HEADER    TRANSCRIPTION                           11-APR-12   4EM9              
TITLE     HUMAN PPAR GAMMA IN COMPLEX WITH NONANOIC ACIDS                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 235-505;               
COMPND   5 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPARG, NR1C3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEAR RECEPTOR, RETINOIC ACID RECEPTOR, NUCLEUS, TRANSCRIPTION      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.V.LIBERATO,A.S.NASCIMENTO,I.POLIKARPOV                              
REVDAT   2   13-SEP-23 4EM9    1       REMARK SEQADV                            
REVDAT   1   06-MAR-13 4EM9    0                                                
JRNL        AUTH   M.V.LIBERATO,A.S.NASCIMENTO,S.D.AYERS,J.Z.LIN,A.CVORO,       
JRNL        AUTH 2 R.L.SILVEIRA,L.MARTINEZ,P.C.SOUZA,D.SAIDEMBERG,T.DENG,       
JRNL        AUTH 3 A.A.AMATO,M.TOGASHI,W.A.HSUEH,K.PHILLIPS,M.S.PALMA,          
JRNL        AUTH 4 F.A.NEVES,M.S.SKAF,P.WEBB,I.POLIKARPOV                       
JRNL        TITL   MEDIUM CHAIN FATTY ACIDS ARE SELECTIVE PEROXISOME            
JRNL        TITL 2 PROLIFERATOR ACTIVATED RECEPTOR (PPAR) GAMMA ACTIVATORS AND  
JRNL        TITL 3 PAN-PPAR PARTIAL AGONISTS                                    
JRNL        REF    PLOS ONE                      V.   7 36297 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22649490                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0036297                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36859                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1860                            
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 32.8000 -  4.9297    0.96     2808   164  0.2080 0.2464        
REMARK   3     2  4.9297 -  3.9149    0.99     2818   173  0.1678 0.1854        
REMARK   3     3  3.9149 -  3.4207    1.00     2850   154  0.1744 0.1877        
REMARK   3     4  3.4207 -  3.1082    1.00     2824   139  0.2006 0.2200        
REMARK   3     5  3.1082 -  2.8855    1.00     2872   155  0.2168 0.2265        
REMARK   3     6  2.8855 -  2.7155    0.99     2796   156  0.2146 0.2770        
REMARK   3     7  2.7155 -  2.5796    0.99     2784   137  0.2097 0.2393        
REMARK   3     8  2.5796 -  2.4673    0.98     2784   156  0.2112 0.2820        
REMARK   3     9  2.4673 -  2.3724    0.97     2779   127  0.2124 0.2720        
REMARK   3    10  2.3724 -  2.2905    0.97     2761   130  0.2322 0.2624        
REMARK   3    11  2.2905 -  2.2189    0.96     2662   157  0.2385 0.2991        
REMARK   3    12  2.2189 -  2.1555    0.89     2529   118  0.2649 0.3114        
REMARK   3    13  2.1555 -  2.1000    0.61     1732    94  0.2994 0.3522        
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              : 0.36                                          
REMARK   3   B_SOL              : 81.82                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.35830                                             
REMARK   3    B22 (A**2) : 2.22940                                              
REMARK   3    B33 (A**2) : -1.87110                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.41070                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.005           4135                                  
REMARK   3   ANGLE     :  0.764           5569                                  
REMARK   3   CHIRALITY :  0.044            644                                  
REMARK   3   PLANARITY :  0.003            704                                  
REMARK   3   DIHEDRAL  : 15.199           1555                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND ( RESID 207:477 OR RESID 501:503 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3685  -0.5311  16.9623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2739 T22:   0.3107                                     
REMARK   3      T33:   0.2108 T12:   0.1475                                     
REMARK   3      T13:  -0.0211 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9049 L22:   1.6142                                     
REMARK   3      L33:   2.1620 L12:   0.4198                                     
REMARK   3      L13:  -0.2332 L23:  -0.0079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1813 S12:  -0.1631 S13:  -0.0690                       
REMARK   3      S21:   0.0815 S22:   0.2108 S23:  -0.1730                       
REMARK   3      S31:  -0.1340 S32:   0.2534 S33:  -0.0368                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN B AND ( RESID 207:474 OR RESID 501:502 ) )     
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0097 -23.4979  33.7397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3202 T22:   0.2397                                     
REMARK   3      T33:   0.2577 T12:   0.1127                                     
REMARK   3      T13:   0.0269 T23:   0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3921 L22:   1.0948                                     
REMARK   3      L33:   2.6420 L12:   0.2000                                     
REMARK   3      L13:  -0.3545 L23:  -0.0319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0281 S12:  -0.1960 S13:  -0.0085                       
REMARK   3      S21:   0.1231 S22:   0.0171 S23:   0.0823                       
REMARK   3      S31:  -0.1172 S32:   0.1700 S33:  -0.0505                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 601:771 ) OR ( CHAIN B AND RESID   
REMARK   3               601:740 )                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2558 -12.7485  23.1014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3116 T22:   0.3040                                     
REMARK   3      T33:   0.2939 T12:   0.0458                                     
REMARK   3      T13:   0.0206 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3292 L22:   0.3516                                     
REMARK   3      L33:   0.7289 L12:  -0.2189                                     
REMARK   3      L13:   0.4390 L23:  -0.3063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   0.0012 S13:  -0.0024                       
REMARK   3      S21:   0.0028 S22:   0.0301 S23:   0.0254                       
REMARK   3      S31:  -0.0480 S32:   0.0185 S33:   0.0086                       
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 4EM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071795.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LNLS                               
REMARK 200  BEAMLINE                       : W01B-MX2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.46                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZEO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.9M SODIUM CITRATE, PH   
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.36550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.12750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.36550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.12750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       92.73100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       46.36550            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -31.12750            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       46.36550            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000      -31.12750            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     MET A   206                                                      
REMARK 465     ILE A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     PHE A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     ILE A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     PRO A   269                                                      
REMARK 465     LEU A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     GLN A   273                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     SER B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     MET B   206                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     THR B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     LYS B   244                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     ILE B   262                                                      
REMARK 465     LYS B   263                                                      
REMARK 465     THR B   268                                                      
REMARK 465     PRO B   269                                                      
REMARK 465     LEU B   270                                                      
REMARK 465     GLN B   271                                                      
REMARK 465     GLU B   272                                                      
REMARK 465     GLN B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     LYS B   275                                                      
REMARK 465     ILE B   456                                                      
REMARK 465     LYS B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     THR B   459                                                      
REMARK 465     GLU B   460                                                      
REMARK 465     THR B   461                                                      
REMARK 465     ASP B   462                                                      
REMARK 465     MET B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     ASP B   475                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     TYR B   477                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     MET A 257    CG   SD   CE                                        
REMARK 470     ARG A 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     GLU A 471    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 474    CG   CD   CE   NZ                                   
REMARK 470     GLN B 283    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 343    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 357    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 358    CG   CD   CE   NZ                                   
REMARK 470     LYS B 373    CG   CD   CE   NZ                                   
REMARK 470     GLN B 451    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 474    CG   CD   CE   NZ                                   
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   CB   CYS B   285     O9   TCE B   502              2.12            
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   NZ   LYS B   265     O    HOH A   771     3545     2.05            
REMARK 500   CD   LYS B   265     O    HOH A   758     3545     2.06            
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    THR B 238      -90.87   -110.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCE B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VV1   RELATED DB: PDB                                   
REMARK 900 HPPARGAMMA LIGAND BINDING DOMAIN IN COMPLEX WITH 4-HDHA              
REMARK 900 RELATED ID: 1PRG   RELATED DB: PDB                                   
REMARK 900 LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR           
REMARK 900 ACTIVATED RECEPTOR GAMMA                                             
REMARK 900 RELATED ID: 3GWX   RELATED DB: PDB                                   
REMARK 900 MOLECULAR RECOGNITION OF FATTY ACIDS BY PEROXISOME PROLIFERATOR-     
REMARK 900 ACTIVATED RECEPTORS                                                  
REMARK 900 RELATED ID: 1ZEO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PPAR-GAMMA LIGAND BINDING DOMAIN          
REMARK 900 COMPLEXED WITH AN ALPHA-ARYLOXYPHENYLACETIC ACID AGONIST             
REMARK 900 RELATED ID: 3DZU   RELATED DB: PDB                                   
REMARK 900 INTACT PPAR GAMMA - RXR ALPHA NUCLEAR RECEPTOR COMPLEX ON DNA BOUND  
REMARK 900 WITH BVT.13, 9-CIS RETINOIC ACID AND NCOA2 PEPTIDE                   
REMARK 900 RELATED ID: 3DZY   RELATED DB: PDB                                   
REMARK 900 INTACT PPAR GAMMA - RXR ALPHA NUCLEAR RECEPTOR COMPLEX ON DNA BOUND  
REMARK 900 WITH ROSIGLITAZONE, 9-CIS RETINOIC ACID AND NCOA2 PEPTIDE            
REMARK 900 RELATED ID: 4EMA   RELATED DB: PDB                                   
DBREF  4EM9 A  207   477  UNP    P37231   PPARG_HUMAN    235    505             
DBREF  4EM9 B  207   477  UNP    P37231   PPARG_HUMAN    235    505             
SEQADV 4EM9 GLY A  203  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 SER A  204  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 HIS A  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 MET A  206  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 GLY B  203  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 SER B  204  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 HIS B  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 MET B  206  UNP  P37231              EXPRESSION TAG                 
SEQRES   1 A  275  GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA          
SEQRES   2 A  275  LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU          
SEQRES   3 A  275  THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR          
SEQRES   4 A  275  THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER          
SEQRES   5 A  275  LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE          
SEQRES   6 A  275  THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG          
SEQRES   7 A  275  ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL          
SEQRES   8 A  275  GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE          
SEQRES   9 A  275  VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS          
SEQRES  10 A  275  TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER          
SEQRES  11 A  275  LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN          
SEQRES  12 A  275  GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS          
SEQRES  13 A  275  PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA          
SEQRES  14 A  275  VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU          
SEQRES  15 A  275  ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG          
SEQRES  16 A  275  PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN          
SEQRES  17 A  275  ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU          
SEQRES  18 A  275  ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU          
SEQRES  19 A  275  GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS          
SEQRES  20 A  275  VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP          
SEQRES  21 A  275  MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP          
SEQRES  22 A  275  LEU TYR                                                      
SEQRES   1 B  275  GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA          
SEQRES   2 B  275  LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU          
SEQRES   3 B  275  THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR          
SEQRES   4 B  275  THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER          
SEQRES   5 B  275  LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE          
SEQRES   6 B  275  THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG          
SEQRES   7 B  275  ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL          
SEQRES   8 B  275  GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE          
SEQRES   9 B  275  VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS          
SEQRES  10 B  275  TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER          
SEQRES  11 B  275  LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN          
SEQRES  12 B  275  GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS          
SEQRES  13 B  275  PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA          
SEQRES  14 B  275  VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU          
SEQRES  15 B  275  ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG          
SEQRES  16 B  275  PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN          
SEQRES  17 B  275  ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU          
SEQRES  18 B  275  ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU          
SEQRES  19 B  275  GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS          
SEQRES  20 B  275  VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP          
SEQRES  21 B  275  MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP          
SEQRES  22 B  275  LEU TYR                                                      
HET    KNA  A 501      11                                                       
HET    KNA  A 502      11                                                       
HET    KNA  A 503      11                                                       
HET    GOL  A 504       6                                                       
HET    KNA  B 501      11                                                       
HET    TCE  B 502      16                                                       
HET    GOL  B 503       6                                                       
HET    GOL  B 504       6                                                       
HETNAM     KNA NONANOIC ACID                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     TCE 3,3',3''-PHOSPHANETRIYLTRIPROPANOIC ACID                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TCE 3-[BIS(2-CARBOXYETHYL)PHOSPHANYL]PROPANOIC ACID                  
FORMUL   3  KNA    4(C9 H18 O2)                                                 
FORMUL   6  GOL    3(C3 H8 O3)                                                  
FORMUL   8  TCE    C9 H15 O6 P                                                  
FORMUL  11  HOH   *311(H2 O)                                                    
HELIX    1   1 GLU A  207  PHE A  226  1                                  20    
HELIX    2   2 THR A  229  THR A  238  1                                  10    
HELIX    3   3 ASP A  251  GLU A  259  1                                   9    
HELIX    4   4 GLU A  276  ILE A  303  1                                  28    
HELIX    5   5 GLY A  305  LEU A  309  5                                   5    
HELIX    6   6 ASP A  310  ALA A  331  1                                  22    
HELIX    7   7 SER A  342  GLY A  344  5                                   3    
HELIX    8   8 ARG A  350  SER A  355  1                                   6    
HELIX    9   9 PRO A  359  PHE A  363  5                                   5    
HELIX   10  10 MET A  364  ALA A  376  1                                  13    
HELIX   11  11 ASP A  380  LEU A  393  1                                  14    
HELIX   12  12 ASN A  402  HIS A  425  1                                  24    
HELIX   13  13 GLN A  430  GLU A  460  1                                  31    
HELIX   14  14 HIS A  466  LYS A  474  1                                   9    
HELIX   15  15 SER B  208  PHE B  226  1                                  19    
HELIX   16  16 THR B  229  THR B  238  1                                  10    
HELIX   17  17 ASP B  251  GLU B  259  1                                   9    
HELIX   18  18 VAL B  277  SER B  302  1                                  26    
HELIX   19  19 GLY B  305  LEU B  309  5                                   5    
HELIX   20  20 ASP B  310  LEU B  333  1                                  24    
HELIX   21  21 ARG B  350  SER B  355  1                                   6    
HELIX   22  22 PRO B  359  PHE B  363  5                                   5    
HELIX   23  23 MET B  364  ALA B  376  1                                  13    
HELIX   24  24 ASP B  380  LEU B  393  1                                  14    
HELIX   25  25 ASN B  402  HIS B  425  1                                  24    
HELIX   26  26 GLN B  430  LEU B  453  1                                  24    
HELIX   27  27 HIS B  466  TYR B  473  1                                   8    
SHEET    1   A 4 PHE A 247  ILE A 249  0                                        
SHEET    2   A 4 GLY A 346  THR A 349  1  O  PHE A 347   N  ILE A 249           
SHEET    3   A 4 GLY A 338  ILE A 341 -1  N  VAL A 339   O  MET A 348           
SHEET    4   A 4 MET A 334  ASN A 335 -1  N  ASN A 335   O  GLY A 338           
SHEET    1   B 4 PHE B 247  ILE B 249  0                                        
SHEET    2   B 4 GLY B 346  THR B 349  1  O  PHE B 347   N  ILE B 249           
SHEET    3   B 4 GLY B 338  ILE B 341 -1  N  VAL B 339   O  MET B 348           
SHEET    4   B 4 MET B 334  ASN B 335 -1  N  ASN B 335   O  GLY B 338           
CISPEP   1 LYS A  358    PRO A  359          0         0.56                     
CISPEP   2 LYS B  358    PRO B  359          0        -2.28                     
SITE     1 AC1  8 CYS A 285  ARG A 288  SER A 289  ILE A 326                    
SITE     2 AC1  8 LEU A 333  MET A 364  KNA A 503  GOL A 504                    
SITE     1 AC2  7 PHE A 282  CYS A 285  SER A 289  HIS A 323                    
SITE     2 AC2  7 PHE A 363  HIS A 449  TYR A 473                               
SITE     1 AC3  6 ARG A 288  LEU A 340  ILE A 341  SER A 342                    
SITE     2 AC3  6 KNA A 501  HOH A 733                                          
SITE     1 AC4  8 PHE A 226  LEU A 228  ARG A 288  GLU A 295                    
SITE     2 AC4  8 MET A 329  LEU A 333  KNA A 501  HOH A 637                    
SITE     1 AC5  9 CYS B 285  ARG B 288  SER B 289  ALA B 292                    
SITE     2 AC5  9 ILE B 326  TYR B 327  MET B 364  HIS B 449                    
SITE     3 AC5  9 GOL B 504                                                     
SITE     1 AC6  7 GLU B 259  PHE B 264  HIS B 266  CYS B 285                    
SITE     2 AC6  7 ILE B 341  SER B 342  HOH B 664                               
SITE     1 AC7  1 ASN B 312                                                     
SITE     1 AC8  8 PRO B 227  LEU B 228  ARG B 288  GLU B 295                    
SITE     2 AC8  8 MET B 329  LEU B 333  KNA B 501  HOH B 613                    
CRYST1   92.731   62.255  118.649  90.00 101.94  90.00 C 1 2 1       8          
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      0.010784  0.000000  0.002280        0.00000                         
SCALE2      0.000000  0.016063  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008615        0.00000                         
ATOM      1  N   GLU A 207      -7.639 -22.023  27.198  1.00 74.26           N  
ATOM      2  CA  GLU A 207      -6.436 -21.206  27.306  1.00 68.36           C  
ATOM      3  C   GLU A 207      -5.971 -20.713  25.940  1.00 60.97           C  
ATOM      4  O   GLU A 207      -5.644 -19.538  25.775  1.00 61.74           O  
ATOM      5  CB  GLU A 207      -5.314 -21.987  27.997  1.00 73.42           C  
ATOM      6  CG  GLU A 207      -4.004 -21.219  28.133  1.00 75.79           C  
ATOM      7  CD  GLU A 207      -4.142 -19.970  28.987  1.00 80.68           C  
ATOM      8  OE1 GLU A 207      -3.186 -19.166  29.030  1.00 80.77           O  
ATOM      9  OE2 GLU A 207      -5.208 -19.791  29.614  1.00 84.75           O  
ATOM     10  N   SER A 208      -5.940 -21.617  24.965  1.00 58.36           N  
ATOM     11  CA  SER A 208      -5.552 -21.263  23.604  1.00 57.13           C  
ATOM     12  C   SER A 208      -6.408 -20.120  23.073  1.00 53.55           C  
ATOM     13  O   SER A 208      -5.904 -19.203  22.428  1.00 52.26           O  
ATOM     14  CB  SER A 208      -5.665 -22.476  22.680  1.00 63.32           C  
ATOM     15  OG  SER A 208      -4.706 -23.462  23.016  1.00 70.66           O  
ATOM     16  N   ALA A 209      -7.706 -20.183  23.350  1.00 55.39           N  
ATOM     17  CA  ALA A 209      -8.634 -19.140  22.929  1.00 55.33           C  
ATOM     18  C   ALA A 209      -8.264 -17.801  23.560  1.00 53.93           C  
ATOM     19  O   ALA A 209      -8.344 -16.759  22.913  1.00 49.89           O  
ATOM     20  CB  ALA A 209     -10.062 -19.524  23.285  1.00 57.18           C  
ATOM     21  N   ASP A 210      -7.855 -17.839  24.825  1.00 53.29           N  
ATOM     22  CA  ASP A 210      -7.424 -16.637  25.529  1.00 53.02           C  
ATOM     23  C   ASP A 210      -6.131 -16.088  24.926  1.00 56.24           C  
ATOM     24  O   ASP A 210      -5.946 -14.875  24.828  1.00 56.69           O  
ATOM     25  CB  ASP A 210      -7.230 -16.931  27.019  1.00 55.90           C  
ATOM     26  CG  ASP A 210      -8.527 -17.314  27.714  1.00 62.30           C  
ATOM     27  OD1 ASP A 210      -9.554 -16.645  27.479  1.00 62.25           O  
ATOM     28  OD2 ASP A 210      -8.519 -18.283  28.501  1.00 64.96           O  
ATOM     29  N   LEU A 211      -5.240 -16.985  24.520  1.00 55.51           N  
