24.602  31.158  1.00 53.81           O  
ATOM   1664  CB  PHE A 208      40.861 -26.932  31.185  1.00 49.48           C  
ATOM   1665  CG  PHE A 208      41.359 -25.968  32.209  1.00 50.78           C  
ATOM   1666  CD1 PHE A 208      41.328 -26.293  33.555  1.00 52.08           C  
ATOM   1667  CD2 PHE A 208      41.843 -24.725  31.833  1.00 52.18           C  
ATOM   1668  CE1 PHE A 208      41.783 -25.395  34.520  1.00 56.99           C  
ATOM   1669  CE2 PHE A 208      42.297 -23.815  32.792  1.00 53.45           C  
ATOM   1670  CZ  PHE A 208      42.270 -24.152  34.138  1.00 54.32           C  
ATOM   1671  N   VAL A 209      39.102 -25.353  29.099  1.00 57.17           N  
ATOM   1672  CA  VAL A 209      38.829 -24.087  28.436  1.00 56.05           C  
ATOM   1673  C   VAL A 209      37.326 -23.919  28.207  1.00 56.12           C  
ATOM   1674  O   VAL A 209      36.685 -23.095  28.855  1.00 56.68           O  
ATOM   1675  CB  VAL A 209      39.615 -23.977  27.108  1.00 54.23           C  
ATOM   1676  CG1 VAL A 209      39.217 -22.732  26.350  1.00 47.64           C  
ATOM   1677  CG2 VAL A 209      41.114 -23.983  27.382  1.00 49.02           C  
ATOM   1678  N   VAL A 210      36.762 -24.721  27.310  1.00 54.22           N  
ATOM   1679  CA  VAL A 210      35.354 -24.592  26.941  1.00 52.17           C  
ATOM   1680  C   VAL A 210      34.352 -24.808  28.088  1.00 52.17           C  
ATOM   1681  O   VAL A 210      33.399 -24.054  28.223  1.00 55.03           O  
ATOM   1682  CB  VAL A 210      35.009 -25.491  25.725  1.00 52.75           C  
ATOM   1683  CG1 VAL A 210      33.517 -25.663  25.563  1.00 50.44           C  
ATOM   1684  CG2 VAL A 210      35.608 -24.906  24.466  1.00 52.21           C  
ATOM   1685  N   HIS A 211      34.548 -25.831  28.907  1.00 53.42           N  
ATOM   1686  CA  HIS A 211      33.587 -26.127  29.976  1.00 54.47           C  
ATOM   1687  C   HIS A 211      33.955 -25.597  31.356  1.00 51.08           C  
ATOM   1688  O   HIS A 211      33.249 -25.829  32.329  1.00 50.90           O  
ATOM   1689  CB  HIS A 211      33.222 -27.620  29.990  1.00 54.25           C  
ATOM   1690  CG  HIS A 211      32.652 -28.085  28.691  1.00 54.12           C  
ATOM   1691  ND1 HIS A 211      31.298 -28.132  28.449  1.00 52.75           N  
ATOM   1692  CD2 HIS A 211      33.255 -28.460  27.537  1.00 58.15           C  
ATOM   1693  CE1 HIS A 211      31.087 -28.545  27.212  1.00 55.88           C  
ATOM   1694  NE2 HIS A 211      32.258 -28.750  26.636  1.00 59.40           N  
ATOM   1695  N   PHE A 212      35.065 -24.886  31.444  1.00 50.23           N  
ATOM   1696  CA  PHE A 212      35.380 -24.215  32.696  1.00 56.15           C  
ATOM   1697  C   PHE A 212      35.672 -22.709  32.537  1.00 56.14           C  
ATOM   1698  O   PHE A 212      34.971 -21.880  33.110  1.00 55.07           O  
ATOM   1699  CB  PHE A 212      36.468 -24.938  33.498  1.00 56.00           C  
ATOM   1700  CG  PHE A 212      36.802 -24.251  34.794  1.00 62.03           C  
ATOM   1701  CD1 PHE A 212      35.873 -24.203  35.826  1.00 58.84           C  
ATOM   1702  CD2 PHE A 212      38.037 -23.638  34.979  1.00 60.01           C  
ATOM   1703  CE1 PHE A 212      36.174 -23.554  37.026  1.00 59.38           C  
ATOM   1704  CE2 PHE A 212      38.340 -22.985  36.176  1.00 60.46           C  
ATOM   1705  CZ  PHE A 212      37.411 -22.946  37.199  1.00 59.15           C  
ATOM   1706  N   ILE A 213      36.720 -22.365  31.794  1.00 57.09           N  
ATOM   1707  CA  ILE A 213      37.093 -20.961  31.576  1.00 56.32           C  
ATOM   1708  C   ILE A 213      35.972 -20.122  30.922  1.00 53.74           C  
ATOM   1709  O   ILE A 213      35.583 -19.091  31.473  1.00 52.12           O  
ATOM   1710  CB  ILE A 213      38.433 -20.834  30.794  1.00 52.50           C  
ATOM   1711  CG1 ILE A 213      39.561 -21.473  31.583  1.00 51.54           C  
ATOM   1712  CG2 ILE A 213      38.792 -19.389  30.579  1.00 51.31           C  
ATOM   1713  CD1 ILE A 213      39.823 -20.786  32.887  1.00 51.79           C  
ATOM   1714  N   ILE A 214      35.449 -20.557  29.776  1.00 48.96           N  
ATOM   1715  CA  ILE A 214      34.285 -19.882  29.202  1.00 49.36           C  
ATOM   1716  C   ILE A 214      33.181 -19.671  30.264  1.00 53.96           C  
ATOM   1717  O   ILE A 214      32.853 -18.524  30.545  1.00 53.59           O  
ATOM   1718  CB  ILE A 214      33.706 -20.579  27.927  1.00 51.44           C  
ATOM   1719  CG1 ILE A 214      34.768 -20.744  26.828  1.00 49.48           C  
ATOM   1720  CG2 ILE A 214      32.445 -19.881  27.442  1.00 39.62           C  
ATOM   1721  CD1 ILE A 214      35.635 -19.568  26.617  1.00 51.74           C  
ATOM   1722  N   PRO A 215      32.662 -20.751  30.911  1.00 57.32           N  
ATOM   1723  CA  PRO A 215      31.672 -20.520  31.972  1.00 54.27           C  
ATOM   1724  C   PRO A 215      32.089 -19.511  33.036  1.00 53.39           C  
ATOM   1725  O   PRO A 215      31.281 -18.674  33.428  1.00 51.68           O  
ATOM   1726  CB  PRO A 215      31.540 -21.905  32.609  1.00 50.37           C  
ATOM   1727  CG  PRO A 215      31.689 -22.793  31.468  1.00 51.85           C  
ATOM   1728  CD  PRO A 215      32.837 -22.199  30.697  1.00 54.00           C  
ATOM   1729  N   LEU A 216      33.336 -19.586  33.483  1.00 56.29           N  
ATOM   1730  CA  LEU A 216      33.812 -18.710  34.542  1.00 54.86           C  
ATOM   1731  C   LEU A 216      33.826 -17.273  34.084  1.00 53.32           C  
ATOM   1732  O   LEU A 216      33.482 -16.377  34.847  1.00 51.45           O  
ATOM   1733  CB  LEU A 216      35.212 -19.113  35.002  1.00 57.31           C  
ATOM   1734  CG  LEU A 216      35.654 -18.297  36.213  1.00 57.94           C  
ATOM   1735  CD1 LEU A 216      34.765 -18.610  37.409  1.00 59.60           C  
ATOM   1736  CD2 LEU A 216      37.114 -18.545  36.542  1.00 58.14           C  
ATOM   1737  N   ILE A 217      34.233 -17.059  32.838  1.00 51.61           N  
ATOM   1738  CA  ILE A 217      34.357 -15.703  32.310  1.00 55.45           C  
ATOM   1739  C   ILE A 217      32.990 -15.068  32.092  1.00 52.16           C  
ATOM   1740  O   ILE A 217      32.720 -13.971  32.585  1.00 51.08           O  
ATOM   1741  CB  ILE A 217      35.200 -15.658  31.014  1.00 53.35           C  
ATOM   1742  CG1 ILE A 217      36.688 -15.700  31.341  1.00 48.38           C  
ATOM   1743  CG2 ILE A 217      34.938 -14.389  30.246  1.00 53.88           C  
ATOM   1744  CD1 ILE A 217      37.531 -16.022  30.144  1.00 46.32           C  
ATOM   1745  N   VAL A 218      32.134 -15.772  31.355  1.00 50.13           N  
ATOM   1746  CA  VAL A 218      30.749 -15.348  31.116  1.00 50.24           C  
ATOM   1747  C   VAL A 218      30.004 -15.007  32.422  1.00 51.14           C  
ATOM   1748  O   VAL A 218      29.472 -13.906  32.570  1.00 47.47           O  
ATOM   1749  CB  VAL A 218      29.971 -16.406  30.297  1.00 46.79           C  
ATOM   1750  CG1 VAL A 218      28.486 -16.170  30.388  1.00 46.47           C  
ATOM   1751  CG2 VAL A 218      30.423 -16.391  28.847  1.00 41.36           C  
ATOM   1752  N   ILE A 219      29.997 -15.942  33.371  1.00 50.82           N  
ATOM   1753  CA  ILE A 219      29.396 -15.711  34.688  1.00 50.19           C  
ATOM   1754  C   ILE A 219      29.972 -14.512  35.442  1.00 49.34           C  
ATOM   1755  O   ILE A 219      29.238 -13.814  36.124  1.00 50.83           O  
ATOM   1756  CB  ILE A 219      29.418 -16.980  35.573  1.00 47.38           C  
ATOM   1757  CG1 ILE A 219      28.347 -17.945  35.087  1.00 51.51           C  
ATOM   1758  CG2 ILE A 219      29.190 -16.652  37.046  1.00 41.88           C  
ATOM   1759  CD1 ILE A 219      28.261 -19.228  35.891  1.00 55.92           C  
ATOM   1760  N   PHE A 220      31.267 -14.251  35.324  1.00 52.91           N  
ATOM   1761  CA  PHE A 220      31.814 -13.074  35.991  1.00 55.50           C  
ATOM   1762  C   PHE A 220      31.415 -11.792  35.267  1.00 55.12           C  
ATOM   1763  O   PHE A 220      31.001 -10.810  35.893  1.00 50.36           O  
ATOM   1764  CB  PHE A 220      33.328 -13.169  36.156  1.00 50.36           C  
ATOM   1765  CG  PHE A 220      33.758 -13.534  37.552  1.00 61.90           C  
ATOM   1766  CD1 PHE A 220      33.834 -14.865  37.952  1.00 64.60           C  
ATOM   1767  CD2 PHE A 220      34.080 -12.548  38.470  1.00 60.83           C  
ATOM   1768  CE1 PHE A 220      34.229 -15.200  39.244  1.00 62.68           C  
ATOM   1769  CE2 PHE A 220      34.473 -12.876  39.762  1.00 62.06           C  
ATOM   1770  CZ  PHE A 220      34.547 -14.200  40.148  1.00 68.91           C  
ATOM   1771  N   PHE A 221      31.523 -11.811  33.945  1.00 50.83           N  
ATOM   1772  CA  PHE A 221      31.184 -10.636  33.161  1.00 51.09           C  
ATOM   1773  C   PHE A 221      29.726 -10.252  33.346  1.00 54.23           C  
ATOM   1774  O   PHE A 221      29.425  -9.143  33.774  1.00 52.54           O  
ATOM   1775  CB  PHE A 221      31.459 -10.866  31.678  1.00 50.88           C  
ATOM   1776  CG  PHE A 221      30.982  -9.741  30.800  1.00 54.82           C  
ATOM   1777  CD1 PHE A 221      31.710  -8.565  30.699  1.00 50.98           C  
ATOM   1778  CD2 PHE A 221      29.797  -9.852  30.087  1.00 53.89           C  
ATOM   1779  CE1 PHE A 221      31.272  -7.529  29.898  1.00 52.36           C  
ATOM   1780  CE2 PHE A 221      29.361  -8.820  29.280  1.00 55.26           C  
ATOM   1781  CZ  PHE A 221      30.101  -7.658  29.187  1.00 55.21           C  
ATOM   1782  N   CYS A 222      28.830 -11.187  33.035  1.00 54.06           N  
ATOM   1783  CA  CYS A 222      27.396 -10.969  33.143  1.00 49.46           C  
ATOM   1784  C   CYS A 222      26.971 -10.441  34.498  1.00 53.16           C  
ATOM   1785  O   CYS A 222      26.323  -9.396  34.580  1.00 55.56           O  
ATOM   1786  CB  CYS A 222      26.645 -12.247  32.834  1.00 45.65           C  
ATOM   1787  SG  CYS A 222      26.462 -12.501  31.077  1.00 50.97           S  
ATOM   1788  N   TYR A 223      27.337 -11.137  35.564  1.00 50.46           N  
ATOM   1789  CA  TYR A 223      26.977 -10.657  36.888  1.00 50.40           C  
ATOM   1790  C   TYR A 223      27.756  -9.421  37.276  1.00 51.84           C  
ATOM   1791  O   TYR A 223      27.280  -8.639  38.091  1.00 50.97           O  
ATOM   1792  CB  TYR A 223      27.120 -11.749  37.941  1.00 48.48           C  
ATOM   1793  CG  TYR A 223      26.020 -12.774  37.838  1.00 55.53           C  
ATOM   1794  CD1 TYR A 223      24.700 -12.380  37.655  1.00 56.08           C  
ATOM   1795  CD2 TYR A 223      26.295 -14.137  37.897  1.00 52.34           C  
ATOM   1796  CE1 TYR A 223      23.685 -13.316  37.553  1.00 53.98           C  
ATOM   1797  CE2 TYR A 223      25.284 -15.076  37.794  1.00 49.66           C  
ATOM   1798  CZ  TYR A 223      23.984 -14.657  37.622  1.00 50.32           C  
ATOM   1799  OH  TYR A 223      22.980 -15.581  37.519  1.00 49.38           O  
ATOM   1800  N   GLY A 224      28.945  -9.244  36.698  1.00 52.68           N  
ATOM   1801  CA  GLY A 224      29.721  -8.036  36.928  1.00 49.93           C  
ATOM   1802  C   GLY A 224      28.978  -6.814  36.420  1.00 53.20           C  
ATOM   1803  O   GLY A 224      28.753  -5.868  37.165  1.00 51.88           O  
ATOM   1804  N   GLN A 225      28.587  -6.857  35.150  1.00 53.03           N  
ATOM   1805  CA  GLN A 225      27.775  -5.823  34.529  1.00 53.97           C  
ATOM   1806  C   GLN A 225      26.501  -5.519  35.319  1.00 59.09           C  
ATOM   1807  O   GLN A 225      26.079  -4.369  35.414  1.00 62.16           O  
ATOM   1808  CB  GLN A 225      27.408  -6.239  33.106  1.00 54.33           C  
ATOM   1809  CG  GLN A 225      28.596  -6.346  32.173  1.00 57.85           C  
ATOM   1810  CD  GLN A 225      29.244  -5.003  31.902  1.00 65.33           C  
ATOM   1811  OE1 GLN A 225      28.697  -4.175  31.169  1.00 70.89           O  
ATOM   1812  NE2 GLN A 225      30.415  -4.776  32.495  1.00 60.76           N  
ATOM   1813  N   LEU A 226      25.892  -6.552  35.887  1.00 58.54           N  
ATOM   1814  CA  LEU A 226      24.651  -6.398  36.639  1.00 58.71           C  
ATOM   1815  C   LEU A 226      24.861  -5.624  37.932  1.00 57.73           C  
ATOM   1816  O   LEU A 226      24.110  -4.700  38.235  1.00 59.31           O  
ATOM   1817  CB  LEU A 226      24.060  -7.762  36.978  1.00 53.10           C  
ATOM   1818  CG  LEU A 226      22.556  -7.771  37.205  1.00 49.92           C  
ATOM   1819  CD1 LEU A 226      21.888  -8.230  35.931  1.00 51.99           C  