ATOM     30  CA  LEU A 211      -3.973 -16.578  23.922  1.00 54.47           C  
ATOM     31  C   LEU A 211      -4.179 -15.984  22.530  1.00 54.65           C  
ATOM     32  O   LEU A 211      -3.502 -15.031  22.148  1.00 56.06           O  
ATOM     33  CB  LEU A 211      -3.000 -17.758  23.865  1.00 49.00           C  
ATOM     34  CG  LEU A 211      -2.574 -18.334  25.218  1.00 49.15           C  
ATOM     35  CD1 LEU A 211      -1.743 -19.597  25.034  1.00 47.19           C  
ATOM     36  CD2 LEU A 211      -1.811 -17.294  26.026  1.00 48.71           C  
ATOM     37  N   ARG A 212      -5.113 -16.552  21.773  1.00 50.58           N  
ATOM     38  CA  ARG A 212      -5.448 -16.016  20.460  1.00 46.99           C  
ATOM     39  C   ARG A 212      -5.995 -14.602  20.602  1.00 43.93           C  
ATOM     40  O   ARG A 212      -5.662 -13.715  19.818  1.00 49.73           O  
ATOM     41  CB  ARG A 212      -6.479 -16.903  19.761  1.00 52.09           C  
ATOM     42  CG  ARG A 212      -5.931 -18.215  19.228  1.00 58.24           C  
ATOM     43  CD  ARG A 212      -5.149 -17.988  17.950  1.00 67.42           C  
ATOM     44  NE  ARG A 212      -3.847 -17.392  18.221  1.00 70.18           N  
ATOM     45  CZ  ARG A 212      -3.098 -16.779  17.313  1.00 64.06           C  
ATOM     46  NH1 ARG A 212      -3.522 -16.668  16.060  1.00 63.79           N  
ATOM     47  NH2 ARG A 212      -1.926 -16.272  17.664  1.00 57.52           N  
ATOM     48  N   ALA A 213      -6.838 -14.400  21.612  1.00 45.27           N  
ATOM     49  CA  ALA A 213      -7.434 -13.094  21.867  1.00 47.09           C  
ATOM     50  C   ALA A 213      -6.367 -12.062  22.210  1.00 48.69           C  
ATOM     51  O   ALA A 213      -6.429 -10.919  21.761  1.00 47.44           O  
ATOM     52  CB  ALA A 213      -8.466 -13.188  22.985  1.00 46.28           C  
ATOM     53  N   LEU A 214      -5.385 -12.473  23.007  1.00 50.24           N  
ATOM     54  CA  LEU A 214      -4.300 -11.584  23.399  1.00 47.16           C  
ATOM     55  C   LEU A 214      -3.456 -11.188  22.193  1.00 44.85           C  
ATOM     56  O   LEU A 214      -3.103 -10.019  22.026  1.00 42.93           O  
ATOM     57  CB  LEU A 214      -3.421 -12.249  24.458  1.00 45.55           C  
ATOM     58  CG  LEU A 214      -2.186 -11.474  24.927  1.00 41.89           C  
ATOM     59  CD1 LEU A 214      -2.563 -10.073  25.381  1.00 42.55           C  
ATOM     60  CD2 LEU A 214      -1.472 -12.229  26.043  1.00 42.92           C  
ATOM     61  N   ALA A 215      -3.132 -12.169  21.357  1.00 42.19           N  
ATOM     62  CA  ALA A 215      -2.335 -11.924  20.161  1.00 41.50           C  
ATOM     63  C   ALA A 215      -3.032 -10.924  19.245  1.00 41.89           C  
ATOM     64  O   ALA A 215      -2.391 -10.047  18.669  1.00 42.56           O  
ATOM     65  CB  ALA A 215      -2.069 -13.229  19.422  1.00 39.86           C  
ATOM     66  N   LYS A 216      -4.349 -11.057  19.123  1.00 44.50           N  
ATOM     67  CA  LYS A 216      -5.130 -10.181  18.253  1.00 45.29           C  
ATOM     68  C   LYS A 216      -5.244  -8.766  18.810  1.00 44.15           C  
ATOM     69  O   LYS A 216      -5.189  -7.792  18.060  1.00 45.49           O  
ATOM     70  CB  LYS A 216      -6.523 -10.766  18.009  1.00 50.18           C  
ATOM     71  CG  LYS A 216      -6.506 -12.102  17.283  0.80 56.55           C  
ATOM     72  CD  LYS A 216      -7.898 -12.516  16.840  0.50 60.53           C  
ATOM     73  CE  LYS A 216      -7.879 -13.896  16.205  0.50 63.03           C  
ATOM     74  NZ  LYS A 216      -6.867 -13.988  15.117  0.50 62.55           N  
ATOM     75  N   HIS A 217      -5.414  -8.659  20.126  1.00 42.67           N  
ATOM     76  CA  HIS A 217      -5.461  -7.362  20.788  1.00 41.32           C  
ATOM     77  C   HIS A 217      -4.179  -6.585  20.518  1.00 39.69           C  
ATOM     78  O   HIS A 217      -4.216  -5.418  20.127  1.00 38.25           O  
ATOM     79  CB  HIS A 217      -5.663  -7.532  22.296  1.00 48.33           C  
ATOM     80  CG  HIS A 217      -5.338  -6.305  23.090  1.00 52.91           C  
ATOM     81  ND1 HIS A 217      -6.216  -5.252  23.230  1.00 56.29           N  
ATOM     82  CD2 HIS A 217      -4.227  -5.960  23.785  1.00 54.56           C  
ATOM     83  CE1 HIS A 217      -5.662  -4.312  23.974  1.00 58.15           C  
ATOM     84  NE2 HIS A 217      -4.455  -4.717  24.323  1.00 54.52           N  
ATOM     85  N   LEU A 218      -3.045  -7.248  20.719  1.00 38.38           N  
ATOM     86  CA  LEU A 218      -1.742  -6.614  20.552  1.00 36.23           C  
ATOM     87  C   LEU A 218      -1.472  -6.209  19.104  1.00 35.19           C  
ATOM     88  O   LEU A 218      -0.934  -5.131  18.849  1.00 38.09           O  
ATOM     89  CB  LEU A 218      -0.630  -7.531  21.067  1.00 35.18           C  
ATOM     90  CG  LEU A 218      -0.614  -7.771  22.578  1.00 33.65           C  
ATOM     91  CD1 LEU A 218       0.367  -8.877  22.939  1.00 29.03           C  
ATOM     92  CD2 LEU A 218      -0.267  -6.481  23.296  1.00 35.31           C  
ATOM     93  N   TYR A 219      -1.838  -7.070  18.160  1.00 36.53           N  
ATOM     94  CA  TYR A 219      -1.669  -6.748  16.746  1.00 38.21           C  
ATOM     95  C   TYR A 219      -2.511  -5.529  16.391  1.00 40.20           C  
ATOM     96  O   TYR A 219      -2.081  -4.657  15.634  1.00 39.77           O  
ATOM     97  CB  TYR A 219      -2.055  -7.937  15.862  1.00 38.31           C  
ATOM     98  CG  TYR A 219      -1.856  -7.688  14.382  1.00 43.31           C  
ATOM     99  CD1 TYR A 219      -0.676  -7.140  13.906  1.00 44.45           C  
ATOM    100  CD2 TYR A 219      -2.842  -8.016  13.462  1.00 53.92           C  
ATOM    101  CE1 TYR A 219      -0.487  -6.915  12.558  1.00 50.08           C  
ATOM    102  CE2 TYR A 219      -2.660  -7.795  12.110  1.00 53.89           C  
ATOM    103  CZ  TYR A 219      -1.481  -7.244  11.665  1.00 50.82           C  
ATOM    104  OH  TYR A 219      -1.291  -7.017  10.322  1.00 53.30           O  
ATOM    105  N   ASP A 220      -3.711  -5.476  16.957  1.00 42.24           N  
ATOM    106  CA  ASP A 220      -4.631  -4.366  16.737  1.00 44.15           C  
ATOM    107  C   ASP A 220      -4.024  -3.054  17.236  1.00 39.10           C  
ATOM    108  O   ASP A 220      -4.086  -2.033  16.550  1.00 36.31           O  
ATOM    109  CB  ASP A 220      -5.958  -4.650  17.447  1.00 47.29           C  
ATOM    110  CG  ASP A 220      -7.014  -3.599  17.169  1.00 50.45           C  
ATOM    111  OD1 ASP A 220      -7.450  -3.475  16.006  1.00 54.24           O  
ATOM    112  OD2 ASP A 220      -7.424  -2.908  18.124  1.00 50.77           O  
ATOM    113  N   SER A 221      -3.430  -3.097  18.428  1.00 36.76           N  
ATOM    114  CA  SER A 221      -2.836  -1.914  19.051  1.00 33.29           C  
ATOM    115  C   SER A 221      -1.557  -1.521  18.336  1.00 33.45           C  
ATOM    116  O   SER A 221      -1.251  -0.340  18.189  1.00 35.62           O  
ATOM    117  CB  SER A 221      -2.514  -2.183  20.522  1.00 34.15           C  
ATOM    118  OG  SER A 221      -3.584  -2.840  21.173  1.00 48.99           O  
ATOM    119  N   TYR A 222      -0.796  -2.530  17.933  1.00 35.87           N  
ATOM    120  CA  TYR A 222       0.414  -2.337  17.148  1.00 32.80           C  
ATOM    121  C   TYR A 222       0.086  -1.532  15.891  1.00 35.92           C  
ATOM    122  O   TYR A 222       0.706  -0.503  15.619  1.00 39.36           O  
ATOM    123  CB  TYR A 222       0.984  -3.710  16.790  1.00 32.03           C  
ATOM    124  CG  TYR A 222       2.189  -3.751  15.872  1.00 33.79           C  
ATOM    125  CD1 TYR A 222       2.037  -3.757  14.490  1.00 37.72           C  
ATOM    126  CD2 TYR A 222       3.477  -3.855  16.389  1.00 32.72           C  
ATOM    127  CE1 TYR A 222       3.138  -3.831  13.645  1.00 35.22           C  
ATOM    128  CE2 TYR A 222       4.585  -3.929  15.554  1.00 32.29           C  
ATOM    129  CZ  TYR A 222       4.410  -3.917  14.183  1.00 33.83           C  
ATOM    130  OH  TYR A 222       5.509  -3.996  13.350  1.00 33.97           O  
ATOM    131  N   ILE A 223      -0.900  -2.001  15.131  1.00 34.05           N  
ATOM    132  CA  ILE A 223      -1.327  -1.304  13.920  1.00 32.56           C  
ATOM    133  C   ILE A 223      -1.747   0.127  14.236  1.00 38.34           C  
ATOM    134  O   ILE A 223      -1.452   1.053  13.485  1.00 34.33           O  
ATOM    135  CB  ILE A 223      -2.499  -2.025  13.224  1.00 38.65           C  
ATOM    136  CG1 ILE A 223      -2.090  -3.436  12.806  1.00 46.33           C  
ATOM    137  CG2 ILE A 223      -2.961  -1.239  12.007  1.00 43.69           C  
ATOM    138  CD1 ILE A 223      -0.856  -3.472  11.945  1.00 52.74           C  
ATOM    139  N   LYS A 224      -2.425   0.305  15.364  1.00 38.34           N  
ATOM    140  CA  LYS A 224      -2.911   1.621  15.760  1.00 41.08           C  
ATOM    141  C   LYS A 224      -1.802   2.543  16.271  1.00 39.80           C  
ATOM    142  O   LYS A 224      -1.940   3.765  16.237  1.00 39.01           O  
ATOM    143  CB  LYS A 224      -4.030   1.479  16.795  1.00 46.13           C  
ATOM    144  CG  LYS A 224      -5.329   0.932  16.205  1.00 41.06           C  
ATOM    145  CD  LYS A 224      -6.282   0.420  17.276  1.00 40.97           C  
ATOM    146  CE  LYS A 224      -7.610  -0.011  16.663  1.00 42.65           C  
ATOM    147  NZ  LYS A 224      -8.587  -0.474  17.692  1.00 43.58           N  
ATOM    148  N   SER A 225      -0.698   1.958  16.726  1.00 39.36           N  
ATOM    149  CA  SER A 225       0.392   2.732  17.318  1.00 38.82           C  
ATOM    150  C   SER A 225       1.526   3.061  16.341  1.00 39.62           C  
ATOM    151  O   SER A 225       2.191   4.088  16.480  1.00 36.92           O  
ATOM    152  CB  SER A 225       0.965   1.997  18.535  1.00 38.26           C  
ATOM    153  OG  SER A 225      -0.001   1.859  19.560  1.00 37.80           O  
ATOM    154  N   PHE A 226       1.755   2.184  15.368  1.00 33.73           N  
ATOM    155  CA  PHE A 226       2.905   2.312  14.475  1.00 35.08           C  
ATOM    156  C   PHE A 226       2.477   2.559  13.033  1.00 35.64           C  
ATOM    157  O   PHE A 226       2.056   1.633  12.342  1.00 41.83           O  
ATOM    158  CB  PHE A 226       3.795   1.067  14.566  1.00 29.58           C  
ATOM    159  CG  PHE A 226       4.239   0.742  15.966  1.00 31.74           C  
ATOM    160  CD1 PHE A 226       5.136   1.564  16.630  1.00 33.38           C  
ATOM    161  CD2 PHE A 226       3.756  -0.383  16.621  1.00 32.17           C  
ATOM    162  CE1 PHE A 226       5.545   1.273  17.923  1.00 34.68           C  
ATOM    163  CE2 PHE A 226       4.165  -0.683  17.913  1.00 33.69           C  
ATOM    164  CZ  PHE A 226       5.060   0.146  18.563  1.00 32.60           C  
ATOM    165  N   PRO A 227       2.586   3.818  12.579  1.00 33.79           N  
ATOM    166  CA  PRO A 227       2.127   4.259  11.257  1.00 39.90           C  
ATOM    167  C   PRO A 227       2.763   3.495  10.097  1.00 44.04           C  
ATOM    168  O   PRO A 227       2.097   3.288   9.084  1.00 50.21           O  
ATOM    169  CB  PRO A 227       2.553   5.733  11.209  1.00 40.46           C  
ATOM    170  CG  PRO A 227       2.689   6.139  12.631  1.00 40.63           C  
ATOM    171  CD  PRO A 227       3.178   4.922  13.352  1.00 32.17           C  
ATOM    172  N   LEU A 228       4.022   3.091  10.231  1.00 40.25           N  
ATOM    173  CA  LEU A 228       4.711   2.404   9.140  1.00 39.58           C  
ATOM    174  C   LEU A 228       5.030   0.965   9.498  1.00 38.40           C  
ATOM    175  O   LEU A 228       6.060   0.687  10.098  1.00 37.54           O  
ATOM    176  CB  LEU A 228       6.003   3.131   8.759  1.00 42.42           C  
ATOM    177  CG  LEU A 228       6.811   2.446   7.648  1.00 46.50           C  
ATOM    178  CD1 LEU A 228       5.940   2.189   6.426  1.00 45.96           C  
ATOM    179  CD2 LEU A 228       8.048   3.257   7.264  1.00 44.41           C  
ATOM    180  N   THR A 229       4.145   0.053   9.119  1.00 38.21           N  
ATOM    181  CA  THR A 229       4.293  -1.355   9.460  1.00 34.93           C  
ATOM    182  C   THR A 229       5.374  -2.029   8.620  1.00 35.15           C  
ATOM    183  O   THR A 229       5.871  -1.453   7.651  1.00 33.70           O  
ATOM    184  CB  THR A 229       2.973  -2.106   9.235  1.00 34.26           C  
ATOM    185  OG1 THR A 229       2.592  -1.990   7.857  1.00 32.88           O  
ATOM    186  CG2 THR A 229       1.873  -1.525  10.111  1.00 36.43           C  
ATOM    187  N   LYS A 230       5.732  -3.255   8.988  1.00 32.27           N  
ATOM    188  CA  LYS A 230       6.643  -4.045   8.172  1.00 32.94           C  
ATOM    189  C   LYS A 230       5.994  -4.384   6.834  1.00 28.70           C  
ATOM    190  O   LYS A 230       6.661  -4.413   5.800  1.00 31.87           O  
ATOM    191  CB  LYS A 230       7.055  -5.334   8.885  1.00 33.71           C  
ATOM    192  CG  LYS A 230       7.994  -6.192   8.053  1.00 35.54           C  
ATOM    193  CD  LYS A 230       8.509  -7.414   8.812  1.00 34.82           C  
ATOM    194  CE  LYS A 230       9.490  -8.211   7.954  1.00 36.01           C  
ATOM    195  NZ  LYS A 230      10.171  -9.317   8.694  1.00 38.26           N  
ATOM    196  N   ALA A 231       4.692  -4.649   6.866  1.00 29.71           N  
ATOM    197  CA  ALA A 231       3.943  -4.967   5.654  1.00 35.15           C  
ATOM    198  C   ALA A 231       4.069  -3.846   4.616  1.00 37.14           C  
ATOM    199  O   ALA A 231       4.338  -4.097   3.442  1.00 37.14           O  
ATOM    200  CB  ALA A 231       2.477  -5.232   5.989  1.00 36.50           C  
ATOM    201  N   LYS A 232       3.890  -2.606   5.057  1.00 32.29           N  
ATOM    202  CA  LYS A 232       4.009  -1.467   4.155  1.00 30.58           C  
ATOM    203  C   LYS A 232       5.459  -1.256   3.736  1.00 31.79           C  
ATOM    204  O   LYS A 232       5.754  -1.018   2.563  1.00 33.82           O  
ATOM    205  CB  LYS A 232       3.452  -0.201   4.804  1.00 32.33           C  
ATOM    206  CG  LYS A 232       3.592   1.036   3.928  1.00 41.95           C  
ATOM    207  CD  LYS A 232       2.870   2.240   4.514  1.00 47.82           C  
ATOM    208  CE  LYS A 232       3.002   3.451   3.598  1.00 51.38           C  
ATOM    209  NZ  LYS A 232       2.339   4.660   4.153  1.00 48.40           N  
ATOM    210  N   ALA A 233       6.366  -1.355   4.702  1.00 31.50           N  
ATOM    211  CA  ALA A 233       7.786  -1.189   4.431  1.00 31.42           C  
ATOM    212  C   ALA A 233       8.271  -2.145   3.339  1.00 36.97           C  
ATOM    213  O   ALA A 233       9.046  -1.755   2.464  1.00 39.13           O  
ATOM    214  CB  ALA A 233       8.592  -1.378   5.709  1.00 34.15           C  
ATOM    215  N   ARG A 234       7.812  -3.393   3.388  1.00 34.28           N  
ATOM    216  CA  ARG A 234       8.218  -4.382   2.393  1.00 36.91           C  
ATOM    217  C   ARG A 234       7.609  -4.058   1.032  1.00 41.40           C  
ATOM    218  O   ARG A 234       8.263  -4.214   0.001  1.00 42.17           O  
ATOM    219  CB  ARG A 234       7.833  -5.805   2.814  1.00 38.18           C  
ATOM    220  CG  ARG A 234       8.283  -6.218   4.212  1.00 45.18           C  
ATOM    221  CD  ARG A 234       9.592  -5.556   4.632  1.00 53.07           C  
ATOM    222  NE  ARG A 234      10.744  -6.052   3.886  1.00 59.67           N  
ATOM    223  CZ  ARG A 234      12.007  -5.754   4.180  1.00 64.28           C  
ATOM    224  NH1 ARG A 234      12.995  -6.248   3.443  1.00 69.26           N  
ATOM    225  NH2 ARG A 234      12.284  -4.964   5.211  1.00 49.15           N  
ATOM    226  N   ALA A 235       6.356  -3.609   1.035  1.00 36.34           N  
ATOM    227  CA  ALA A 235       5.676  -3.248  -0.205  1.00 38.51           C  
ATOM    228  C   ALA A 235       6.420  -2.123  -0.916  1.00 43.13           C  
ATOM    229  O   ALA A 235       6.470  -2.079  -2.144  1.00 48.72           O  
ATOM    230  CB  ALA A 235       4.234  -2.848   0.066  1.00 31.42           C  
ATOM    231  N   ILE A 236       6.997  -1.216  -0.136  1.00 41.05           N  
ATOM    232  CA  ILE A 236       7.771  -0.112  -0.689  1.00 41.68           C  
ATOM    233  C   ILE A 236       9.124  -0.594  -1.214  1.00 40.10           C  
ATOM    234  O   ILE A 236       9.529  -0.250  -2.324  1.00 39.41           O  
ATOM    235  CB  ILE A 236       8.008   0.985   0.361  1.00 38.75           C  
ATOM    236  CG1 ILE A 236       6.681   1.621   0.780  1.00 41.49           C  
ATOM    237  CG2 ILE A 236       8.973   2.037  -0.175  1.00 40.44           C  
ATOM    238  CD1 ILE A 236       6.818   2.617   1.916  1.00 37.04           C  
ATOM    239  N   LEU A 237       9.813  -1.396  -0.408  1.00 38.56           N  
ATOM    240  CA  LEU A 237      11.137  -1.904  -0.764  1.00 42.88           C  
ATOM    241  C   LEU A 237      11.128  -2.851  -1.966  1.00 47.34           C  
ATOM    242  O   LEU A 237      12.069  -2.861  -2.756  1.00 52.95           O  
ATOM    243  CB  LEU A 237      11.784  -2.604   0.437  1.00 35.82           C  
ATOM    244  CG  LEU A 237      12.169  -1.729   1.630  1.00 40.62           C  
ATOM    245  CD1 LEU A 237      12.452  -2.577   2.867  1.00 40.39           C  
ATOM    246  CD2 LEU A 237      13.361  -0.846   1.284  1.00 46.02           C  
ATOM    247  N   THR A 238      10.070  -3.643  -2.103  1.00 49.91           N  
ATOM    248  CA  THR A 238      10.034  -4.683  -3.130  1.00 54.63           C  
ATOM    249  C   THR A 238       9.172  -4.337  -4.347  1.00 62.97           C  
ATOM    250  O   THR A 238       8.912  -5.194  -5.193  1.00 64.19           O  
ATOM    251  CB  THR A 238       9.548  -6.018  -2.548  1.00 55.15           C  
ATOM    252  OG1 THR A 238       8.169  -5.901  -2.175  1.00 56.99           O  
ATOM    253  CG2 THR A 238      10.376  -6.396  -1.328  1.00 54.23           C  
ATOM    254  N   GLY A 239       8.827  -3.071  -4.534  1.00 64.66           N  
ATOM    255  CA  GLY A 239       7.971  -2.639  -5.632  1.00 65.61           C  
ATOM    256  C   GLY A 239       6.515  -3.081  -5.805  1.00 64.46           C  
ATOM    257  O   GLY A 239       6.139  -3.530  -6.866  1.00 63.85           O  
ATOM    258  N   LYS A 240       5.685  -2.942  -4.768  1.00 62.81           N  
ATOM    259  CA  LYS A 240       4.290  -3.351  -4.854  1.00 62.51           C  
ATOM    260  C   LYS A 240       3.462  -2.162  -5.346  1.00 63.02           C  
ATOM    261  O   LYS A 240       3.847  -1.009  -5.146  1.00 65.77           O  
ATOM    262  CB  LYS A 240       3.783  -3.847  -3.494  1.00 58.89           C  
ATOM    263  N   THR A 241       2.341  -2.439  -6.002  1.00 62.23           N  
ATOM    264  CA  THR A 241       1.486  -1.375  -6.523  1.00 63.64           C  
ATOM    265  C   THR A 241       0.583  -0.790  -5.437  1.00 61.73           C  
ATOM    266  O   THR A 241      -0.182   0.145  -5.681  1.00 62.93           O  
ATOM    267  CB  THR A 241       0.635  -1.871  -7.704  1.00 63.03           C  
ATOM    268  OG1 THR A 241      -0.233  -2.922  -7.262  1.00 58.58           O  
ATOM    269  CG2 THR A 241       1.535  -2.404  -8.805  1.00 67.79           C  
ATOM    270  N   THR A 242       0.684  -1.346  -4.235  1.00 60.35           N  
ATOM    271  CA  THR A 242      -0.074  -0.852  -3.093  1.00 58.83           C  
ATOM    272  C   THR A 242       0.592   0.394  -2.517  1.00 62.19           C  
ATOM    273  O   THR A 242      -0.038   1.176  -1.808  1.00 58.66           O  
ATOM    274  CB  THR A 242      -0.168  -1.918  -1.986  1.00 50.19           C  
ATOM    275  OG1 THR A 242       1.152  -2.367  -1.650  1.00 48.08           O  
ATOM    276  CG2 THR A 242      -0.997  -3.102  -2.454  1.00 46.47           C  
ATOM    277  N   ASP A 243       1.870   0.576  -2.827  1.00 66.89           N  
ATOM    278  CA  ASP A 243       2.626   1.702  -2.291  1.00 71.50           C  
ATOM    279  C   ASP A 243       3.502   2.384  -3.336  1.00 72.80           C  
ATOM    280  O   ASP A 243       3.507   2.000  -4.507  1.00 76.24           O  
ATOM    281  CB  ASP A 243       3.462   1.259  -1.092  1.00 73.65           C  
ATOM    282  CG  ASP A 243       2.641   1.155   0.174  1.00 80.34           C  
ATOM    283  OD1 ASP A 243       1.839   2.075   0.432  1.00 81.45           O  
ATOM    284  OD2 ASP A 243       2.798   0.159   0.910  1.00 84.90           O  
ATOM    285  N   LYS A 244       4.243   3.398  -2.902  1.00 67.70           N  
ATOM    286  CA  LYS A 244       5.014   4.226  -3.820  1.00 64.17           C  
ATOM    287  C   LYS A 244       6.521   4.071  -3.651  1.00 56.60           C  
ATOM    288  O   LYS A 244       7.016   3.771  -2.564  1.00 51.17           O  
ATOM    289  CB  LYS A 244       4.627   5.695  -3.664  1.00 68.08           C  
ATOM    290  CG  LYS A 244       3.322   6.068  -4.338  1.00 73.23           C  
ATOM    291  CD  LYS A 244       3.037   7.547  -4.153  1.00 79.99           C  
ATOM    292  CE  LYS A 244       4.290   8.376  -4.399  1.00 83.69           C  
ATOM    293  NZ  LYS A 244       4.088   9.816  -4.079  1.00 85.33           N  
ATOM    294  N   SER A 245       7.238   4.290  -4.746  1.00 52.32           N  
ATOM    295  CA  SER A 245       8.688   4.176  -4.773  1.00 51.05           C  
ATOM    296  C   SER A 245       9.346   5.284  -3.966  1.00 48.57           C  
ATOM    297  O   SER A 245       8.903   6.432  -4.010  1.00 49.59           O  
ATOM    298  CB  SER A 245       9.181   4.238  -6.216  1.00 59.08           C  
ATOM    299  OG  SER A 245       8.586   3.219  -7.000  1.00 61.46           O  
ATOM    300  N   PRO A 246      10.418   4.943  -3.235  1.00 42.84           N  
ATOM    301  CA  PRO A 246      11.153   5.912  -2.420  1.00 37.76           C  
ATOM    302  C   PRO A 246      12.145   6.702  -3.260  1.00 43.32           C  
ATOM    303  O   PRO A 246      12.628   6.200  -4.276  1.00 44.11           O  
ATOM    304  CB  PRO A 246      11.933   5.027  -1.435  1.00 41.21           C  
ATOM    305  CG  PRO A 246      11.597   3.592  -1.792  1.00 42.21           C  
ATOM    306  CD  PRO A 246      11.023   3.606  -3.162  1.00 39.71           C  
ATOM    307  N   PHE A 247      12.440   7.929  -2.847  1.00 47.88           N  
ATOM    308  CA  PHE A 247      13.563   8.649  -3.424  1.00 50.76           C  
ATOM    309  C   PHE A 247      14.823   8.149  -2.732  1.00 48.01           C  
ATOM    310  O   PHE A 247      14.867   8.052  -1.508  1.00 44.73           O  
ATOM    311  CB  PHE A 247      13.416  10.159  -3.243  1.00 52.33           C  
ATOM    312  CG  PHE A 247      14.586  10.943  -3.771  1.00 55.24           C  
ATOM    313  CD1 PHE A 247      15.643  11.277  -2.941  1.00 55.89           C  
ATOM    314  CD2 PHE A 247      14.635  11.332  -5.100  1.00 53.69           C  
ATOM    315  CE1 PHE A 247      16.724  11.995  -3.426  1.00 57.46           C  
ATOM    316  CE2 PHE A 247      15.713  12.049  -5.590  1.00 54.01           C  
ATOM    317  CZ  PHE A 247      16.760  12.379  -4.752  1.00 56.18           C  
ATOM    318  N   VAL A 248      15.843   7.820  -3.515  1.00 46.03           N  
ATOM    319  CA  VAL A 248      17.033   7.188  -2.962  1.00 44.91           C  
ATOM    320  C   VAL A 248      18.181   8.166  -2.734  1.00 47.02           C  
ATOM    321  O   VAL A 248      18.643   8.834  -3.662  1.00 49.17           O  
ATOM    322  CB  VAL A 248      17.512   6.021  -3.844  1.00 42.44           C  
ATOM    323  CG1 VAL A 248      18.822   5.456  -3.313  1.00 38.38           C  
ATOM    324  CG2 VAL A 248      16.440   4.940  -3.907  1.00 36.80           C  
ATOM    325  N   ILE A 249      18.630   8.238  -1.486  1.00 43.42           N  
ATOM    326  CA  ILE A 249      19.755   9.080  -1.106  1.00 45.73           C  
ATOM    327  C   ILE A 249      21.005   8.225  -0.960  1.00 42.33           C  
ATOM    328  O   ILE A 249      21.056   7.324  -0.125  1.00 44.19           O  
ATOM    329  CB  ILE A 249      19.476   9.824   0.216  1.00 46.99           C  
ATOM    330  CG1 ILE A 249      18.321  10.812   0.030  1.00 50.71           C  
ATOM    331  CG2 ILE A 249      20.729  10.537   0.706  1.00 45.86           C  
ATOM    332  CD1 ILE A 249      17.763  11.360   1.328  1.00 51.60           C  
ATOM    333  N   TYR A 250      22.011   8.509  -1.779  1.00 45.28           N  
ATOM    334  CA  TYR A 250      23.213   7.687  -1.827  1.00 48.07           C  
ATOM    335  C   TYR A 250      24.485   8.534  -1.846  1.00 50.29           C  
ATOM    336  O   TYR A 250      25.592   7.997  -1.882  1.00 50.11           O  
ATOM    337  CB  TYR A 250      23.178   6.782  -3.060  1.00 46.12           C  
ATOM    338  CG  TYR A 250      23.210   7.547  -4.365  1.00 47.79           C  
ATOM    339  CD1 TYR A 250      22.046   8.065  -4.919  1.00 49.96           C  
ATOM    340  CD2 TYR A 250      24.405   7.754  -5.040  1.00 51.15           C  
ATOM    341  CE1 TYR A 250      22.071   8.768  -6.112  1.00 50.38           C  
ATOM    342  CE2 TYR A 250      24.441   8.456  -6.233  1.00 55.32           C  
ATOM    343  CZ  TYR A 250      23.271   8.961  -6.764  1.00 52.40           C  
ATOM    344  OH  TYR A 250      23.307   9.661  -7.948  1.00 49.66           O  
ATOM    345  N   ASP A 251      24.321   9.854  -1.838  1.00 53.52           N  
ATOM    346  CA  ASP A 251      25.458  10.774  -1.812  1.00 59.72           C  
ATOM    347  C   ASP A 251      25.026  12.191  -1.433  1.00 66.50           C  
ATOM    348  O   ASP A 251      23.883  12.411  -1.028  1.00 66.05           O  
ATOM    349  CB  ASP A 251      26.215  10.767  -3.145  1.00 59.05           C  
ATOM    350  CG  ASP A 251      25.397  11.331  -4.292  1.00 62.86           C  
ATOM    351  OD1 ASP A 251      24.289  11.851  -4.050  1.00 61.79           O  
ATOM    352  OD2 ASP A 251      25.869  11.258  -5.446  1.00 70.06           O  
ATOM    353  N   MET A 252      25.939  13.148  -1.573  1.00 68.83           N  
ATOM    354  CA AMET A 252      25.674  14.522  -1.166  0.50 70.08           C  
ATOM    355  CA BMET A 252      25.672  14.526  -1.167  0.50 70.08           C  
ATOM    356  C   MET A 252      24.575  15.179  -2.001  1.00 68.64           C  
ATOM    357  O   MET A 252      23.613  15.720  -1.459  1.00 72.13           O  
ATOM    358  CB AMET A 252      26.959  15.351  -1.217  0.50 74.39           C  
ATOM    359  CB BMET A 252      26.943  15.382  -1.217  0.50 74.40           C  
ATOM    360  CG AMET A 252      28.109  14.751  -0.417  0.50 76.47           C  
ATOM    361  CG BMET A 252      27.985  15.039  -0.160  0.50 75.18           C  
ATOM    362  SD AMET A 252      27.673  14.423   1.303  0.50 70.69           S  
ATOM    363  SD BMET A 252      29.295  13.967  -0.779  0.50 82.04           S  
ATOM    364  CE AMET A 252      29.185  13.675   1.907  0.50249.32           C  
ATOM    365  CE BMET A 252      30.174  13.607   0.739  0.50251.23           C  
ATOM    366  N   ASN A 253      24.722  15.133  -3.320  1.00 64.82           N  
ATOM    367  CA  ASN A 253      23.739  15.752  -4.204  1.00 69.15           C  
ATOM    368  C   ASN A 253      22.335  15.171  -4.042  1.00 68.29           C  
ATOM    369  O   ASN A 253      21.367  15.910  -3.856  1.00 69.01           O  
ATOM    370  CB  ASN A 253      24.185  15.658  -5.665  1.00 73.30           C  
ATOM    371  CG  ASN A 253      25.282  16.650  -6.008  1.00 76.87           C  
ATOM    372  OD1 ASN A 253      25.817  17.338  -5.137  1.00 74.29           O  
ATOM    373  ND2 ASN A 253      25.622  16.726  -7.289  1.00 80.62           N  
ATOM    374  N   SER A 254      22.229  13.848  -4.118  1.00 63.32           N  
ATOM    375  CA  SER A 254      20.943  13.180  -3.963  1.00 61.44           C  
ATOM    376  C   SER A 254      20.338  13.502  -2.597  1.00 63.00           C  
ATOM    377  O   SER A 254      19.118  13.522  -2.434  1.00 65.23           O  
ATOM    378  CB  SER A 254      21.088  11.668  -4.157  1.00 56.33           C  
ATOM    379  OG  SER A 254      21.959  11.104  -3.193  1.00 56.04           O  
ATOM    380  N   LEU A 255      21.199  13.762  -1.618  1.00 60.78           N  
ATOM    381  CA  LEU A 255      20.742  14.184  -0.300  1.00 64.26           C  
ATOM    382  C   LEU A 255      20.108  15.568  -0.368  1.00 69.02           C  
ATOM    383  O   LEU A 255      19.053  15.807   0.217  1.00 67.34           O  
ATOM    384  CB  LEU A 255      21.899  14.194   0.698  1.00 65.05           C  
ATOM    385  CG  LEU A 255      21.618  14.920   2.016  1.00 67.96           C  
ATOM    386  CD1 LEU A 255      20.537  14.204   2.817  1.00 65.92           C  
ATOM    387  CD2 LEU A 255      22.891  15.055   2.832  1.00 69.51           C  
ATOM    388  N   MET A 256      20.760  16.476  -1.088  1.00 74.65           N  
ATOM    389  CA  MET A 256      20.277  17.847  -1.217  1.00 76.96           C  
ATOM    390  C   MET A 256      18.978  17.906  -2.013  1.00 77.07           C  
ATOM    391  O   MET A 256      18.039  18.608  -1.635  1.00 78.68           O  
ATOM    392  CB  MET A 256      21.336  18.725  -1.884  1.00 80.51           C  
ATOM    393  CG  MET A 256      22.727  18.573  -1.295  1.00 81.41           C  
ATOM    394  SD  MET A 256      22.812  18.970   0.461  1.00169.69           S  
ATOM    395  CE  MET A 256      24.564  18.755   0.764  1.00 70.82           C  
ATOM    396  N   MET A 257      18.930  17.169  -3.117  1.00 74.25           N  
ATOM    397  CA  MET A 257      17.729  17.106  -3.939  1.00 76.29           C  
ATOM    398  C   MET A 257      16.584  16.475  -3.152  1.00 81.70           C  
ATOM    399  O   MET A 257      15.436  16.912  -3.244  1.00 83.72           O  
ATOM    400  CB  MET A 257      17.996  16.312  -5.218  1.00 75.90           C  
ATOM    401  N   GLY A 258      16.908  15.447  -2.375  1.00 81.62           N  
ATOM    402  CA  GLY A 258      15.920  14.773  -1.555  1.00 82.71           C  
ATOM    403  C   GLY A 258      15.612  15.541  -0.285  1.00 88.68           C  
ATOM    404  O   GLY A 258      14.636  15.248   0.404  1.00 90.57           O  
ATOM    405  N   GLU A 259      16.432  16.538  -0.011  1.00 95.45           N  
ATOM    406  CA  GLU A 259      16.264  17.309   1.184  1.00100.81           C  
ATOM    407  C   GLU A 259      15.144  18.293   0.965  1.00105.25           C  
ATOM    408  O   GLU A 259      15.301  19.470   1.225  1.00107.42           O  
ATOM    409  CB  GLU A 259      17.559  18.067   1.512  1.00103.10           C  
ATOM    410  CG  GLU A 259      18.046  17.938   2.961  1.00103.81           C  
ATOM    411  CD  GLU A 259      19.291  18.764   3.262  1.00107.49           C  
ATOM    412  OE1 GLU A 259      20.212  18.256   3.922  1.00106.70           O  
ATOM    413  OE2 GLU A 259      19.348  19.932   2.848  1.00110.54           O  
ATOM    414  N   ASP A 260      13.998  17.774   0.526  1.00105.84           N  
ATOM    415  CA  ASP A 260      12.768  18.538   0.370  1.00106.20           C  
ATOM    416  C   ASP A 260      11.643  17.854   1.138  1.00107.82           C  
ATOM    417  O   ASP A 260      10.763  18.512   1.692  1.00109.31           O  
ATOM    418  CB  ASP A 260      12.389  18.647  -1.108  1.00103.59           C  
ATOM    419  CG  ASP A 260      13.514  19.195  -1.963  1.00103.46           C  
ATOM    420  OD1 ASP A 260      13.311  19.341  -3.187  1.00104.61           O  
ATOM    421  OD2 ASP A 260      14.601  19.482  -1.418  1.00102.52           O  
ATOM    422  N   LYS A 261      11.685  16.526   1.163  1.00106.28           N  
ATOM    423  CA  LYS A 261      10.660  15.728   1.825  1.00103.30           C  
ATOM    424  C   LYS A 261      10.595  16.034   3.317  1.00105.86           C  
ATOM    425  O   LYS A 261      11.623  16.108   3.991  1.00107.28           O  
ATOM    426  CB  LYS A 261      10.928  14.237   1.608  1.00 97.19           C  
ATOM    427  CG  LYS A 261      11.252  13.869   0.169  1.00 93.72           C  
ATOM    428  CD  LYS A 261      11.373  12.361  -0.008  1.00 88.40           C  
ATOM    429  CE  LYS A 261      12.442  11.776   0.900  1.00 83.92           C  
ATOM    430  NZ  LYS A 261      13.788  12.347   0.623  1.00 82.65           N  
ATOM    431  N   SER A 274      23.606  21.500  11.827  0.79120.83           N  
ATOM    432  CA  SER A 274      24.822  22.132  12.318  0.51123.08           C  
ATOM    433  C   SER A 274      25.948  22.131  11.283  0.55120.99           C  
ATOM    434  O   SER A 274      27.072  21.743  11.570  0.89121.71           O  
ATOM    435  CB  SER A 274      25.276  21.525  13.659  1.00125.33           C  
ATOM    436  OG  SER A 274      26.241  22.331  14.338  1.00127.78           O  
ATOM    437  N   LYS A 275      25.609  22.543  10.070  1.00117.85           N  
ATOM    438  CA  LYS A 275      26.559  22.733   8.980  1.00116.39           C  
ATOM    439  C   LYS A 275      27.480  21.610   8.589  1.00110.98           C  
ATOM    440  O   LYS A 275      28.618  21.880   8.247  1.00115.80           O  
ATOM    441  CB  LYS A 275      27.450  23.946   9.234  1.00119.94           C  
ATOM    442  CG  LYS A 275      28.490  24.170   8.131  1.00122.33           C  
ATOM    443  CD  LYS A 275      29.525  25.247   8.471  1.00126.37           C  
ATOM    444  CE  LYS A 275      30.937  24.660   8.663  1.00127.44           C  
ATOM    445  NZ  LYS A 275      32.050  25.677   8.679  1.00129.85           N  
ATOM    446  N   GLU A 276      27.021  20.377   8.600  1.00 97.86           N  
ATOM    447  CA  GLU A 276      27.866  19.280   8.193  1.00 87.45           C  
ATOM    448  C   GLU A 276      26.890  18.164   7.978  1.00 77.92           C  
ATOM    449  O   GLU A 276      26.134  17.863   8.858  1.00 75.96           O  
ATOM    450  CB  GLU A 276      28.851  18.927   9.280  1.00 86.69           C  
ATOM    451  CG  GLU A 276      29.770  17.858   8.858  1.00 87.81           C  
ATOM    452  CD  GLU A 276      30.649  17.346   9.957  1.00 89.02           C  
ATOM    453  OE1 GLU A 276      30.652  17.894  11.061  1.00 89.57           O  
ATOM    454  OE2 GLU A 276      31.357  16.380   9.698  1.00 89.12           O  
ATOM    455  N   VAL A 277      26.879  17.560   6.806  1.00 70.72           N  
ATOM    456  CA  VAL A 277      25.873  16.534   6.552  1.00 68.25           C  
ATOM    457  C   VAL A 277      25.805  15.458   7.637  1.00 61.06           C  
ATOM    458  O   VAL A 277      24.718  15.032   8.025  1.00 57.73           O  
ATOM    459  CB  VAL A 277      26.095  15.876   5.171  1.00 69.26           C  
ATOM    460  CG1 VAL A 277      27.582  15.680   4.910  1.00 71.96           C  
ATOM    461  CG2 VAL A 277      25.362  14.552   5.088  1.00 66.11           C  
ATOM    462  N   ALA A 278      26.962  15.022   8.125  1.00 58.86           N  
ATOM    463  CA  ALA A 278      27.017  13.988   9.154  1.00 54.30           C  
ATOM    464  C   ALA A 278      26.206  14.381  10.384  1.00 53.80           C  
ATOM    465  O   ALA A 278      25.441  13.576  10.917  1.00 52.81           O  
ATOM    466  CB  ALA A 278      28.457  13.696   9.539  1.00 54.40           C  
ATOM    467  N   ILE A 279      26.383  15.621  10.832  1.00 56.10           N  
ATOM    468  CA  ILE A 279      25.643  16.137  11.977  1.00 55.31           C  
ATOM    469  C   ILE A 279      24.158  16.233  11.654  1.00 55.30           C  
ATOM    470  O   ILE A 279      23.312  15.814  12.443  1.00 56.08           O  
ATOM    471  CB  ILE A 279      26.147  17.535  12.398  1.00 56.41           C  
ATOM    472  CG1 ILE A 279      27.623  17.484  12.797  1.00 61.11           C  
ATOM    473  CG2 ILE A 279      25.311  18.081  13.544  1.00 53.54           C  
ATOM    474  CD1 ILE A 279      27.882  16.803  14.120  1.00 60.12           C  
ATOM    475  N   ARG A 280      23.852  16.786  10.484  1.00 56.15           N  
ATOM    476  CA  ARG A 280      22.471  16.993  10.058  1.00 54.56           C  
ATOM    477  C   ARG A 280      21.697  15.682   9.980  1.00 51.58           C  
ATOM    478  O   ARG A 280      20.534  15.612  10.378  1.00 48.53           O  
ATOM    479  CB  ARG A 280      22.431  17.711   8.708  1.00 56.95           C  
ATOM    480  N   ILE A 281      22.344  14.643   9.464  1.00 50.32           N  
ATOM    481  CA  ILE A 281      21.719  13.331   9.387  1.00 47.23           C  
ATOM    482  C   ILE A 281      21.487  12.778  10.790  1.00 48.98           C  
ATOM    483  O   ILE A 281      20.422  12.236  11.087  1.00 47.08           O  
ATOM    484  CB  ILE A 281      22.572  12.347   8.569  1.00 49.48           C  
ATOM    485  CG1 ILE A 281      22.729  12.847   7.131  1.00 49.13           C  
ATOM    486  CG2 ILE A 281      21.950  10.959   8.586  1.00 49.58           C  
ATOM    487  CD1 ILE A 281      23.560  11.933   6.257  1.00 50.24           C  
ATOM    488  N   PHE A 282      22.485  12.930  11.655  1.00 50.17           N  
ATOM    489  CA  PHE A 282      22.371  12.465  13.033  1.00 51.33           C  
ATOM    490  C   PHE A 282      21.197  13.133  13.739  1.00 50.52           C  
ATOM    491  O   PHE A 282      20.374  12.462  14.357  1.00 49.38           O  
ATOM    492  CB  PHE A 282      23.662  12.729  13.810  1.00 49.80           C  
ATOM    493  CG  PHE A 282      23.635  12.206  15.220  1.00 54.83           C  
ATOM    494  CD1 PHE A 282      23.227  13.016  16.268  1.00 57.75           C  
ATOM    495  CD2 PHE A 282      24.009  10.900  15.496  1.00 54.12           C  
ATOM    496  CE1 PHE A 282      23.200  12.537  17.564  1.00 60.02           C  
ATOM    497  CE2 PHE A 282      23.984  10.413  16.789  1.00 54.99           C  
ATOM    498  CZ  PHE A 282      23.577  11.233  17.825  1.00 59.26           C  
ATOM    499  N   GLN A 283      21.130  14.457  13.650  1.00 51.30           N  
ATOM    500  CA  GLN A 283      20.044  15.209  14.267  1.00 52.17           C  
ATOM    501  C   GLN A 283      18.694  14.714  13.763  1.00 48.57           C  
ATOM    502  O   GLN A 283      17.754  14.550  14.539  1.00 54.47           O  
ATOM    503  CB  GLN A 283      20.196  16.706  13.987  1.00 59.68           C  
ATOM    504  CG  GLN A 283      21.492  17.326  14.502  1.00 66.56           C  
ATOM    505  CD  GLN A 283      21.473  17.591  15.999  1.00 71.79           C  
ATOM    506  OE1 GLN A 283      22.034  18.581  16.472  1.00 74.29           O  
ATOM    507  NE2 GLN A 283      20.826  16.707  16.751  1.00 71.28           N  
ATOM    508  N   GLY A 284      18.604  14.475  12.458  1.00 47.82           N  
ATOM    509  CA  GLY A 284      17.387  13.961  11.859  1.00 48.61           C  
ATOM    510  C   GLY A 284      17.005  12.608  12.425  1.00 52.77           C  
ATOM    511  O   GLY A 284      15.860  12.395  12.825  1.00 49.30           O  
ATOM    512  N   CYS A 285      17.970  11.692  12.463  1.00 54.03           N  
ATOM    513  CA  CYS A 285      17.746  10.357  13.007  1.00 52.52           C  
ATOM    514  C   CYS A 285      17.319  10.437  14.465  1.00 54.21           C  
ATOM    515  O   CYS A 285      16.558   9.598  14.948  1.00 53.00           O  
ATOM    516  CB  CYS A 285      19.015   9.511  12.897  1.00 57.19           C  
ATOM    517  SG  CYS A 285      19.706   9.400  11.234  1.00 82.67           S  
ATOM    518  N   GLN A 286      17.823  11.451  15.161  1.00 55.02           N  
ATOM    519  CA  GLN A 286      17.511  11.647  16.570  1.00 58.11           C  
ATOM    520  C   GLN A 286      16.042  12.010  16.770  1.00 53.31           C  
ATOM    521  O   GLN A 286      15.399  11.535  17.707  1.00 54.38           O  
ATOM    522  CB  GLN A 286      18.415  12.724  17.170  1.00 64.97           C  
ATOM    523  CG  GLN A 286      18.099  13.060  18.612  1.00 73.68           C  
ATOM    524  CD  GLN A 286      19.071  14.060  19.206  1.00 80.25           C  
ATOM    525  OE1 GLN A 286      20.283  13.837  19.218  1.00 79.09           O  
ATOM    526  NE2 GLN A 286      18.541  15.171  19.707  1.00 83.73           N  
ATOM    527  N   PHE A 287      15.514  12.855  15.890  1.00 50.71           N  
ATOM    528  CA APHE A 287      14.110  13.251  15.949  0.59 53.00           C  
ATOM    529  CA BPHE A 287      14.114  13.248  15.970  0.41 53.02           C  
ATOM    530  C   PHE A 287      13.199  12.053  15.719  1.00 49.62           C  
ATOM    531  O   PHE A 287      12.145  11.929  16.338  1.00 51.18           O  
ATOM    532  CB APHE A 287      13.806  14.335  14.912  0.59 56.31           C  
ATOM    533  CB BPHE A 287      13.808  14.382  14.989  0.41 56.35           C  
ATOM    534  CG APHE A 287      12.338  14.599  14.726  0.59 59.31           C  
ATOM    535  CG BPHE A 287      14.373  15.711  15.406  0.41 58.23           C  
ATOM    536  CD1APHE A 287      11.675  15.504  15.537  0.59 64.38           C  
ATOM    537  CD1BPHE A 287      13.881  16.366  16.522  0.41 60.38           C  
ATOM    538  CD2APHE A 287      11.619  13.936  13.743  0.59 59.97           C  
ATOM    539  CD2BPHE A 287      15.390  16.307  14.679  0.41 59.79           C  
ATOM    540  CE1APHE A 287      10.324  15.747  15.369  0.59 66.51           C  
ATOM    541  CE1BPHE A 287      14.397  17.590  16.910  0.41 64.07           C  
ATOM    542  CE2APHE A 287      10.269  14.173  13.572  0.59 60.20           C  
ATOM    543  CE2BPHE A 287      15.909  17.531  15.061  0.41 62.93           C  
ATOM    544  CZ APHE A 287       9.621  15.079  14.386  0.59 62.96           C  
ATOM    545  CZ BPHE A 287      15.411  18.173  16.177  0.41 64.81           C  
ATOM    546  N   ARG A 288      13.613  11.173  14.816  1.00 46.33           N  
ATOM    547  CA  ARG A 288      12.845   9.972  14.525  1.00 45.78           C  
ATOM    548  C   ARG A 288      12.839   9.036  15.735  1.00 43.55           C  
ATOM    549  O   ARG A 288      11.809   8.457  16.075  1.00 42.08           O  
ATOM    550  CB  ARG A 288      13.399   9.269  13.282  1.00 48.24           C  
ATOM    551  CG  ARG A 288      12.789   7.907  13.002  1.00 48.68           C  
ATOM    552  CD  ARG A 288      11.267   7.936  13.065  1.00 50.98           C  
ATOM    553  NE  ARG A 288      10.719   6.601  13.290  1.00 48.50           N  
ATOM    554  CZ  ARG A 288       9.479   6.353  13.699  1.00 50.47           C  
ATOM    555  NH1 ARG A 288       8.640   7.354  13.934  1.00 47.10           N  
ATOM    556  NH2 ARG A 288       9.079   5.100  13.879  1.00 51.86           N  
ATOM    557  N   SER A 289      13.990   8.901  16.388  1.00 42.52           N  
ATOM    558  CA  SER A 289      14.086   8.098  17.603  1.00 42.07           C  
ATOM    559  C   SER A 289      13.116   8.621  18.659  1.00 39.79           C  
ATOM    560  O   SER A 289      12.403   7.851  19.298  1.00 41.71           O  
ATOM    561  CB  SER A 289      15.514   8.109  18.152  1.00 47.47           C  
ATOM    562  OG  SER A 289      16.391   7.381  17.313  1.00 58.60           O  
ATOM    563  N   VAL A 290      13.098   9.937  18.836  1.00 40.54           N  
ATOM    564  CA  VAL A 290      12.165  10.574  19.757  1.00 42.09           C  
ATOM    565  C   VAL A 290      10.730  10.247  19.375  1.00 41.85           C  
ATOM    566  O   VAL A 290       9.909   9.919  20.231  1.00 39.33           O  
ATOM    567  CB  VAL A 290      12.347  12.098  19.772  1.00 45.61           C  
ATOM    568  CG1 VAL A 290      11.084  12.792  20.284  1.00 46.95           C  
ATOM    569  CG2 VAL A 290      13.557  12.468  20.616  1.00 43.92           C  
ATOM    570  N   GLU A 291      10.437  10.327  18.082  1.00 40.63           N  
ATOM    571  CA  GLU A 291       9.104  10.014  17.586  1.00 43.20           C  
ATOM    572  C   GLU A 291       8.756   8.554  17.866  1.00 43.00           C  
ATOM    573  O   GLU A 291       7.632   8.238  18.262  1.00 45.00           O  
ATOM    574  CB  GLU A 291       9.012  10.306  16.088  1.00 44.68           C  
ATOM    575  CG  GLU A 291       7.593  10.413  15.559  1.00 56.43           C  
ATOM    576  CD  GLU A 291       7.544  10.772  14.079  1.00 66.37           C  
ATOM    577  OE1 GLU A 291       8.421  10.309  13.314  1.00 63.36           O  
ATOM    578  OE2 GLU A 291       6.621  11.517  13.680  1.00 70.48           O  
ATOM    579  N   ALA A 292       9.729   7.669  17.662  1.00 35.51           N  
ATOM    580  CA  ALA A 292       9.541   6.242  17.912  1.00 36.39           C  
ATOM    581  C   ALA A 292       9.257   5.957  19.388  1.00 36.71           C  
ATOM    582  O   ALA A 292       8.385   5.156  19.721  1.00 38.55           O  
ATOM    583  CB  ALA A 292      10.756   5.452  17.435  1.00 32.66           C  
ATOM    584  N   VAL A 293       9.994   6.614  20.274  1.00 35.24           N  
ATOM    585  CA  VAL A 293       9.779   6.428  21.704  1.00 35.61           C  
ATOM    586  C   VAL A 293       8.342   6.786  22.075  1.00 36.70           C  
ATOM    587  O   VAL A 293       7.734   6.152  22.936  1.00 42.12           O  
ATOM    588  CB  VAL A 293      10.755   7.271  22.535  1.00 42.78           C  
ATOM    589  CG1 VAL A 293      10.412   7.180  24.021  1.00 45.57           C  
ATOM    590  CG2 VAL A 293      12.184   6.820  22.277  1.00 42.77           C  
ATOM    591  N   GLN A 294       7.802   7.797  21.406  1.00 37.82           N  
ATOM    592  CA  GLN A 294       6.426   8.221  21.632  1.00 40.15           C  
ATOM    593  C   GLN A 294       5.453   7.136  21.187  1.00 37.08           C  
ATOM    594  O   GLN A 294       4.506   6.814  21.899  1.00 38.94           O  
ATOM    595  CB  GLN A 294       6.145   9.535  20.899  1.00 39.50           C  
ATOM    596  CG  GLN A 294       7.036  10.680  21.356  1.00 47.70           C  
ATOM    597  CD  GLN A 294       6.815  11.957  20.570  1.00 56.81           C  
ATOM    598  OE1 GLN A 294       7.114  13.049  21.050  1.00 62.90           O  
ATOM    599  NE2 GLN A 294       6.286  11.829  19.358  1.00 59.03           N  
ATOM    600  N   GLU A 295       5.700   6.570  20.010  1.00 34.73           N  
ATOM    601  CA  GLU A 295       4.878   5.478  19.495  1.00 34.45           C  
ATOM    602  C   GLU A 295       4.956   4.247  20.401  1.00 34.03           C  
ATOM    603  O   GLU A 295       3.943   3.623  20.710  1.00 34.78           O  
ATOM    604  CB  GLU A 295       5.308   5.112  18.071  1.00 35.62           C  
ATOM    605  CG  GLU A 295       5.060   6.208  17.043  1.00 38.93           C  
ATOM    606  CD  GLU A 295       5.896   6.033  15.788  1.00 44.40           C  
ATOM    607  OE1 GLU A 295       6.435   4.927  15.572  1.00 45.56           O  
ATOM    608  OE2 GLU A 295       6.025   7.006  15.020  1.00 47.10           O  
ATOM    609  N   ILE A 296       6.166   3.899  20.821  1.00 35.57           N  
ATOM    610  CA  ILE A 296       6.367   2.736  21.680  1.00 34.50           C  
ATOM    611  C   ILE A 296       5.682   2.929  23.035  1.00 36.85           C  
ATOM    612  O   ILE A 296       5.065   2.004  23.571  1.00 37.98           O  
ATOM    613  CB  ILE A 296       7.862   2.458  21.874  1.00 36.34           C  
ATOM    614  CG1 ILE A 296       8.499   2.055  20.538  1.00 35.64           C  
ATOM    615  CG2 ILE A 296       8.078   1.397  22.945  1.00 39.15           C  
ATOM    616  CD1 ILE A 296      10.014   2.174  20.524  1.00 38.00           C  
ATOM    617  N   THR A 297       5.786   4.136  23.583  1.00 37.14           N  
ATOM    618  CA  THR A 297       5.123   4.455  24.842  1.00 41.71           C  
ATOM    619  C   THR A 297       3.614   4.240  24.724  1.00 41.76           C  
ATOM    620  O   THR A 297       2.980   3.673  25.614  1.00 37.99           O  
ATOM    621  CB  THR A 297       5.392   5.908  25.275  1.00 41.69           C  
ATOM    622  OG1 THR A 297       6.787   6.080  25.558  1.00 42.58           O  
ATOM    623  CG2 THR A 297       4.586   6.246  26.523  1.00 38.88           C  
ATOM    624  N   GLU A 298       3.045   4.692  23.612  1.00 38.63           N  
ATOM    625  CA  GLU A 298       1.615   4.539  23.371  1.00 42.83           C  
ATOM    626  C   GLU A 298       1.224   3.063  23.280  1.00 38.29           C  
ATOM    627  O   GLU A 298       0.215   2.640  23.842  1.00 35.75           O  
ATOM    628  CB  GLU A 298       1.212   5.282  22.098  1.00 49.00           C  
ATOM    629  CG  GLU A 298      -0.282   5.384  21.884  1.00 59.72           C  
ATOM    630  CD  GLU A 298      -0.635   6.204  20.660  1.00 69.16           C  
ATOM    631  OE1 GLU A 298       0.203   7.021  20.226  1.00 71.68           O  
ATOM    632  OE2 GLU A 298      -1.752   6.033  20.132  1.00 74.35           O  
ATOM    633  N   TYR A 299       2.032   2.282  22.570  1.00 36.80           N  
ATOM    634  CA  TYR A 299       1.792   0.848  22.448  1.00 34.55           C  
ATOM    635  C   TYR A 299       1.849   0.147  23.803  1.00 35.58           C  
ATOM    636  O   TYR A 299       1.034  -0.726  24.095  1.00 40.42           O  
ATOM    637  CB  TYR A 299       2.806   0.207  21.497  1.00 32.78           C  
ATOM    638  CG  TYR A 299       2.613  -1.284  21.337  1.00 36.03           C  
ATOM    639  CD1 TYR A 299       1.454  -1.793  20.769  1.00 35.42           C  
ATOM    640  CD2 TYR A 299       3.586  -2.184  21.759  1.00 35.37           C  
ATOM    641  CE1 TYR A 299       1.264  -3.155  20.626  1.00 34.91           C  
ATOM    642  CE2 TYR A 299       3.407  -3.551  21.616  1.00 35.71           C  
ATOM    643  CZ  TYR A 299       2.244  -4.029  21.049  1.00 35.63           C  
ATOM    644  OH  TYR A 299       2.053  -5.383  20.894  1.00 38.56           O  
ATOM    645  N   ALA A 300       2.822   0.527  24.623  1.00 34.97           N  
ATOM    646  CA  ALA A 300       3.031  -0.122  25.913  1.00 36.70           C  