ATOM   1820  CD2 LEU A 226      22.197  -8.673  38.358  1.00 54.41           C  
ATOM   1821  N   VAL A 227      25.872  -6.012  38.702  1.00 54.13           N  
ATOM   1822  CA  VAL A 227      26.172  -5.327  39.951  1.00 55.56           C  
ATOM   1823  C   VAL A 227      26.638  -3.913  39.638  1.00 58.37           C  
ATOM   1824  O   VAL A 227      26.616  -3.030  40.494  1.00 59.28           O  
ATOM   1825  CB  VAL A 227      27.211  -6.090  40.786  1.00 49.20           C  
ATOM   1826  CG1 VAL A 227      27.469  -5.396  42.096  1.00 50.59           C  
ATOM   1827  CG2 VAL A 227      26.690  -7.447  41.072  1.00 52.01           C  
ATOM   1828  N   PHE A 228      27.040  -3.692  38.393  1.00 59.44           N  
ATOM   1829  CA  PHE A 228      27.352  -2.344  37.955  1.00 60.12           C  
ATOM   1830  C   PHE A 228      26.059  -1.576  37.684  1.00 60.00           C  
ATOM   1831  O   PHE A 228      25.742  -0.620  38.385  1.00 58.50           O  
ATOM   1832  CB  PHE A 228      28.263  -2.358  36.735  1.00 55.73           C  
ATOM   1833  CG  PHE A 228      28.772  -1.008  36.366  1.00 65.80           C  
ATOM   1834  CD1 PHE A 228      29.440  -0.227  37.298  1.00 61.10           C  
ATOM   1835  CD2 PHE A 228      28.574  -0.506  35.094  1.00 71.59           C  
ATOM   1836  CE1 PHE A 228      29.899   1.016  36.964  1.00 59.23           C  
ATOM   1837  CE2 PHE A 228      29.035   0.740  34.757  1.00 69.47           C  
ATOM   1838  CZ  PHE A 228      29.700   1.500  35.692  1.00 69.57           C  
ATOM   1839  N   THR A 229      25.303  -2.045  36.695  1.00 57.84           N  
ATOM   1840  CA  THR A 229      24.026  -1.459  36.293  1.00 56.44           C  
ATOM   1841  C   THR A 229      23.108  -1.132  37.476  1.00 54.91           C  
ATOM   1842  O   THR A 229      22.441  -0.104  37.489  1.00 60.30           O  
ATOM   1843  CB  THR A 229      23.280  -2.416  35.311  1.00 55.64           C  
ATOM   1844  OG1 THR A 229      23.560  -2.047  33.956  1.00 56.19           O  
ATOM   1845  CG2 THR A 229      21.781  -2.381  35.515  1.00 57.85           C  
ATOM   1846  N   VAL A 230      23.074  -2.003  38.469  1.00 56.35           N  
ATOM   1847  CA  VAL A 230      22.196  -1.819  39.620  1.00 59.34           C  
ATOM   1848  C   VAL A 230      22.764  -0.846  40.657  1.00 55.63           C  
ATOM   1849  O   VAL A 230      22.008  -0.174  41.360  1.00 52.98           O  
ATOM   1850  CB  VAL A 230      21.829  -3.192  40.261  1.00 58.14           C  
ATOM   1851  CG1 VAL A 230      20.908  -3.019  41.447  1.00 53.40           C  
ATOM   1852  CG2 VAL A 230      21.160  -4.076  39.227  1.00 57.40           C  
ATOM   1853  N   LYS A 231      24.092  -0.782  40.762  1.00 59.76           N  
ATOM   1854  CA  LYS A 231      24.734   0.160  41.682  1.00 63.79           C  
ATOM   1855  C   LYS A 231      24.667   1.587  41.114  1.00 65.38           C  
ATOM   1856  O   LYS A 231      24.520   2.570  41.849  1.00 54.64           O  
ATOM   1857  CB  LYS A 231      26.176  -0.263  42.000  1.00 53.77           C  
ATOM   1858  CG  LYS A 231      26.266  -1.355  43.069  1.00 63.77           C  
ATOM   1859  CD  LYS A 231      27.678  -1.533  43.624  1.00 64.60           C  
ATOM   1860  CE  LYS A 231      27.779  -2.710  44.591  1.00 58.54           C  
ATOM   1861  NZ  LYS A 231      26.939  -2.542  45.813  1.00 60.34           N  
ATOM   1862  N   GLU A 232      24.750   1.661  39.791  1.00 79.47           N  
ATOM   1863  CA  GLU A 232      24.606   2.891  39.037  1.00 79.47           C  
ATOM   1864  C   GLU A 232      23.226   3.488  39.270  1.00 79.47           C  
ATOM   1865  O   GLU A 232      23.083   4.634  39.692  1.00 79.47           O  
ATOM   1866  CB  GLU A 232      24.756   2.566  37.553  1.00 79.47           C  
ATOM   1867  CG  GLU A 232      24.720   3.761  36.626  1.00 79.47           C  
ATOM   1868  CD  GLU A 232      26.089   4.105  36.056  1.00 95.52           C  
ATOM   1869  OE1 GLU A 232      27.065   4.187  36.834  1.00 97.03           O  
ATOM   1870  OE2 GLU A 232      26.188   4.296  34.824  1.00102.20           O  
ATOM   1871  N   ALA A 233      22.211   2.685  38.974  1.00 64.96           N  
ATOM   1872  CA  ALA A 233      20.810   3.052  39.148  1.00 60.89           C  
ATOM   1873  C   ALA A 233      20.476   3.550  40.553  1.00 60.98           C  
ATOM   1874  O   ALA A 233      19.771   4.534  40.710  1.00 60.88           O  
ATOM   1875  CB  ALA A 233      19.922   1.882  38.784  1.00 52.98           C  
ATOM   1876  N   ALA A 234      20.967   2.866  41.576  1.00 61.64           N  
ATOM   1877  CA  ALA A 234      20.717   3.304  42.943  1.00 60.95           C  
ATOM   1878  C   ALA A 234      21.372   4.655  43.253  1.00 61.36           C  
ATOM   1879  O   ALA A 234      20.808   5.456  43.990  1.00 61.81           O  
ATOM   1880  CB  ALA A 234      21.167   2.244  43.947  1.00 60.09           C  
ATOM   1881  N   ALA A 235      22.550   4.913  42.686  1.00 64.17           N  
ATOM   1882  CA  ALA A 235      23.291   6.143  42.975  1.00 58.00           C  
ATOM   1883  C   ALA A 235      22.641   7.359  42.320  1.00 62.19           C  
ATOM   1884  O   ALA A 235      22.800   8.489  42.770  1.00 64.83           O  
ATOM   1885  CB  ALA A 235      24.717   6.016  42.499  1.00 50.13           C  
ATOM   1886  N   GLN A 236      21.984   7.106  41.196  1.00 57.80           N  
ATOM   1887  CA  GLN A 236      21.184   8.080  40.463  1.00 55.85           C  
ATOM   1888  C   GLN A 236      19.737   8.199  41.034  1.00 56.60           C  
ATOM   1889  O   GLN A 236      19.000   9.152  40.790  1.00 53.14           O  
ATOM   1890  CB  GLN A 236      21.243   7.665  38.982  1.00 53.14           C  
ATOM   1891  CG  GLN A 236      20.877   8.704  37.953  1.00 59.38           C  
ATOM   1892  CD  GLN A 236      21.800   9.897  37.931  1.00 63.36           C  
ATOM   1893  OE1 GLN A 236      21.504  10.936  38.532  1.00 59.66           O  
ATOM   1894  NE2 GLN A 236      22.910   9.776  37.209  1.00 67.54           N  
ATOM   1895  N   GLN A 237      19.336   7.160  41.751  1.00 59.05           N  
ATOM   1896  CA  GLN A 237      18.056   7.081  42.486  1.00 55.65           C  
ATOM   1897  C   GLN A 237      17.902   7.359  43.999  1.00 56.39           C  
ATOM   1898  O   GLN A 237      16.881   6.970  44.553  1.00 55.38           O  
ATOM   1899  CB  GLN A 237      17.230   5.853  42.087  1.00 56.98           C  
ATOM   1900  CG  GLN A 237      15.800   6.209  41.832  1.00 56.29           C  
ATOM   1901  CD  GLN A 237      15.249   5.579  40.572  1.00 69.07           C  
ATOM   1902  OE1 GLN A 237      15.999   5.084  39.709  1.00 71.10           O  
ATOM   1903  NE2 GLN A 237      13.921   5.593  40.454  1.00 68.21           N  
ATOM   1904  N   GLN A 238      18.916   7.873  44.690  1.00 50.90           N  
ATOM   1905  CA  GLN A 238      18.943   7.761  46.162  1.00 51.68           C  
ATOM   1906  C   GLN A 238      17.693   8.138  46.996  1.00 53.98           C  
ATOM   1907  O   GLN A 238      17.594   7.764  48.170  1.00 51.51           O  
ATOM   1908  CB  GLN A 238      20.112   8.540  46.749  1.00 55.45           C  
ATOM   1909  CG  GLN A 238      21.430   7.861  46.623  1.00 63.24           C  
ATOM   1910  CD  GLN A 238      22.420   8.752  45.951  1.00 68.20           C  
ATOM   1911  OE1 GLN A 238      22.052   9.539  45.067  1.00 71.65           O  
ATOM   1912  NE2 GLN A 238      23.680   8.671  46.370  1.00 67.16           N  
ATOM   1913  N   GLU A 239      16.815   8.980  46.452  1.00 58.41           N  
ATOM   1914  CA  GLU A 239      15.542   9.320  47.094  1.00 51.74           C  
ATOM   1915  C   GLU A 239      14.632   8.079  47.286  1.00 56.30           C  
ATOM   1916  O   GLU A 239      13.642   8.111  48.034  1.00 58.34           O  
ATOM   1917  CB  GLU A 239      14.826  10.392  46.286  1.00 44.70           C  
ATOM   1918  CG  GLU A 239      14.244   9.877  44.987  1.00 45.96           C  
ATOM   1919  CD  GLU A 239      15.171  10.021  43.815  1.00 43.50           C  
ATOM   1920  OE1 GLU A 239      16.337  10.368  44.046  1.00 43.98           O  
ATOM   1921  OE2 GLU A 239      14.723   9.806  42.668  1.00 44.45           O  
ATOM   1922  N   SER A 240      14.970   6.983  46.613  1.00 54.81           N  
ATOM   1923  CA  SER A 240      14.229   5.736  46.758  1.00 54.48           C  
ATOM   1924  C   SER A 240      14.949   4.754  47.671  1.00 53.48           C  
ATOM   1925  O   SER A 240      15.988   4.239  47.304  1.00 54.04           O  
ATOM   1926  CB  SER A 240      14.038   5.091  45.390  1.00 53.41           C  
ATOM   1927  OG  SER A 240      13.995   3.690  45.518  1.00 55.23           O  
ATOM   1928  N   ALA A 241      14.388   4.489  48.849  1.00 54.49           N  
ATOM   1929  CA  ALA A 241      14.960   3.517  49.790  1.00 58.88           C  
ATOM   1930  C   ALA A 241      14.857   2.072  49.264  1.00 58.92           C  
ATOM   1931  O   ALA A 241      15.720   1.231  49.517  1.00 52.33           O  
ATOM   1932  CB  ALA A 241      14.296   3.641  51.169  1.00 51.58           C  
ATOM   1933  N   THR A 242      13.797   1.806  48.513  1.00 56.50           N  
ATOM   1934  CA  THR A 242      13.587   0.495  47.926  1.00 56.92           C  
ATOM   1935  C   THR A 242      14.635   0.175  46.862  1.00 56.74           C  
ATOM   1936  O   THR A 242      15.161  -0.933  46.832  1.00 58.10           O  
ATOM   1937  CB  THR A 242      12.134   0.322  47.404  1.00 51.03           C  
ATOM   1938  OG1 THR A 242      11.383  -0.418  48.370  1.00 54.12           O  
ATOM   1939  CG2 THR A 242      12.103  -0.421  46.100  1.00 46.37           C  
ATOM   1940  N   THR A 243      14.956   1.141  46.009  1.00 53.61           N  
ATOM   1941  CA  THR A 243      16.008   0.947  45.015  1.00 57.88           C  
ATOM   1942  C   THR A 243      17.356   0.758  45.729  1.00 58.06           C  
ATOM   1943  O   THR A 243      18.281   0.150  45.190  1.00 52.93           O  
ATOM   1944  CB  THR A 243      16.092   2.143  44.007  1.00 59.61           C  
ATOM   1945  OG1 THR A 243      14.830   2.316  43.335  1.00 58.29           O  
ATOM   1946  CG2 THR A 243      17.207   1.941  42.965  1.00 62.47           C  
ATOM   1947  N   GLN A 244      17.461   1.284  46.946  1.00 56.15           N  
ATOM   1948  CA  GLN A 244      18.696   1.158  47.698  1.00 56.20           C  
ATOM   1949  C   GLN A 244      18.814  -0.255  48.224  1.00 58.27           C  
ATOM   1950  O   GLN A 244      19.869  -0.865  48.103  1.00 60.07           O  
ATOM   1951  CB  GLN A 244      18.778   2.176  48.841  1.00 55.70           C  
ATOM   1952  CG  GLN A 244      18.896   3.643  48.402  1.00 56.76           C  
ATOM   1953  CD  GLN A 244      19.775   3.853  47.174  1.00 57.59           C  
ATOM   1954  OE1 GLN A 244      20.991   3.656  47.218  1.00 57.56           O  
ATOM   1955  NE2 GLN A 244      19.155   4.263  46.071  1.00 55.07           N  
ATOM   1956  N   LYS A 245      17.725  -0.755  48.811  1.00 59.11           N  
ATOM   1957  CA  LYS A 245      17.597  -2.143  49.263  1.00 55.17           C  
ATOM   1958  C   LYS A 245      17.913  -3.125  48.149  1.00 55.53           C  
ATOM   1959  O   LYS A 245      18.646  -4.085  48.357  1.00 52.91           O  
ATOM   1960  CB  LYS A 245      16.169  -2.413  49.754  1.00 52.78           C  
ATOM   1961  CG  LYS A 245      15.971  -2.324  51.262  1.00 54.43           C  
ATOM   1962  CD  LYS A 245      14.487  -2.481  51.642  1.00 65.94           C  
ATOM   1963  CE  LYS A 245      13.749  -1.117  51.761  1.00 69.43           C  
ATOM   1964  NZ  LYS A 245      12.243  -1.195  51.667  1.00 60.93           N  
ATOM   1965  N   ALA A 246      17.344  -2.878  46.972  1.00 54.22           N  
ATOM   1966  CA  ALA A 246      17.483  -3.773  45.827  1.00 54.30           C  
ATOM   1967  C   ALA A 246      18.928  -3.980  45.420  1.00 58.18           C  
ATOM   1968  O   ALA A 246      19.368  -5.114  45.209  1.00 59.80           O  
ATOM   1969  CB  ALA A 246      16.699  -3.259  44.656  1.00 51.49           C  
ATOM   1970  N   GLU A 247      19.662  -2.879  45.316  1.00 58.53           N  
ATOM   1971  CA  GLU A 247      21.055  -2.913  44.915  1.00 57.24           C  
ATOM   1972  C   GLU A 247      21.881  -3.646  45.958  1.00 60.11           C  
ATOM   1973  O   GLU A 247      22.898  -4.251  45.642  1.00 59.48           O  
ATOM   1974  CB  GLU A 247      21.552  -1.486  44.681  1.00 57.96           C  
ATOM   1975  CG  GLU A 247      23.045  -1.325  44.566  1.00 62.37           C  
ATOM   1976  CD  GLU A 247      23.691  -1.087  45.914  1.00 69.69           C  