ATOM    647  C   ALA A 300       1.783  -0.053  26.785  1.00 38.44           C  
ATOM    648  O   ALA A 300       1.420  -1.025  27.444  1.00 39.82           O  
ATOM    649  CB  ALA A 300       4.220   0.496  26.636  1.00 34.51           C  
ATOM    650  N   LYS A 301       1.125   1.099  26.779  1.00 40.80           N  
ATOM    651  CA  LYS A 301      -0.067   1.300  27.596  1.00 43.37           C  
ATOM    652  C   LYS A 301      -1.192   0.333  27.226  1.00 43.63           C  
ATOM    653  O   LYS A 301      -2.089   0.079  28.030  1.00 45.66           O  
ATOM    654  CB  LYS A 301      -0.545   2.751  27.487  1.00 44.70           C  
ATOM    655  CG  LYS A 301       0.505   3.764  27.921  1.00 51.77           C  
ATOM    656  CD  LYS A 301       0.303   5.116  27.250  1.00 56.53           C  
ATOM    657  CE  LYS A 301      -0.799   5.920  27.918  1.00 60.51           C  
ATOM    658  NZ  LYS A 301      -0.945   7.270  27.302  1.00 61.33           N  
ATOM    659  N   SER A 302      -1.138  -0.209  26.013  1.00 39.42           N  
ATOM    660  CA  SER A 302      -2.163  -1.134  25.537  1.00 39.02           C  
ATOM    661  C   SER A 302      -1.885  -2.568  25.987  1.00 39.76           C  
ATOM    662  O   SER A 302      -2.770  -3.421  25.960  1.00 40.87           O  
ATOM    663  CB  SER A 302      -2.263  -1.085  24.011  1.00 41.55           C  
ATOM    664  OG  SER A 302      -1.291  -1.933  23.418  1.00 45.33           O  
ATOM    665  N   ILE A 303      -0.650  -2.842  26.386  1.00 38.50           N  
ATOM    666  CA  ILE A 303      -0.311  -4.168  26.885  1.00 40.41           C  
ATOM    667  C   ILE A 303      -1.002  -4.385  28.232  1.00 44.81           C  
ATOM    668  O   ILE A 303      -0.729  -3.669  29.195  1.00 46.08           O  
ATOM    669  CB  ILE A 303       1.208  -4.345  27.034  1.00 37.34           C  
ATOM    670  CG1 ILE A 303       1.919  -4.007  25.720  1.00 35.56           C  
ATOM    671  CG2 ILE A 303       1.535  -5.762  27.477  1.00 35.10           C  
ATOM    672  CD1 ILE A 303       3.432  -3.994  25.835  1.00 35.65           C  
ATOM    673  N   PRO A 304      -1.912  -5.370  28.298  1.00 43.38           N  
ATOM    674  CA  PRO A 304      -2.746  -5.561  29.490  1.00 44.59           C  
ATOM    675  C   PRO A 304      -1.894  -5.750  30.737  1.00 43.73           C  
ATOM    676  O   PRO A 304      -1.008  -6.607  30.754  1.00 42.11           O  
ATOM    677  CB  PRO A 304      -3.521  -6.844  29.173  1.00 45.54           C  
ATOM    678  CG  PRO A 304      -3.509  -6.938  27.679  1.00 46.30           C  
ATOM    679  CD  PRO A 304      -2.171  -6.394  27.273  1.00 41.72           C  
ATOM    680  N   GLY A 305      -2.156  -4.944  31.761  1.00 38.89           N  
ATOM    681  CA  GLY A 305      -1.421  -5.030  33.007  1.00 38.86           C  
ATOM    682  C   GLY A 305      -0.343  -3.972  33.141  1.00 39.49           C  
ATOM    683  O   GLY A 305       0.038  -3.612  34.250  1.00 42.86           O  
ATOM    684  N   PHE A 306       0.148  -3.461  32.015  1.00 38.72           N  
ATOM    685  CA  PHE A 306       1.232  -2.480  32.048  1.00 38.53           C  
ATOM    686  C   PHE A 306       0.894  -1.221  32.856  1.00 40.63           C  
ATOM    687  O   PHE A 306       1.643  -0.834  33.754  1.00 40.68           O  
ATOM    688  CB  PHE A 306       1.677  -2.092  30.634  1.00 34.81           C  
ATOM    689  CG  PHE A 306       2.823  -1.123  30.616  1.00 37.63           C  
ATOM    690  CD1 PHE A 306       4.131  -1.576  30.681  1.00 42.24           C  
ATOM    691  CD2 PHE A 306       2.595   0.242  30.558  1.00 41.03           C  
ATOM    692  CE1 PHE A 306       5.190  -0.688  30.674  1.00 41.73           C  
ATOM    693  CE2 PHE A 306       3.648   1.136  30.546  1.00 41.96           C  
ATOM    694  CZ  PHE A 306       4.948   0.670  30.607  1.00 42.86           C  
ATOM    695  N   VAL A 307      -0.224  -0.577  32.530  1.00 38.24           N  
ATOM    696  CA  VAL A 307      -0.596   0.669  33.197  1.00 38.42           C  
ATOM    697  C   VAL A 307      -1.000   0.446  34.651  1.00 41.67           C  
ATOM    698  O   VAL A 307      -1.131   1.400  35.415  1.00 44.71           O  
ATOM    699  CB  VAL A 307      -1.728   1.425  32.453  1.00 47.70           C  
ATOM    700  CG1 VAL A 307      -1.261   1.850  31.070  1.00 47.10           C  
ATOM    701  CG2 VAL A 307      -2.990   0.575  32.366  1.00 42.15           C  
ATOM    702  N   ASN A 308      -1.186  -0.816  35.028  1.00 38.94           N  
ATOM    703  CA  ASN A 308      -1.576  -1.162  36.392  1.00 40.96           C  
ATOM    704  C   ASN A 308      -0.351  -1.361  37.283  1.00 45.62           C  
ATOM    705  O   ASN A 308      -0.465  -1.486  38.504  1.00 40.49           O  
ATOM    706  CB  ASN A 308      -2.450  -2.421  36.399  1.00 42.41           C  
ATOM    707  CG  ASN A 308      -3.659  -2.301  35.480  1.00 48.41           C  
ATOM    708  OD1 ASN A 308      -3.791  -3.045  34.506  1.00 45.78           O  
ATOM    709  ND2 ASN A 308      -4.541  -1.353  35.781  1.00 46.73           N  
ATOM    710  N   LEU A 309       0.821  -1.387  36.658  1.00 43.68           N  
ATOM    711  CA  LEU A 309       2.076  -1.567  37.374  1.00 46.52           C  
ATOM    712  C   LEU A 309       2.473  -0.283  38.084  1.00 45.44           C  
ATOM    713  O   LEU A 309       2.024   0.805  37.720  1.00 44.10           O  
ATOM    714  CB  LEU A 309       3.188  -1.973  36.402  1.00 46.31           C  
ATOM    715  CG  LEU A 309       3.040  -3.304  35.660  1.00 41.98           C  
ATOM    716  CD1 LEU A 309       4.095  -3.438  34.560  1.00 40.37           C  
ATOM    717  CD2 LEU A 309       3.126  -4.468  36.637  1.00 45.91           C  
ATOM    718  N   ASP A 310       3.328  -0.421  39.093  1.00 46.73           N  
ATOM    719  CA  ASP A 310       3.904   0.719  39.791  1.00 49.60           C  
ATOM    720  C   ASP A 310       4.479   1.698  38.777  1.00 48.25           C  
ATOM    721  O   ASP A 310       5.158   1.298  37.832  1.00 47.99           O  
ATOM    722  CB  ASP A 310       4.996   0.243  40.752  1.00 54.91           C  
ATOM    723  CG  ASP A 310       5.559   1.365  41.603  1.00 60.78           C  
ATOM    724  OD1 ASP A 310       6.118   2.328  41.038  1.00 60.93           O  
ATOM    725  OD2 ASP A 310       5.454   1.276  42.845  1.00 66.68           O  
ATOM    726  N   LEU A 311       4.202   2.982  38.975  1.00 50.99           N  
ATOM    727  CA  LEU A 311       4.563   4.006  38.000  1.00 52.22           C  
ATOM    728  C   LEU A 311       6.072   4.061  37.769  1.00 51.87           C  
ATOM    729  O   LEU A 311       6.529   4.311  36.653  1.00 48.23           O  
ATOM    730  CB  LEU A 311       4.049   5.374  38.451  1.00 56.81           C  
ATOM    731  CG  LEU A 311       3.395   6.254  37.383  1.00 58.26           C  
ATOM    732  CD1 LEU A 311       3.182   7.662  37.916  1.00 59.92           C  
ATOM    733  CD2 LEU A 311       4.211   6.282  36.101  1.00 55.46           C  
ATOM    734  N   ASN A 312       6.839   3.836  38.831  1.00 49.34           N  
ATOM    735  CA  ASN A 312       8.293   3.825  38.733  1.00 52.07           C  
ATOM    736  C   ASN A 312       8.783   2.707  37.826  1.00 50.59           C  
ATOM    737  O   ASN A 312       9.732   2.885  37.065  1.00 48.96           O  
ATOM    738  CB  ASN A 312       8.924   3.687  40.117  1.00 55.74           C  
ATOM    739  CG  ASN A 312       8.476   4.775  41.070  1.00 63.72           C  
ATOM    740  OD1 ASN A 312       8.565   5.962  40.763  1.00 67.24           O  
ATOM    741  ND2 ASN A 312       7.992   4.373  42.239  1.00 66.66           N  
ATOM    742  N   ASP A 313       8.127   1.554  37.911  1.00 49.07           N  
ATOM    743  CA  ASP A 313       8.482   0.411  37.080  1.00 47.40           C  
ATOM    744  C   ASP A 313       8.062   0.616  35.624  1.00 47.08           C  
ATOM    745  O   ASP A 313       8.784   0.226  34.709  1.00 45.36           O  
ATOM    746  CB  ASP A 313       7.874  -0.874  37.644  1.00 43.20           C  
ATOM    747  CG  ASP A 313       8.547  -1.322  38.935  1.00 49.23           C  
ATOM    748  OD1 ASP A 313       9.546  -0.684  39.345  1.00 45.76           O  
ATOM    749  OD2 ASP A 313       8.076  -2.315  39.535  1.00 49.80           O  
ATOM    750  N   GLN A 314       6.897   1.222  35.411  1.00 45.39           N  
ATOM    751  CA  GLN A 314       6.469   1.567  34.059  1.00 43.08           C  
ATOM    752  C   GLN A 314       7.558   2.385  33.369  1.00 45.76           C  
ATOM    753  O   GLN A 314       7.958   2.087  32.243  1.00 42.22           O  
ATOM    754  CB  GLN A 314       5.159   2.363  34.087  1.00 43.65           C  
ATOM    755  CG  GLN A 314       3.944   1.585  34.581  1.00 43.13           C  
ATOM    756  CD  GLN A 314       2.659   2.394  34.503  1.00 45.45           C  
ATOM    757  OE1 GLN A 314       1.801   2.306  35.382  1.00 50.38           O  
ATOM    758  NE2 GLN A 314       2.523   3.191  33.450  1.00 37.17           N  
ATOM    759  N   VAL A 315       8.032   3.418  34.059  1.00 51.36           N  
ATOM    760  CA  VAL A 315       9.093   4.275  33.545  1.00 51.78           C  
ATOM    761  C   VAL A 315      10.372   3.481  33.280  1.00 50.31           C  
ATOM    762  O   VAL A 315      11.000   3.631  32.233  1.00 48.30           O  
ATOM    763  CB  VAL A 315       9.408   5.424  34.526  1.00 53.38           C  
ATOM    764  CG1 VAL A 315      10.643   6.192  34.071  1.00 57.70           C  
ATOM    765  CG2 VAL A 315       8.209   6.354  34.660  1.00 46.64           C  
ATOM    766  N   THR A 316      10.751   2.635  34.233  1.00 49.46           N  
ATOM    767  CA  THR A 316      11.961   1.829  34.100  1.00 47.65           C  
ATOM    768  C   THR A 316      11.874   0.845  32.935  1.00 44.97           C  
ATOM    769  O   THR A 316      12.843   0.653  32.201  1.00 48.06           O  
ATOM    770  CB  THR A 316      12.270   1.067  35.399  1.00 49.24           C  
ATOM    771  OG1 THR A 316      12.650   2.001  36.415  1.00 51.75           O  
ATOM    772  CG2 THR A 316      13.404   0.072  35.179  1.00 49.06           C  
ATOM    773  N   LEU A 317      10.712   0.228  32.764  1.00 44.68           N  
ATOM    774  CA  LEU A 317      10.493  -0.692  31.651  1.00 48.11           C  
ATOM    775  C   LEU A 317      10.653   0.008  30.299  1.00 45.60           C  
ATOM    776  O   LEU A 317      11.228  -0.548  29.361  1.00 42.67           O  
ATOM    777  CB  LEU A 317       9.112  -1.342  31.759  1.00 45.52           C  
ATOM    778  CG  LEU A 317       8.936  -2.326  32.918  1.00 45.01           C  
ATOM    779  CD1 LEU A 317       7.587  -3.018  32.825  1.00 44.89           C  
ATOM    780  CD2 LEU A 317      10.067  -3.351  32.931  1.00 44.29           C  
ATOM    781  N   LEU A 318      10.151   1.233  30.207  1.00 44.10           N  
ATOM    782  CA  LEU A 318      10.264   2.012  28.979  1.00 42.81           C  
ATOM    783  C   LEU A 318      11.697   2.498  28.772  1.00 42.50           C  
ATOM    784  O   LEU A 318      12.207   2.506  27.655  1.00 45.29           O  
ATOM    785  CB  LEU A 318       9.296   3.197  29.011  1.00 41.56           C  
ATOM    786  CG  LEU A 318       7.828   2.876  28.716  1.00 43.12           C  
ATOM    787  CD1 LEU A 318       6.931   4.051  29.074  1.00 40.22           C  
ATOM    788  CD2 LEU A 318       7.646   2.484  27.255  1.00 38.77           C  
ATOM    789  N   LYS A 319      12.342   2.895  29.863  1.00 44.31           N  
ATOM    790  CA  LYS A 319      13.705   3.413  29.817  1.00 48.53           C  
ATOM    791  C   LYS A 319      14.674   2.440  29.145  1.00 47.84           C  
ATOM    792  O   LYS A 319      15.449   2.822  28.267  1.00 43.09           O  
ATOM    793  CB  LYS A 319      14.178   3.729  31.238  1.00 56.83           C  
ATOM    794  CG  LYS A 319      15.572   4.327  31.332  1.00 62.23           C  
ATOM    795  CD  LYS A 319      15.862   4.801  32.749  1.00 65.89           C  
ATOM    796  CE  LYS A 319      17.153   5.600  32.823  1.00 66.63           C  
ATOM    797  NZ  LYS A 319      18.351   4.731  32.698  1.00 70.74           N  
ATOM    798  N   TYR A 320      14.621   1.179  29.562  1.00 46.42           N  
ATOM    799  CA  TYR A 320      15.548   0.167  29.072  1.00 46.34           C  
ATOM    800  C   TYR A 320      15.009  -0.577  27.855  1.00 48.67           C  
ATOM    801  O   TYR A 320      15.762  -1.226  27.134  1.00 56.19           O  
ATOM    802  CB  TYR A 320      15.867  -0.831  30.185  1.00 44.55           C  
ATOM    803  CG  TYR A 320      16.710  -0.253  31.296  1.00 49.27           C  
ATOM    804  CD1 TYR A 320      16.131   0.460  32.335  1.00 52.05           C  
ATOM    805  CD2 TYR A 320      18.088  -0.420  31.304  1.00 57.04           C  
ATOM    806  CE1 TYR A 320      16.900   0.992  33.355  1.00 60.65           C  
ATOM    807  CE2 TYR A 320      18.867   0.106  32.319  1.00 62.66           C  
ATOM    808  CZ  TYR A 320      18.269   0.811  33.341  1.00 64.86           C  
ATOM    809  OH  TYR A 320      19.040   1.338  34.351  1.00 69.67           O  
ATOM    810  N   GLY A 321      13.705  -0.477  27.624  1.00 45.55           N  
ATOM    811  CA  GLY A 321      13.072  -1.233  26.560  1.00 40.47           C  
ATOM    812  C   GLY A 321      12.982  -0.553  25.205  1.00 40.59           C  
ATOM    813  O   GLY A 321      13.008  -1.226  24.175  1.00 40.74           O  
ATOM    814  N   VAL A 322      12.877   0.773  25.191  1.00 40.86           N  
ATOM    815  CA  VAL A 322      12.600   1.486  23.943  1.00 43.20           C  
ATOM    816  C   VAL A 322      13.626   1.238  22.838  1.00 43.53           C  
ATOM    817  O   VAL A 322      13.259   1.062  21.679  1.00 42.33           O  
ATOM    818  CB  VAL A 322      12.434   3.008  24.156  1.00 43.58           C  
ATOM    819  CG1 VAL A 322      11.133   3.295  24.882  1.00 43.64           C  
ATOM    820  CG2 VAL A 322      13.619   3.574  24.919  1.00 44.29           C  
ATOM    821  N   HIS A 323      14.906   1.221  23.188  1.00 41.53           N  
ATOM    822  CA  HIS A 323      15.943   1.077  22.170  1.00 47.72           C  
ATOM    823  C   HIS A 323      16.046  -0.328  21.575  1.00 45.38           C  
ATOM    824  O   HIS A 323      16.345  -0.480  20.391  1.00 46.23           O  
ATOM    825  CB  HIS A 323      17.297   1.570  22.684  1.00 53.18           C  
ATOM    826  CG  HIS A 323      17.442   3.058  22.639  1.00 59.18           C  
ATOM    827  ND1 HIS A 323      17.312   3.854  23.757  1.00 65.22           N  
ATOM    828  CD2 HIS A 323      17.679   3.898  21.604  1.00 58.26           C  
ATOM    829  CE1 HIS A 323      17.474   5.119  23.414  1.00 67.50           C  
ATOM    830  NE2 HIS A 323      17.698   5.173  22.113  1.00 63.80           N  
ATOM    831  N   GLU A 324      15.794  -1.349  22.388  1.00 41.79           N  
ATOM    832  CA  GLU A 324      15.785  -2.719  21.886  1.00 38.40           C  
ATOM    833  C   GLU A 324      14.642  -2.877  20.887  1.00 39.30           C  
ATOM    834  O   GLU A 324      14.759  -3.588  19.890  1.00 39.08           O  
ATOM    835  CB  GLU A 324      15.654  -3.724  23.038  1.00 37.72           C  
ATOM    836  CG  GLU A 324      16.842  -3.719  23.994  1.00 37.42           C  
ATOM    837  CD  GLU A 324      16.624  -4.585  25.226  1.00 43.44           C  
ATOM    838  OE1 GLU A 324      15.550  -5.209  25.341  1.00 48.56           O  
ATOM    839  OE2 GLU A 324      17.530  -4.642  26.083  1.00 44.23           O  
ATOM    840  N   ILE A 325      13.539  -2.192  21.160  1.00 36.07           N  
ATOM    841  CA  ILE A 325      12.387  -2.213  20.272  1.00 37.64           C  
ATOM    842  C   ILE A 325      12.646  -1.385  19.013  1.00 34.32           C  
ATOM    843  O   ILE A 325      12.267  -1.779  17.914  1.00 39.59           O  
ATOM    844  CB  ILE A 325      11.127  -1.692  20.990  1.00 36.08           C  
ATOM    845  CG1 ILE A 325      10.722  -2.656  22.107  1.00 38.25           C  
ATOM    846  CG2 ILE A 325       9.985  -1.503  20.004  1.00 29.55           C  
ATOM    847  CD1 ILE A 325       9.608  -2.133  22.974  1.00 41.25           C  
ATOM    848  N   ILE A 326      13.300  -0.241  19.181  1.00 31.80           N  
ATOM    849  CA  ILE A 326      13.626   0.624  18.052  1.00 37.45           C  
ATOM    850  C   ILE A 326      14.455  -0.097  16.987  1.00 36.87           C  
ATOM    851  O   ILE A 326      14.187   0.030  15.795  1.00 38.61           O  
ATOM    852  CB  ILE A 326      14.366   1.898  18.515  1.00 40.33           C  
ATOM    853  CG1 ILE A 326      13.374   2.900  19.111  1.00 38.50           C  
ATOM    854  CG2 ILE A 326      15.133   2.531  17.358  1.00 40.54           C  
ATOM    855  CD1 ILE A 326      14.023   4.158  19.635  1.00 42.50           C  
ATOM    856  N   TYR A 327      15.456  -0.857  17.415  1.00 35.47           N  
ATOM    857  CA  TYR A 327      16.308  -1.569  16.466  1.00 40.25           C  
ATOM    858  C   TYR A 327      15.620  -2.816  15.921  1.00 40.32           C  
ATOM    859  O   TYR A 327      15.931  -3.274  14.825  1.00 40.86           O  
ATOM    860  CB  TYR A 327      17.648  -1.939  17.102  1.00 43.70           C  
ATOM    861  CG  TYR A 327      18.345  -0.773  17.758  1.00 52.60           C  
ATOM    862  CD1 TYR A 327      18.488   0.440  17.093  1.00 54.29           C  
ATOM    863  CD2 TYR A 327      18.870  -0.885  19.038  1.00 60.29           C  
ATOM    864  CE1 TYR A 327      19.125   1.513  17.693  1.00 57.59           C  
ATOM    865  CE2 TYR A 327      19.511   0.180  19.645  1.00 63.24           C  
ATOM    866  CZ  TYR A 327      19.638   1.376  18.968  1.00 64.10           C  
ATOM    867  OH  TYR A 327      20.277   2.437  19.569  1.00 69.58           O  
ATOM    868  N   THR A 328      14.689  -3.364  16.694  1.00 38.28           N  
ATOM    869  CA  THR A 328      13.902  -4.505  16.249  1.00 36.70           C  
ATOM    870  C   THR A 328      13.005  -4.090  15.090  1.00 38.32           C  
ATOM    871  O   THR A 328      12.922  -4.776  14.070  1.00 41.12           O  
ATOM    872  CB  THR A 328      13.020  -5.052  17.387  1.00 37.31           C  
ATOM    873  OG1 THR A 328      13.841  -5.714  18.360  1.00 37.73           O  
ATOM    874  CG2 THR A 328      11.995  -6.031  16.842  1.00 32.29           C  
ATOM    875  N   MET A 329      12.336  -2.955  15.254  1.00 35.88           N  
ATOM    876  CA  MET A 329      11.408  -2.459  14.247  1.00 36.46           C  
ATOM    877  C   MET A 329      12.137  -1.780  13.091  1.00 33.53           C  
ATOM    878  O   MET A 329      11.649  -1.776  11.966  1.00 35.69           O  
ATOM    879  CB  MET A 329      10.386  -1.518  14.885  1.00 37.34           C  
ATOM    880  CG  MET A 329       9.698  -2.134  16.091  1.00 37.04           C  
ATOM    881  SD  MET A 329       8.294  -1.183  16.687  1.00 42.78           S  
ATOM    882  CE  MET A 329       7.235  -1.223  15.247  1.00 45.36           C  
ATOM    883  N   LEU A 330      13.311  -1.222  13.371  1.00 39.16           N  
ATOM    884  CA  LEU A 330      14.143  -0.641  12.321  1.00 39.63           C  
ATOM    885  C   LEU A 330      14.510  -1.694  11.278  1.00 38.41           C  
ATOM    886  O   LEU A 330      14.665  -1.384  10.096  1.00 36.30           O  
ATOM    887  CB  LEU A 330      15.414  -0.031  12.912  1.00 39.60           C  
ATOM    888  CG  LEU A 330      16.295   0.774  11.952  1.00 41.50           C  
ATOM    889  CD1 LEU A 330      15.513   1.931  11.343  1.00 41.85           C  
ATOM    890  CD2 LEU A 330      17.526   1.285  12.677  1.00 45.00           C  
ATOM    891  N   ALA A 331      14.648  -2.939  11.726  1.00 35.59           N  
ATOM    892  CA  ALA A 331      14.925  -4.053  10.827  1.00 35.64           C  
ATOM    893  C   ALA A 331      13.845  -4.157   9.754  1.00 35.15           C  
ATOM    894  O   ALA A 331      14.130  -4.475   8.599  1.00 34.45           O  
ATOM    895  CB  ALA A 331      15.025  -5.357  11.607  1.00 34.30           C  
ATOM    896  N   SER A 332      12.603  -3.880  10.140  1.00 33.61           N  
ATOM    897  CA  SER A 332      11.490  -3.929   9.198  1.00 35.42           C  
ATOM    898  C   SER A 332      11.676  -2.939   8.054  1.00 35.96           C  
ATOM    899  O   SER A 332      11.122  -3.124   6.971  1.00 33.90           O  
ATOM    900  CB  SER A 332      10.171  -3.629   9.907  1.00 35.19           C  
ATOM    901  OG  SER A 332       9.955  -4.529  10.973  1.00 35.70           O  
ATOM    902  N   LEU A 333      12.455  -1.890   8.305  1.00 33.07           N  
ATOM    903  CA  LEU A 333      12.642  -0.812   7.338  1.00 37.48           C  
ATOM    904  C   LEU A 333      13.939  -0.987   6.559  1.00 38.22           C  
ATOM    905  O   LEU A 333      14.284  -0.164   5.707  1.00 36.06           O  
ATOM    906  CB  LEU A 333      12.648   0.542   8.053  1.00 38.97           C  
ATOM    907  CG  LEU A 333      11.292   1.162   8.408  1.00 46.13           C  
ATOM    908  CD1 LEU A 333      10.325   0.130   8.966  1.00 46.00           C  
ATOM    909  CD2 LEU A 333      11.474   2.319   9.385  1.00 45.43           C  
ATOM    910  N   MET A 334      14.653  -2.067   6.856  1.00 35.73           N  
ATOM    911  CA  MET A 334      15.968  -2.293   6.278  1.00 35.90           C  
ATOM    912  C   MET A 334      16.021  -3.487   5.331  1.00 35.94           C  
ATOM    913  O   MET A 334      15.331  -4.486   5.522  1.00 39.69           O  
ATOM    914  CB  MET A 334      16.994  -2.508   7.389  1.00 36.10           C  
ATOM    915  CG  MET A 334      17.316  -1.281   8.214  1.00 35.34           C  
ATOM    916  SD  MET A 334      18.502  -1.685   9.514  1.00 42.52           S  
ATOM    917  CE  MET A 334      19.226  -0.079   9.834  1.00 41.94           C  
ATOM    918  N   ASN A 335      16.841  -3.368   4.297  1.00 41.31           N  
ATOM    919  CA  ASN A 335      17.329  -4.542   3.592  1.00 42.86           C  
ATOM    920  C   ASN A 335      18.850  -4.480   3.581  1.00 45.27           C  
ATOM    921  O   ASN A 335      19.441  -3.640   4.260  1.00 44.16           O  
ATOM    922  CB  ASN A 335      16.740  -4.664   2.183  1.00 38.04           C  
ATOM    923  CG  ASN A 335      17.137  -3.519   1.274  1.00 40.05           C  
ATOM    924  OD1 ASN A 335      18.155  -2.860   1.483  1.00 43.23           O  
ATOM    925  ND2 ASN A 335      16.330  -3.281   0.248  1.00 38.22           N  
ATOM    926  N   LYS A 336      19.480  -5.367   2.824  1.00 46.44           N  
ATOM    927  CA  LYS A 336      20.936  -5.424   2.772  1.00 54.10           C  
ATOM    928  C   LYS A 336      21.556  -4.094   2.338  1.00 48.20           C  
ATOM    929  O   LYS A 336      22.683  -3.773   2.714  1.00 46.92           O  
ATOM    930  CB  LYS A 336      21.379  -6.538   1.819  1.00 62.37           C  
ATOM    931  CG  LYS A 336      22.878  -6.636   1.610  1.00 72.06           C  
ATOM    932  CD  LYS A 336      23.243  -7.759   0.639  1.00 79.80           C  
ATOM    933  CE  LYS A 336      22.777  -7.465  -0.785  1.00 80.38           C  
ATOM    934  NZ  LYS A 336      21.314  -7.677  -0.971  1.00 78.15           N  
ATOM    935  N   ASP A 337      20.807  -3.318   1.559  1.00 44.03           N  
ATOM    936  CA  ASP A 337      21.363  -2.163   0.855  1.00 41.12           C  
ATOM    937  C   ASP A 337      21.095  -0.795   1.489  1.00 41.70           C  
ATOM    938  O   ASP A 337      21.748   0.187   1.133  1.00 44.83           O  
ATOM    939  CB  ASP A 337      20.876  -2.157  -0.596  1.00 42.01           C  
ATOM    940  CG  ASP A 337      21.379  -3.352  -1.383  1.00 54.38           C  
ATOM    941  OD1 ASP A 337      22.508  -3.814  -1.110  1.00 54.54           O  
ATOM    942  OD2 ASP A 337      20.645  -3.830  -2.273  1.00 61.43           O  
ATOM    943  N   GLY A 338      20.140  -0.719   2.409  1.00 36.24           N  
ATOM    944  CA  GLY A 338      19.826   0.552   3.039  1.00 35.49           C  
ATOM    945  C   GLY A 338      18.564   0.548   3.877  1.00 37.51           C  
ATOM    946  O   GLY A 338      17.980  -0.507   4.133  1.00 39.88           O  
ATOM    947  N   VAL A 339      18.140   1.737   4.298  1.00 34.74           N  
ATOM    948  CA  VAL A 339      17.019   1.872   5.222  1.00 35.38           C  
ATOM    949  C   VAL A 339      15.991   2.917   4.775  1.00 37.18           C  
ATOM    950  O   VAL A 339      16.346   4.023   4.369  1.00 38.14           O  
ATOM    951  CB  VAL A 339      17.514   2.235   6.638  1.00 34.41           C  
ATOM    952  CG1 VAL A 339      18.288   3.547   6.611  1.00 35.69           C  
ATOM    953  CG2 VAL A 339      16.347   2.308   7.622  1.00 30.36           C  
ATOM    954  N   LEU A 340      14.716   2.551   4.857  1.00 35.74           N  
ATOM    955  CA  LEU A 340      13.620   3.487   4.622  1.00 33.96           C  