ATOM   1977  OE1 GLU A 247      22.948  -0.759  46.869  1.00 72.65           O  
ATOM   1978  OE2 GLU A 247      24.928  -1.238  46.024  1.00 72.16           O  
ATOM   1979  N   LYS A 248      21.423  -3.612  47.201  1.00 61.04           N  
ATOM   1980  CA  LYS A 248      22.094  -4.324  48.272  1.00 60.79           C  
ATOM   1981  C   LYS A 248      21.844  -5.850  48.237  1.00 62.84           C  
ATOM   1982  O   LYS A 248      22.778  -6.635  48.423  1.00 62.80           O  
ATOM   1983  CB  LYS A 248      21.734  -3.709  49.625  1.00 60.79           C  
ATOM   1984  CG  LYS A 248      22.191  -4.514  50.824  1.00 73.32           C  
ATOM   1985  CD  LYS A 248      23.725  -4.587  50.954  1.00 99.10           C  
ATOM   1986  CE  LYS A 248      24.177  -5.920  51.598  1.00 96.78           C  
ATOM   1987  NZ  LYS A 248      25.648  -6.005  51.845  1.00 84.79           N  
ATOM   1988  N   GLU A 249      20.611  -6.281  47.974  1.00 57.59           N  
ATOM   1989  CA  GLU A 249      20.336  -7.718  47.914  1.00 60.76           C  
ATOM   1990  C   GLU A 249      20.861  -8.357  46.634  1.00 60.05           C  
ATOM   1991  O   GLU A 249      21.316  -9.493  46.651  1.00 61.83           O  
ATOM   1992  CB  GLU A 249      18.848  -8.034  48.099  1.00 57.26           C  
ATOM   1993  CG  GLU A 249      18.578  -9.306  48.930  1.00 71.38           C  
ATOM   1994  CD  GLU A 249      18.417 -10.586  48.088  1.00 79.45           C  
ATOM   1995  OE1 GLU A 249      17.770 -10.541  47.015  1.00 81.79           O  
ATOM   1996  OE2 GLU A 249      18.922 -11.650  48.511  1.00 73.49           O  
ATOM   1997  N   VAL A 250      20.805  -7.631  45.527  1.00 53.81           N  
ATOM   1998  CA  VAL A 250      21.315  -8.155  44.268  1.00 50.46           C  
ATOM   1999  C   VAL A 250      22.825  -8.389  44.348  1.00 54.90           C  
ATOM   2000  O   VAL A 250      23.353  -9.362  43.793  1.00 53.50           O  
ATOM   2001  CB  VAL A 250      20.983  -7.223  43.080  1.00 53.97           C  
ATOM   2002  CG1 VAL A 250      21.703  -7.668  41.823  1.00 51.29           C  
ATOM   2003  CG2 VAL A 250      19.481  -7.178  42.833  1.00 58.92           C  
ATOM   2004  N   THR A 251      23.532  -7.510  45.049  1.00 57.70           N  
ATOM   2005  CA  THR A 251      24.972  -7.678  45.190  1.00 56.77           C  
ATOM   2006  C   THR A 251      25.284  -8.899  46.047  1.00 54.34           C  
ATOM   2007  O   THR A 251      26.081  -9.743  45.644  1.00 50.65           O  
ATOM   2008  CB  THR A 251      25.656  -6.409  45.741  1.00 52.69           C  
ATOM   2009  OG1 THR A 251      25.681  -5.431  44.705  1.00 55.84           O  
ATOM   2010  CG2 THR A 251      27.091  -6.692  46.163  1.00 48.68           C  
ATOM   2011  N   ARG A 252      24.640  -8.993  47.208  1.00 56.80           N  
ATOM   2012  CA  ARG A 252      24.835 -10.121  48.107  1.00 57.01           C  
ATOM   2013  C   ARG A 252      24.578 -11.408  47.349  1.00 57.62           C  
ATOM   2014  O   ARG A 252      25.372 -12.347  47.402  1.00 58.47           O  
ATOM   2015  CB  ARG A 252      23.890 -10.025  49.295  1.00 56.82           C  
ATOM   2016  CG  ARG A 252      24.315 -10.851  50.486  1.00 57.17           C  
ATOM   2017  CD  ARG A 252      23.147 -11.062  51.417  1.00 68.92           C  
ATOM   2018  NE  ARG A 252      21.973 -11.497  50.662  1.00 80.42           N  
ATOM   2019  CZ  ARG A 252      21.125 -12.444  51.055  1.00 84.95           C  
ATOM   2020  NH1 ARG A 252      21.305 -13.074  52.212  1.00 84.95           N  
ATOM   2021  NH2 ARG A 252      20.095 -12.760  50.281  1.00 83.88           N  
ATOM   2022  N   MET A 253      23.473 -11.429  46.616  1.00 52.02           N  
ATOM   2023  CA  MET A 253      23.118 -12.588  45.813  1.00 51.70           C  
ATOM   2024  C   MET A 253      24.156 -12.942  44.757  1.00 51.10           C  
ATOM   2025  O   MET A 253      24.435 -14.112  44.540  1.00 53.50           O  
ATOM   2026  CB  MET A 253      21.731 -12.422  45.186  1.00 49.64           C  
ATOM   2027  CG  MET A 253      20.615 -12.973  46.058  1.00 53.17           C  
ATOM   2028  SD  MET A 253      20.818 -14.748  46.395  1.00 63.63           S  
ATOM   2029  CE  MET A 253      20.951 -15.388  44.720  1.00 44.16           C  
ATOM   2030  N   VAL A 254      24.722 -11.942  44.099  1.00 49.36           N  
ATOM   2031  CA  VAL A 254      25.774 -12.190  43.112  1.00 52.92           C  
ATOM   2032  C   VAL A 254      27.073 -12.723  43.761  1.00 50.63           C  
ATOM   2033  O   VAL A 254      27.803 -13.515  43.168  1.00 51.65           O  
ATOM   2034  CB  VAL A 254      26.025 -10.927  42.228  1.00 53.41           C  
ATOM   2035  CG1 VAL A 254      27.335 -11.023  41.460  1.00 46.09           C  
ATOM   2036  CG2 VAL A 254      24.862 -10.727  41.267  1.00 51.36           C  
ATOM   2037  N   ILE A 255      27.342 -12.305  44.989  1.00 45.98           N  
ATOM   2038  CA  ILE A 255      28.489 -12.812  45.710  1.00 46.88           C  
ATOM   2039  C   ILE A 255      28.290 -14.299  46.037  1.00 54.65           C  
ATOM   2040  O   ILE A 255      29.177 -15.138  45.776  1.00 52.51           O  
ATOM   2041  CB  ILE A 255      28.762 -11.967  46.961  1.00 46.75           C  
ATOM   2042  CG1 ILE A 255      29.249 -10.579  46.520  1.00 51.04           C  
ATOM   2043  CG2 ILE A 255      29.779 -12.648  47.866  1.00 43.35           C  
ATOM   2044  CD1 ILE A 255      29.257  -9.509  47.605  1.00 50.78           C  
ATOM   2045  N   ILE A 256      27.120 -14.626  46.588  1.00 52.44           N  
ATOM   2046  CA  ILE A 256      26.726 -16.015  46.828  1.00 45.63           C  
ATOM   2047  C   ILE A 256      26.769 -16.860  45.560  1.00 44.82           C  
ATOM   2048  O   ILE A 256      27.320 -17.936  45.573  1.00 48.38           O  
ATOM   2049  CB  ILE A 256      25.324 -16.091  47.457  1.00 49.27           C  
ATOM   2050  CG1 ILE A 256      25.346 -15.464  48.859  1.00 49.49           C  
ATOM   2051  CG2 ILE A 256      24.823 -17.533  47.480  1.00 47.24           C  
ATOM   2052  CD1 ILE A 256      24.000 -14.988  49.352  1.00 52.82           C  
ATOM   2053  N   MET A 257      26.203 -16.375  44.464  1.00 47.10           N  
ATOM   2054  CA  MET A 257      26.201 -17.149  43.230  1.00 49.54           C  
ATOM   2055  C   MET A 257      27.591 -17.378  42.690  1.00 48.74           C  
ATOM   2056  O   MET A 257      27.867 -18.408  42.085  1.00 50.19           O  
ATOM   2057  CB  MET A 257      25.368 -16.470  42.151  1.00 47.97           C  
ATOM   2058  CG  MET A 257      23.886 -16.662  42.298  1.00 47.32           C  
ATOM   2059  SD  MET A 257      23.031 -15.855  40.936  1.00 59.48           S  
ATOM   2060  CE  MET A 257      23.343 -14.130  41.320  1.00 51.54           C  
ATOM   2061  N   VAL A 258      28.459 -16.398  42.880  1.00 49.13           N  
ATOM   2062  CA  VAL A 258      29.798 -16.472  42.314  1.00 49.98           C  
ATOM   2063  C   VAL A 258      30.730 -17.365  43.154  1.00 51.11           C  
ATOM   2064  O   VAL A 258      31.462 -18.196  42.615  1.00 47.53           O  
ATOM   2065  CB  VAL A 258      30.371 -15.054  42.033  1.00 48.21           C  
ATOM   2066  CG1 VAL A 258      31.837 -14.965  42.405  1.00 52.71           C  
ATOM   2067  CG2 VAL A 258      30.157 -14.700  40.565  1.00 51.36           C  
ATOM   2068  N   ILE A 259      30.657 -17.214  44.474  1.00 48.91           N  
ATOM   2069  CA  ILE A 259      31.372 -18.079  45.398  1.00 46.46           C  
ATOM   2070  C   ILE A 259      30.926 -19.543  45.267  1.00 49.02           C  
ATOM   2071  O   ILE A 259      31.754 -20.468  45.269  1.00 47.46           O  
ATOM   2072  CB  ILE A 259      31.160 -17.600  46.834  1.00 43.28           C  
ATOM   2073  CG1 ILE A 259      31.952 -16.315  47.067  1.00 42.85           C  
ATOM   2074  CG2 ILE A 259      31.511 -18.699  47.843  1.00 35.66           C  
ATOM   2075  CD1 ILE A 259      31.827 -15.801  48.465  1.00 42.38           C  
ATOM   2076  N   ALA A 260      29.615 -19.741  45.141  1.00 49.14           N  
ATOM   2077  CA  ALA A 260      29.026 -21.069  45.004  1.00 47.91           C  
ATOM   2078  C   ALA A 260      29.509 -21.770  43.752  1.00 49.65           C  
ATOM   2079  O   ALA A 260      29.764 -22.970  43.776  1.00 50.71           O  
ATOM   2080  CB  ALA A 260      27.528 -20.985  44.989  1.00 43.75           C  
ATOM   2081  N   PHE A 261      29.620 -21.032  42.654  1.00 45.29           N  
ATOM   2082  CA  PHE A 261      30.118 -21.611  41.417  1.00 46.96           C  
ATOM   2083  C   PHE A 261      31.569 -22.052  41.568  1.00 54.75           C  
ATOM   2084  O   PHE A 261      31.995 -23.050  40.970  1.00 51.27           O  
ATOM   2085  CB  PHE A 261      30.027 -20.604  40.285  1.00 48.95           C  
ATOM   2086  CG  PHE A 261      30.674 -21.067  39.012  1.00 52.02           C  
ATOM   2087  CD1 PHE A 261      32.009 -20.803  38.743  1.00 55.65           C  
ATOM   2088  CD2 PHE A 261      29.944 -21.756  38.078  1.00 54.66           C  
ATOM   2089  CE1 PHE A 261      32.590 -21.240  37.564  1.00 56.52           C  
ATOM   2090  CE2 PHE A 261      30.518 -22.180  36.906  1.00 54.37           C  
ATOM   2091  CZ  PHE A 261      31.837 -21.923  36.645  1.00 55.83           C  
ATOM   2092  N   LEU A 262      32.331 -21.283  42.341  1.00 50.05           N  
ATOM   2093  CA  LEU A 262      33.736 -21.567  42.503  1.00 47.79           C  
ATOM   2094  C   LEU A 262      33.866 -22.799  43.365  1.00 51.08           C  
ATOM   2095  O   LEU A 262      34.582 -23.724  43.002  1.00 55.09           O  
ATOM   2096  CB  LEU A 262      34.490 -20.379  43.110  1.00 50.77           C  
ATOM   2097  CG  LEU A 262      34.665 -19.123  42.238  1.00 49.96           C  
ATOM   2098  CD1 LEU A 262      35.378 -18.019  43.004  1.00 39.23           C  
ATOM   2099  CD2 LEU A 262      35.361 -19.412  40.905  1.00 45.56           C  
ATOM   2100  N   ILE A 263      33.164 -22.832  44.494  1.00 48.65           N  
ATOM   2101  CA  ILE A 263      33.237 -23.988  45.397  1.00 52.44           C  
ATOM   2102  C   ILE A 263      32.895 -25.301  44.656  1.00 50.60           C  
ATOM   2103  O   ILE A 263      33.348 -26.383  45.021  1.00 50.77           O  
ATOM   2104  CB  ILE A 263      32.312 -23.792  46.641  1.00 53.56           C  
ATOM   2105  CG1 ILE A 263      32.737 -22.561  47.439  1.00 50.76           C  
ATOM   2106  CG2 ILE A 263      32.346 -24.987  47.558  1.00 46.97           C  
ATOM   2107  CD1 ILE A 263      31.936 -22.330  48.703  1.00 46.92           C  
ATOM   2108  N   CYS A 264      32.066 -25.206  43.631  1.00 51.11           N  
ATOM   2109  CA  CYS A 264      31.753 -26.378  42.839  1.00 52.76           C  
ATOM   2110  C   CYS A 264      32.774 -26.820  41.794  1.00 51.40           C  
ATOM   2111  O   CYS A 264      33.160 -27.972  41.794  1.00 50.93           O  
ATOM   2112  CB  CYS A 264      30.372 -26.182  42.169  1.00 53.93           C  
ATOM   2113  SG  CYS A 264      29.879 -27.562  41.182  1.00 49.83           S  
ATOM   2114  N   TRP A 265      33.211 -25.916  40.918  1.00 56.58           N  
ATOM   2115  CA  TRP A 265      34.146 -26.314  39.863  1.00 58.82           C  
ATOM   2116  C   TRP A 265      35.629 -26.048  40.095  1.00 60.95           C  
ATOM   2117  O   TRP A 265      36.466 -26.542  39.341  1.00 61.91           O  
ATOM   2118  CB  TRP A 265      33.734 -25.724  38.518  1.00 51.67           C  
ATOM   2119  CG  TRP A 265      32.439 -26.256  38.103  1.00 55.40           C  
ATOM   2120  CD1 TRP A 265      31.224 -25.642  38.211  1.00 58.53           C  
ATOM   2121  CD2 TRP A 265      32.188 -27.555  37.560  1.00 59.37           C  
ATOM   2122  NE1 TRP A 265      30.230 -26.472  37.743  1.00 57.31           N  
ATOM   2123  CE2 TRP A 265      30.796 -27.654  37.340  1.00 56.87           C  
ATOM   2124  CE3 TRP A 265      33.010 -28.642  37.219  1.00 56.76           C  
ATOM   2125  CZ2 TRP A 265      30.210 -28.795  36.801  1.00 57.16           C  
ATOM   2126  CZ3 TRP A 265      32.428 -29.767  36.680  1.00 50.33           C  
ATOM   2127  CH2 TRP A 265      31.042 -29.838  36.476  1.00 56.95           C  
ATOM   2128  N   LEU A 266      35.971 -25.342  41.163  1.00 57.44           N  
ATOM   2129  CA  LEU A 266      37.371 -25.006  41.381  1.00 59.33           C  
ATOM   2130  C   LEU A 266      38.214 -26.240  41.756  1.00 60.94           C  
ATOM   2131  O   LEU A 266      39.315 -26.430  41.214  1.00 61.34           O  
ATOM   2132  CB  LEU A 266      37.555 -23.820  42.348  1.00 52.18           C  
ATOM   2133  CG  LEU A 266      38.761 -22.911  42.051  1.00 53.86           C  
ATOM   2134  CD1 LEU A 266      38.677 -22.368  40.634  1.00 53.47           C  
ATOM   2135  CD2 LEU A 266      38.907 -21.773  43.054  1.00 49.26           C  
ATOM   2136  N   PRO A 267      37.710 -27.085  42.682  1.00 59.58           N  
ATOM   2137  CA  PRO A 267      38.505 -28.274  43.008  1.00 61.44           C  
ATOM   2138  C   PRO A 267      38.730 -29.155  41.793  1.00 60.16           C  
ATOM   2139  O   PRO A 267      39.841 -29.624  41.572  1.00 59.88           O  
ATOM   2140  CB  PRO A 267      37.643 -28.994  44.042  1.00 58.09           C  
ATOM   2141  CG  PRO A 267      36.936 -27.902  44.730  1.00 58.58           C  
ATOM   2142  CD  PRO A 267      36.608 -26.905  43.644  1.00 54.99           C  
ATOM   2143  N   TYR A 268      37.692 -29.367  41.001  1.00 58.89           N  
ATOM   2144  CA  TYR A 268      37.846 -30.182  39.809  1.00 60.48           C  
ATOM   2145  C   TYR A 268      38.810 -29.516  38.830  1.00 60.39           C  
ATOM   2146  O   TYR A 268      39.553 -30.183  38.119  1.00 63.27           O  
ATOM   2147  CB  TYR A 268      36.489 -30.454  39.160  1.00 57.49           C  
ATOM   2148  CG  TYR A 268      36.002 -31.865  39.379  1.00 57.95           C  
ATOM   2149  CD1 TYR A 268      36.881 -32.945  39.287  1.00 54.96           C  
ATOM   2150  CD2 TYR A 268      34.667 -32.121  39.685  1.00 53.91           C  
ATOM   2151  CE1 TYR A 268      36.441 -34.244  39.486  1.00 57.98           C  
ATOM   2152  CE2 TYR A 268      34.214 -33.419  39.891  1.00 51.79           C  
ATOM   2153  CZ  TYR A 268      35.102 -34.481  39.791  1.00 58.71           C  
ATOM   2154  OH  TYR A 268      34.658 -35.779  39.994  1.00 53.33           O  
ATOM   2155  N   ALA A 269      38.804 -28.193  38.811  1.00 59.75           N  
ATOM   2156  CA  ALA A 269      39.700 -27.450  37.947  1.00 60.46           C  
ATOM   2157  C   ALA A 269      41.132 -27.483  38.495  1.00 60.27           C  
ATOM   2158  O   ALA A 269      42.073 -27.773  37.757  1.00 56.69           O  
ATOM   2159  CB  ALA A 269      39.201 -26.009  37.789  1.00 57.75           C  
ATOM   2160  N   GLY A 270      41.280 -27.200  39.790  1.00 59.62           N  
ATOM   2161  CA  GLY A 270      42.586 -27.098  40.419  1.00 60.55           C  
ATOM   2162  C   GLY A 270      43.351 -28.408  40.412  1.00 65.55           C  
ATOM   2163  O   GLY A 270      44.574 -28.446  40.257  1.00 63.40           O  
ATOM   2164  N   VAL A 271      42.597 -29.489  40.584  1.00 67.10           N  
ATOM   2165  CA  VAL A 271      43.113 -30.850  40.564  1.00 60.14           C  
ATOM   2166  C   VAL A 271      43.462 -31.288  39.137  1.00 61.24           C  
ATOM   2167  O   VAL A 271      44.564 -31.755  38.900  1.00 60.53           O  
ATOM   2168  CB  VAL A 271      42.099 -31.805  41.204  1.00 58.05           C  
ATOM   2169  CG1 VAL A 271      42.313 -33.232  40.713  1.00 65.17           C  
ATOM   2170  CG2 VAL A 271      42.152 -31.690  42.728  1.00 50.58           C  
ATOM   2171  N   ALA A 272      42.535 -31.130  38.190  1.00 61.13           N  
ATOM   2172  CA  ALA A 272      42.828 -31.431  36.785  1.00 60.06           C  
ATOM   2173  C   ALA A 272      44.074 -30.690  36.286  1.00 62.44           C  
ATOM   2174  O   ALA A 272      44.888 -31.260  35.558  1.00 62.81           O  
ATOM   2175  CB  ALA A 272      41.643 -31.126  35.897  1.00 52.14           C  
ATOM   2176  N   PHE A 273      44.221 -29.429  36.693  1.00 63.83           N  
ATOM   2177  CA  PHE A 273      45.356 -28.608  36.289  1.00 63.40           C  
ATOM   2178  C   PHE A 273      46.644 -29.125  36.923  1.00 65.06           C  
ATOM   2179  O   PHE A 273      47.654 -29.296  36.244  1.00 63.71           O  
ATOM   2180  CB  PHE A 273      45.127 -27.139  36.673  1.00 60.83           C  
ATOM   2181  CG  PHE A 273      46.306 -26.249  36.390  1.00 63.24           C  
ATOM   2182  CD1 PHE A 273      46.488 -25.687  35.132  1.00 62.32           C  
ATOM   2183  CD2 PHE A 273      47.245 -25.982  37.379  1.00 63.36           C  
ATOM   2184  CE1 PHE A 273      47.589 -24.880  34.867  1.00 56.95           C  
ATOM   2185  CE2 PHE A 273      48.345 -25.183  37.115  1.00 59.75           C  
ATOM   2186  CZ  PHE A 273      48.512 -24.632  35.858  1.00 58.17           C  
ATOM   2187  N   TYR A 274      46.594 -29.371  38.228  1.00 67.33           N  
ATOM   2188  CA  TYR A 274      47.753 -29.831  38.984  1.00 68.58           C  
ATOM   2189  C   TYR A 274      48.260 -31.184  38.490  1.00 72.54           C  
ATOM   2190  O   TYR A 274      49.451 -31.417  38.441  1.00 74.44           O  
ATOM   2191  CB  TYR A 274      47.398 -29.909  40.469  1.00 66.62           C  
ATOM   2192  CG  TYR A 274      48.530 -30.290  41.396  1.00 74.61           C  
ATOM   2193  CD1 TYR A 274      48.871 -31.622  41.600  1.00 78.11           C  
ATOM   2194  CD2 TYR A 274      49.232 -29.321  42.096  1.00 74.54           C  
ATOM   2195  CE1 TYR A 274      49.894 -31.975  42.459  1.00 82.70           C  
ATOM   2196  CE2 TYR A 274      50.256 -29.661  42.956  1.00 82.47           C  
ATOM   2197  CZ  TYR A 274      50.584 -30.988  43.138  1.00 90.78           C  
ATOM   2198  OH  TYR A 274      51.611 -31.319  43.998  1.00101.94           O  
ATOM   2199  N   ILE A 275      47.352 -32.073  38.122  1.00 69.76           N  
ATOM   2200  CA  ILE A 275      47.736 -33.391  37.642  1.00 73.99           C  
ATOM   2201  C   ILE A 275      48.359 -33.266  36.254  1.00 74.48           C  
ATOM   2202  O   ILE A 275      49.294 -33.991  35.908  1.00 79.66           O  
ATOM   2203  CB  ILE A 275      46.513 -34.372  37.647  1.00 71.78           C  
ATOM   2204  CG1 ILE A 275      46.115 -34.680  39.092  1.00 69.48           C  
ATOM   2205  CG2 ILE A 275      46.800 -35.657  36.874  1.00 62.39           C  
ATOM   2206  CD1 ILE A 275      45.103 -35.750  39.232  1.00 66.51           C  
ATOM   2207  N   PHE A 276      47.845 -32.329  35.469  1.00 69.29           N  
ATOM   2208  CA  PHE A 276      48.301 -32.143  34.100  1.00 72.88           C  
ATOM   2209  C   PHE A 276      49.754 -31.659  34.078  1.00 79.38           C  
ATOM   2210  O   PHE A 276      50.578 -32.126  33.284  1.00 86.18           O  
ATOM   2211  CB  PHE A 276      47.381 -31.141  33.393  1.00 71.81           C  
ATOM   2212  CG  PHE A 276      47.654 -30.976  31.924  1.00 71.63           C  
ATOM   2213  CD1 PHE A 276      48.661 -30.137  31.483  1.00 73.79           C  
ATOM   2214  CD2 PHE A 276      46.884 -31.637  30.983  1.00 72.62           C  
ATOM   2215  CE1 PHE A 276      48.912 -29.979  30.137  1.00 72.92           C  
ATOM   2216  CE2 PHE A 276      47.133 -31.473  29.627  1.00 74.93           C  
ATOM   2217  CZ  PHE A 276      48.148 -30.644  29.208  1.00 71.89           C  
ATOM   2218  N   THR A 277      50.057 -30.704  34.947  1.00 78.65           N  
ATOM   2219  CA  THR A 277      51.402 -30.157  35.037  1.00 78.99           C  
ATOM   2220  C   THR A 277      52.311 -30.870  36.054  1.00 83.12           C  
ATOM   2221  O   THR A 277      53.518 -30.625  36.119  1.00 87.50           O  
ATOM   2222  CB  THR A 277      51.278 -28.676  35.381  1.00 74.66           C  
ATOM   2223  OG1 THR A 277      50.830 -28.546  36.732  1.00 72.52           O  
ATOM   2224  CG2 THR A 277      50.248 -28.040  34.451  1.00 66.08           C  
ATOM   2225  N   HIS A 278      51.707 -31.721  36.870  1.00 83.33           N  
ATOM   2226  CA  HIS A 278      52.410 -32.620  37.806  1.00 80.84           C  
ATOM   2227  C   HIS A 278      52.670 -34.068  37.393  1.00 84.67           C  
ATOM   2228  O   HIS A 278      52.888 -34.893  38.242  1.00 90.92           O  
ATOM   2229  CB  HIS A 278      52.117 -32.386  39.296  1.00 84.65           C  
ATOM   2230  CG  HIS A 278      52.590 -31.051  39.767  1.00 86.57           C  
ATOM   2231  ND1 HIS A 278      52.503 -29.932  38.972  1.00 84.03           N  
ATOM   2232  CD2 HIS A 278      53.179 -30.656  40.921  1.00 84.42           C  
ATOM   2233  CE1 HIS A 278      53.009 -28.899  39.620  1.00 88.09           C  
ATOM   2234  NE2 HIS A 278      53.423 -29.311  40.805  1.00 86.84           N  
ATOM   2235  N   GLN A 279      52.532 -34.372  36.106  1.00 84.61           N  
ATOM   2236  CA  GLN A 279      52.272 -35.724  35.631  1.00 82.40           C  
ATOM   2237  C   GLN A 279      53.071 -36.877  36.286  1.00 90.06           C  
ATOM   2238  O   GLN A 279      52.428 -37.837  36.736  1.00 95.04           O  
ATOM   2239  CB  GLN A 279      52.469 -35.767  34.114  1.00 80.31           C  
ATOM   2240  CG  GLN A 279      51.928 -37.012  33.452  1.00 93.35           C  
ATOM   2241  CD  GLN A 279      50.427 -37.056  33.508  1.00 90.58           C  
ATOM   2242  OE1 GLN A 279      49.831 -38.030  33.985  1.00 82.55           O  
ATOM   2243  NE2 GLN A 279      49.799 -35.976  33.065  1.00 84.07           N  
ATOM   2244  N   GLY A 280      54.399 -36.847  36.388  1.00 89.85           N  
ATOM   2245  CA  GLY A 280      54.936 -37.777  37.346  1.00 88.40           C  
ATOM   2246  C   GLY A 280      54.537 -37.276  38.708  1.00 89.65           C  
ATOM   2247  O   GLY A 280      55.050 -36.254  39.166  1.00 91.22           O  
ATOM   2248  N   SER A 281      53.704 -38.063  39.388  1.00 88.19           N  
ATOM   2249  CA  SER A 281      53.239 -37.877  40.778  1.00 88.48           C  
ATOM   2250  C   SER A 281      52.140 -38.914  40.965  1.00 86.05           C  
ATOM   2251  O   SER A 281      51.524 -39.354  39.988  1.00 83.67           O  
ATOM   2252  CB  SER A 281      52.587 -36.515  41.007  1.00 90.77           C  
ATOM   2253  OG  SER A 281      53.281 -35.452  40.408  1.00 96.31           O  
ATOM   2254  N   CYS A 282      51.815 -39.216  42.212  1.00 79.47           N  
ATOM   2255  CA  CYS A 282      50.853 -40.256  42.512  1.00 70.32           C  
ATOM   2256  C   CYS A 282      49.690 -39.701  43.294  1.00 68.61           C  
ATOM   2257  O   CYS A 282      49.896 -39.130  44.346  1.00 67.12           O  
ATOM   2258  CB  CYS A 282      51.527 -41.394  43.307  1.00 65.02           C  
ATOM   2259  SG  CYS A 282      52.668 -42.510  42.304  1.00 67.98           S  
ATOM   2260  N   PHE A 283      48.476 -39.922  42.792  1.00 66.95           N  
ATOM   2261  CA  PHE A 283      47.260 -39.373  43.383  1.00 62.76           C  
ATOM   2262  C   PHE A 283      46.310 -40.447  43.905  1.00 60.34           C  
ATOM   2263  O   PHE A 283      45.723 -41.187  43.122  1.00 56.05           O  
ATOM   2264  CB  PHE A 283      46.568 -38.426  42.385  1.00 64.46           C  
ATOM   2265  CG  PHE A 283      47.450 -37.287  41.941  1.00 77.77           C  
ATOM   2266  CD1 PHE A 283      47.577 -36.147  42.725  1.00 79.53           C  
ATOM   2267  CD2 PHE A 283      48.189 -37.372  40.765  1.00 80.84           C  
ATOM   2268  CE1 PHE A 283      48.402 -35.107  42.342  1.00 84.08           C  
ATOM   2269  CE2 PHE A 283      49.031 -36.324  40.372  1.00 81.94           C  
ATOM   2270  CZ  PHE A 283      49.135 -35.194  41.164  1.00 84.35           C  
ATOM   2271  N   GLY A 284      46.155 -40.511  45.227  1.00 56.31           N  
ATOM   2272  CA  GLY A 284      45.333 -41.524  45.881  1.00 58.84           C  
ATOM   2273  C   GLY A 284      43.832 -41.496  45.595  1.00 59.94           C  
ATOM   2274  O   GLY A 284      43.297 -40.494  45.123  1.00 59.66           O  
ATOM   2275  N   PRO A 285      43.136 -42.609  45.883  1.00 59.13           N  
ATOM   2276  CA  PRO A 285      41.707 -42.733  45.593  1.00 58.23           C  
ATOM   2277  C   PRO A 285      40.812 -41.709  46.307  1.00 60.24           C  
ATOM   2278  O   PRO A 285      39.921 -41.169  45.657  1.00 61.19           O  
ATOM   2279  CB  PRO A 285      41.386 -44.148  46.084  1.00 56.58           C  
ATOM   2280  CG  PRO A 285      42.446 -44.453  47.072  1.00 56.82           C  
ATOM   2281  CD  PRO A 285      43.661 -43.840  46.490  1.00 58.55           C  
ATOM   2282  N   ILE A 286      41.038 -41.464  47.598  1.00 60.80           N  
ATOM   2283  CA  ILE A 286      40.277 -40.475  48.382  1.00 64.46           C  
ATOM   2284  C   ILE A 286      40.490 -39.020  47.891  1.00 64.92           C  
ATOM   2285  O   ILE A 286      39.545 -38.238  47.798  1.00 67.71           O  
ATOM   2286  CB  ILE A 286      40.639 -40.553  49.905  1.00 63.37           C  
ATOM   2287  CG1 ILE A 286      40.575 -41.989  50.420  1.00 54.08           C  
ATOM   2288  CG2 ILE A 286      39.751 -39.639  50.748  1.00 59.98           C  
ATOM   2289  CD1 ILE A 286      39.203 -42.522  50.553  1.00 54.08           C  