ATOM    956  C   LEU A 340      13.695   4.653   5.603  1.00 38.95           C  
ATOM    957  O   LEU A 340      14.010   4.463   6.777  1.00 38.42           O  
ATOM    958  CB  LEU A 340      12.281   2.770   4.803  1.00 36.85           C  
ATOM    959  CG  LEU A 340      11.427   2.395   3.592  1.00 48.10           C  
ATOM    960  CD1 LEU A 340      12.238   2.313   2.306  1.00 48.98           C  
ATOM    961  CD2 LEU A 340      10.665   1.102   3.863  1.00 43.71           C  
ATOM    962  N   ILE A 341      13.399   5.856   5.122  1.00 39.71           N  
ATOM    963  CA  ILE A 341      13.344   7.030   5.986  1.00 39.68           C  
ATOM    964  C   ILE A 341      12.144   7.897   5.636  1.00 40.92           C  
ATOM    965  O   ILE A 341      11.502   7.700   4.602  1.00 35.92           O  
ATOM    966  CB  ILE A 341      14.618   7.898   5.875  1.00 43.93           C  
ATOM    967  CG1 ILE A 341      14.759   8.462   4.461  1.00 46.32           C  
ATOM    968  CG2 ILE A 341      15.858   7.105   6.273  1.00 46.42           C  
ATOM    969  CD1 ILE A 341      15.877   9.469   4.320  1.00 47.00           C  
ATOM    970  N   SER A 342      11.846   8.856   6.507  1.00 42.66           N  
ATOM    971  CA  SER A 342      10.785   9.824   6.255  1.00 46.68           C  
ATOM    972  C   SER A 342       9.462   9.136   5.931  1.00 44.18           C  
ATOM    973  O   SER A 342       8.843   9.407   4.900  1.00 44.90           O  
ATOM    974  CB  SER A 342      11.191  10.765   5.119  1.00 54.15           C  
ATOM    975  OG  SER A 342      10.301  11.861   5.022  1.00 63.53           O  
ATOM    976  N   GLU A 343       9.037   8.241   6.817  1.00 42.73           N  
ATOM    977  CA  GLU A 343       7.799   7.494   6.627  1.00 49.67           C  
ATOM    978  C   GLU A 343       7.786   6.730   5.304  1.00 46.82           C  
ATOM    979  O   GLU A 343       6.730   6.536   4.703  1.00 46.46           O  
ATOM    980  CB  GLU A 343       6.590   8.429   6.699  1.00 60.17           C  
ATOM    981  CG  GLU A 343       6.596   9.367   7.895  1.00 69.09           C  
ATOM    982  CD  GLU A 343       5.369  10.256   7.940  1.00 78.47           C  
ATOM    983  OE1 GLU A 343       4.259   9.755   7.659  1.00 81.76           O  
ATOM    984  OE2 GLU A 343       5.514  11.456   8.259  1.00 81.00           O  
ATOM    985  N   GLY A 344       8.960   6.304   4.850  1.00 41.18           N  
ATOM    986  CA  GLY A 344       9.052   5.470   3.666  1.00 38.54           C  
ATOM    987  C   GLY A 344       9.141   6.217   2.348  1.00 41.06           C  
ATOM    988  O   GLY A 344       9.218   5.595   1.288  1.00 46.38           O  
ATOM    989  N   GLN A 345       9.139   7.546   2.403  1.00 39.60           N  
ATOM    990  CA  GLN A 345       9.237   8.354   1.188  1.00 44.94           C  
ATOM    991  C   GLN A 345      10.673   8.401   0.680  1.00 43.18           C  
ATOM    992  O   GLN A 345      10.919   8.631  -0.502  1.00 44.51           O  
ATOM    993  CB  GLN A 345       8.727   9.775   1.431  1.00 49.61           C  
ATOM    994  CG  GLN A 345       7.284   9.842   1.891  1.00 58.26           C  
ATOM    995  CD  GLN A 345       6.828  11.259   2.171  1.00 71.62           C  
ATOM    996  OE1 GLN A 345       7.202  12.197   1.465  1.00 76.67           O  
ATOM    997  NE2 GLN A 345       6.012  11.423   3.205  1.00 77.22           N  
ATOM    998  N   GLY A 346      11.622   8.188   1.583  1.00 38.18           N  
ATOM    999  CA  GLY A 346      13.021   8.176   1.208  1.00 38.91           C  
ATOM   1000  C   GLY A 346      13.678   6.840   1.489  1.00 38.94           C  
ATOM   1001  O   GLY A 346      13.129   5.998   2.201  1.00 37.78           O  
ATOM   1002  N   PHE A 347      14.863   6.650   0.924  1.00 39.77           N  
ATOM   1003  CA  PHE A 347      15.648   5.447   1.156  1.00 38.61           C  
ATOM   1004  C   PHE A 347      17.125   5.817   1.156  1.00 40.80           C  
ATOM   1005  O   PHE A 347      17.681   6.185   0.122  1.00 45.77           O  
ATOM   1006  CB  PHE A 347      15.359   4.394   0.081  1.00 34.86           C  
ATOM   1007  CG  PHE A 347      16.131   3.110   0.258  1.00 37.15           C  
ATOM   1008  CD1 PHE A 347      15.701   2.143   1.153  1.00 40.05           C  
ATOM   1009  CD2 PHE A 347      17.284   2.869  -0.476  1.00 41.71           C  
ATOM   1010  CE1 PHE A 347      16.409   0.962   1.318  1.00 40.58           C  
ATOM   1011  CE2 PHE A 347      17.996   1.689  -0.317  1.00 42.26           C  
ATOM   1012  CZ  PHE A 347      17.556   0.734   0.580  1.00 43.60           C  
ATOM   1013  N   MET A 348      17.754   5.730   2.321  1.00 39.45           N  
ATOM   1014  CA  MET A 348      19.163   6.076   2.458  1.00 40.61           C  
ATOM   1015  C   MET A 348      20.021   4.820   2.433  1.00 40.07           C  
ATOM   1016  O   MET A 348      19.798   3.894   3.210  1.00 40.26           O  
ATOM   1017  CB  MET A 348      19.391   6.847   3.756  1.00 44.10           C  
ATOM   1018  CG  MET A 348      20.807   7.364   3.936  1.00 50.42           C  
ATOM   1019  SD  MET A 348      20.906   8.631   5.217  1.00 60.81           S  
ATOM   1020  CE  MET A 348      20.032   9.985   4.430  1.00 54.01           C  
ATOM   1021  N   THR A 349      21.004   4.790   1.538  1.00 42.31           N  
ATOM   1022  CA  THR A 349      21.810   3.591   1.341  1.00 42.45           C  
ATOM   1023  C   THR A 349      22.754   3.321   2.511  1.00 44.68           C  
ATOM   1024  O   THR A 349      23.165   4.237   3.223  1.00 44.42           O  
ATOM   1025  CB  THR A 349      22.625   3.659   0.036  1.00 45.69           C  
ATOM   1026  OG1 THR A 349      23.661   4.639   0.168  1.00 43.38           O  
ATOM   1027  CG2 THR A 349      21.724   4.019  -1.140  1.00 45.90           C  
ATOM   1028  N   ARG A 350      23.086   2.048   2.690  1.00 46.03           N  
ATOM   1029  CA  ARG A 350      23.983   1.598   3.745  1.00 47.82           C  
ATOM   1030  C   ARG A 350      25.396   2.137   3.529  1.00 48.76           C  
ATOM   1031  O   ARG A 350      26.067   2.546   4.478  1.00 50.89           O  
ATOM   1032  CB  ARG A 350      23.993   0.069   3.772  1.00 50.36           C  
ATOM   1033  CG  ARG A 350      24.926  -0.573   4.782  1.00 49.77           C  
ATOM   1034  CD  ARG A 350      24.738  -2.081   4.754  1.00 45.86           C  
ATOM   1035  NE  ARG A 350      25.606  -2.789   5.690  1.00 48.50           N  
ATOM   1036  CZ  ARG A 350      25.506  -4.089   5.947  1.00 49.65           C  
ATOM   1037  NH1 ARG A 350      24.573  -4.810   5.340  1.00 50.02           N  
ATOM   1038  NH2 ARG A 350      26.331  -4.670   6.808  1.00 48.53           N  
ATOM   1039  N   GLU A 351      25.839   2.137   2.274  1.00 50.27           N  
ATOM   1040  CA AGLU A 351      27.172   2.623   1.934  0.50 50.95           C  
ATOM   1041  CA BGLU A 351      27.170   2.626   1.926  0.50 50.96           C  
ATOM   1042  C   GLU A 351      27.316   4.112   2.238  1.00 51.68           C  
ATOM   1043  O   GLU A 351      28.347   4.553   2.745  1.00 50.89           O  
ATOM   1044  CB AGLU A 351      27.491   2.346   0.463  0.50 52.95           C  
ATOM   1045  CB BGLU A 351      27.466   2.374   0.446  0.50 52.23           C  
ATOM   1046  CG AGLU A 351      27.799   0.888   0.149  0.50 57.02           C  
ATOM   1047  CG BGLU A 351      28.806   2.922  -0.019  0.50 52.64           C  
ATOM   1048  CD AGLU A 351      29.171   0.457   0.640  0.50 61.83           C  
ATOM   1049  CD BGLU A 351      29.023   2.758  -1.513  0.50 54.05           C  
ATOM   1050  OE1AGLU A 351      29.848   1.262   1.315  0.50 59.06           O  
ATOM   1051  OE1BGLU A 351      28.075   2.348  -2.215  0.50 50.39           O  
ATOM   1052  OE2AGLU A 351      29.576  -0.688   0.346  0.50 66.53           O  
ATOM   1053  OE2BGLU A 351      30.143   3.044  -1.986  0.50 55.82           O  
ATOM   1054  N   PHE A 352      26.280   4.885   1.929  1.00 49.87           N  
ATOM   1055  CA  PHE A 352      26.315   6.318   2.190  1.00 50.50           C  
ATOM   1056  C   PHE A 352      26.450   6.582   3.685  1.00 51.52           C  
ATOM   1057  O   PHE A 352      27.249   7.415   4.110  1.00 51.52           O  
ATOM   1058  CB  PHE A 352      25.062   7.000   1.643  1.00 46.53           C  
ATOM   1059  CG  PHE A 352      25.021   8.481   1.892  1.00 46.87           C  
ATOM   1060  CD1 PHE A 352      25.989   9.313   1.356  1.00 51.12           C  
ATOM   1061  CD2 PHE A 352      24.008   9.042   2.651  1.00 48.32           C  
ATOM   1062  CE1 PHE A 352      25.953  10.678   1.580  1.00 53.54           C  
ATOM   1063  CE2 PHE A 352      23.966  10.406   2.880  1.00 50.99           C  
ATOM   1064  CZ  PHE A 352      24.941  11.225   2.343  1.00 52.52           C  
ATOM   1065  N   LEU A 353      25.664   5.862   4.477  1.00 53.75           N  
ATOM   1066  CA  LEU A 353      25.717   5.990   5.926  1.00 55.03           C  
ATOM   1067  C   LEU A 353      27.078   5.561   6.467  1.00 59.58           C  
ATOM   1068  O   LEU A 353      27.619   6.188   7.377  1.00 62.32           O  
ATOM   1069  CB  LEU A 353      24.596   5.174   6.576  1.00 49.16           C  
ATOM   1070  CG  LEU A 353      23.194   5.779   6.468  1.00 44.55           C  
ATOM   1071  CD1 LEU A 353      22.122   4.714   6.632  1.00 41.22           C  
ATOM   1072  CD2 LEU A 353      23.011   6.894   7.489  1.00 44.18           C  
ATOM   1073  N   LYS A 354      27.634   4.498   5.895  1.00 59.23           N  
ATOM   1074  CA  LYS A 354      28.922   3.977   6.339  1.00 61.40           C  
ATOM   1075  C   LYS A 354      30.070   4.919   5.980  1.00 61.58           C  
ATOM   1076  O   LYS A 354      31.135   4.881   6.598  1.00 61.63           O  
ATOM   1077  CB  LYS A 354      29.165   2.581   5.754  1.00 63.17           C  
ATOM   1078  CG  LYS A 354      30.471   1.936   6.192  1.00 67.98           C  
ATOM   1079  CD  LYS A 354      30.434   0.424   6.015  1.00 72.56           C  
ATOM   1080  CE  LYS A 354      30.388   0.025   4.549  1.00 77.93           C  
ATOM   1081  NZ  LYS A 354      31.703   0.203   3.868  1.00 83.34           N  
ATOM   1082  N   SER A 355      29.844   5.776   4.990  1.00 61.20           N  
ATOM   1083  CA  SER A 355      30.892   6.666   4.500  1.00 65.01           C  
ATOM   1084  C   SER A 355      31.002   7.950   5.316  1.00 65.64           C  
ATOM   1085  O   SER A 355      31.934   8.730   5.126  1.00 65.52           O  
ATOM   1086  CB  SER A 355      30.660   7.008   3.027  1.00 67.36           C  
ATOM   1087  OG  SER A 355      29.558   7.887   2.875  1.00 67.60           O  
ATOM   1088  N   LEU A 356      30.051   8.169   6.219  1.00 62.02           N  
ATOM   1089  CA  LEU A 356      30.046   9.380   7.034  1.00 62.94           C  
ATOM   1090  C   LEU A 356      31.266   9.437   7.948  1.00 63.99           C  
ATOM   1091  O   LEU A 356      31.708   8.414   8.470  1.00 66.57           O  
ATOM   1092  CB  LEU A 356      28.759   9.473   7.856  1.00 61.74           C  
ATOM   1093  CG  LEU A 356      27.471   9.634   7.046  1.00 61.85           C  
ATOM   1094  CD1 LEU A 356      26.248   9.595   7.954  1.00 60.02           C  
ATOM   1095  CD2 LEU A 356      27.504  10.919   6.228  1.00 63.69           C  
ATOM   1096  N   ARG A 357      31.805  10.638   8.140  1.00 63.27           N  
ATOM   1097  CA  ARG A 357      33.007  10.818   8.949  1.00 67.83           C  
ATOM   1098  C   ARG A 357      32.815  10.299  10.372  1.00 70.22           C  
ATOM   1099  O   ARG A 357      31.747  10.460  10.966  1.00 67.65           O  
ATOM   1100  CB  ARG A 357      33.445  12.288   8.947  1.00 69.52           C  
ATOM   1101  CG  ARG A 357      32.646  13.210   9.855  1.00 69.31           C  
ATOM   1102  CD  ARG A 357      33.466  13.621  11.070  1.00 73.46           C  
ATOM   1103  NE  ARG A 357      32.968  14.849  11.684  1.00 74.38           N  
ATOM   1104  CZ  ARG A 357      32.529  14.937  12.935  1.00 75.40           C  
ATOM   1105  NH1 ARG A 357      32.534  13.866  13.717  1.00 76.03           N  
ATOM   1106  NH2 ARG A 357      32.096  16.098  13.409  1.00 72.94           N  
ATOM   1107  N   LYS A 358      33.856   9.668  10.907  1.00 73.06           N  
ATOM   1108  CA  LYS A 358      33.791   9.050  12.227  1.00 73.81           C  
ATOM   1109  C   LYS A 358      33.440  10.064  13.310  1.00 74.28           C  
ATOM   1110  O   LYS A 358      33.845  11.225  13.233  1.00 75.34           O  
ATOM   1111  CB  LYS A 358      35.116   8.361  12.562  1.00 74.64           C  
ATOM   1112  N   PRO A 359      32.686   9.623  14.328  1.00 73.72           N  
ATOM   1113  CA  PRO A 359      32.202   8.249  14.460  1.00 70.50           C  
ATOM   1114  C   PRO A 359      30.776   8.073  13.939  1.00 64.00           C  
ATOM   1115  O   PRO A 359      30.145   7.054  14.218  1.00 62.83           O  
ATOM   1116  CB  PRO A 359      32.221   8.057  15.969  1.00 71.55           C  
ATOM   1117  CG  PRO A 359      31.747   9.396  16.476  1.00 73.76           C  
ATOM   1118  CD  PRO A 359      32.278  10.438  15.487  1.00 75.16           C  
ATOM   1119  N   PHE A 360      30.277   9.052  13.192  1.00 59.98           N  
ATOM   1120  CA  PHE A 360      28.907   8.998  12.689  1.00 57.03           C  
ATOM   1121  C   PHE A 360      28.686   7.857  11.697  1.00 55.58           C  
ATOM   1122  O   PHE A 360      27.578   7.332  11.581  1.00 56.10           O  
ATOM   1123  CB  PHE A 360      28.509  10.339  12.068  1.00 54.12           C  
ATOM   1124  CG  PHE A 360      28.466  11.468  13.057  1.00 57.33           C  
ATOM   1125  CD1 PHE A 360      27.410  11.585  13.946  1.00 56.85           C  
ATOM   1126  CD2 PHE A 360      29.483  12.407  13.105  1.00 58.92           C  
ATOM   1127  CE1 PHE A 360      27.367  12.618  14.861  1.00 55.80           C  
ATOM   1128  CE2 PHE A 360      29.444  13.443  14.016  1.00 59.77           C  
ATOM   1129  CZ  PHE A 360      28.385  13.548  14.896  1.00 58.42           C  
ATOM   1130  N   GLY A 361      29.744   7.470  10.992  1.00 54.08           N  
ATOM   1131  CA  GLY A 361      29.662   6.387  10.029  1.00 56.04           C  
ATOM   1132  C   GLY A 361      29.630   5.009  10.668  1.00 59.91           C  
ATOM   1133  O   GLY A 361      29.442   4.006   9.981  1.00 61.52           O  
ATOM   1134  N   ASP A 362      29.807   4.961  11.986  1.00 59.86           N  
ATOM   1135  CA  ASP A 362      29.846   3.693  12.712  1.00 61.38           C  
ATOM   1136  C   ASP A 362      28.512   3.343  13.369  1.00 55.12           C  
ATOM   1137  O   ASP A 362      28.326   2.231  13.864  1.00 56.54           O  
ATOM   1138  CB  ASP A 362      30.950   3.719  13.775  1.00 65.89           C  
ATOM   1139  CG  ASP A 362      32.340   3.745  13.172  1.00 71.61           C  
ATOM   1140  OD1 ASP A 362      32.457   3.579  11.940  1.00 74.55           O  
ATOM   1141  OD2 ASP A 362      33.315   3.930  13.931  1.00 74.96           O  
ATOM   1142  N   PHE A 363      27.586   4.294  13.370  1.00 47.98           N  
ATOM   1143  CA  PHE A 363      26.318   4.115  14.068  1.00 48.83           C  
ATOM   1144  C   PHE A 363      25.420   3.027  13.475  1.00 50.37           C  
ATOM   1145  O   PHE A 363      24.943   2.153  14.196  1.00 48.80           O  
ATOM   1146  CB  PHE A 363      25.555   5.443  14.149  1.00 52.18           C  
ATOM   1147  CG  PHE A 363      25.939   6.293  15.328  1.00 58.00           C  
ATOM   1148  CD1 PHE A 363      25.411   6.036  16.583  1.00 60.57           C  
ATOM   1149  CD2 PHE A 363      26.825   7.348  15.185  1.00 62.36           C  
ATOM   1150  CE1 PHE A 363      25.762   6.811  17.672  1.00 61.94           C  
ATOM   1151  CE2 PHE A 363      27.179   8.128  16.271  1.00 62.62           C  
ATOM   1152  CZ  PHE A 363      26.646   7.859  17.515  1.00 61.94           C  
ATOM   1153  N   MET A 364      25.192   3.079  12.167  1.00 53.34           N  
ATOM   1154  CA  MET A 364      24.156   2.252  11.551  1.00 48.95           C  
ATOM   1155  C   MET A 364      24.605   0.854  11.123  1.00 47.68           C  
ATOM   1156  O   MET A 364      23.790  -0.065  11.056  1.00 47.33           O  
ATOM   1157  CB  MET A 364      23.518   2.985  10.368  1.00 48.49           C  
ATOM   1158  CG  MET A 364      22.794   4.267  10.758  1.00 51.57           C  
ATOM   1159  SD  MET A 364      21.493   4.001  11.981  1.00 54.68           S  
ATOM   1160  CE  MET A 364      20.360   2.985  11.041  1.00 43.06           C  
ATOM   1161  N   GLU A 365      25.893   0.690  10.840  1.00 43.77           N  
ATOM   1162  CA  GLU A 365      26.389  -0.580  10.312  1.00 47.84           C  
ATOM   1163  C   GLU A 365      25.988  -1.807  11.148  1.00 48.30           C  
ATOM   1164  O   GLU A 365      25.498  -2.795  10.602  1.00 51.21           O  
ATOM   1165  CB  GLU A 365      27.906  -0.532  10.098  1.00 52.86           C  
ATOM   1166  CG  GLU A 365      28.477  -1.762   9.404  1.00 54.52           C  
ATOM   1167  CD  GLU A 365      27.969  -1.933   7.983  1.00 59.56           C  
ATOM   1168  OE1 GLU A 365      28.394  -2.897   7.314  1.00 64.26           O  
ATOM   1169  OE2 GLU A 365      27.148  -1.105   7.531  1.00 56.74           O  
ATOM   1170  N   PRO A 366      26.199  -1.753  12.472  1.00 48.59           N  
ATOM   1171  CA  PRO A 366      25.797  -2.883  13.320  1.00 51.87           C  
ATOM   1172  C   PRO A 366      24.289  -3.160  13.270  1.00 50.05           C  
ATOM   1173  O   PRO A 366      23.878  -4.316  13.393  1.00 45.95           O  
ATOM   1174  CB  PRO A 366      26.216  -2.425  14.726  1.00 56.41           C  
ATOM   1175  CG  PRO A 366      26.368  -0.925  14.605  1.00 54.81           C  
ATOM   1176  CD  PRO A 366      26.945  -0.750  13.247  1.00 49.67           C  
ATOM   1177  N   LYS A 367      23.480  -2.119  13.094  1.00 46.55           N  
ATOM   1178  CA  LYS A 367      22.036  -2.297  12.971  1.00 43.77           C  
ATOM   1179  C   LYS A 367      21.688  -3.049  11.688  1.00 43.15           C  
ATOM   1180  O   LYS A 367      20.777  -3.876  11.673  1.00 44.83           O  
ATOM   1181  CB  LYS A 367      21.305  -0.952  13.006  1.00 38.45           C  
ATOM   1182  CG  LYS A 367      21.199  -0.327  14.388  1.00 38.04           C  
ATOM   1183  CD  LYS A 367      22.529   0.247  14.843  1.00 47.70           C  
ATOM   1184  CE  LYS A 367      22.398   0.944  16.187  1.00 48.52           C  
ATOM   1185  NZ  LYS A 367      23.689   1.546  16.629  1.00 49.64           N  
ATOM   1186  N   PHE A 368      22.415  -2.754  10.615  1.00 39.60           N  
ATOM   1187  CA  PHE A 368      22.222  -3.453   9.348  1.00 40.77           C  
ATOM   1188  C   PHE A 368      22.592  -4.924   9.479  1.00 45.23           C  
ATOM   1189  O   PHE A 368      21.886  -5.799   8.974  1.00 47.25           O  
ATOM   1190  CB  PHE A 368      23.049  -2.807   8.235  1.00 42.27           C  
ATOM   1191  CG  PHE A 368      22.415  -1.585   7.639  1.00 39.25           C  
ATOM   1192  CD1 PHE A 368      21.282  -1.695   6.848  1.00 39.24           C  
ATOM   1193  CD2 PHE A 368      22.951  -0.327   7.862  1.00 41.26           C  
ATOM   1194  CE1 PHE A 368      20.694  -0.573   6.293  1.00 40.01           C  
ATOM   1195  CE2 PHE A 368      22.368   0.800   7.309  1.00 39.09           C  
ATOM   1196  CZ  PHE A 368      21.237   0.676   6.525  1.00 39.50           C  
ATOM   1197  N   GLU A 369      23.703  -5.191  10.160  1.00 47.39           N  
ATOM   1198  CA  GLU A 369      24.164  -6.560  10.360  1.00 48.45           C  
ATOM   1199  C   GLU A 369      23.114  -7.361  11.116  1.00 44.19           C  
ATOM   1200  O   GLU A 369      22.807  -8.495  10.758  1.00 45.19           O  
ATOM   1201  CB  GLU A 369      25.495  -6.580  11.116  1.00 52.08           C  
ATOM   1202  CG  GLU A 369      26.639  -5.911  10.375  1.00 58.24           C  
ATOM   1203  CD  GLU A 369      27.958  -6.012  11.120  1.00 69.40           C  
ATOM   1204  OE1 GLU A 369      27.932  -6.167  12.359  1.00 71.41           O  
ATOM   1205  OE2 GLU A 369      29.020  -5.937  10.465  1.00 74.31           O  
ATOM   1206  N   PHE A 370      22.558  -6.760  12.162  1.00 43.71           N  
ATOM   1207  CA  PHE A 370      21.505  -7.407  12.935  1.00 43.90           C  
ATOM   1208  C   PHE A 370      20.243  -7.607  12.099  1.00 40.92           C  
ATOM   1209  O   PHE A 370      19.632  -8.676  12.118  1.00 41.55           O  
ATOM   1210  CB  PHE A 370      21.177  -6.583  14.179  1.00 42.24           C  
ATOM   1211  CG  PHE A 370      19.860  -6.935  14.809  1.00 45.16           C  
ATOM   1212  CD1 PHE A 370      19.762  -7.995  15.694  1.00 48.48           C  
ATOM   1213  CD2 PHE A 370      18.720  -6.205  14.518  1.00 47.65           C  
ATOM   1214  CE1 PHE A 370      18.551  -8.319  16.279  1.00 48.92           C  
ATOM   1215  CE2 PHE A 370      17.506  -6.524  15.099  1.00 47.45           C  
ATOM   1216  CZ  PHE A 370      17.422  -7.584  15.979  1.00 47.84           C  
ATOM   1217  N   ALA A 371      19.859  -6.569  11.367  1.00 35.63           N  
ATOM   1218  CA  ALA A 371      18.632  -6.601  10.581  1.00 38.12           C  
ATOM   1219  C   ALA A 371      18.654  -7.703   9.520  1.00 41.09           C  
ATOM   1220  O   ALA A 371      17.673  -8.424   9.347  1.00 45.08           O  
ATOM   1221  CB  ALA A 371      18.380  -5.246   9.945  1.00 37.22           C  
ATOM   1222  N   VAL A 372      19.772  -7.835   8.816  1.00 44.19           N  
ATOM   1223  CA  VAL A 372      19.907  -8.879   7.804  1.00 49.16           C  
ATOM   1224  C   VAL A 372      19.653 -10.261   8.404  1.00 46.21           C  
ATOM   1225  O   VAL A 372      18.993 -11.104   7.797  1.00 47.33           O  
ATOM   1226  CB  VAL A 372      21.293  -8.847   7.132  1.00 54.24           C  
ATOM   1227  CG1 VAL A 372      21.542 -10.135   6.365  1.00 57.35           C  
ATOM   1228  CG2 VAL A 372      21.404  -7.644   6.210  1.00 52.67           C  
ATOM   1229  N   LYS A 373      20.171 -10.480   9.608  1.00 45.52           N  
ATOM   1230  CA  LYS A 373      19.972 -11.743  10.309  1.00 50.25           C  
ATOM   1231  C   LYS A 373      18.552 -11.862  10.867  1.00 47.18           C  
ATOM   1232  O   LYS A 373      17.899 -12.896  10.714  1.00 49.30           O  
ATOM   1233  CB  LYS A 373      21.003 -11.895  11.430  1.00 55.23           C  
ATOM   1234  CG  LYS A 373      22.445 -11.865  10.939  1.00 66.02           C  
ATOM   1235  CD  LYS A 373      23.432 -12.043  12.081  1.00 72.93           C  
ATOM   1236  CE  LYS A 373      24.867 -11.880  11.602  1.00 79.87           C  
ATOM   1237  NZ  LYS A 373      25.853 -12.117  12.694  1.00 84.84           N  
ATOM   1238  N   PHE A 374      18.076 -10.801  11.508  1.00 40.63           N  
ATOM   1239  CA  PHE A 374      16.735 -10.802  12.083  1.00 41.93           C  
ATOM   1240  C   PHE A 374      15.687 -10.984  10.988  1.00 41.10           C  
ATOM   1241  O   PHE A 374      14.719 -11.725  11.156  1.00 39.59           O  
ATOM   1242  CB  PHE A 374      16.484  -9.508  12.865  1.00 41.20           C  
ATOM   1243  CG  PHE A 374      15.235  -9.534  13.705  1.00 40.69           C  
ATOM   1244  CD1 PHE A 374      15.226 -10.172  14.936  1.00 38.16           C  
ATOM   1245  CD2 PHE A 374      14.075  -8.914  13.268  1.00 36.44           C  
ATOM   1246  CE1 PHE A 374      14.085 -10.197  15.714  1.00 37.66           C  
ATOM   1247  CE2 PHE A 374      12.927  -8.937  14.038  1.00 34.02           C  
ATOM   1248  CZ  PHE A 374      12.931  -9.579  15.263  1.00 36.20           C  
ATOM   1249  N   ASN A 375      15.894 -10.312   9.861  1.00 44.02           N  
ATOM   1250  CA  ASN A 375      14.958 -10.380   8.744  1.00 43.70           C  
ATOM   1251  C   ASN A 375      14.858 -11.776   8.137  1.00 45.33           C  
ATOM   1252  O   ASN A 375      13.854 -12.113   7.511  1.00 44.30           O  
ATOM   1253  CB  ASN A 375      15.320  -9.351   7.668  1.00 39.64           C  
ATOM   1254  CG  ASN A 375      14.946  -7.933   8.071  1.00 41.60           C  
ATOM   1255  OD1 ASN A 375      14.191  -7.728   9.020  1.00 36.79           O  
ATOM   1256  ND2 ASN A 375      15.470  -6.950   7.348  1.00 35.85           N  
ATOM   1257  N   ALA A 376      15.897 -12.585   8.329  1.00 48.49           N  
ATOM   1258  CA  ALA A 376      15.904 -13.957   7.828  1.00 53.19           C  
ATOM   1259  C   ALA A 376      14.838 -14.808   8.519  1.00 51.98           C  
ATOM   1260  O   ALA A 376      14.414 -15.836   7.991  1.00 52.19           O  
ATOM   1261  CB  ALA A 376      17.286 -14.583   7.994  1.00 55.76           C  
ATOM   1262  N   LEU A 377      14.408 -14.373   9.700  1.00 48.68           N  
ATOM   1263  CA  LEU A 377      13.354 -15.064  10.435  1.00 46.53           C  
ATOM   1264  C   LEU A 377      11.996 -14.876   9.761  1.00 45.98           C  
ATOM   1265  O   LEU A 377      11.047 -15.607  10.040  1.00 47.35           O  
ATOM   1266  CB  LEU A 377      13.299 -14.567  11.881  1.00 45.12           C  
ATOM   1267  CG  LEU A 377      14.209 -15.248  12.908  1.00 49.68           C  
ATOM   1268  CD1 LEU A 377      15.603 -15.506  12.359  1.00 51.93           C  
ATOM   1269  CD2 LEU A 377      14.267 -14.427  14.195  1.00 46.58           C  
ATOM   1270  N   GLU A 378      11.913 -13.887   8.877  1.00 42.32           N  
ATOM   1271  CA  GLU A 378      10.694 -13.628   8.112  1.00 42.09           C  
ATOM   1272  C   GLU A 378       9.454 -13.458   8.995  1.00 41.70           C  
ATOM   1273  O   GLU A 378       8.391 -14.006   8.708  1.00 43.02           O  
ATOM   1274  CB  GLU A 378      10.477 -14.735   7.075  1.00 45.01           C  
ATOM   1275  CG  GLU A 378      11.628 -14.864   6.079  1.00 53.48           C  
ATOM   1276  CD  GLU A 378      11.499 -16.080   5.179  1.00 64.19           C  
ATOM   1277  OE1 GLU A 378      10.382 -16.631   5.074  1.00 65.19           O  
ATOM   1278  OE2 GLU A 378      12.516 -16.489   4.578  1.00 70.66           O  
ATOM   1279  N   LEU A 379       9.594 -12.693  10.071  1.00 41.37           N  
ATOM   1280  CA  LEU A 379       8.460 -12.404  10.938  1.00 39.23           C  
ATOM   1281  C   LEU A 379       7.558 -11.372  10.276  1.00 41.41           C  
ATOM   1282  O   LEU A 379       8.024 -10.552   9.488  1.00 41.05           O  
ATOM   1283  CB  LEU A 379       8.940 -11.868  12.287  1.00 38.78           C  
ATOM   1284  CG  LEU A 379       9.893 -12.745  13.098  1.00 42.28           C  
ATOM   1285  CD1 LEU A 379      10.245 -12.053  14.398  1.00 41.02           C  
ATOM   1286  CD2 LEU A 379       9.284 -14.113  13.366  1.00 43.24           C  
ATOM   1287  N   ASP A 380       6.268 -11.407  10.590  1.00 39.19           N  
ATOM   1288  CA  ASP A 380       5.377 -10.346  10.136  1.00 39.57           C  
ATOM   1289  C   ASP A 380       4.889  -9.502  11.309  1.00 34.32           C  
ATOM   1290  O   ASP A 380       5.195  -9.794  12.465  1.00 36.43           O  
ATOM   1291  CB  ASP A 380       4.218 -10.891   9.291  1.00 42.16           C  
ATOM   1292  CG  ASP A 380       3.285 -11.788  10.076  1.00 47.77           C  
ATOM   1293  OD1 ASP A 380       3.198 -11.631  11.311  1.00 48.77           O  
ATOM   1294  OD2 ASP A 380       2.628 -12.649   9.449  1.00 52.39           O  
ATOM   1295  N   ASP A 381       4.149  -8.445  11.003  1.00 30.72           N  
ATOM   1296  CA  ASP A 381       3.715  -7.493  12.019  1.00 30.59           C  
ATOM   1297  C   ASP A 381       3.002  -8.139  13.206  1.00 36.45           C  
ATOM   1298  O   ASP A 381       3.193  -7.721  14.346  1.00 36.59           O  
ATOM   1299  CB  ASP A 381       2.815  -6.432  11.392  1.00 33.01           C  
ATOM   1300  CG  ASP A 381       3.562  -5.529  10.445  1.00 32.60           C  
ATOM   1301  OD1 ASP A 381       4.542  -4.893  10.883  1.00 33.92           O  
ATOM   1302  OD2 ASP A 381       3.163  -5.448   9.266  1.00 37.33           O  
ATOM   1303  N   SER A 382       2.174  -9.144  12.935  1.00 36.71           N  
ATOM   1304  CA  SER A 382       1.427  -9.818  13.993  1.00 39.63           C  
ATOM   1305  C   SER A 382       2.352 -10.577  14.949  1.00 38.60           C  
ATOM   1306  O   SER A 382       2.067 -10.687  16.142  1.00 38.79           O  
ATOM   1307  CB  SER A 382       0.365 -10.751  13.403  1.00 40.01           C  
ATOM   1308  OG  SER A 382       0.956 -11.822  12.691  1.00 46.36           O  
ATOM   1309  N   ASP A 383       3.457 -11.098  14.421  1.00 35.60           N  
ATOM   1310  CA  ASP A 383       4.480 -11.725  15.251  1.00 36.36           C  
ATOM   1311  C   ASP A 383       5.191 -10.659  16.069  1.00 38.11           C  
ATOM   1312  O   ASP A 383       5.311 -10.765  17.292  1.00 37.96           O  
ATOM   1313  CB  ASP A 383       5.511 -12.453  14.382  1.00 39.24           C  
ATOM   1314  CG  ASP A 383       4.897 -13.540  13.523  1.00 41.11           C  
ATOM   1315  OD1 ASP A 383       3.939 -14.195  13.981  1.00 44.41           O  
ATOM   1316  OD2 ASP A 383       5.385 -13.744  12.390  1.00 38.07           O  
ATOM   1317  N   LEU A 384       5.669  -9.633  15.373  1.00 36.62           N  
ATOM   1318  CA  LEU A 384       6.423  -8.551  15.991  1.00 36.99           C  
ATOM   1319  C   LEU A 384       5.657  -7.896  17.138  1.00 36.64           C  
ATOM   1320  O   LEU A 384       6.240  -7.549  18.163  1.00 37.15           O  
ATOM   1321  CB  LEU A 384       6.808  -7.509  14.935  1.00 29.00           C  
ATOM   1322  CG  LEU A 384       7.790  -8.005  13.866  1.00 34.46           C  
ATOM   1323  CD1 LEU A 384       7.888  -7.026  12.692  1.00 29.78           C  
ATOM   1324  CD2 LEU A 384       9.165  -8.258  14.474  1.00 33.33           C  
ATOM   1325  N   ALA A 385       4.349  -7.734  16.964  1.00 34.26           N  
ATOM   1326  CA  ALA A 385       3.529  -7.085  17.979  1.00 35.08           C  
ATOM   1327  C   ALA A 385       3.680  -7.778  19.331  1.00 36.26           C  
ATOM   1328  O   ALA A 385       3.838  -7.121  20.359  1.00 38.61           O  
ATOM   1329  CB  ALA A 385       2.063  -7.043  17.546  1.00 30.30           C  
ATOM   1330  N   ILE A 386       3.638  -9.106  19.330  1.00 32.00           N  
ATOM   1331  CA  ILE A 386       3.793  -9.856  20.569  1.00 33.43           C  
ATOM   1332  C   ILE A 386       5.240  -9.843  21.061  1.00 37.46           C  
ATOM   1333  O   ILE A 386       5.493  -9.716  22.259  1.00 40.65           O  
ATOM   1334  CB  ILE A 386       3.321 -11.310  20.430  1.00 34.98           C  
ATOM   1335  CG1 ILE A 386       1.973 -11.369  19.707  1.00 39.06           C  
ATOM   1336  CG2 ILE A 386       3.211 -11.949  21.803  1.00 33.71           C  
ATOM   1337  CD1 ILE A 386       1.368 -12.760  19.651  1.00 37.27           C  
ATOM   1338  N   PHE A 387       6.184  -9.972  20.133  1.00 33.32           N  
ATOM   1339  CA  PHE A 387       7.600  -9.990  20.487  1.00 32.03           C  
ATOM   1340  C   PHE A 387       8.018  -8.710  21.206  1.00 33.29           C  
ATOM   1341  O   PHE A 387       8.723  -8.763  22.210  1.00 37.54           O  
ATOM   1342  CB  PHE A 387       8.474 -10.216  19.249  1.00 36.07           C  
ATOM   1343  CG  PHE A 387       9.952 -10.179  19.532  1.00 41.36           C  
ATOM   1344  CD1 PHE A 387      10.510 -11.022  20.481  1.00 40.32           C  
ATOM   1345  CD2 PHE A 387      10.784  -9.309  18.844  1.00 43.76           C  
ATOM   1346  CE1 PHE A 387      11.869 -10.991  20.747  1.00 41.36           C  
ATOM   1347  CE2 PHE A 387      12.145  -9.276  19.103  1.00 40.22           C  
ATOM   1348  CZ  PHE A 387      12.687 -10.118  20.056  1.00 43.23           C  
ATOM   1349  N   ILE A 388       7.582  -7.560  20.702  1.00 33.85           N  
ATOM   1350  CA  ILE A 388       7.959  -6.292  21.323  1.00 37.81           C  
ATOM   1351  C   ILE A 388       7.302  -6.105  22.691  1.00 35.25           C  
ATOM   1352  O   ILE A 388       7.871  -5.462  23.571  1.00 34.94           O  
ATOM   1353  CB  ILE A 388       7.671  -5.076  20.416  1.00 42.94           C  
ATOM   1354  CG1 ILE A 388       6.181  -4.972  20.102  1.00 48.18           C  
ATOM   1355  CG2 ILE A 388       8.490  -5.158  19.128  1.00 44.71           C  
ATOM   1356  CD1 ILE A 388       5.835  -3.778  19.234  1.00 47.27           C  
ATOM   1357  N   ALA A 389       6.112  -6.673  22.864  1.00 35.67           N  
ATOM   1358  CA  ALA A 389       5.445  -6.666  24.161  1.00 34.25           C  
ATOM   1359  C   ALA A 389       6.282  -7.459  25.154  1.00 38.18           C  
ATOM   1360  O   ALA A 389       6.454  -7.049  26.303  1.00 40.54           O  
ATOM   1361  CB  ALA A 389       4.042  -7.257  24.051  1.00 27.91           C  
ATOM   1362  N   VAL A 390       6.806  -8.593  24.696  1.00 36.25           N  
ATOM   1363  CA  VAL A 390       7.670  -9.429  25.521  1.00 36.12           C  
ATOM   1364  C   VAL A 390       8.889  -8.644  25.989  1.00 37.92           C  
ATOM   1365  O   VAL A 390       9.280  -8.722  27.153  1.00 40.99           O  
ATOM   1366  CB  VAL A 390       8.136 -10.694  24.765  1.00 38.43           C  
ATOM   1367  CG1 VAL A 390       9.300 -11.369  25.501  1.00 36.13           C  
ATOM   1368  CG2 VAL A 390       6.975 -11.659  24.576  1.00 34.72           C  
ATOM   1369  N   ILE A 391       9.481  -7.883  25.074  1.00 40.28           N  
ATOM   1370  CA  ILE A 391      10.661  -7.078  25.378  1.00 40.77           C  
ATOM   1371  C   ILE A 391      10.375  -6.019  26.446  1.00 42.09           C  
ATOM   1372  O   ILE A 391      11.145  -5.855  27.389  1.00 41.21           O  
ATOM   1373  CB  ILE A 391      11.217  -6.390  24.110  1.00 40.94           C  
ATOM   1374  CG1 ILE A 391      11.793  -7.429  23.143  1.00 42.81           C  
ATOM   1375  CG2 ILE A 391      12.272  -5.356  24.480  1.00 40.55           C  
ATOM   1376  CD1 ILE A 391      12.345  -6.835  21.859  1.00 38.00           C  
ATOM   1377  N   ILE A 392       9.270  -5.298  26.293  1.00 41.55           N  
ATOM   1378  CA  ILE A 392       8.912  -4.254  27.249  1.00 40.26           C  
ATOM   1379  C   ILE A 392       8.779  -4.807  28.666  1.00 38.95           C  
ATOM   1380  O   ILE A 392       9.287  -4.223  29.623  1.00 42.59           O  
ATOM   1381  CB  ILE A 392       7.594  -3.564  26.862  1.00 42.30           C  
ATOM   1382  CG1 ILE A 392       7.733  -2.873  25.508  1.00 41.03           C  
ATOM   1383  CG2 ILE A 392       7.183  -2.564  27.936  1.00 46.38           C  
ATOM   1384  CD1 ILE A 392       6.452  -2.254  25.005  1.00 41.08           C  
ATOM   1385  N   LEU A 393       8.097  -5.939  28.792  1.00 33.82           N  
ATOM   1386  CA  LEU A 393       7.845  -6.537  30.097  1.00 38.18           C  
ATOM   1387  C   LEU A 393       9.005  -7.425  30.547  1.00 42.39           C  
ATOM   1388  O   LEU A 393       8.819  -8.602  30.847  1.00 44.74           O  
ATOM   1389  CB  LEU A 393       6.531  -7.326  30.072  1.00 32.10           C  
ATOM   1390  CG  LEU A 393       5.234  -6.511  30.213  1.00 37.79           C  
ATOM   1391  CD1 LEU A 393       5.066  -5.990  31.633  1.00 39.53           C  
ATOM   1392  CD2 LEU A 393       5.156  -5.358  29.211  1.00 35.40           C  
ATOM   1393  N   SER A 394      10.204  -6.853  30.589  1.00 45.62           N  
ATOM   1394  CA  SER A 394      11.390  -7.589  31.021  1.00 50.10           C  
ATOM   1395  C   SER A 394      11.670  -7.342  32.497  1.00 50.82           C  
ATOM   1396  O   SER A 394      11.982  -6.223  32.899  1.00 50.72           O  
ATOM   1397  CB  SER A 394      12.609  -7.186  30.189  1.00 51.70           C  
ATOM   1398  OG  SER A 394      12.447  -7.550  28.831  1.00 54.22           O  
ATOM   1399  N   GLY A 395      11.563  -8.393  33.302  1.00 50.46           N  
ATOM   1400  CA  GLY A 395      11.732  -8.266  34.737  1.00 50.87           C  
ATOM   1401  C   GLY A 395      13.175  -8.176  35.201  1.00 53.78           C  
ATOM   1402  O   GLY A 395      13.440  -8.152  36.404  1.00 57.39           O  
ATOM   1403  N   ASP A 396      14.110  -8.121  34.257  1.00 54.62           N  
ATOM   1404  CA AASP A 396      15.536  -8.063  34.566  0.46 60.11           C  
ATOM   1405  CA BASP A 396      15.521  -8.056  34.623  0.54 59.47           C  
ATOM   1406  C   ASP A 396      16.066  -6.634  34.539  1.00 57.84           C  
ATOM   1407  O   ASP A 396      17.246  -6.398  34.790  1.00 59.75           O  
ATOM   1408  CB AASP A 396      16.336  -8.899  33.565  0.46 63.31           C  
ATOM   1409  CB BASP A 396      16.359  -9.010  33.767  0.54 62.83           C  
ATOM   1410  CG AASP A 396      15.817 -10.316  33.433  0.46 66.95           C  
ATOM   1411  CG BASP A 396      16.466  -8.561  32.325  0.54 60.36           C  
ATOM   1412  OD1AASP A 396      14.901 -10.697  34.191  0.46 69.45           O  
ATOM   1413  OD1BASP A 396      17.502  -8.851  31.692  0.54 61.01           O  
ATOM   1414  OD2AASP A 396      16.331 -11.051  32.563  0.46 70.18           O  
ATOM   1415  OD2BASP A 396      15.520  -7.917  31.827  0.54 55.12           O  
ATOM   1416  N   ARG A 397      15.201  -5.683  34.205  1.00 50.28           N  
ATOM   1417  CA  ARG A 397      15.618  -4.288  34.134  1.00 52.30           C  
ATOM   1418  C   ARG A 397      16.101  -3.796  35.498  1.00 60.62           C  
ATOM   1419  O   ARG A 397      15.465  -4.056  36.521  1.00 61.16           O  
ATOM   1420  CB  ARG A 397      14.479  -3.404  33.625  1.00 49.48           C  
ATOM   1421  CG  ARG A 397      13.847  -3.871  32.324  1.00 48.50           C  
ATOM   1422  CD  ARG A 397      14.875  -4.056  31.220  1.00 46.07           C  
ATOM   1423  NE  ARG A 397      14.232  -4.077  29.909  1.00 43.87           N  
ATOM   1424  CZ  ARG A 397      14.858  -4.345  28.769  1.00 41.91           C  
ATOM   1425  NH1 ARG A 397      16.153  -4.623  28.774  1.00 40.04           N  
ATOM   1426  NH2 ARG A 397      14.187  -4.339  27.625  1.00 39.65           N  
ATOM   1427  N   PRO A 398      17.238  -3.085  35.516  1.00 63.23           N  
ATOM   1428  CA  PRO A 398      17.791  -2.548  36.764  1.00 62.99           C  
ATOM   1429  C   PRO A 398      16.826  -1.590  37.461  1.00 60.45           C  
ATOM   1430  O   PRO A 398      16.211  -0.745  36.808  1.00 53.86           O  
ATOM   1431  CB  PRO A 398      19.036  -1.787  36.295  1.00 61.35           C  
ATOM   1432  CG  PRO A 398      19.400  -2.417  34.992  1.00 59.76           C  
ATOM   1433  CD  PRO A 398      18.101  -2.799  34.357  1.00 59.00           C  
ATOM   1434  N   GLY A 399      16.693  -1.734  38.777  1.00 64.83           N  
ATOM   1435  CA  GLY A 399      15.914  -0.804  39.574  1.00 66.10           C  
ATOM   1436  C   GLY A 399      14.421  -1.070  39.636  1.00 63.96           C  
ATOM   1437  O   GLY A 399      13.660  -0.220  40.100  1.00 62.54           O  
ATOM   1438  N   LEU A 400      13.995  -2.240  39.171  1.00 62.68           N  
ATOM   1439  CA  LEU A 400      12.582  -2.606  39.239  1.00 59.58           C  
ATOM   1440  C   LEU A 400      12.170  -2.885  40.681  1.00 59.28           C  
ATOM   1441  O   LEU A 400      12.837  -3.635  41.389  1.00 61.19           O  
ATOM   1442  CB  LEU A 400      12.287  -3.821  38.355  1.00 54.17           C  
ATOM   1443  CG  LEU A 400      12.164  -3.553  36.853  1.00 48.03           C  
ATOM   1444  CD1 LEU A 400      11.895  -4.845  36.107  1.00 47.51           C  
ATOM   1445  CD2 LEU A 400      11.071  -2.534  36.568  1.00 45.58           C  
ATOM   1446  N   LEU A 401      11.069  -2.276  41.110  1.00 57.47           N  
ATOM   1447  CA  LEU A 401      10.605  -2.407  42.486  1.00 59.39           C  
ATOM   1448  C   LEU A 401       9.836  -3.707  42.705  1.00 59.59           C  
ATOM   1449  O   LEU A 401      10.074  -4.417  43.678  1.00 61.10           O  
ATOM   1450  CB  LEU A 401       9.737  -1.207  42.872  1.00 61.62           C  
ATOM   1451  CG  LEU A 401      10.383   0.174  42.741  1.00 62.99           C  
ATOM   1452  CD1 LEU A 401       9.340   1.278  42.855  1.00 65.56           C  
ATOM   1453  CD2 LEU A 401      11.473   0.351  43.785  1.00 64.11           C  
ATOM   1454  N   ASN A 402       8.911  -4.008  41.799  1.00 61.64           N  
ATOM   1455  CA  ASN A 402       8.098  -5.215  41.901  1.00 61.00           C  
ATOM   1456  C   ASN A 402       8.281  -6.104  40.678  1.00 54.89           C  
ATOM   1457  O   ASN A 402       7.548  -5.978  39.697  1.00 51.67           O  
ATOM   1458  CB  ASN A 402       6.617  -4.855  42.048  1.00 64.69           C  
ATOM   1459  CG  ASN A 402       6.369  -3.805  43.110  1.00 67.92           C  
ATOM   1460  OD1 ASN A 402       7.074  -3.742  44.117  1.00 70.58           O  
ATOM   1461  ND2 ASN A 402       5.354  -2.974  42.892  1.00 66.42           N  
ATOM   1462  N   VAL A 403       9.258  -7.004  40.740  1.00 53.78           N  
ATOM   1463  CA  VAL A 403       9.577  -7.875  39.611  1.00 53.39           C  
ATOM   1464  C   VAL A 403       8.449  -8.851  39.275  1.00 50.50           C  
ATOM   1465  O   VAL A 403       8.104  -9.032  38.109  1.00 53.81           O  
ATOM   1466  CB  VAL A 403      10.879  -8.668  39.861  1.00 61.36           C  
ATOM   1467  CG1 VAL A 403      11.064  -9.743  38.800  1.00 63.03           C  
ATOM   1468  CG2 VAL A 403      12.074  -7.731  39.890  1.00 63.45           C  
ATOM   1469  N   LYS A 404       7.872  -9.468  40.300  1.00 51.33           N  
ATOM   1470  CA  LYS A 404       6.873 -10.522  40.115  1.00 55.67           C  
ATOM   1471  C   LYS A 404       5.717 -10.166  39.166  1.00 54.78           C  
ATOM   1472  O   LYS A 404       5.422 -10.924  38.242  1.00 53.61           O  
ATOM   1473  CB  LYS A 404       6.332 -10.989  41.470  1.00 63.02           C  
ATOM   1474  CG  LYS A 404       5.232 -12.036  41.387  1.00 73.59           C  
ATOM   1475  CD  LYS A 404       5.728 -13.328  40.755  1.00 83.30           C  
ATOM   1476  CE  LYS A 404       4.672 -14.422  40.838  1.00 90.27           C  
ATOM   1477  NZ  LYS A 404       5.069 -15.641  40.078  1.00 94.17           N  
ATOM   1478  N   PRO A 405       5.054  -9.021  39.394  1.00 55.98           N  
ATOM   1479  CA  PRO A 405       3.929  -8.640  38.528  1.00 51.56           C  
ATOM   1480  C   PRO A 405       4.347  -8.522  37.063  1.00 48.87           C  
ATOM   1481  O   PRO A 405       3.583  -8.876  36.164  1.00 51.12           O  
ATOM   1482  CB  PRO A 405       3.517  -7.267  39.070  1.00 48.01           C  
ATOM   1483  CG  PRO A 405       4.016  -7.243  40.473  1.00 53.12           C  
ATOM   1484  CD  PRO A 405       5.281  -8.041  40.470  1.00 54.93           C  
ATOM   1485  N   ILE A 406       5.554  -8.022  36.831  1.00 49.10           N  
ATOM   1486  CA  ILE A 406       6.077  -7.884  35.478  1.00 43.60           C  
ATOM   1487  C   ILE A 406       6.290  -9.250  34.828  1.00 45.75           C  
ATOM   1488  O   ILE A 406       5.941  -9.463  33.666  1.00 43.27           O  
ATOM   1489  CB  ILE A 406       7.403  -7.104  35.478  1.00 44.41           C  
ATOM   1490  CG1 ILE A 406       7.164  -5.666  35.950  1.00 47.48           C  
ATOM   1491  CG2 ILE A 406       8.047  -7.141  34.096  1.00 42.66           C  
ATOM   1492  CD1 ILE A 406       8.428  -4.850  36.128  1.00 47.39           C  
ATOM   1493  N   GLU A 407       6.862 -10.174  35.588  1.00 47.12           N  
ATOM   1494  CA  GLU A 407       7.141 -11.516  35.087  1.00 49.12           C  
ATOM   1495  C   GLU A 407       5.865 -12.297  34.789  1.00 48.33           C  
ATOM   1496  O   GLU A 407       5.813 -13.070  33.835  1.00 46.21           O  
ATOM   1497  CB  GLU A 407       8.016 -12.285  36.077  1.00 49.63           C  
ATOM   1498  CG  GLU A 407       9.461 -11.816  36.114  1.00 57.01           C  
ATOM   1499  CD  GLU A 407      10.310 -12.614  37.085  1.00 65.22           C  
ATOM   1500  OE1 GLU A 407       9.819 -12.942  38.185  1.00 65.69           O  
ATOM   1501  OE2 GLU A 407      11.475 -12.909  36.750  1.00 72.60           O  
ATOM   1502  N   ASP A 408       4.836 -12.095  35.606  1.00 49.68           N  
ATOM   1503  CA  ASP A 408       3.551 -12.744  35.373  1.00 49.38           C  
ATOM   1504  C   ASP A 408       2.960 -12.320  34.031  1.00 47.13           C  
ATOM   1505  O   ASP A 408       2.413 -13.139  33.291  1.00 48.05           O  
ATOM   1506  CB  ASP A 408       2.576 -12.438  36.510  1.00 52.90           C  
ATOM   1507  CG  ASP A 408       2.975 -13.106  37.813  1.00 58.83           C  
ATOM   1508  OD1 ASP A 408       3.701 -14.122  37.763  1.00 63.31           O  
ATOM   1509  OD2 ASP A 408       2.564 -12.618  38.886  1.00 58.53           O  
ATOM   1510  N   ILE A 409       3.078 -11.035  33.718  1.00 44.60           N  
ATOM   1511  CA  ILE A 409       2.604 -10.523  32.438  1.00 43.55           C  
ATOM   1512  C   ILE A 409       3.432 -11.078  31.278  1.00 42.46           C  
ATOM   1513  O   ILE A 409       2.881 -11.519  30.269  1.00 43.79           O  
ATOM   1514  CB  ILE A 409       2.618  -8.987  32.401  1.00 41.82           C  
ATOM   1515  CG1 ILE A 409       1.681  -8.425  33.479  1.00 44.81           C  
ATOM   1516  CG2 ILE A 409       2.224  -8.490  31.009  1.00 39.29           C  
ATOM   1517  CD1 ILE A 409       1.732  -6.911  33.635  1.00 40.81           C  
ATOM   1518  N   GLN A 410       4.753 -11.064  31.426  1.00 46.26           N  
ATOM   1519  CA  GLN A 410       5.633 -11.576  30.378  1.00 44.19           C  
ATOM   1520  C   GLN A 410       5.379 -13.058  30.128  1.00 45.31           C  
ATOM   1521  O   GLN A 410       5.463 -13.523  28.992  1.00 46.29           O  
ATOM   1522  CB  GLN A 410       7.109 -11.347  30.718  1.00 38.75           C  
ATOM   1523  CG  GLN A 410       8.012 -11.317  29.483  1.00 38.36           C  
ATOM   1524  CD  GLN A 410       9.485 -11.450  29.817  1.00 36.44           C  
ATOM   1525  OE1 GLN A 410       9.870 -12.239  30.677  1.00 41.64           O  
ATOM   1526  NE2 GLN A 410      10.319 -10.682  29.127  1.00 36.52           N  
ATOM   1527  N   ASP A 411       5.073 -13.793  31.194  1.00 45.44           N  
ATOM   1528  CA  ASP A 411       4.726 -15.208  31.085  1.00 50.27           C  
ATOM   1529  C   ASP A 411       3.591 -15.421  30.085  1.00 49.87           C  
ATOM   1530  O   ASP A 411       3.687 -16.260  29.191  1.00 51.08           O  
ATOM   1531  CB  ASP A 411       4.320 -15.765  32.451  1.00 60.55           C  
ATOM   1532  CG  ASP A 411       3.780 -17.181  32.367  1.00 72.97           C  
ATOM   1533  OD1 ASP A 411       2.803 -17.490  33.080  1.00 81.66           O  
ATOM   1534  OD2 ASP A 411       4.329 -17.985  31.587  1.00 77.45           O  
ATOM   1535  N   ASN A 412       2.512 -14.663  30.254  1.00 48.09           N  
ATOM   1536  CA  ASN A 412       1.377 -14.735  29.343  1.00 49.52           C  
ATOM   1537  C   ASN A 412       1.767 -14.339  27.922  1.00 45.04           C  
ATOM   1538  O   ASN A 412       1.396 -15.007  26.957  1.00 48.29           O  
ATOM   1539  CB  ASN A 412       0.236 -13.844  29.838  1.00 53.91           C  
ATOM   1540  CG  ASN A 412      -0.322 -14.296  31.174  1.00 64.36           C  
ATOM   1541  OD1 ASN A 412      -0.954 -13.519  31.889  1.00 69.94           O  
ATOM   1542  ND2 ASN A 412      -0.092 -15.559  31.518  1.00 67.71           N  
ATOM   1543  N   LEU A 413       2.513 -13.247  27.799  1.00 37.73           N  
ATOM   1544  CA  LEU A 413       2.965 -12.778  26.494  1.00 39.19           C  
ATOM   1545  C   LEU A 413       3.806 -13.844  25.793  1.00 38.70           C  
ATOM   1546  O   LEU A 413       3.656 -14.078  24.593  1.00 38.23           O  
ATOM   1547  CB  LEU A 413       3.760 -11.476  26.635  1.00 37.98           C  
ATOM   1548  CG  LEU A 413       2.981 -10.267  27.161  1.00 39.03           C  
ATOM   1549  CD1 LEU A 413       3.918  -9.118  27.512  1.00 34.68           C  
ATOM   1550  CD2 LEU A 413       1.933  -9.832  26.137  1.00 39.20           C  
ATOM   1551  N   LEU A 414       4.687 -14.490  26.551  1.00 39.48           N  
ATOM   1552  CA  LEU A 414       5.522 -15.559  26.014  1.00 40.15           C  
ATOM   1553  C   LEU A 414       4.663 -16.724  25.534  1.00 43.45           C  
ATOM   1554  O   LEU A 414       4.902 -17.280  24.464  1.00 42.01           O  
ATOM   1555  CB  LEU A 414       6.536 -16.037  27.056  1.00 40.80           C  
ATOM   1556  CG  LEU A 414       7.693 -15.079  27.353  1.00 39.42           C  
ATOM   1557  CD1 LEU A 414       8.457 -15.524  28.590  1.00 38.86           C  
ATOM   1558  CD2 LEU A 414       8.621 -14.957  26.149  1.00 40.21           C  
ATOM   1559  N   GLN A 415       3.664 -17.096  26.330  1.00 42.15           N  
ATOM   1560  CA  GLN A 415       2.707 -18.115  25.912  1.00 44.17           C  
ATOM   1561  C   GLN A 415       2.021 -17.709  24.610  1.00 43.27           C  
ATOM   1562  O   GLN A 415       1.869 -18.524  23.699  1.00 44.17           O  
ATOM   1563  CB  GLN A 415       1.646 -18.343  26.989  1.00 50.56           C  
ATOM   1564  CG  GLN A 415       2.101 -19.186  28.166  1.00 54.85           C  
ATOM   1565  CD  GLN A 415       0.950 -19.553  29.084  1.00 58.48           C  
ATOM   1566  OE1 GLN A 415       0.061 -20.319  28.710  1.00 54.68           O  
ATOM   1567  NE2 GLN A 415       0.962 -19.007  30.294  1.00 62.85           N  
ATOM   1568  N   ALA A 416       1.603 -16.449  24.536  1.00 35.67           N  
ATOM   1569  CA  ALA A 416       0.915 -15.929  23.358  1.00 41.92           C  
ATOM   1570  C   ALA A 416       1.827 -15.951  22.132  1.00 45.08           C  
ATOM   1571  O   ALA A 416       1.403 -16.324  21.038  1.00 43.87           O  
ATOM   1572  CB  ALA A 416       0.399 -14.513  23.622  1.00 39.12           C  