ATOM   2290  N   PHE A 287      41.738 -38.670  47.599  1.00 53.63           N  
ATOM   2291  CA  PHE A 287      42.102 -37.378  47.019  1.00 56.92           C  
ATOM   2292  C   PHE A 287      41.354 -37.090  45.716  1.00 60.77           C  
ATOM   2293  O   PHE A 287      41.004 -35.945  45.435  1.00 60.36           O  
ATOM   2294  CB  PHE A 287      43.616 -37.358  46.767  1.00 60.61           C  
ATOM   2295  CG  PHE A 287      44.096 -36.251  45.850  1.00 63.11           C  
ATOM   2296  CD1 PHE A 287      44.086 -36.412  44.464  1.00 68.04           C  
ATOM   2297  CD2 PHE A 287      44.617 -35.074  46.377  1.00 62.84           C  
ATOM   2298  CE1 PHE A 287      44.541 -35.393  43.624  1.00 71.99           C  
ATOM   2299  CE2 PHE A 287      45.082 -34.060  45.549  1.00 61.34           C  
ATOM   2300  CZ  PHE A 287      45.051 -34.220  44.170  1.00 66.44           C  
ATOM   2301  N   MET A 288      41.142 -38.120  44.905  1.00 59.86           N  
ATOM   2302  CA  MET A 288      40.406 -37.977  43.647  1.00 60.97           C  
ATOM   2303  C   MET A 288      38.904 -37.918  43.894  1.00 59.91           C  
ATOM   2304  O   MET A 288      38.118 -37.521  43.026  1.00 58.65           O  
ATOM   2305  CB  MET A 288      40.715 -39.158  42.739  1.00 61.78           C  
ATOM   2306  CG  MET A 288      42.176 -39.277  42.369  1.00 67.17           C  
ATOM   2307  SD  MET A 288      42.652 -37.988  41.212  1.00 69.07           S  
ATOM   2308  CE  MET A 288      41.496 -38.310  39.896  1.00 57.48           C  
ATOM   2309  N   THR A 289      38.540 -38.336  45.100  1.00 56.53           N  
ATOM   2310  CA  THR A 289      37.177 -38.324  45.593  1.00 57.70           C  
ATOM   2311  C   THR A 289      36.726 -36.900  46.041  1.00 57.17           C  
ATOM   2312  O   THR A 289      35.546 -36.542  45.901  1.00 46.81           O  
ATOM   2313  CB  THR A 289      37.017 -39.425  46.706  1.00 55.54           C  
ATOM   2314  OG1 THR A 289      36.614 -40.656  46.097  1.00 55.72           O  
ATOM   2315  CG2 THR A 289      35.995 -39.034  47.741  1.00 61.07           C  
ATOM   2316  N   ILE A 290      37.688 -36.084  46.501  1.00 57.33           N  
ATOM   2317  CA  ILE A 290      37.459 -34.708  47.018  1.00 53.85           C  
ATOM   2318  C   ILE A 290      36.784 -33.703  46.065  1.00 53.63           C  
ATOM   2319  O   ILE A 290      35.757 -33.123  46.422  1.00 48.08           O  
ATOM   2320  CB  ILE A 290      38.752 -34.067  47.616  1.00 56.05           C  
ATOM   2321  CG1 ILE A 290      39.179 -34.720  48.933  1.00 57.81           C  
ATOM   2322  CG2 ILE A 290      38.568 -32.581  47.857  1.00 50.42           C  
ATOM   2323  CD1 ILE A 290      40.473 -34.099  49.527  1.00 55.83           C  
ATOM   2324  N   PRO A 291      37.357 -33.482  44.861  1.00 55.45           N  
ATOM   2325  CA  PRO A 291      36.740 -32.503  43.953  1.00 56.00           C  
ATOM   2326  C   PRO A 291      35.357 -32.965  43.486  1.00 48.64           C  
ATOM   2327  O   PRO A 291      34.512 -32.150  43.140  1.00 47.95           O  
ATOM   2328  CB  PRO A 291      37.738 -32.431  42.781  1.00 51.91           C  
ATOM   2329  CG  PRO A 291      38.440 -33.699  42.802  1.00 53.43           C  
ATOM   2330  CD  PRO A 291      38.538 -34.110  44.246  1.00 51.38           C  
ATOM   2331  N   ALA A 292      35.150 -34.281  43.558  1.00 49.30           N  
ATOM   2332  CA  ALA A 292      33.862 -34.939  43.295  1.00 47.16           C  
ATOM   2333  C   ALA A 292      32.836 -34.717  44.422  1.00 45.86           C  
ATOM   2334  O   ALA A 292      31.691 -34.417  44.150  1.00 41.16           O  
ATOM   2335  CB  ALA A 292      34.061 -36.387  43.015  1.00 42.63           C  
ATOM   2336  N   PHE A 293      33.265 -34.827  45.673  1.00 46.18           N  
ATOM   2337  CA  PHE A 293      32.445 -34.439  46.829  1.00 45.61           C  
ATOM   2338  C   PHE A 293      31.837 -33.046  46.624  1.00 50.43           C  
ATOM   2339  O   PHE A 293      30.644 -32.837  46.830  1.00 51.49           O  
ATOM   2340  CB  PHE A 293      33.311 -34.484  48.112  1.00 52.23           C  
ATOM   2341  CG  PHE A 293      32.769 -33.676  49.298  1.00 56.40           C  
ATOM   2342  CD1 PHE A 293      32.904 -32.293  49.345  1.00 55.50           C  
ATOM   2343  CD2 PHE A 293      32.193 -34.313  50.398  1.00 56.34           C  
ATOM   2344  CE1 PHE A 293      32.423 -31.559  50.422  1.00 58.45           C  
ATOM   2345  CE2 PHE A 293      31.724 -33.579  51.492  1.00 53.73           C  
ATOM   2346  CZ  PHE A 293      31.841 -32.203  51.499  1.00 52.15           C  
ATOM   2347  N   PHE A 294      32.685 -32.109  46.198  1.00 51.03           N  
ATOM   2348  CA  PHE A 294      32.344 -30.700  45.962  1.00 49.60           C  
ATOM   2349  C   PHE A 294      31.340 -30.469  44.822  1.00 48.22           C  
ATOM   2350  O   PHE A 294      30.299 -29.833  45.018  1.00 45.81           O  
ATOM   2351  CB  PHE A 294      33.637 -29.874  45.760  1.00 48.11           C  
ATOM   2352  CG  PHE A 294      34.197 -29.328  47.045  1.00 52.11           C  
ATOM   2353  CD1 PHE A 294      33.590 -28.247  47.638  1.00 52.58           C  
ATOM   2354  CD2 PHE A 294      35.287 -29.909  47.682  1.00 51.47           C  
ATOM   2355  CE1 PHE A 294      34.051 -27.735  48.818  1.00 53.95           C  
ATOM   2356  CE2 PHE A 294      35.758 -29.398  48.875  1.00 48.09           C  
ATOM   2357  CZ  PHE A 294      35.137 -28.305  49.438  1.00 54.45           C  
ATOM   2358  N   ALA A 295      31.647 -31.000  43.642  1.00 42.57           N  
ATOM   2359  CA  ALA A 295      30.764 -30.843  42.491  1.00 44.46           C  
ATOM   2360  C   ALA A 295      29.397 -31.538  42.633  1.00 50.56           C  
ATOM   2361  O   ALA A 295      28.398 -31.082  42.064  1.00 47.13           O  
ATOM   2362  CB  ALA A 295      31.456 -31.283  41.234  1.00 37.44           C  
ATOM   2363  N   LYS A 296      29.348 -32.624  43.400  1.00 50.44           N  
ATOM   2364  CA  LYS A 296      28.115 -33.391  43.533  1.00 46.96           C  
ATOM   2365  C   LYS A 296      27.107 -32.746  44.479  1.00 47.83           C  
ATOM   2366  O   LYS A 296      25.907 -32.788  44.212  1.00 48.28           O  
ATOM   2367  CB  LYS A 296      28.405 -34.817  43.996  1.00 45.83           C  
ATOM   2368  CG  LYS A 296      28.908 -35.743  42.925  1.00 44.78           C  
ATOM   2369  CD  LYS A 296      29.323 -37.057  43.547  1.00 51.97           C  
ATOM   2370  CE  LYS A 296      30.117 -37.949  42.588  1.00 53.30           C  
ATOM   2371  NZ  LYS A 296      29.333 -38.466  41.425  1.00 48.38           N  
ATOM   2372  N   THR A 297      27.597 -32.182  45.587  1.00 43.77           N  
ATOM   2373  CA  THR A 297      26.756 -31.497  46.591  1.00 47.64           C  
ATOM   2374  C   THR A 297      26.024 -30.249  46.043  1.00 45.31           C  
ATOM   2375  O   THR A 297      25.114 -29.714  46.668  1.00 43.19           O  
ATOM   2376  CB  THR A 297      27.586 -31.117  47.831  1.00 43.97           C  
ATOM   2377  OG1 THR A 297      28.426 -32.218  48.175  1.00 45.78           O  
ATOM   2378  CG2 THR A 297      26.689 -30.772  49.020  1.00 40.10           C  
ATOM   2379  N   SER A 298      26.457 -29.794  44.872  1.00 45.74           N  
ATOM   2380  CA  SER A 298      25.835 -28.683  44.181  1.00 44.77           C  
ATOM   2381  C   SER A 298      24.399 -29.028  43.866  1.00 45.61           C  
ATOM   2382  O   SER A 298      23.533 -28.158  43.809  1.00 49.38           O  
ATOM   2383  CB  SER A 298      26.586 -28.357  42.897  1.00 44.63           C  
ATOM   2384  OG  SER A 298      26.173 -29.160  41.809  1.00 38.94           O  
ATOM   2385  N   ALA A 299      24.146 -30.318  43.684  1.00 42.19           N  
ATOM   2386  CA  ALA A 299      22.806 -30.815  43.404  1.00 42.80           C  
ATOM   2387  C   ALA A 299      21.850 -30.516  44.568  1.00 42.58           C  
ATOM   2388  O   ALA A 299      20.633 -30.620  44.423  1.00 41.84           O  
ATOM   2389  CB  ALA A 299      22.849 -32.289  43.107  1.00 39.52           C  
ATOM   2390  N   VAL A 300      22.419 -30.153  45.718  1.00 40.51           N  
ATOM   2391  CA  VAL A 300      21.674 -29.663  46.876  1.00 38.05           C  
ATOM   2392  C   VAL A 300      21.737 -28.127  47.017  1.00 44.94           C  
ATOM   2393  O   VAL A 300      20.680 -27.469  47.038  1.00 42.06           O  
ATOM   2394  CB  VAL A 300      22.076 -30.375  48.170  1.00 38.74           C  
ATOM   2395  CG1 VAL A 300      21.589 -29.624  49.394  1.00 39.19           C  
ATOM   2396  CG2 VAL A 300      21.528 -31.779  48.165  1.00 42.84           C  
ATOM   2397  N   TYR A 301      22.945 -27.571  47.174  1.00 41.30           N  
ATOM   2398  CA  TYR A 301      23.117 -26.115  47.353  1.00 45.97           C  
ATOM   2399  C   TYR A 301      22.713 -25.194  46.183  1.00 47.08           C  
ATOM   2400  O   TYR A 301      22.230 -24.087  46.413  1.00 43.30           O  
ATOM   2401  CB  TYR A 301      24.498 -25.735  47.931  1.00 47.34           C  
ATOM   2402  CG  TYR A 301      25.731 -26.020  47.104  1.00 48.35           C  
ATOM   2403  CD1 TYR A 301      26.019 -25.288  45.959  1.00 49.46           C  
ATOM   2404  CD2 TYR A 301      26.646 -26.978  47.512  1.00 44.72           C  
ATOM   2405  CE1 TYR A 301      27.159 -25.546  45.219  1.00 49.52           C  
ATOM   2406  CE2 TYR A 301      27.776 -27.233  46.791  1.00 44.66           C  
ATOM   2407  CZ  TYR A 301      28.033 -26.517  45.644  1.00 48.07           C  
ATOM   2408  OH  TYR A 301      29.173 -26.779  44.920  1.00 49.51           O  
ATOM   2409  N   ASN A 302      22.903 -25.640  44.948  1.00 43.91           N  
ATOM   2410  CA  ASN A 302      22.350 -24.904  43.817  1.00 44.92           C  
ATOM   2411  C   ASN A 302      20.853 -24.634  43.887  1.00 46.71           C  
ATOM   2412  O   ASN A 302      20.427 -23.487  43.794  1.00 47.96           O  
ATOM   2413  CB  ASN A 302      22.659 -25.581  42.493  1.00 45.47           C  
ATOM   2414  CG  ASN A 302      24.001 -25.239  41.985  1.00 47.57           C  
ATOM   2415  OD1 ASN A 302      24.691 -24.391  42.546  1.00 46.31           O  
ATOM   2416  ND2 ASN A 302      24.389 -25.880  40.892  1.00 50.49           N  
ATOM   2417  N   PRO A 303      20.030 -25.684  44.028  1.00 51.41           N  
ATOM   2418  CA  PRO A 303      18.629 -25.243  44.089  1.00 47.03           C  
ATOM   2419  C   PRO A 303      18.261 -24.472  45.375  1.00 44.55           C  
ATOM   2420  O   PRO A 303      17.297 -23.752  45.340  1.00 47.50           O  
ATOM   2421  CB  PRO A 303      17.822 -26.549  43.925  1.00 46.85           C  
ATOM   2422  CG  PRO A 303      18.833 -27.664  43.856  1.00 45.14           C  
ATOM   2423  CD  PRO A 303      20.176 -27.145  44.193  1.00 42.24           C  
ATOM   2424  N   VAL A 304      19.013 -24.582  46.461  1.00 44.06           N  
ATOM   2425  CA  VAL A 304      18.767 -23.736  47.619  1.00 43.53           C  
ATOM   2426  C   VAL A 304      19.075 -22.271  47.294  1.00 50.95           C  
ATOM   2427  O   VAL A 304      18.285 -21.384  47.602  1.00 53.03           O  
ATOM   2428  CB  VAL A 304      19.611 -24.156  48.826  1.00 47.05           C  
ATOM   2429  CG1 VAL A 304      19.534 -23.117  49.930  1.00 45.35           C  
ATOM   2430  CG2 VAL A 304      19.170 -25.509  49.337  1.00 50.12           C  
ATOM   2431  N   ILE A 305      20.227 -22.008  46.680  1.00 49.25           N  
ATOM   2432  CA  ILE A 305      20.578 -20.652  46.255  1.00 43.60           C  
ATOM   2433  C   ILE A 305      19.635 -20.182  45.155  1.00 45.58           C  
ATOM   2434  O   ILE A 305      18.954 -19.180  45.315  1.00 47.54           O  
ATOM   2435  CB  ILE A 305      22.047 -20.584  45.766  1.00 47.19           C  
ATOM   2436  CG1 ILE A 305      23.000 -20.722  46.953  1.00 46.34           C  
ATOM   2437  CG2 ILE A 305      22.335 -19.293  44.999  1.00 45.59           C  
ATOM   2438  CD1 ILE A 305      24.379 -21.033  46.551  1.00 46.21           C  
ATOM   2439  N   TYR A 306      19.548 -20.945  44.072  1.00 42.93           N  
ATOM   2440  CA  TYR A 306      18.788 -20.549  42.887  1.00 44.97           C  
ATOM   2441  C   TYR A 306      17.271 -20.799  42.880  1.00 44.91           C  
ATOM   2442  O   TYR A 306      16.595 -20.404  41.932  1.00 44.51           O  
ATOM   2443  CB  TYR A 306      19.374 -21.224  41.655  1.00 44.42           C  
ATOM   2444  CG  TYR A 306      20.688 -20.653  41.251  1.00 47.18           C  
ATOM   2445  CD1 TYR A 306      20.742 -19.578  40.384  1.00 47.08           C  
ATOM   2446  CD2 TYR A 306      21.889 -21.181  41.737  1.00 46.93           C  