ATOM   1573  N   LEU A 417       3.080 -15.551  22.327  1.00 46.35           N  
ATOM   1574  CA  LEU A 417       4.059 -15.533  21.246  1.00 42.41           C  
ATOM   1575  C   LEU A 417       4.324 -16.947  20.751  1.00 41.82           C  
ATOM   1576  O   LEU A 417       4.364 -17.194  19.548  1.00 44.61           O  
ATOM   1577  CB  LEU A 417       5.368 -14.890  21.714  1.00 41.01           C  
ATOM   1578  CG  LEU A 417       6.491 -14.764  20.680  1.00 39.31           C  
ATOM   1579  CD1 LEU A 417       6.031 -13.971  19.457  1.00 31.34           C  
ATOM   1580  CD2 LEU A 417       7.719 -14.119  21.304  1.00 38.08           C  
ATOM   1581  N   GLU A 418       4.497 -17.874  21.686  1.00 42.77           N  
ATOM   1582  CA  GLU A 418       4.761 -19.268  21.343  1.00 46.20           C  
ATOM   1583  C   GLU A 418       3.678 -19.850  20.437  1.00 47.57           C  
ATOM   1584  O   GLU A 418       3.979 -20.455  19.410  1.00 45.78           O  
ATOM   1585  CB  GLU A 418       4.895 -20.121  22.606  1.00 45.83           C  
ATOM   1586  CG  GLU A 418       5.271 -21.572  22.333  1.00 50.24           C  
ATOM   1587  CD  GLU A 418       5.437 -22.380  23.603  1.00 55.34           C  
ATOM   1588  OE1 GLU A 418       4.894 -21.963  24.647  1.00 59.56           O  
ATOM   1589  OE2 GLU A 418       6.109 -23.431  23.561  1.00 60.90           O  
ATOM   1590  N   LEU A 419       2.419 -19.671  20.823  1.00 47.40           N  
ATOM   1591  CA  LEU A 419       1.300 -20.183  20.038  1.00 47.76           C  
ATOM   1592  C   LEU A 419       1.178 -19.460  18.696  1.00 44.16           C  
ATOM   1593  O   LEU A 419       0.895 -20.081  17.673  1.00 49.44           O  
ATOM   1594  CB  LEU A 419      -0.007 -20.065  20.824  1.00 51.53           C  
ATOM   1595  CG  LEU A 419      -1.250 -20.638  20.140  1.00 51.97           C  
ATOM   1596  CD1 LEU A 419      -1.029 -22.097  19.769  1.00 53.86           C  
ATOM   1597  CD2 LEU A 419      -2.474 -20.483  21.030  1.00 52.12           C  
ATOM   1598  N   GLN A 420       1.391 -18.148  18.708  1.00 39.57           N  
ATOM   1599  CA  GLN A 420       1.346 -17.346  17.486  1.00 39.31           C  
ATOM   1600  C   GLN A 420       2.346 -17.844  16.447  1.00 45.38           C  
ATOM   1601  O   GLN A 420       2.012 -17.997  15.273  1.00 46.54           O  
ATOM   1602  CB  GLN A 420       1.612 -15.872  17.802  1.00 39.80           C  
ATOM   1603  CG  GLN A 420       1.969 -15.022  16.590  1.00 37.24           C  
ATOM   1604  CD  GLN A 420       0.786 -14.768  15.671  1.00 42.40           C  
ATOM   1605  OE1 GLN A 420      -0.361 -15.054  16.016  1.00 40.91           O  
ATOM   1606  NE2 GLN A 420       1.062 -14.222  14.492  1.00 39.16           N  
ATOM   1607  N   LEU A 421       3.575 -18.097  16.883  1.00 46.75           N  
ATOM   1608  CA  LEU A 421       4.615 -18.569  15.977  1.00 47.02           C  
ATOM   1609  C   LEU A 421       4.317 -19.975  15.461  1.00 46.23           C  
ATOM   1610  O   LEU A 421       4.508 -20.263  14.281  1.00 42.68           O  
ATOM   1611  CB  LEU A 421       5.986 -18.508  16.654  1.00 46.43           C  
ATOM   1612  CG  LEU A 421       6.446 -17.088  17.000  1.00 43.40           C  
ATOM   1613  CD1 LEU A 421       7.796 -17.107  17.697  1.00 42.51           C  
ATOM   1614  CD2 LEU A 421       6.505 -16.224  15.746  1.00 40.47           C  
ATOM   1615  N   LYS A 422       3.838 -20.845  16.343  1.00 50.86           N  
ATOM   1616  CA  LYS A 422       3.439 -22.188  15.940  1.00 55.51           C  
ATOM   1617  C   LYS A 422       2.357 -22.149  14.859  1.00 55.72           C  
ATOM   1618  O   LYS A 422       2.435 -22.869  13.861  1.00 57.70           O  
ATOM   1619  CB  LYS A 422       2.946 -22.988  17.149  1.00 60.68           C  
ATOM   1620  CG  LYS A 422       4.047 -23.714  17.910  1.00 67.09           C  
ATOM   1621  CD  LYS A 422       3.504 -24.363  19.177  1.00 71.47           C  
ATOM   1622  CE  LYS A 422       4.434 -25.455  19.697  1.00 73.01           C  
ATOM   1623  NZ  LYS A 422       5.819 -24.962  19.930  1.00 72.96           N  
ATOM   1624  N   LEU A 423       1.351 -21.306  15.065  1.00 49.08           N  
ATOM   1625  CA  LEU A 423       0.233 -21.200  14.133  1.00 53.49           C  
ATOM   1626  C   LEU A 423       0.625 -20.504  12.831  1.00 50.86           C  
ATOM   1627  O   LEU A 423       0.270 -20.961  11.746  1.00 51.83           O  
ATOM   1628  CB  LEU A 423      -0.940 -20.458  14.780  1.00 53.39           C  
ATOM   1629  CG  LEU A 423      -1.602 -21.107  15.998  1.00 54.65           C  
ATOM   1630  CD1 LEU A 423      -2.754 -20.250  16.494  1.00 51.72           C  
ATOM   1631  CD2 LEU A 423      -2.082 -22.510  15.669  1.00 56.32           C  
ATOM   1632  N   ASN A 424       1.357 -19.399  12.947  1.00 45.44           N  
ATOM   1633  CA  ASN A 424       1.699 -18.579  11.788  1.00 44.50           C  
ATOM   1634  C   ASN A 424       2.867 -19.141  10.977  1.00 51.79           C  
ATOM   1635  O   ASN A 424       2.978 -18.886   9.778  1.00 55.44           O  
ATOM   1636  CB  ASN A 424       1.999 -17.142  12.225  1.00 47.67           C  
ATOM   1637  CG  ASN A 424       1.854 -16.140  11.091  1.00 48.90           C  
ATOM   1638  OD1 ASN A 424       1.072 -16.341  10.160  1.00 48.89           O  
ATOM   1639  ND2 ASN A 424       2.606 -15.049  11.171  1.00 47.95           N  
ATOM   1640  N   HIS A 425       3.736 -19.902  11.635  1.00 51.81           N  
ATOM   1641  CA  HIS A 425       4.895 -20.489  10.969  1.00 49.21           C  
ATOM   1642  C   HIS A 425       5.047 -21.975  11.292  1.00 52.64           C  
ATOM   1643  O   HIS A 425       6.081 -22.393  11.812  1.00 56.64           O  
ATOM   1644  CB  HIS A 425       6.173 -19.757  11.383  1.00 48.25           C  
ATOM   1645  CG  HIS A 425       6.126 -18.277  11.162  1.00 45.16           C  
ATOM   1646  ND1 HIS A 425       6.597 -17.682  10.012  1.00 48.38           N  
ATOM   1647  CD2 HIS A 425       5.679 -17.272  11.950  1.00 43.71           C  
ATOM   1648  CE1 HIS A 425       6.434 -16.374  10.097  1.00 48.69           C  
ATOM   1649  NE2 HIS A 425       5.881 -16.099  11.264  1.00 44.42           N  
ATOM   1650  N   PRO A 426       4.021 -22.782  10.975  1.00 53.69           N  
ATOM   1651  CA  PRO A 426       3.999 -24.205  11.341  1.00 58.28           C  
ATOM   1652  C   PRO A 426       5.185 -24.991  10.788  1.00 59.34           C  
ATOM   1653  O   PRO A 426       5.444 -26.105  11.239  1.00 64.77           O  
ATOM   1654  CB  PRO A 426       2.696 -24.705  10.697  1.00 57.42           C  
ATOM   1655  CG  PRO A 426       2.410 -23.698   9.615  1.00 58.04           C  
ATOM   1656  CD  PRO A 426       2.799 -22.404  10.249  1.00 54.53           C  
ATOM   1657  N   GLU A 427       5.897 -24.415   9.826  1.00 59.33           N  
ATOM   1658  CA  GLU A 427       7.001 -25.110   9.174  1.00 63.92           C  
ATOM   1659  C   GLU A 427       8.361 -24.673   9.713  1.00 62.30           C  
ATOM   1660  O   GLU A 427       9.374 -25.322   9.455  1.00 60.90           O  
ATOM   1661  CB  GLU A 427       6.948 -24.884   7.661  1.00 69.72           C  
ATOM   1662  CG  GLU A 427       7.406 -23.496   7.220  1.00 75.47           C  
ATOM   1663  CD  GLU A 427       6.482 -22.383   7.689  1.00 75.28           C  
ATOM   1664  OE1 GLU A 427       5.317 -22.671   8.033  1.00 75.76           O  
ATOM   1665  OE2 GLU A 427       6.921 -21.213   7.706  1.00 74.97           O  
ATOM   1666  N   SER A 428       8.379 -23.572  10.458  1.00 64.06           N  
ATOM   1667  CA  SER A 428       9.626 -23.024  10.981  1.00 62.18           C  
ATOM   1668  C   SER A 428       9.902 -23.538  12.390  1.00 61.64           C  
ATOM   1669  O   SER A 428       9.510 -22.914  13.377  1.00 60.23           O  
ATOM   1670  CB  SER A 428       9.583 -21.493  10.973  1.00 58.82           C  
ATOM   1671  OG  SER A 428      10.857 -20.942  11.261  1.00 59.78           O  
ATOM   1672  N   SER A 429      10.587 -24.674  12.473  1.00 60.29           N  
ATOM   1673  CA  SER A 429      10.853 -25.331  13.751  1.00 61.65           C  
ATOM   1674  C   SER A 429      11.722 -24.490  14.683  1.00 53.11           C  
ATOM   1675  O   SER A 429      12.719 -23.904  14.261  1.00 52.87           O  
ATOM   1676  CB  SER A 429      11.503 -26.700  13.527  1.00 67.12           C  
ATOM   1677  OG  SER A 429      12.666 -26.587  12.726  1.00 69.00           O  
ATOM   1678  N   GLN A 430      11.334 -24.451  15.954  1.00 50.06           N  
ATOM   1679  CA  GLN A 430      12.065 -23.711  16.980  1.00 52.90           C  
ATOM   1680  C   GLN A 430      12.264 -22.233  16.633  1.00 49.34           C  
ATOM   1681  O   GLN A 430      13.260 -21.627  17.028  1.00 49.51           O  
ATOM   1682  CB  GLN A 430      13.416 -24.373  17.269  1.00 53.03           C  
ATOM   1683  CG  GLN A 430      13.314 -25.798  17.804  1.00 55.98           C  
ATOM   1684  CD  GLN A 430      12.616 -25.874  19.150  1.00 60.00           C  
ATOM   1685  OE1 GLN A 430      12.939 -25.130  20.076  1.00 59.42           O  
ATOM   1686  NE2 GLN A 430      11.656 -26.782  19.267  1.00 63.91           N  
ATOM   1687  N   LEU A 431      11.319 -21.660  15.895  1.00 46.62           N  
ATOM   1688  CA  LEU A 431      11.366 -20.234  15.581  1.00 47.19           C  
ATOM   1689  C   LEU A 431      11.248 -19.418  16.863  1.00 46.61           C  
ATOM   1690  O   LEU A 431      11.821 -18.334  16.982  1.00 47.23           O  
ATOM   1691  CB  LEU A 431      10.246 -19.853  14.610  1.00 43.19           C  
ATOM   1692  CG  LEU A 431      10.174 -18.370  14.241  1.00 39.60           C  
ATOM   1693  CD1 LEU A 431      11.524 -17.894  13.715  1.00 39.76           C  
ATOM   1694  CD2 LEU A 431       9.070 -18.100  13.224  1.00 34.56           C  
ATOM   1695  N   PHE A 432      10.497 -19.953  17.819  1.00 46.13           N  
ATOM   1696  CA  PHE A 432      10.318 -19.317  19.118  1.00 44.79           C  
ATOM   1697  C   PHE A 432      11.665 -19.186  19.826  1.00 42.62           C  
ATOM   1698  O   PHE A 432      12.051 -18.100  20.256  1.00 45.34           O  
ATOM   1699  CB  PHE A 432       9.335 -20.134  19.961  1.00 46.16           C  
ATOM   1700  CG  PHE A 432       9.100 -19.584  21.340  1.00 44.70           C  
ATOM   1701  CD1 PHE A 432       8.679 -18.277  21.518  1.00 42.18           C  
ATOM   1702  CD2 PHE A 432       9.274 -20.384  22.456  1.00 46.13           C  
ATOM   1703  CE1 PHE A 432       8.453 -17.772  22.787  1.00 37.91           C  
ATOM   1704  CE2 PHE A 432       9.047 -19.887  23.727  1.00 47.34           C  
ATOM   1705  CZ  PHE A 432       8.634 -18.578  23.892  1.00 42.32           C  
ATOM   1706  N   ALA A 433      12.377 -20.301  19.938  1.00 43.98           N  
ATOM   1707  CA  ALA A 433      13.709 -20.309  20.534  1.00 45.62           C  
ATOM   1708  C   ALA A 433      14.659 -19.379  19.780  1.00 48.36           C  
ATOM   1709  O   ALA A 433      15.410 -18.617  20.386  1.00 50.21           O  
ATOM   1710  CB  ALA A 433      14.262 -21.724  20.568  1.00 49.22           C  
ATOM   1711  N   LYS A 434      14.615 -19.440  18.454  1.00 48.75           N  
ATOM   1712  CA  LYS A 434      15.495 -18.628  17.622  1.00 45.30           C  
ATOM   1713  C   LYS A 434      15.222 -17.136  17.795  1.00 46.85           C  
ATOM   1714  O   LYS A 434      16.148 -16.326  17.821  1.00 50.24           O  
ATOM   1715  CB  LYS A 434      15.372 -19.042  16.154  1.00 50.75           C  
ATOM   1716  CG  LYS A 434      15.964 -20.414  15.864  1.00 57.71           C  
ATOM   1717  CD  LYS A 434      15.583 -20.924  14.481  1.00 65.41           C  
ATOM   1718  CE  LYS A 434      16.149 -22.319  14.251  1.00 75.07           C  
ATOM   1719  NZ  LYS A 434      15.635 -22.963  13.008  1.00 79.87           N  
ATOM   1720  N   LEU A 435      13.950 -16.777  17.931  1.00 39.32           N  
ATOM   1721  CA  LEU A 435      13.574 -15.384  18.144  1.00 40.49           C  
ATOM   1722  C   LEU A 435      14.065 -14.865  19.496  1.00 43.13           C  
ATOM   1723  O   LEU A 435      14.599 -13.760  19.589  1.00 43.53           O  
ATOM   1724  CB  LEU A 435      12.059 -15.213  18.018  1.00 37.80           C  
ATOM   1725  CG  LEU A 435      11.498 -13.816  18.285  1.00 37.77           C  
ATOM   1726  CD1 LEU A 435      12.321 -12.757  17.562  1.00 40.61           C  
ATOM   1727  CD2 LEU A 435      10.029 -13.738  17.872  1.00 38.94           C  
ATOM   1728  N   LEU A 436      13.882 -15.663  20.543  1.00 45.18           N  
ATOM   1729  CA  LEU A 436      14.319 -15.272  21.879  1.00 45.23           C  
ATOM   1730  C   LEU A 436      15.834 -15.079  21.939  1.00 48.02           C  
ATOM   1731  O   LEU A 436      16.334 -14.222  22.668  1.00 47.44           O  
ATOM   1732  CB  LEU A 436      13.877 -16.309  22.914  1.00 47.13           C  
ATOM   1733  CG  LEU A 436      12.370 -16.439  23.145  1.00 49.51           C  
ATOM   1734  CD1 LEU A 436      12.090 -17.408  24.282  1.00 51.28           C  
ATOM   1735  CD2 LEU A 436      11.757 -15.082  23.435  1.00 49.11           C  
ATOM   1736  N   GLN A 437      16.562 -15.881  21.170  1.00 51.88           N  
ATOM   1737  CA  GLN A 437      18.016 -15.783  21.135  1.00 52.08           C  
ATOM   1738  C   GLN A 437      18.478 -14.477  20.496  1.00 51.63           C  
ATOM   1739  O   GLN A 437      19.624 -14.066  20.667  1.00 53.41           O  
ATOM   1740  CB  GLN A 437      18.619 -16.971  20.385  1.00 59.27           C  
ATOM   1741  CG  GLN A 437      18.508 -18.292  21.122  1.00 70.12           C  
ATOM   1742  CD  GLN A 437      19.366 -19.374  20.498  1.00 79.56           C  
ATOM   1743  OE1 GLN A 437      19.846 -19.229  19.374  1.00 86.55           O  
ATOM   1744  NE2 GLN A 437      19.565 -20.466  21.226  1.00 80.77           N  
ATOM   1745  N   LYS A 438      17.582 -13.829  19.757  1.00 48.95           N  
ATOM   1746  CA  LYS A 438      17.906 -12.565  19.101  1.00 52.34           C  
ATOM   1747  C   LYS A 438      18.037 -11.427  20.110  1.00 53.64           C  
ATOM   1748  O   LYS A 438      18.477 -10.330  19.769  1.00 50.96           O  
ATOM   1749  CB  LYS A 438      16.866 -12.226  18.030  1.00 51.86           C  
ATOM   1750  CG  LYS A 438      16.918 -13.146  16.820  1.00 52.41           C  
ATOM   1751  CD  LYS A 438      18.288 -13.095  16.161  1.00 51.59           C  
ATOM   1752  CE  LYS A 438      18.428 -14.156  15.082  1.00 57.80           C  
ATOM   1753  NZ  LYS A 438      18.606 -15.514  15.672  1.00 67.19           N  
ATOM   1754  N   MET A 439      17.658 -11.699  21.354  1.00 58.36           N  
ATOM   1755  CA  MET A 439      17.802 -10.724  22.427  1.00 55.74           C  
ATOM   1756  C   MET A 439      19.272 -10.451  22.717  1.00 63.12           C  
ATOM   1757  O   MET A 439      19.648  -9.337  23.083  1.00 68.53           O  
ATOM   1758  CB  MET A 439      17.105 -11.219  23.694  1.00 52.20           C  
ATOM   1759  CG  MET A 439      15.599 -11.335  23.560  1.00 51.02           C  
ATOM   1760  SD  MET A 439      14.875  -9.834  22.874  1.00 88.70           S  
ATOM   1761  CE  MET A 439      15.467  -8.603  24.034  1.00 62.19           C  
ATOM   1762  N   THR A 440      20.098 -11.477  22.550  1.00 62.03           N  
ATOM   1763  CA  THR A 440      21.533 -11.352  22.767  1.00 64.32           C  
ATOM   1764  C   THR A 440      22.130 -10.288  21.853  1.00 63.62           C  
ATOM   1765  O   THR A 440      22.831  -9.384  22.306  1.00 65.25           O  
ATOM   1766  CB  THR A 440      22.254 -12.690  22.520  1.00 63.80           C  
ATOM   1767  OG1 THR A 440      21.761 -13.676  23.436  1.00 64.18           O  
ATOM   1768  CG2 THR A 440      23.755 -12.530  22.707  1.00 65.10           C  
ATOM   1769  N   ASP A 441      21.848 -10.405  20.562  1.00 62.62           N  
ATOM   1770  CA  ASP A 441      22.345  -9.449  19.582  1.00 66.92           C  
ATOM   1771  C   ASP A 441      21.747  -8.068  19.828  1.00 61.50           C  
ATOM   1772  O   ASP A 441      22.408  -7.046  19.640  1.00 62.02           O  
ATOM   1773  CB  ASP A 441      22.005  -9.924  18.170  1.00 73.04           C  
ATOM   1774  CG  ASP A 441      22.424 -11.360  17.924  1.00 83.09           C  
ATOM   1775  OD1 ASP A 441      23.491 -11.770  18.431  1.00 90.22           O  
ATOM   1776  OD2 ASP A 441      21.686 -12.080  17.220  1.00 84.54           O  
ATOM   1777  N   LEU A 442      20.491  -8.050  20.257  1.00 53.49           N  
ATOM   1778  CA  LEU A 442      19.781  -6.802  20.498  1.00 51.90           C  
ATOM   1779  C   LEU A 442      20.477  -5.985  21.588  1.00 51.31           C  
ATOM   1780  O   LEU A 442      20.817  -4.820  21.382  1.00 51.57           O  
ATOM   1781  CB  LEU A 442      18.328  -7.095  20.874  1.00 50.73           C  
ATOM   1782  CG  LEU A 442      17.272  -6.051  20.515  1.00 51.20           C  
ATOM   1783  CD1 LEU A 442      17.494  -5.513  19.105  1.00 47.82           C  
ATOM   1784  CD2 LEU A 442      15.879  -6.648  20.654  1.00 49.39           C  
ATOM   1785  N   ARG A 443      20.702  -6.604  22.742  1.00 53.46           N  
ATOM   1786  CA  ARG A 443      21.364  -5.921  23.849  1.00 59.19           C  
ATOM   1787  C   ARG A 443      22.815  -5.566  23.532  1.00 57.29           C  
ATOM   1788  O   ARG A 443      23.370  -4.627  24.099  1.00 59.12           O  
ATOM   1789  CB  ARG A 443      21.276  -6.752  25.130  1.00 67.44           C  
ATOM   1790  CG  ARG A 443      19.853  -6.922  25.635  1.00 71.91           C  
ATOM   1791  CD  ARG A 443      19.811  -7.255  27.112  1.00 73.38           C  
ATOM   1792  NE  ARG A 443      18.441  -7.459  27.572  1.00 77.27           N  
ATOM   1793  CZ  ARG A 443      18.117  -7.906  28.780  1.00 81.69           C  
ATOM   1794  NH1 ARG A 443      19.069  -8.198  29.657  1.00 83.46           N  
ATOM   1795  NH2 ARG A 443      16.842  -8.063  29.111  1.00 80.68           N  
ATOM   1796  N   GLN A 444      23.425  -6.319  22.625  1.00 56.94           N  
ATOM   1797  CA  GLN A 444      24.780  -6.018  22.187  1.00 61.33           C  
ATOM   1798  C   GLN A 444      24.776  -4.703  21.418  1.00 56.71           C  
ATOM   1799  O   GLN A 444      25.644  -3.853  21.612  1.00 53.65           O  
ATOM   1800  CB  GLN A 444      25.319  -7.140  21.301  1.00 71.14           C  
ATOM   1801  CG  GLN A 444      26.832  -7.207  21.250  1.00 84.17           C  
ATOM   1802  CD  GLN A 444      27.429  -7.676  22.561  1.00 97.51           C  
ATOM   1803  OE1 GLN A 444      28.558  -7.325  22.904  1.00103.20           O  
ATOM   1804  NE2 GLN A 444      26.669  -8.472  23.307  1.00100.59           N  
ATOM   1805  N   ILE A 445      23.783  -4.543  20.549  1.00 56.46           N  
ATOM   1806  CA  ILE A 445      23.630  -3.326  19.760  1.00 58.17           C  
ATOM   1807  C   ILE A 445      23.562  -2.071  20.626  1.00 55.56           C  
ATOM   1808  O   ILE A 445      24.240  -1.082  20.348  1.00 55.42           O  
ATOM   1809  CB  ILE A 445      22.366  -3.384  18.885  1.00 61.30           C  
ATOM   1810  CG1 ILE A 445      22.557  -4.378  17.741  1.00 65.64           C  
ATOM   1811  CG2 ILE A 445      22.031  -2.005  18.340  1.00 61.49           C  
ATOM   1812  CD1 ILE A 445      21.320  -4.560  16.897  1.00 69.18           C  
ATOM   1813  N   VAL A 446      22.744  -2.114  21.674  1.00 54.45           N  
ATOM   1814  CA  VAL A 446      22.543  -0.946  22.528  1.00 55.99           C  
ATOM   1815  C   VAL A 446      23.810  -0.546  23.289  1.00 59.16           C  
ATOM   1816  O   VAL A 446      24.117   0.640  23.410  1.00 60.23           O  
ATOM   1817  CB  VAL A 446      21.367  -1.143  23.518  1.00 60.15           C  
ATOM   1818  CG1 VAL A 446      20.123  -1.602  22.776  1.00 57.17           C  
ATOM   1819  CG2 VAL A 446      21.735  -2.137  24.602  1.00 66.55           C  
ATOM   1820  N   THR A 447      24.546  -1.533  23.793  1.00 58.57           N  
ATOM   1821  CA  THR A 447      25.778  -1.254  24.525  1.00 62.29           C  
ATOM   1822  C   THR A 447      26.778  -0.551  23.614  1.00 63.18           C  
ATOM   1823  O   THR A 447      27.455   0.393  24.022  1.00 63.92           O  
ATOM   1824  CB  THR A 447      26.415  -2.540  25.093  1.00 67.67           C  
ATOM   1825  OG1 THR A 447      26.698  -3.448  24.022  1.00 73.45           O  
ATOM   1826  CG2 THR A 447      25.478  -3.212  26.086  1.00 65.14           C  
ATOM   1827  N   GLU A 448      26.857  -1.015  22.372  1.00 62.18           N  
ATOM   1828  CA  GLU A 448      27.737  -0.410  21.384  1.00 61.64           C  
ATOM   1829  C   GLU A 448      27.277   1.012  21.064  1.00 57.75           C  
ATOM   1830  O   GLU A 448      28.081   1.943  21.013  1.00 56.80           O  
ATOM   1831  CB  GLU A 448      27.759  -1.262  20.114  1.00 64.13           C  
ATOM   1832  CG  GLU A 448      28.846  -0.891  19.125  1.00 72.54           C  
ATOM   1833  CD  GLU A 448      28.847  -1.789  17.899  1.00 78.08           C  
ATOM   1834  OE1 GLU A 448      27.807  -2.426  17.624  1.00 76.06           O  
ATOM   1835  OE2 GLU A 448      29.887  -1.855  17.211  1.00 80.72           O  
ATOM   1836  N   HIS A 449      25.975   1.172  20.858  1.00 55.52           N  
ATOM   1837  CA  HIS A 449      25.402   2.471  20.531  1.00 59.91           C  
ATOM   1838  C   HIS A 449      25.702   3.511  21.609  1.00 63.04           C  
ATOM   1839  O   HIS A 449      26.082   4.642  21.307  1.00 65.32           O  
ATOM   1840  CB  HIS A 449      23.893   2.346  20.324  1.00 62.63           C  
ATOM   1841  CG  HIS A 449      23.239   3.613  19.870  1.00 66.87           C  
ATOM   1842  ND1 HIS A 449      23.183   3.988  18.545  1.00 66.87           N  
ATOM   1843  CD2 HIS A 449      22.614   4.592  20.565  1.00 68.01           C  
ATOM   1844  CE1 HIS A 449      22.551   5.144  18.443  1.00 68.38           C  
ATOM   1845  NE2 HIS A 449      22.196   5.532  19.655  1.00 67.88           N  
ATOM   1846  N   VAL A 450      25.528   3.121  22.867  1.00 63.50           N  
ATOM   1847  CA  VAL A 450      25.775   4.018  23.989  1.00 61.08           C  
ATOM   1848  C   VAL A 450      27.213   4.527  23.991  1.00 65.22           C  
ATOM   1849  O   VAL A 450      27.465   5.705  24.248  1.00 67.20           O  
ATOM   1850  CB  VAL A 450      25.473   3.328  25.331  1.00 61.85           C  
ATOM   1851  CG1 VAL A 450      26.078   4.114  26.486  1.00 61.60           C  
ATOM   1852  CG2 VAL A 450      23.969   3.155  25.510  1.00 58.99           C  
ATOM   1853  N   GLN A 451      28.155   3.634  23.704  1.00 65.39           N  
ATOM   1854  CA  GLN A 451      29.562   4.009  23.654  1.00 69.55           C  
ATOM   1855  C   GLN A 451      29.807   5.084  22.599  1.00 67.70           C  
ATOM   1856  O   GLN A 451      30.590   6.009  22.814  1.00 68.95           O  
ATOM   1857  CB  GLN A 451      30.442   2.786  23.383  1.00 75.16           C  
ATOM   1858  CG  GLN A 451      30.527   1.813  24.548  1.00 80.79           C  
ATOM   1859  CD  GLN A 451      31.444   0.639  24.263  1.00 89.44           C  
ATOM   1860  OE1 GLN A 451      31.686   0.290  23.107  1.00 92.64           O  
ATOM   1861  NE2 GLN A 451      31.960   0.021  25.321  1.00 91.78           N  
ATOM   1862  N   LEU A 452      29.131   4.960  21.462  1.00 64.15           N  
ATOM   1863  CA  LEU A 452      29.280   5.927  20.379  1.00 65.93           C  
ATOM   1864  C   LEU A 452      28.729   7.301  20.759  1.00 63.17           C  
ATOM   1865  O   LEU A 452      29.309   8.328  20.407  1.00 66.75           O  
ATOM   1866  CB  LEU A 452      28.613   5.417  19.100  1.00 67.59           C  
ATOM   1867  CG  LEU A 452      29.330   4.269  18.387  1.00 72.05           C  
ATOM   1868  CD1 LEU A 452      28.570   3.851  17.138  1.00 71.51           C  
ATOM   1869  CD2 LEU A 452      30.760   4.663  18.044  1.00 74.59           C  
ATOM   1870  N   LEU A 453      27.610   7.316  21.477  1.00 55.27           N  
ATOM   1871  CA  LEU A 453      27.014   8.567  21.934  1.00 55.66           C  
ATOM   1872  C   LEU A 453      27.940   9.296  22.906  1.00 61.08           C  
ATOM   1873  O   LEU A 453      27.998  10.526  22.923  1.00 65.86           O  
ATOM   1874  CB  LEU A 453      25.663   8.309  22.602  1.00 54.73           C  
ATOM   1875  CG  LEU A 453      24.537   7.737  21.740  1.00 56.45           C  
ATOM   1876  CD1 LEU A 453      23.315   7.462  22.600  1.00 57.55           C  
ATOM   1877  CD2 LEU A 453      24.186   8.676  20.594  1.00 56.73           C  
ATOM   1878  N   GLN A 454      28.662   8.531  23.718  1.00 59.16           N  
ATOM   1879  CA  GLN A 454      29.579   9.113  24.690  1.00 59.21           C  
ATOM   1880  C   GLN A 454      30.719   9.849  23.994  1.00 59.25           C  
ATOM   1881  O   GLN A 454      31.187  10.882  24.472  1.00 64.59           O  