ATOM   2447  CE1 TYR A 306      21.956 -19.041  39.996  1.00 54.21           C  
ATOM   2448  CE2 TYR A 306      23.111 -20.648  41.367  1.00 46.30           C  
ATOM   2449  CZ  TYR A 306      23.143 -19.573  40.491  1.00 47.82           C  
ATOM   2450  OH  TYR A 306      24.343 -19.013  40.100  1.00 44.42           O  
ATOM   2451  N   ILE A 307      16.732 -21.475  43.887  1.00 43.33           N  
ATOM   2452  CA  ILE A 307      15.299 -21.753  43.883  1.00 44.57           C  
ATOM   2453  C   ILE A 307      14.673 -21.323  45.198  1.00 45.19           C  
ATOM   2454  O   ILE A 307      13.845 -20.435  45.213  1.00 40.95           O  
ATOM   2455  CB  ILE A 307      14.942 -23.247  43.568  1.00 41.59           C  
ATOM   2456  CG1 ILE A 307      15.496 -23.701  42.208  1.00 38.67           C  
ATOM   2457  CG2 ILE A 307      13.439 -23.451  43.629  1.00 45.04           C  
ATOM   2458  CD1 ILE A 307      14.872 -23.030  41.012  1.00 39.20           C  
ATOM   2459  N   MET A 308      15.077 -21.945  46.297  1.00 45.20           N  
ATOM   2460  CA  MET A 308      14.504 -21.624  47.595  1.00 48.21           C  
ATOM   2461  C   MET A 308      14.734 -20.177  48.017  1.00 46.67           C  
ATOM   2462  O   MET A 308      13.973 -19.625  48.795  1.00 46.90           O  
ATOM   2463  CB  MET A 308      15.052 -22.572  48.658  1.00 47.33           C  
ATOM   2464  CG  MET A 308      15.193 -23.999  48.162  1.00 58.56           C  
ATOM   2465  SD  MET A 308      14.728 -25.273  49.350  1.00 78.05           S  
ATOM   2466  CE  MET A 308      15.467 -24.612  50.852  1.00 55.04           C  
ATOM   2467  N   MET A 309      15.802 -19.571  47.519  1.00 47.91           N  
ATOM   2468  CA  MET A 309      16.144 -18.209  47.895  1.00 45.04           C  
ATOM   2469  C   MET A 309      15.532 -17.201  46.926  1.00 46.75           C  
ATOM   2470  O   MET A 309      15.580 -15.999  47.153  1.00 50.45           O  
ATOM   2471  CB  MET A 309      17.662 -18.044  47.985  1.00 44.80           C  
ATOM   2472  CG  MET A 309      18.283 -18.623  49.247  1.00 45.47           C  
ATOM   2473  SD  MET A 309      19.975 -18.032  49.494  1.00 65.18           S  
ATOM   2474  CE  MET A 309      20.017 -17.671  51.260  1.00 60.15           C  
ATOM   2475  N   ASN A 310      14.971 -17.715  45.839  1.00 45.10           N  
ATOM   2476  CA  ASN A 310      14.185 -16.933  44.891  1.00 44.90           C  
ATOM   2477  C   ASN A 310      12.808 -16.712  45.520  1.00 47.61           C  
ATOM   2478  O   ASN A 310      12.130 -17.668  45.878  1.00 47.41           O  
ATOM   2479  CB  ASN A 310      14.158 -17.673  43.533  1.00 46.28           C  
ATOM   2480  CG  ASN A 310      13.127 -17.139  42.559  1.00 44.35           C  
ATOM   2481  OD1 ASN A 310      11.997 -16.914  42.921  1.00 48.89           O  
ATOM   2482  ND2 ASN A 310      13.509 -16.992  41.299  1.00 44.73           N  
ATOM   2483  N   LYS A 311      12.420 -15.446  45.663  1.00 55.23           N  
ATOM   2484  CA  LYS A 311      11.228 -15.031  46.409  1.00 55.44           C  
ATOM   2485  C   LYS A 311       9.939 -15.708  45.954  1.00 58.72           C  
ATOM   2486  O   LYS A 311       9.138 -16.168  46.772  1.00 54.31           O  
ATOM   2487  CB  LYS A 311      11.066 -13.519  46.272  1.00 57.78           C  
ATOM   2488  CG  LYS A 311       9.984 -12.866  47.127  1.00 60.11           C  
ATOM   2489  CD  LYS A 311       9.832 -11.403  46.695  1.00 72.82           C  
ATOM   2490  CE  LYS A 311       9.017 -10.580  47.674  1.00 83.63           C  
ATOM   2491  NZ  LYS A 311       9.777 -10.245  48.905  1.00 85.09           N  
ATOM   2492  N   GLN A 312       9.746 -15.751  44.641  1.00 68.49           N  
ATOM   2493  CA  GLN A 312       8.526 -16.287  44.066  1.00 68.49           C  
ATOM   2494  C   GLN A 312       8.430 -17.786  44.310  1.00 68.49           C  
ATOM   2495  O   GLN A 312       7.410 -18.283  44.789  1.00 68.49           O  
ATOM   2496  CB  GLN A 312       8.455 -15.979  42.569  1.00 68.49           C  
ATOM   2497  CG  GLN A 312       7.029 -15.919  42.033  1.00 73.05           C  
ATOM   2498  CD  GLN A 312       6.946 -15.702  40.530  1.00 78.06           C  
ATOM   2499  OE1 GLN A 312       7.965 -15.628  39.833  1.00 76.28           O  
ATOM   2500  NE2 GLN A 312       5.720 -15.606  40.021  1.00 70.01           N  
ATOM   2501  N   PHE A 313       9.504 -18.500  43.983  0.38 51.72           N  
ATOM   2502  CA  PHE A 313       9.558 -19.943  44.197  1.00 48.94           C  
ATOM   2503  C   PHE A 313       9.331 -20.307  45.662  1.00 50.63           C  
ATOM   2504  O   PHE A 313       8.468 -21.128  45.971  1.00 47.37           O  
ATOM   2505  CB  PHE A 313      10.870 -20.546  43.663  1.00 46.57           C  
ATOM   2506  CG  PHE A 313      10.810 -20.938  42.205  1.00 44.97           C  
ATOM   2507  CD1 PHE A 313      10.192 -22.119  41.815  1.00 43.93           C  
ATOM   2508  CD2 PHE A 313      11.364 -20.127  41.228  1.00 45.08           C  
ATOM   2509  CE1 PHE A 313      10.121 -22.479  40.480  1.00 42.99           C  
ATOM   2510  CE2 PHE A 313      11.305 -20.483  39.889  1.00 44.61           C  
ATOM   2511  CZ  PHE A 313      10.680 -21.663  39.515  1.00 45.43           C  
ATOM   2512  N   ARG A 314      10.085 -19.685  46.559  1.00 46.96           N  
ATOM   2513  CA  ARG A 314       9.944 -19.966  47.978  1.00 47.71           C  
ATOM   2514  C   ARG A 314       8.502 -19.855  48.496  1.00 54.15           C  
ATOM   2515  O   ARG A 314       8.069 -20.720  49.252  1.00 53.82           O  
ATOM   2516  CB  ARG A 314      10.875 -19.077  48.788  1.00 47.12           C  
ATOM   2517  CG  ARG A 314      10.809 -19.303  50.271  1.00 44.04           C  
ATOM   2518  CD  ARG A 314      11.789 -18.412  50.986  1.00 49.77           C  
ATOM   2519  NE  ARG A 314      11.552 -16.979  50.776  1.00 56.07           N  
ATOM   2520  CZ  ARG A 314      12.262 -16.187  49.966  1.00 57.34           C  
ATOM   2521  NH1 ARG A 314      13.269 -16.678  49.250  1.00 52.81           N  
ATOM   2522  NH2 ARG A 314      11.965 -14.891  49.865  1.00 60.27           N  
ATOM   2523  N   ASN A 315       7.765 -18.817  48.072  1.00 56.92           N  
ATOM   2524  CA  ASN A 315       6.368 -18.575  48.487  1.00 50.61           C  
ATOM   2525  C   ASN A 315       5.409 -19.677  48.091  1.00 52.16           C  
ATOM   2526  O   ASN A 315       4.701 -20.233  48.923  1.00 53.81           O  
ATOM   2527  CB  ASN A 315       5.847 -17.274  47.888  1.00 54.94           C  
ATOM   2528  CG  ASN A 315       6.297 -16.059  48.655  1.00 60.63           C  
ATOM   2529  OD1 ASN A 315       6.923 -16.175  49.709  1.00 62.48           O  
ATOM   2530  ND2 ASN A 315       5.975 -14.879  48.136  1.00 59.64           N  
ATOM   2531  N   CYS A 316       5.375 -19.965  46.798  1.00 50.61           N  
ATOM   2532  CA  CYS A 316       4.678 -21.137  46.282  1.00 50.85           C  
ATOM   2533  C   CYS A 316       5.074 -22.442  46.972  1.00 54.98           C  
ATOM   2534  O   CYS A 316       4.235 -23.322  47.155  1.00 54.82           O  
ATOM   2535  CB  CYS A 316       4.923 -21.259  44.788  1.00 49.45           C  
ATOM   2536  SG  CYS A 316       4.463 -19.748  43.938  1.00 50.34           S  
ATOM   2537  N   MET A 317       6.339 -22.577  47.351  1.00 57.33           N  
ATOM   2538  CA  MET A 317       6.772 -23.769  48.065  1.00 57.44           C  
ATOM   2539  C   MET A 317       6.200 -23.840  49.474  1.00 60.63           C  
ATOM   2540  O   MET A 317       5.822 -24.910  49.941  1.00 61.36           O  
ATOM   2541  CB  MET A 317       8.293 -23.846  48.114  1.00 53.61           C  
ATOM   2542  CG  MET A 317       8.903 -24.524  46.905  1.00 55.96           C  
ATOM   2543  SD  MET A 317      10.698 -24.612  46.982  1.00 73.16           S  
ATOM   2544  CE  MET A 317      11.001 -25.747  45.631  1.00 57.79           C  
ATOM   2545  N   VAL A 318       6.143 -22.699  50.150  1.00 56.77           N  
ATOM   2546  CA  VAL A 318       5.635 -22.651  51.519  1.00 59.24           C  
ATOM   2547  C   VAL A 318       4.127 -22.864  51.518  1.00 61.08           C  
ATOM   2548  O   VAL A 318       3.564 -23.443  52.447  1.00 62.17           O  
ATOM   2549  CB  VAL A 318       6.015 -21.326  52.226  1.00 54.77           C  
ATOM   2550  CG1 VAL A 318       5.392 -21.245  53.599  1.00 54.70           C  
ATOM   2551  CG2 VAL A 318       7.513 -21.225  52.351  1.00 52.43           C  
ATOM   2552  N   THR A 319       3.489 -22.397  50.451  1.00 59.67           N  
ATOM   2553  CA  THR A 319       2.068 -22.618  50.212  1.00 63.26           C  
ATOM   2554  C   THR A 319       1.799 -24.111  50.079  1.00 64.85           C  
ATOM   2555  O   THR A 319       0.977 -24.676  50.796  1.00 67.56           O  
ATOM   2556  CB  THR A 319       1.640 -21.935  48.898  1.00 60.89           C  
ATOM   2557  OG1 THR A 319       1.457 -20.530  49.111  1.00 59.04           O  
ATOM   2558  CG2 THR A 319       0.367 -22.538  48.368  1.00 62.13           C  
ATOM   2559  N   THR A 320       2.522 -24.746  49.162  1.00 60.78           N  
ATOM   2560  CA  THR A 320       2.360 -26.161  48.879  1.00 58.46           C  
ATOM   2561  C   THR A 320       2.735 -27.059  50.054  1.00 59.00           C  
ATOM   2562  O   THR A 320       2.075 -28.057  50.300  1.00 62.14           O  
ATOM   2563  CB  THR A 320       3.167 -26.552  47.640  1.00 53.81           C  
ATOM   2564  OG1 THR A 320       2.665 -25.832  46.508  1.00 55.24           O  
ATOM   2565  CG2 THR A 320       3.065 -28.027  47.369  1.00 47.77           C  
ATOM   2566  N   LEU A 321       3.772 -26.705  50.800  1.00 61.05           N  
ATOM   2567  CA  LEU A 321       4.212 -27.549  51.913  1.00 63.69           C  
ATOM   2568  C   LEU A 321       3.268 -27.424  53.089  1.00 65.22           C  
ATOM   2569  O   LEU A 321       3.066 -28.354  53.870  1.00 63.42           O  
ATOM   2570  CB  LEU A 321       5.640 -27.190  52.340  1.00 59.71           C  
ATOM   2571  CG  LEU A 321       6.750 -27.757  51.455  1.00 54.26           C  
ATOM   2572  CD1 LEU A 321       8.038 -27.758  52.220  1.00 50.87           C  
ATOM   2573  CD2 LEU A 321       6.381 -29.149  51.027  1.00 49.64           C  
ATOM   2574  N   CYS A 322       2.669 -26.246  53.171  1.00 72.14           N  
ATOM   2575  CA  CYS A 322       1.795 -25.856  54.275  1.00 75.22           C  
ATOM   2576  C   CYS A 322       0.318 -26.188  54.068  1.00 78.62           C  
ATOM   2577  O   CYS A 322      -0.561 -25.662  54.761  1.00 88.28           O  
ATOM   2578  CB  CYS A 322       2.144 -24.496  54.884  1.00 80.30           C  
ATOM   2579  SG  CYS A 322       3.602 -24.715  55.974  1.00 79.49           S  
ATOM   2580  N   CYS A 323       0.095 -27.010  53.041  1.00 76.34           N  
ATOM   2581  CA  CYS A 323      -1.194 -27.621  52.750  1.00 77.37           C  
ATOM   2582  C   CYS A 323      -2.216 -26.613  52.221  1.00 86.09           C  
ATOM   2583  O   CYS A 323      -3.403 -26.655  52.546  1.00 93.62           O  
ATOM   2584  CB  CYS A 323      -1.700 -28.325  54.012  1.00 69.75           C  
ATOM   2585  SG  CYS A 323      -0.580 -29.637  54.592  1.00 85.61           S  
ATOM   2586  N   GLY A 324      -1.704 -25.695  51.401  1.00 84.01           N  
ATOM   2587  CA  GLY A 324      -2.512 -24.874  50.522  1.00 85.36           C  
ATOM   2588  C   GLY A 324      -2.807 -23.500  51.075  1.00 92.45           C  
ATOM   2589  O   GLY A 324      -3.082 -22.564  50.323  1.00 88.21           O  
ATOM   2590  N   LYS A 325      -2.763 -23.376  52.396  1.00 94.62           N  
ATOM   2591  CA  LYS A 325      -3.007 -22.087  53.011  1.00105.09           C  
ATOM   2592  C   LYS A 325      -1.803 -21.622  53.791  1.00112.20           C  
ATOM   2593  O   LYS A 325      -1.197 -22.409  54.518  1.00114.35           O  
ATOM   2594  CB  LYS A 325      -4.264 -22.083  53.883  1.00117.77           C  
ATOM   2595  CG  LYS A 325      -5.156 -20.892  53.547  1.00123.44           C  
ATOM   2596  CD  LYS A 325      -5.750 -20.201  54.763  1.00124.92           C  
ATOM   2597  CE  LYS A 325      -7.000 -20.901  55.251  1.00116.71           C  
ATOM   2598  NZ  LYS A 325      -6.683 -21.703  56.448  1.00105.41           N  
ATOM   2599  N   ASN A 326      -1.519 -20.325  53.630  1.00118.71           N  
ATOM   2600  CA  ASN A 326      -0.290 -19.606  54.027  1.00124.36           C  
ATOM   2601  C   ASN A 326       0.633 -19.415  52.829  1.00109.92           C  
ATOM   2602  O   ASN A 326       0.629 -20.225  51.901  1.00103.67           O  
ATOM   2603  CB  ASN A 326       0.472 -20.248  55.196  1.00123.67           C  
ATOM   2604  CG  ASN A 326      -0.237 -20.074  56.525  1.00126.82           C  
ATOM   2605  OD1 ASN A 326       0.238 -19.351  57.398  1.00124.57           O  
ATOM   2606  ND2 ASN A 326      -1.377 -20.741  56.688  1.00118.89           N  
TER    2607      ASN A 326                                                      
ATOM   2608  N   ILE B 340      14.670  -0.265  37.575  1.00 72.04           N  
ATOM   2609  CA  ILE B 340      15.058  -1.628  37.232  1.00 69.98           C  
ATOM   2610  C   ILE B 340      14.276  -2.666  38.034  1.00 69.04           C  
ATOM   2611  O   ILE B 340      14.205  -3.823  37.636  1.00 69.55           O  
ATOM   2612  CB  ILE B 340      16.562  -1.884  37.477  1.00 63.95           C  
ATOM   2613  CG1 ILE B 340      17.070  -1.056  38.653  1.00 54.75           C  
ATOM   2614  CG2 ILE B 340      17.381  -1.614  36.224  1.00 64.00           C  
ATOM   2615  CD1 ILE B 340      18.490  -1.393  39.016  1.00 61.87           C  
ATOM   2616  N   LEU B 341      13.704  -2.243  39.160  1.00 63.81           N  
ATOM   2617  CA  LEU B 341      13.137  -3.151  40.152  1.00 63.46           C  
ATOM   2618  C   LEU B 341      12.131  -4.118  39.533  1.00 67.77           C  
ATOM   2619  O   LEU B 341      11.946  -5.242  40.000  1.00 61.78           O  
ATOM   2620  CB  LEU B 341      12.472  -2.354  41.267  1.00 58.78           C  
ATOM   2621  CG  LEU B 341      13.295  -1.184  41.788  1.00 61.30           C  
ATOM   2622  CD1 LEU B 341      12.490  -0.343  42.737  1.00 57.38           C  
ATOM   2623  CD2 LEU B 341      14.560  -1.650  42.465  1.00 60.14           C  
ATOM   2624  N   GLU B 342      11.485  -3.661  38.471  1.00 72.63           N  
ATOM   2625  CA  GLU B 342      10.497  -4.447  37.755  1.00 67.41           C  
ATOM   2626  C   GLU B 342      11.185  -5.651  37.093  1.00 63.32           C  
ATOM   2627  O   GLU B 342      10.743  -6.785  37.237  1.00 62.22           O  
ATOM   2628  CB  GLU B 342       9.769  -3.545  36.740  1.00 75.05           C  
ATOM   2629  CG  GLU B 342      10.577  -2.250  36.324  1.00 85.72           C  
ATOM   2630  CD  GLU B 342      10.225  -0.934  37.105  1.00 82.44           C  
ATOM   2631  OE1 GLU B 342       9.248  -0.906  37.893  1.00 80.31           O  
ATOM   2632  OE2 GLU B 342      10.941   0.081  36.909  1.00 69.33           O  
ATOM   2633  N   ASN B 343      12.298  -5.402  36.410  1.00 63.20           N  
ATOM   2634  CA  ASN B 343      13.095  -6.466  35.780  1.00 61.58           C  
ATOM   2635  C   ASN B 343      13.875  -7.328  36.778  1.00 60.74           C  
ATOM   2636  O   ASN B 343      14.114  -8.508  36.541  1.00 56.95           O  
ATOM   2637  CB  ASN B 343      14.069  -5.881  34.759  1.00 60.91           C  
ATOM   2638  CG  ASN B 343      13.423  -5.609  33.423  1.00 64.38           C  
ATOM   2639  OD1 ASN B 343      12.397  -6.195  33.078  1.00 63.52           O  
ATOM   2640  ND2 ASN B 343      14.036  -4.726  32.650  1.00 63.55           N  
ATOM   2641  N   LEU B 344      14.284  -6.719  37.884  1.00 60.19           N  
ATOM   2642  CA  LEU B 344      14.899  -7.442  38.986  1.00 56.80           C  
ATOM   2643  C   LEU B 344      13.925  -8.442  39.584  1.00 57.74           C  
ATOM   2644  O   LEU B 344      14.314  -9.557  39.901  1.00 57.20           O  
ATOM   2645  CB  LEU B 344      15.385  -6.473  40.064  1.00 58.59           C  
ATOM   2646  CG  LEU B 344      16.620  -5.665  39.660  1.00 62.23           C  
ATOM   2647  CD1 LEU B 344      17.116  -4.771  40.804  1.00 61.36           C  
ATOM   2648  CD2 LEU B 344      17.721  -6.614  39.163  1.00 55.52           C  
ATOM   2649  N   LYS B 345      12.662  -8.038  39.735  1.00 63.78           N  
ATOM   2650  CA  LYS B 345      11.603  -8.917  40.243  1.00 60.30           C  
ATOM   2651  C   LYS B 345      11.355 -10.096  39.316  1.00 56.70           C  
ATOM   2652  O   LYS B 345      11.237 -11.224  39.777  1.00 53.52           O  
ATOM   2653  CB  LYS B 345      10.300  -8.139  40.481  1.00 58.79           C  
ATOM   2654  CG  LYS B 345      10.331  -7.223  41.709  1.00 66.45           C  
ATOM   2655  CD  LYS B 345       9.145  -6.263  41.726  1.00 81.48           C  
ATOM   2656  CE  LYS B 345       9.478  -4.933  42.421  1.00 82.14           C  
ATOM   2657  NZ  LYS B 345       8.601  -3.809  41.937  1.00 79.70           N  
ATOM   2658  N   ASP B 346      11.290  -9.828  38.013  1.00 56.32           N  
ATOM   2659  CA  ASP B 346      11.117 -10.870  36.990  1.00 58.25           C  
ATOM   2660  C   ASP B 346      12.187 -11.970  37.039  1.00 57.35           C  
ATOM   2661  O   ASP B 346      11.928 -13.117  36.691  1.00 57.66           O  
ATOM   2662  CB  ASP B 346      11.144 -10.259  35.585  1.00 57.85           C  
ATOM   2663  CG  ASP B 346       9.945  -9.379  35.287  1.00 61.78           C  
ATOM   2664  OD1 ASP B 346       8.861  -9.567  35.885  1.00 59.85           O  
ATOM   2665  OD2 ASP B 346      10.093  -8.506  34.414  1.00 64.92           O  
ATOM   2666  N   CYS B 347      13.391 -11.589  37.457  1.00 55.51           N  
ATOM   2667  CA  CYS B 347      14.556 -12.460  37.460  1.00 51.07           C  
ATOM   2668  C   CYS B 347      14.747 -13.156  38.811  1.00 53.33           C  
ATOM   2669  O   CYS B 347      15.658 -13.962  38.998  1.00 53.18           O  
ATOM   2670  CB  CYS B 347      15.796 -11.653  37.079  1.00 52.93           C  
ATOM   2671  SG  CYS B 347      15.878 -11.205  35.328  1.00 53.76           S  
ATOM   2672  N   GLY B 348      13.873 -12.850  39.754  1.00 52.30           N  
ATOM   2673  CA  GLY B 348      13.900 -13.520  41.033  1.00 52.51           C  
ATOM   2674  C   GLY B 348      15.023 -13.018  41.888  1.00 50.20           C  
ATOM   2675  O   GLY B 348      15.292 -13.589  42.937  1.00 50.49           O  
ATOM   2676  N   LEU B 349      15.662 -11.939  41.434  1.00 56.19           N  
ATOM   2677  CA  LEU B 349      16.779 -11.314  42.146  1.00 58.82           C  
ATOM   2678  C   LEU B 349      16.391 -10.359  43.273  1.00 57.03           C  
ATOM   2679  O   LEU B 349      17.191 -10.119  44.173  1.00 56.94           O  
ATOM   2680  CB  LEU B 349      17.708 -10.608  41.162  1.00 55.37           C  
ATOM   2681  CG  LEU B 349      18.545 -11.560  40.309  1.00 58.08           C  
ATOM   2682  CD1 LEU B 349      18.641 -11.032  38.901  1.00 57.90           C  
ATOM   2683  CD2 LEU B 349      19.930 -11.730  40.900  1.00 56.30           C  
ATOM   2684  N   PHE B 350      15.172  -9.831  43.233  1.00 55.19           N  
ATOM   2685  CA  PHE B 350      14.698  -8.923  44.279  1.00 61.64           C  
ATOM   2686  C   PHE B 350      13.184  -8.971  44.407  1.00 67.32           C  
ATOM   2687  O   PHE B 350      12.602  -9.188  45.482  1.00 71.41           O  
ATOM   2688  CB  PHE B 350      15.126  -7.487  43.975  1.00 61.82           C  
ATOM   2689  CG  PHE B 350      14.637  -6.476  44.981  1.00 61.26           C  
ATOM   2690  CD1 PHE B 350      15.189  -6.413  46.251  1.00 60.72           C  
ATOM   2691  CD2 PHE B 350      13.641  -5.574  44.649  1.00 59.58           C  
ATOM   2692  CE1 PHE B 350      14.750  -5.478  47.173  1.00 54.95           C  
ATOM   2693  CE2 PHE B 350      13.202  -4.642  45.570  1.00 59.07           C  
ATOM   2694  CZ  PHE B 350      13.762  -4.596  46.833  1.00 57.08           C  
ATOM   2695  OXT PHE B 350      12.509  -8.779  43.398  1.00 68.15           O  
TER    2696      PHE B 350                                                      
HETATM 2697  C1  NAG C   1      47.338 -57.881  40.509  1.00 39.76           C  
HETATM 2698  C2  NAG C   1      46.632 -58.037  39.170  1.00 40.29           C  
HETATM 2699  C3  NAG C   1      46.070 -59.451  39.008  1.00 38.20           C  
HETATM 2700  C4  NAG C   1      47.124 -60.508  39.332  1.00 38.52           C  
HETATM 2701  C5  NAG C   1      47.928 -60.178  40.591  1.00 41.06           C  
HETATM 2702  C6  NAG C   1      49.189 -60.997  40.678  1.00 40.24           C  
HETATM 2703  C7  NAG C   1      45.244 -56.474  37.864  1.00 39.12           C  
HETATM 2704  C8  NAG C   1      44.185 -55.423  37.904  1.00 38.52           C  
HETATM 2705  N2  NAG C   1      45.570 -57.025  39.039  1.00 38.59           N  
HETATM 2706  O3  NAG C   1      45.683 -59.664  37.659  1.00 35.90           O  
HETATM 2707  O4  NAG C   1      46.450 -61.740  39.581  1.00 40.66           O  
HETATM 2708  O5  NAG C   1      48.363 -58.813  40.584  1.00 41.53           O  
HETATM 2709  O6  NAG C   1      50.079 -60.616  39.636  1.00 51.15           O  
HETATM 2710  O7  NAG C   1      45.765 -56.818  36.810  1.00 41.29           O  
HETATM 2711  C1  NAG C   2      46.858 -62.910  38.816  1.00 32.15           C  
HETATM 2712  C2  NAG C   2      46.452 -64.089  39.656  1.00 26.80           C  
HETATM 2713  C3  NAG C   2      46.823 -65.375  38.955  1.00 29.62           C  
HETATM 2714  C4  NAG C   2      46.217 -65.401  37.557  1.00 33.34           C  
HETATM 2715  C5  NAG C   2      46.594 -64.162  36.782  1.00 25.54           C  
HETATM 2716  C6  NAG C   2      45.820 -64.060  35.492  1.00 32.04           C  
HETATM 2717  C7  NAG C   2      46.450 -63.604  42.069  1.00 38.95           C  
HETATM 2718  C8  NAG C   2      47.251 -63.598  43.330  1.00 28.17           C  
HETATM 2719  N2  NAG C   2      47.087 -64.023  40.969  1.00 29.87           N  
HETATM 2720  O3  NAG C   2      46.378 -66.477  39.734  1.00 35.50           O  
HETATM 2721  O4  NAG C   2      46.749 -66.469  36.786  1.00 39.54           O  
HETATM 2722  O5  NAG C   2      46.263 -63.005  37.545  1.00 27.51           O  
HETATM 2723  O6  NAG C   2      46.381 -63.179  34.532  1.00 35.58           O  
HETATM 2724  O7  NAG C   2      45.265 -63.257  42.052  1.00 51.76           O  
HETATM 2725  C1  BMA C   3      45.919 -67.622  36.838  1.00 49.28           C  
HETATM 2726  C2  BMA C   3      46.358 -68.411  35.647  1.00 55.90           C  
HETATM 2727  C3  BMA C   3      45.466 -69.627  35.445  1.00 60.87           C  
HETATM 2728  C4  BMA C   3      44.999 -70.299  36.749  1.00 59.96           C  
HETATM 2729  C5  BMA C   3      45.397 -69.601  38.067  1.00 57.99           C  
HETATM 2730  C6  BMA C   3      46.181 -70.548  38.972  1.00 57.82           C  
HETATM 2731  O2  BMA C   3      47.701 -68.845  35.886  1.00 60.08           O  
HETATM 2732  O3  BMA C   3      46.125 -70.564  34.564  1.00 60.76           O  
HETATM 2733  O4  BMA C   3      43.559 -70.358  36.709  1.00 58.57           O  
HETATM 2734  O5  BMA C   3      46.171 -68.396  37.979  1.00 54.89           O  
HETATM 2735  O6  BMA C   3      45.669 -70.479  40.308  1.00 59.47           O  
HETATM 2736  C1  MAN C   4      45.938 -70.189  33.174  1.00 61.12           C  
HETATM 2737  C2  MAN C   4      46.179 -71.388  32.314  1.00 61.91           C  
HETATM 2738  C3  MAN C   4      47.610 -71.835  32.528  1.00 67.14           C  
HETATM 2739  C4  MAN C   4      48.644 -70.676  32.211  1.00 64.03           C  
HETATM 2740  C5  MAN C   4      48.202 -69.295  32.755  1.00 62.57           C  
HETATM 2741  C6  MAN C   4      48.869 -68.123  32.007  1.00 61.31           C  
HETATM 2742  O2  MAN C   4      46.084 -71.026  30.938  1.00 56.49           O  
HETATM 2743  O3  MAN C   4      47.891 -72.991  31.740  1.00 64.38           O  
HETATM 2744  O4  MAN C   4      49.936 -70.974  32.764  1.00 63.83           O  
HETATM 2745  O5  MAN C   4      46.744 -69.123  32.711  1.00 70.07           O  
HETATM 2746  O6  MAN C   4      48.014 -66.960  32.005  1.00 60.47           O  
HETATM 2747  S   SO4 A1327       2.748 -21.894  27.333  1.00137.89           S  
HETATM 2748  O1  SO4 A1327       4.120 -21.955  26.640  1.00124.81           O  
HETATM 2749  O2  SO4 A1327       1.427 -22.069  26.555  1.00135.47           O  
HETATM 2750  O3  SO4 A1327       2.874 -23.192  28.153  1.00127.33           O  
HETATM 2751  O4  SO4 A1327       2.567 -20.480  27.930  1.00125.08           O  
HETATM 2752  C   ACT A1328      44.639 -28.354  31.766  1.00 70.22           C  
HETATM 2753  O   ACT A1328      43.793 -29.127  31.261  1.00 67.05           O  
HETATM 2754  OXT ACT A1328      44.656 -28.307  33.019  1.00 70.08           O  
HETATM 2755  CH3 ACT A1328      45.577 -27.538  30.922  1.00 61.14           C  
HETATM 2756  C1  PLM A1329       0.223 -29.303  56.025  1.00 81.90           C  
HETATM 2757  O2  PLM A1329      -0.060 -28.254  56.653  1.00 76.87           O  
HETATM 2758  C2  PLM A1329       1.310 -30.244  56.650  1.00 66.21           C  
HETATM 2759  C3  PLM A1329       2.121 -29.354  57.606  1.00 67.37           C  
HETATM 2760  C4  PLM A1329       3.274 -29.896  58.496  1.00 53.82           C  
HETATM 2761  C5  PLM A1329       4.478 -30.547  57.828  1.00 49.27           C  
HETATM 2762  C6  PLM A1329       5.523 -30.830  58.939  1.00 48.80           C  
HETATM 2763  C7  PLM A1329       6.762 -31.501  58.318  1.00 61.30           C  
HETATM 2764  C8  PLM A1329       7.918 -31.738  59.311  1.00 52.54           C  
HETATM 2765  C9  PLM A1329       9.068 -32.463  58.573  1.00 51.07           C  
HETATM 2766  CA  PLM A1329      10.284 -32.635  59.496  1.00 53.23           C  
HETATM 2767  CB  PLM A1329      11.430 -33.416  58.836  1.00 46.80           C  
HETATM 2768  CC  PLM A1329      10.871 -34.801  58.517  1.00 50.30           C  
HETATM 2769  CD  PLM A1329      11.874 -35.737  57.841  1.00 45.32           C  
HETATM 2770  CE  PLM A1329      13.103 -36.022  58.686  1.00 42.91           C  
HETATM 2771  CF  PLM A1329      13.957 -36.959  57.839  1.00 42.91           C  
HETATM 2772  CG  PLM A1329      15.246 -37.322  58.563  1.00 43.09           C  
HETATM 2773  C1  BOG A1334      27.388 -57.831  48.914  1.00 73.85           C  
HETATM 2774  O1  BOG A1334      26.194 -57.106  48.492  1.00 63.27           O  
HETATM 2775  C2  BOG A1334      27.142 -59.323  48.712  1.00 74.63           C  
HETATM 2776  O2  BOG A1334      26.024 -59.746  49.494  1.00 77.85           O  
HETATM 2777  C3  BOG A1334      28.346 -60.125  49.175  1.00 76.23           C  
HETATM 2778  O3  BOG A1334      28.109 -61.501  48.920  1.00 92.71           O  
HETATM 2779  C4  BOG A1334      29.563 -59.725  48.404  1.00 78.78           C  
HETATM 2780  O4  BOG A1334      30.687 -60.535  48.818  1.00 69.78           O  
HETATM 2781  C5  BOG A1334      29.787 -58.210  48.656  1.00 76.35           C  
HETATM 2782  O5  BOG A1334      28.616 -57.442  48.210  1.00 67.20           O  
HETATM 2783  C6  BOG A1334      31.119 -57.701  48.093  1.00 64.30           C  
HETATM 2784  O6  BOG A1334      31.299 -56.360  48.546  1.00 61.45           O  
HETATM 2785  C1' BOG A1334      26.073 -55.677  48.578  1.00 61.45           C  
HETATM 2786  C2' BOG A1334      24.573 -55.431  48.336  1.00 61.45           C  
HETATM 2787  C3' BOG A1334      24.057 -53.973  48.309  1.00 61.45           C  
HETATM 2788  C4' BOG A1334      22.566 -54.161  48.001  1.00 61.45           C  
HETATM 2789  C5' BOG A1334      21.686 -52.916  47.780  1.00 61.45           C  
HETATM 2790  C6' BOG A1334      21.523 -51.903  48.901  1.00 61.45           C  
HETATM 2791  C7' BOG A1334      20.562 -50.836  48.342  1.00 61.45           C  
HETATM 2792  C8' BOG A1334      20.283 -49.728  49.363  1.00 61.45           C  
HETATM 2793  O   HOH A2001      43.670 -48.552  30.342  1.00 45.29           O  
HETATM 2794  O   HOH A2002      39.358 -47.011  37.391  1.00 41.41           O  
HETATM 2795  O   HOH A2003      40.667 -43.868  38.539  1.00 47.31           O  
HETATM 2796  O   HOH A2004      50.519 -53.251  46.738  1.00 49.51           O  
HETATM 2797  O   HOH A2005      31.378 -51.683  50.973  1.00 32.66           O  
HETATM 2798  O   HOH A2006      -0.937 -23.186  43.747  1.00 50.72           O  
HETATM 2799  O   HOH A2007       9.502 -14.065  35.972  1.00 56.63           O  
HETATM 2800  O   HOH A2008      12.522 -15.967  38.591  1.00 50.61           O  
HETATM 2801  O   HOH A2009      24.057 -28.650  39.991  1.00 44.47           O  
HETATM 2802  O   HOH A2010      27.841 -44.926  40.304  1.00 44.44           O  
HETATM 2803  O   HOH A2011      24.079 -18.487  37.518  1.00 41.97           O  
HETATM 2804  O   HOH A2012      15.955 -20.057  29.001  1.00 53.72           O  
HETATM 2805  O   HOH A2013      36.348 -42.611  24.697  1.00 56.17           O  
HETATM 2806  O   HOH A2014      37.470 -41.384  36.048  1.00 46.25           O  
HETATM 2807  O   HOH A2015      33.998 -43.712  43.359  1.00 47.67           O  
HETATM 2808  O   HOH A2016      36.411 -38.931  36.356  1.00 54.55           O  
HETATM 2809  O   HOH A2017      16.213   9.764  40.731  1.00 44.98           O  
HETATM 2810  O   HOH A2018      26.642 -20.709  41.353  1.00 43.23           O  
HETATM 2811  O   HOH A2019      26.908 -23.047  42.081  1.00 43.53           O  
HETATM 2812  O   HOH A2020      35.027 -29.798  41.937  1.00 56.36           O  
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1                                                                
CONECT   17 2259                                                                
CONECT  118 2697                                                                
CONECT  888 1489                                                                
CONECT 1489  888                                                                
CONECT 2259   17                                                                
CONECT 2585 2756                                                                
CONECT 2697  118 2698 2708                                                      
CONECT 2698 2697 2699 2705                                                      
CONECT 2699 2698 2700 2706                                                      
CONECT 2700 2699 2701 2707                                                      
CONECT 2701 2700 2702 2708                                                      
CONECT 2702 2701 2709                                                           
CONECT 2703 2704 2705 2710                                                      
CONECT 2704 2703                                                                
CONECT 2705 2698 2703                                                           
CONECT 2706 2699                                                                
CONECT 2707 2700 2711                                                           
CONECT 2708 2697 2701                                                           
CONECT 2709 2702                                                                
CONECT 2710 2703                                                                
CONECT 2711 2707 2712 2722                                                      
CONECT 2712 2711 2713 2719                                                      
CONECT 2713 2712 2714 2720                                                      
CONECT 2714 2713 2715 2721                                                      
CONECT 2715 2714 2716 2722                                                      
CONECT 2716 2715 2723                                                           
CONECT 2717 2718 2719 2724                                                      
CONECT 2718 2717                                                                
CONECT 2719 2712 2717                                                           
CONECT 2720 2713                                                                
CONECT 2721 2714 2725                                                           
CONECT 2722 2711 2715                                                           
CONECT 2723 2716                                                                
CONECT 2724 2717                                                                
CONECT 2725 2721 2726 2734                                                      
CONECT 2726 2725 2727 2731                                                      
CONECT 2727 2726 2728 2732                                                      
CONECT 2728 2727 2729 2733                                                      
CONECT 2729 2728 2730 2734                                                      
CONECT 2730 2729 2735                                                           
CONECT 2731 2726                                                                
CONECT 2732 2727 2736                                                           
CONECT 2733 2728                                                                
CONECT 2734 2725 2729                                                           
CONECT 2735 2730                                                                
CONECT 2736 2732 2737 2745                                                      
CONECT 2737 2736 2738 2742                                                      
CONECT 2738 2737 2739 2743                                                      
CONECT 2739 2738 2740 2744                                                      
CONECT 2740 2739 2741 2745                                                      
CONECT 2741 2740 2746                                                           
CONECT 2742 2737                                                                
CONECT 2743 2738                                                                
CONECT 2744 2739                                                                
CONECT 2745 2736 2740                                                           
CONECT 2746 2741                                                                
CONECT 2747 2748 2749 2750 2751                                                 
CONECT 2748 2747                                                                
CONECT 2749 2747                                                                
CONECT 2750 2747                                                                
CONECT 2751 2747                                                                
CONECT 2752 2753 2754 2755                                                      
CONECT 2753 2752                                                                
CONECT 2754 2752                                                                
CONECT 2755 2752                                                                
CONECT 2756 2585 2757 2758                                                      
CONECT 2757 2756                                                                
CONECT 2758 2756 2759                                                           
CONECT 2759 2758 2760                                                           
CONECT 2760 2759 2761                                                           
CONECT 2761 2760 2762                                                           
CONECT 2762 2761 2763                                                           
CONECT 2763 2762 2764                                                           
CONECT 2764 2763 2765                                                           
CONECT 2765 2764 2766                                                           
CONECT 2766 2765 2767                                                           
CONECT 2767 2766 2768                                                           
CONECT 2768 2767 2769                                                           
CONECT 2769 2768 2770                                                           
CONECT 2770 2769 2771                                                           
CONECT 2771 2770 2772                                                           
CONECT 2772 2771                                                                
CONECT 2773 2774 2775 2782                                                      
CONECT 2774 2773 2785                                                           
CONECT 2775 2773 2776 2777                                                      
CONECT 2776 2775                                                                
CONECT 2777 2775 2778 2779                                                      
CONECT 2778 2777                                                                
CONECT 2779 2777 2780 2781                                                      
CONECT 2780 2779                                                                
CONECT 2781 2779 2782 2783                                                      
CONECT 2782 2773 2781                                                           
CONECT 2783 2781 2784                                                           
CONECT 2784 2783                                                                
CONECT 2785 2774 2786                                                           
CONECT 2786 2785 2787                                                           
CONECT 2787 2786 2788                                                           
CONECT 2788 2787 2789                                                           
CONECT 2789 2788 2790                                                           
CONECT 2790 2789 2791                                                           
CONECT 2791 2790 2792                                                           
CONECT 2792 2791                                                                
MASTER      375    0    9   14    4    0    0    6 2799    2  106   28          
END