ATOM   1882  CB  GLN A 454      30.128   8.036  25.627  1.00 66.42           C  
ATOM   1883  CG  GLN A 454      29.075   7.412  26.532  1.00 71.77           C  
ATOM   1884  CD  GLN A 454      29.642   6.328  27.433  1.00 78.75           C  
ATOM   1885  OE1 GLN A 454      28.949   5.809  28.310  1.00 80.91           O  
ATOM   1886  NE2 GLN A 454      30.908   5.982  27.221  1.00 79.98           N  
ATOM   1887  N   VAL A 455      31.159   9.315  22.860  1.00 58.40           N  
ATOM   1888  CA  VAL A 455      32.212   9.952  22.081  1.00 61.89           C  
ATOM   1889  C   VAL A 455      31.775  11.325  21.577  1.00 59.57           C  
ATOM   1890  O   VAL A 455      32.436  12.332  21.835  1.00 61.72           O  
ATOM   1891  CB  VAL A 455      32.630   9.086  20.879  1.00 63.78           C  
ATOM   1892  CG1 VAL A 455      33.479   9.897  19.913  1.00 65.24           C  
ATOM   1893  CG2 VAL A 455      33.376   7.846  21.350  1.00 65.09           C  
ATOM   1894  N   ILE A 456      30.657  11.361  20.859  1.00 59.44           N  
ATOM   1895  CA  ILE A 456      30.164  12.609  20.283  1.00 62.95           C  
ATOM   1896  C   ILE A 456      29.887  13.666  21.353  1.00 61.34           C  
ATOM   1897  O   ILE A 456      30.099  14.856  21.126  1.00 62.78           O  
ATOM   1898  CB  ILE A 456      28.905  12.389  19.414  1.00 64.84           C  
ATOM   1899  CG1 ILE A 456      27.793  11.730  20.230  1.00 66.42           C  
ATOM   1900  CG2 ILE A 456      29.240  11.542  18.192  1.00 64.55           C  
ATOM   1901  CD1 ILE A 456      26.629  11.250  19.392  1.00 68.14           C  
ATOM   1902  N   LYS A 457      29.424  13.226  22.519  1.00 58.20           N  
ATOM   1903  CA  LYS A 457      29.175  14.138  23.632  1.00 61.59           C  
ATOM   1904  C   LYS A 457      30.439  14.907  24.019  1.00 66.36           C  
ATOM   1905  O   LYS A 457      30.369  16.053  24.464  1.00 71.12           O  
ATOM   1906  CB  LYS A 457      28.631  13.375  24.842  1.00 59.36           C  
ATOM   1907  N   LYS A 458      31.594  14.272  23.842  1.00 64.87           N  
ATOM   1908  CA  LYS A 458      32.870  14.888  24.191  1.00 62.60           C  
ATOM   1909  C   LYS A 458      33.487  15.660  23.026  1.00 60.10           C  
ATOM   1910  O   LYS A 458      34.187  16.653  23.233  1.00 65.89           O  
ATOM   1911  CB  LYS A 458      33.853  13.828  24.694  1.00 65.25           C  
ATOM   1912  CG  LYS A 458      33.541  13.301  26.085  1.00 65.76           C  
ATOM   1913  CD  LYS A 458      34.585  12.291  26.536  1.00 68.79           C  
ATOM   1914  CE  LYS A 458      34.429  11.954  28.011  1.00 72.16           C  
ATOM   1915  NZ  LYS A 458      34.563  13.165  28.870  1.00 76.99           N  
ATOM   1916  N   THR A 459      33.225  15.205  21.805  1.00 55.64           N  
ATOM   1917  CA  THR A 459      33.822  15.818  20.622  1.00 63.84           C  
ATOM   1918  C   THR A 459      32.950  16.918  20.014  1.00 62.80           C  
ATOM   1919  O   THR A 459      33.464  17.858  19.409  1.00 63.39           O  
ATOM   1920  CB  THR A 459      34.159  14.764  19.548  1.00 66.59           C  
ATOM   1921  OG1 THR A 459      32.983  14.011  19.227  1.00 70.52           O  
ATOM   1922  CG2 THR A 459      35.234  13.814  20.054  1.00 72.05           C  
ATOM   1923  N   GLU A 460      31.635  16.794  20.170  1.00 60.35           N  
ATOM   1924  CA  GLU A 460      30.707  17.831  19.718  1.00 65.03           C  
ATOM   1925  C   GLU A 460      29.952  18.459  20.882  1.00 63.42           C  
ATOM   1926  O   GLU A 460      28.811  18.094  21.166  1.00 62.32           O  
ATOM   1927  CB  GLU A 460      29.714  17.281  18.693  1.00 67.93           C  
ATOM   1928  CG  GLU A 460      30.117  17.523  17.250  1.00 74.47           C  
ATOM   1929  CD  GLU A 460      31.267  16.646  16.813  1.00 75.48           C  
ATOM   1930  OE1 GLU A 460      31.232  15.435  17.112  1.00 75.26           O  
ATOM   1931  OE2 GLU A 460      32.200  17.166  16.166  1.00 76.20           O  
ATOM   1932  N   THR A 461      30.593  19.412  21.547  1.00 65.64           N  
ATOM   1933  CA  THR A 461      29.994  20.072  22.697  1.00 65.61           C  
ATOM   1934  C   THR A 461      28.910  21.061  22.276  1.00 60.35           C  
ATOM   1935  O   THR A 461      28.199  21.605  23.116  1.00 57.03           O  
ATOM   1936  CB  THR A 461      31.056  20.806  23.530  1.00 68.93           C  
ATOM   1937  OG1 THR A 461      31.758  21.732  22.693  1.00 72.59           O  
ATOM   1938  CG2 THR A 461      32.045  19.813  24.121  1.00 69.42           C  
ATOM   1939  N   ASP A 462      28.783  21.292  20.974  1.00 56.65           N  
ATOM   1940  CA  ASP A 462      27.777  22.219  20.468  1.00 58.18           C  
ATOM   1941  C   ASP A 462      26.482  21.493  20.110  1.00 58.29           C  
ATOM   1942  O   ASP A 462      25.515  22.112  19.670  1.00 58.54           O  
ATOM   1943  CB  ASP A 462      28.308  22.976  19.252  1.00 62.55           C  
ATOM   1944  CG  ASP A 462      28.463  22.087  18.037  1.00 68.48           C  
ATOM   1945  OD1 ASP A 462      29.077  21.006  18.161  1.00 71.08           O  
ATOM   1946  OD2 ASP A 462      27.970  22.472  16.955  1.00 71.04           O  
ATOM   1947  N   MET A 463      26.470  20.179  20.307  1.00 57.16           N  
ATOM   1948  CA  MET A 463      25.317  19.359  19.955  1.00 60.46           C  
ATOM   1949  C   MET A 463      24.499  18.977  21.177  1.00 65.91           C  
ATOM   1950  O   MET A 463      25.051  18.678  22.235  1.00 64.27           O  
ATOM   1951  CB  MET A 463      25.767  18.088  19.242  1.00 63.00           C  
ATOM   1952  CG  MET A 463      25.956  18.236  17.751  1.00 66.56           C  
ATOM   1953  SD  MET A 463      26.264  16.628  17.007  1.00 78.11           S  
ATOM   1954  CE  MET A 463      25.015  15.637  17.825  1.00 52.93           C  
ATOM   1955  N   SER A 464      23.179  18.972  21.015  1.00 73.92           N  
ATOM   1956  CA  SER A 464      22.273  18.661  22.114  1.00 81.67           C  
ATOM   1957  C   SER A 464      21.414  17.431  21.831  1.00 79.17           C  
ATOM   1958  O   SER A 464      20.712  17.369  20.822  1.00 78.89           O  
ATOM   1959  CB  SER A 464      21.384  19.868  22.432  1.00 82.95           C  
ATOM   1960  OG  SER A 464      20.860  20.451  21.250  1.00 80.57           O  
ATOM   1961  N   LEU A 465      21.480  16.453  22.729  1.00 77.95           N  
ATOM   1962  CA  LEU A 465      20.623  15.279  22.645  1.00 74.19           C  
ATOM   1963  C   LEU A 465      19.255  15.619  23.229  1.00 68.41           C  
ATOM   1964  O   LEU A 465      19.163  16.187  24.315  1.00 70.02           O  
ATOM   1965  CB  LEU A 465      21.247  14.105  23.403  1.00 76.03           C  
ATOM   1966  CG  LEU A 465      20.656  12.714  23.162  1.00 79.22           C  
ATOM   1967  CD1 LEU A 465      20.915  12.258  21.732  1.00 80.88           C  
ATOM   1968  CD2 LEU A 465      21.230  11.710  24.153  1.00 79.92           C  
ATOM   1969  N   HIS A 466      18.201  15.280  22.494  1.00 62.92           N  
ATOM   1970  CA  HIS A 466      16.832  15.581  22.903  1.00 61.78           C  
ATOM   1971  C   HIS A 466      16.570  15.145  24.345  1.00 63.72           C  
ATOM   1972  O   HIS A 466      16.969  14.054  24.749  1.00 63.06           O  
ATOM   1973  CB  HIS A 466      15.843  14.900  21.954  1.00 59.86           C  
ATOM   1974  CG  HIS A 466      14.423  15.337  22.138  1.00 58.85           C  
ATOM   1975  ND1 HIS A 466      13.639  14.901  23.185  1.00 57.46           N  
ATOM   1976  CD2 HIS A 466      13.642  16.162  21.402  1.00 55.76           C  
ATOM   1977  CE1 HIS A 466      12.439  15.445  23.089  1.00 53.94           C  
ATOM   1978  NE2 HIS A 466      12.414  16.213  22.015  1.00 54.69           N  
ATOM   1979  N   PRO A 467      15.894  16.003  25.125  1.00 66.93           N  
ATOM   1980  CA  PRO A 467      15.626  15.757  26.547  1.00 69.50           C  
ATOM   1981  C   PRO A 467      15.039  14.373  26.810  1.00 63.81           C  
ATOM   1982  O   PRO A 467      15.508  13.673  27.709  1.00 57.71           O  
ATOM   1983  CB  PRO A 467      14.602  16.838  26.895  1.00 72.44           C  
ATOM   1984  CG  PRO A 467      14.911  17.949  25.958  1.00 73.61           C  
ATOM   1985  CD  PRO A 467      15.344  17.294  24.676  1.00 71.30           C  
ATOM   1986  N   LEU A 468      14.026  13.989  26.040  1.00 61.80           N  
ATOM   1987  CA  LEU A 468      13.415  12.675  26.192  1.00 56.38           C  
ATOM   1988  C   LEU A 468      14.470  11.583  26.063  1.00 57.12           C  
ATOM   1989  O   LEU A 468      14.474  10.618  26.827  1.00 60.81           O  
ATOM   1990  CB  LEU A 468      12.303  12.467  25.161  1.00 58.97           C  
ATOM   1991  CG  LEU A 468      11.556  11.132  25.237  1.00 61.99           C  
ATOM   1992  CD1 LEU A 468      11.009  10.890  26.638  1.00 65.36           C  
ATOM   1993  CD2 LEU A 468      10.435  11.077  24.211  1.00 60.09           C  
ATOM   1994  N   LEU A 469      15.372  11.751  25.101  1.00 53.97           N  
ATOM   1995  CA  LEU A 469      16.431  10.777  24.862  1.00 52.49           C  
ATOM   1996  C   LEU A 469      17.510  10.818  25.942  1.00 56.63           C  
ATOM   1997  O   LEU A 469      18.154   9.806  26.225  1.00 56.35           O  
ATOM   1998  CB  LEU A 469      17.053  10.986  23.478  1.00 51.75           C  
ATOM   1999  CG  LEU A 469      16.140  10.664  22.292  1.00 47.75           C  
ATOM   2000  CD1 LEU A 469      16.869  10.894  20.978  1.00 45.49           C  
ATOM   2001  CD2 LEU A 469      15.615   9.235  22.379  1.00 40.36           C  
ATOM   2002  N   GLN A 470      17.705  11.988  26.543  1.00 59.35           N  
ATOM   2003  CA  GLN A 470      18.678  12.129  27.621  1.00 68.64           C  
ATOM   2004  C   GLN A 470      18.244  11.362  28.864  1.00 68.86           C  
ATOM   2005  O   GLN A 470      19.031  10.621  29.452  1.00 66.21           O  
ATOM   2006  CB  GLN A 470      18.898  13.601  27.970  1.00 74.35           C  
ATOM   2007  CG  GLN A 470      19.702  14.366  26.941  1.00 79.68           C  
ATOM   2008  CD  GLN A 470      20.459  15.527  27.549  1.00 85.60           C  
ATOM   2009  OE1 GLN A 470      20.466  15.708  28.767  1.00 86.45           O  
ATOM   2010  NE2 GLN A 470      21.109  16.318  26.704  1.00 88.04           N  
ATOM   2011  N   GLU A 471      16.987  11.549  29.258  1.00 68.33           N  
ATOM   2012  CA  GLU A 471      16.445  10.897  30.446  1.00 68.24           C  
ATOM   2013  C   GLU A 471      16.473   9.380  30.302  1.00 69.01           C  
ATOM   2014  O   GLU A 471      16.523   8.652  31.293  1.00 73.02           O  
ATOM   2015  CB  GLU A 471      15.017  11.375  30.720  1.00 64.55           C  
ATOM   2016  N   ILE A 472      16.443   8.908  29.061  1.00 60.77           N  
ATOM   2017  CA  ILE A 472      16.495   7.477  28.790  1.00 59.55           C  
ATOM   2018  C   ILE A 472      17.895   6.917  29.024  1.00 68.56           C  
ATOM   2019  O   ILE A 472      18.055   5.852  29.622  1.00 72.46           O  
ATOM   2020  CB  ILE A 472      16.056   7.162  27.348  1.00 52.67           C  
ATOM   2021  CG1 ILE A 472      14.589   7.544  27.145  1.00 52.32           C  
ATOM   2022  CG2 ILE A 472      16.269   5.691  27.037  1.00 50.21           C  
ATOM   2023  CD1 ILE A 472      14.109   7.386  25.722  1.00 48.84           C  
ATOM   2024  N   TYR A 473      18.907   7.644  28.560  1.00 69.50           N  
ATOM   2025  CA  TYR A 473      20.289   7.178  28.651  1.00 71.17           C  
ATOM   2026  C   TYR A 473      20.950   7.479  29.996  1.00 75.13           C  
ATOM   2027  O   TYR A 473      21.922   6.824  30.373  1.00 76.84           O  
ATOM   2028  CB  TYR A 473      21.128   7.753  27.507  1.00 70.14           C  
ATOM   2029  CG  TYR A 473      20.912   7.048  26.187  1.00 69.09           C  
ATOM   2030  CD1 TYR A 473      21.363   5.750  25.994  1.00 66.93           C  
ATOM   2031  CD2 TYR A 473      20.261   7.678  25.134  1.00 65.91           C  
ATOM   2032  CE1 TYR A 473      21.172   5.097  24.796  1.00 63.89           C  
ATOM   2033  CE2 TYR A 473      20.067   7.031  23.926  1.00 64.13           C  
ATOM   2034  CZ  TYR A 473      20.526   5.739  23.766  1.00 62.87           C  
ATOM   2035  OH  TYR A 473      20.341   5.080  22.573  1.00 60.97           O  
ATOM   2036  N   LYS A 474      20.426   8.467  30.713  1.00 75.91           N  
ATOM   2037  CA  LYS A 474      20.968   8.824  32.019  1.00 79.52           C  
ATOM   2038  C   LYS A 474      20.983   7.611  32.940  1.00 83.80           C  
ATOM   2039  O   LYS A 474      19.947   6.987  33.174  1.00 79.27           O  
ATOM   2040  CB  LYS A 474      20.155   9.956  32.651  1.00 78.50           C  
ATOM   2041  N   ASP A 475      22.163   7.278  33.454  1.00 92.78           N  
ATOM   2042  CA  ASP A 475      22.325   6.137  34.350  1.00 99.48           C  
ATOM   2043  C   ASP A 475      21.830   4.841  33.711  1.00101.64           C  
ATOM   2044  O   ASP A 475      21.173   4.026  34.361  1.00100.82           O  
ATOM   2045  CB  ASP A 475      21.603   6.388  35.675  1.00101.04           C  
ATOM   2046  CG  ASP A 475      22.178   7.566  36.436  1.00104.45           C  
ATOM   2047  OD1 ASP A 475      23.321   7.971  36.135  1.00105.13           O  
ATOM   2048  OD2 ASP A 475      21.489   8.086  37.339  1.00106.80           O  
ATOM   2049  N   LEU A 476      22.151   4.657  32.435  1.00103.48           N  
ATOM   2050  CA  LEU A 476      21.771   3.449  31.715  1.00104.64           C  
ATOM   2051  C   LEU A 476      22.916   2.441  31.745  1.00108.50           C  
ATOM   2052  O   LEU A 476      23.946   2.644  31.100  1.00111.47           O  
ATOM   2053  CB  LEU A 476      21.406   3.788  30.268  1.00102.24           C  
ATOM   2054  CG  LEU A 476      20.594   2.753  29.488  1.00 98.98           C  
ATOM   2055  CD1 LEU A 476      19.204   2.614  30.081  1.00 97.32           C  
ATOM   2056  CD2 LEU A 476      20.510   3.137  28.021  1.00 97.64           C  
ATOM   2057  N   TYR A 477      22.734   1.361  32.499  1.00108.99           N  
ATOM   2058  CA  TYR A 477      23.765   0.334  32.643  1.00113.63           C  
ATOM   2059  C   TYR A 477      25.059   0.900  33.225  1.00118.52           C  
ATOM   2060  O   TYR A 477      25.164   2.091  33.520  1.00120.56           O  
ATOM   2061  CB  TYR A 477      24.053  -0.347  31.301  1.00111.55           C  
ATOM   2062  CG  TYR A 477      22.931  -1.223  30.795  1.00107.78           C  
ATOM   2063  CD1 TYR A 477      22.661  -2.449  31.389  1.00107.15           C  
ATOM   2064  CD2 TYR A 477      22.148  -0.831  29.716  1.00103.48           C  
ATOM   2065  CE1 TYR A 477      21.641  -3.256  30.930  1.00104.52           C  
ATOM   2066  CE2 TYR A 477      21.124  -1.633  29.249  1.00101.18           C  
ATOM   2067  CZ  TYR A 477      20.875  -2.846  29.861  1.00102.04           C  
ATOM   2068  OH  TYR A 477      19.859  -3.654  29.406  1.00100.02           O  
ATOM   2069  OXT TYR A 477      26.034   0.173  33.415  1.00119.85           O  
TER    2070      TYR A 477                                                      
ATOM   2071  N   GLU B 207       8.631 -39.405  17.891  1.00 79.38           N  
ATOM   2072  CA  GLU B 207       9.490 -38.242  18.078  1.00 78.48           C  
ATOM   2073  C   GLU B 207       9.750 -37.986  19.558  1.00 73.85           C  
ATOM   2074  O   GLU B 207      10.878 -37.698  19.955  1.00 74.78           O  
ATOM   2075  CB  GLU B 207       8.871 -37.002  17.426  1.00 82.65           C  
ATOM   2076  CG  GLU B 207       9.700 -35.730  17.567  1.00 83.12           C  
ATOM   2077  CD  GLU B 207      10.945 -35.736  16.699  1.00 87.55           C  
ATOM   2078  OE1 GLU B 207      11.394 -34.642  16.292  1.00 88.27           O  
ATOM   2079  OE2 GLU B 207      11.473 -36.832  16.418  1.00 90.29           O  
ATOM   2080  N   SER B 208       8.704 -38.094  20.370  1.00 71.35           N  
ATOM   2081  CA  SER B 208       8.835 -37.906  21.811  1.00 68.71           C  
ATOM   2082  C   SER B 208       9.844 -38.883  22.398  1.00 65.58           C  
ATOM   2083  O   SER B 208      10.739 -38.491  23.145  1.00 65.50           O  
ATOM   2084  CB  SER B 208       7.483 -38.074  22.505  1.00 74.10           C  
ATOM   2085  OG  SER B 208       6.615 -37.000  22.193  1.00 77.70           O  
ATOM   2086  N   ALA B 209       9.692 -40.159  22.058  1.00 65.15           N  
ATOM   2087  CA  ALA B 209      10.600 -41.194  22.535  1.00 64.59           C  
ATOM   2088  C   ALA B 209      12.038 -40.881  22.139  1.00 62.91           C  
ATOM   2089  O   ALA B 209      12.966 -41.101  22.916  1.00 64.80           O  
ATOM   2090  CB  ALA B 209      10.184 -42.554  21.997  1.00 63.51           C  
ATOM   2091  N   ASP B 210      12.215 -40.368  20.925  1.00 61.01           N  
ATOM   2092  CA  ASP B 210      13.538 -40.008  20.431  1.00 60.64           C  
ATOM   2093  C   ASP B 210      14.144 -38.882  21.264  1.00 55.39           C  
ATOM   2094  O   ASP B 210      15.330 -38.909  21.591  1.00 57.08           O  
ATOM   2095  CB  ASP B 210      13.471 -39.597  18.958  1.00 67.95           C  
ATOM   2096  CG  ASP B 210      13.102 -40.752  18.045  1.00 76.57           C  
ATOM   2097  OD1 ASP B 210      12.663 -41.803  18.557  1.00 79.69           O  
ATOM   2098  OD2 ASP B 210      13.252 -40.607  16.813  1.00 79.75           O  
ATOM   2099  N   LEU B 211      13.322 -37.894  21.603  1.00 50.15           N  
ATOM   2100  CA  LEU B 211      13.770 -36.772  22.417  1.00 46.75           C  
ATOM   2101  C   LEU B 211      14.151 -37.233  23.819  1.00 47.84           C  
ATOM   2102  O   LEU B 211      15.133 -36.760  24.389  1.00 51.27           O  
ATOM   2103  CB  LEU B 211      12.689 -35.692  22.490  1.00 45.03           C  
ATOM   2104  CG  LEU B 211      12.330 -35.018  21.163  1.00 49.84           C  
ATOM   2105  CD1 LEU B 211      11.200 -34.018  21.355  1.00 49.79           C  
ATOM   2106  CD2 LEU B 211      13.551 -34.343  20.549  1.00 50.34           C  
ATOM   2107  N   ARG B 212      13.368 -38.156  24.370  1.00 47.30           N  
ATOM   2108  CA  ARG B 212      13.645 -38.706  25.692  1.00 47.73           C  
ATOM   2109  C   ARG B 212      14.956 -39.487  25.691  1.00 49.26           C  
ATOM   2110  O   ARG B 212      15.732 -39.418  26.644  1.00 46.14           O  
ATOM   2111  CB  ARG B 212      12.495 -39.602  26.157  1.00 51.76           C  
ATOM   2112  CG  ARG B 212      11.172 -38.873  26.308  1.00 58.45           C  
ATOM   2113  CD  ARG B 212      11.357 -37.591  27.101  1.00 62.71           C  
ATOM   2114  NE  ARG B 212      11.763 -37.857  28.477  1.00 65.78           N  
ATOM   2115  CZ  ARG B 212      12.501 -37.033  29.213  1.00 64.84           C  
ATOM   2116  NH1 ARG B 212      12.932 -35.884  28.705  1.00 57.64           N  
ATOM   2117  NH2 ARG B 212      12.817 -37.365  30.456  1.00 67.17           N  
ATOM   2118  N   ALA B 213      15.195 -40.232  24.616  1.00 50.22           N  
ATOM   2119  CA  ALA B 213      16.440 -40.973  24.464  1.00 53.61           C  
ATOM   2120  C   ALA B 213      17.619 -40.008  24.400  1.00 53.42           C  
ATOM   2121  O   ALA B 213      18.636 -40.208  25.062  1.00 52.26           O  
ATOM   2122  CB  ALA B 213      16.393 -41.844  23.217  1.00 55.29           C  
ATOM   2123  N   LEU B 214      17.471 -38.958  23.600  1.00 52.26           N  
ATOM   2124  CA  LEU B 214      18.504 -37.938  23.480  1.00 47.47           C  
ATOM   2125  C   LEU B 214      18.773 -37.301  24.838  1.00 46.24           C  
ATOM   2126  O   LEU B 214      19.922 -37.044  25.199  1.00 39.62           O  
ATOM   2127  CB  LEU B 214      18.084 -36.870  22.469  1.00 46.16           C  
ATOM   2128  CG  LEU B 214      19.032 -35.682  22.295  1.00 42.70           C  
ATOM   2129  CD1 LEU B 214      20.440 -36.169  21.969  1.00 38.25           C  
ATOM   2130  CD2 LEU B 214      18.520 -34.738  21.221  1.00 38.79           C  
ATOM   2131  N   ALA B 215      17.705 -37.054  25.589  1.00 46.60           N  
ATOM   2132  CA  ALA B 215      17.826 -36.472  26.921  1.00 42.01           C  
ATOM   2133  C   ALA B 215      18.615 -37.390  27.849  1.00 41.79           C  
ATOM   2134  O   ALA B 215      19.524 -36.945  28.550  1.00 42.40           O  
ATOM   2135  CB  ALA B 215      16.447 -36.181  27.504  1.00 41.16           C  
ATOM   2136  N   LYS B 216      18.265 -38.673  27.846  1.00 41.96           N  
ATOM   2137  CA  LYS B 216      18.933 -39.646  28.703  1.00 45.32           C  
ATOM   2138  C   LYS B 216      20.395 -39.839  28.301  1.00 46.45           C  
ATOM   2139  O   LYS B 216      21.280 -39.922  29.154  1.00 44.55           O  
ATOM   2140  CB  LYS B 216      18.196 -40.986  28.674  1.00 51.28           C  
ATOM   2141  CG  LYS B 216      18.853 -42.054  29.529  1.00 58.06           C  
ATOM   2142  CD  LYS B 216      18.067 -43.351  29.512  1.00 69.30           C  
ATOM   2143  CE  LYS B 216      18.827 -44.449  30.239  1.00 73.77           C  
ATOM   2144  NZ  LYS B 216      19.378 -43.973  31.538  1.00 75.05           N  
ATOM   2145  N   HIS B 217      20.637 -39.920  26.997  1.00 48.14           N  
ATOM   2146  CA  HIS B 217      21.991 -40.059  26.473  1.00 43.87           C  
ATOM   2147  C   HIS B 217      22.890 -38.931  26.964  1.00 39.73           C  
ATOM   2148  O   HIS B 217      23.992 -39.171  27.454  1.00 40.30           O  
ATOM   2149  CB  HIS B 217      21.975 -40.085  24.943  1.00 43.24           C  
ATOM   2150  CG  HIS B 217      23.329 -39.929  24.326  1.00 41.01           C  
ATOM   2151  ND1 HIS B 217      24.217 -40.977  24.200  1.00 44.44           N  
ATOM   2152  CD2 HIS B 217      23.953 -38.845  23.805  1.00 35.99           C  
ATOM   2153  CE1 HIS B 217      25.325 -40.547  23.625  1.00 42.35           C  
ATOM   2154  NE2 HIS B 217      25.192 -39.257  23.377  1.00 42.74           N  
ATOM   2155  N   LEU B 218      22.411 -37.698  26.829  1.00 38.78           N  
ATOM   2156  CA  LEU B 218      23.163 -36.528  27.268  1.00 33.86           C  
ATOM   2157  C   LEU B 218      23.415 -36.542  28.776  1.00 36.43           C  
ATOM   2158  O   LEU B 218      24.525 -36.258  29.233  1.00 37.21           O  
ATOM   2159  CB  LEU B 218      22.437 -35.242  26.863  1.00 33.74           C  
ATOM   2160  CG  LEU B 218      22.389 -34.967  25.359  1.00 37.93           C  
ATOM   2161  CD1 LEU B 218      21.616 -33.691  25.070  1.00 39.43           C  
ATOM   2162  CD2 LEU B 218      23.798 -34.880  24.804  1.00 32.06           C  
ATOM   2163  N   TYR B 219      22.382 -36.864  29.547  1.00 41.91           N  
ATOM   2164  CA  TYR B 219      22.523 -36.923  30.997  1.00 43.67           C  
ATOM   2165  C   TYR B 219      23.587 -37.939  31.406  1.00 42.66           C  
ATOM   2166  O   TYR B 219      24.432 -37.653  32.251  1.00 43.69           O  
ATOM   2167  CB  TYR B 219      21.190 -37.256  31.668  1.00 45.23           C  
ATOM   2168  CG  TYR B 219      21.319 -37.517  33.152  1.00 51.01           C  
ATOM   2169  CD1 TYR B 219      21.627 -36.489  34.030  1.00 51.86           C  
ATOM   2170  CD2 TYR B 219      21.138 -38.790  33.674  1.00 57.65           C  
ATOM   2171  CE1 TYR B 219      21.748 -36.719  35.385  1.00 53.10           C  
ATOM   2172  CE2 TYR B 219      21.258 -39.028  35.032  1.00 60.62           C  
ATOM   2173  CZ  TYR B 219      21.563 -37.987  35.881  1.00 57.18           C  
ATOM   2174  OH  TYR B 219      21.686 -38.207  37.233  1.00 62.03           O  
ATOM   2175  N   ASP B 220      23.541 -39.124  30.802  1.00 45.15           N  
ATOM   2176  CA  ASP B 220      24.521 -40.168  31.086  1.00 47.36           C  
ATOM   2177  C   ASP B 220      25.943 -39.690  30.799  1.00 46.29           C  
ATOM   2178  O   ASP B 220      26.860 -39.934  31.579  1.00 46.64           O  
ATOM   2179  CB  ASP B 220      24.218 -41.435  30.276  1.00 48.96           C  
ATOM   2180  CG  ASP B 220      23.031 -42.212  30.824  1.00 53.30           C  
ATOM   2181  OD1 ASP B 220      22.730 -42.072  32.028  1.00 53.97           O  
ATOM   2182  OD2 ASP B 220      22.401 -42.968  30.052  1.00 53.80           O  
ATOM   2183  N   SER B 221      26.120 -39.005  29.674  1.00 44.40           N  
ATOM   2184  CA  SER B 221      27.432 -38.497  29.290  1.00 42.61           C  
ATOM   2185  C   SER B 221      27.886 -37.380  30.224  1.00 43.80           C  
ATOM   2186  O   SER B 221      29.057 -37.295  30.596  1.00 42.09           O  
ATOM   2187  CB  SER B 221      27.395 -37.987  27.852  1.00 45.76           C  
ATOM   2188  OG  SER B 221      28.543 -37.213  27.571  1.00 50.47           O  
ATOM   2189  N   TYR B 222      26.941 -36.521  30.585  1.00 43.97           N  
ATOM   2190  CA  TYR B 222      27.171 -35.434  31.526  1.00 38.99           C  
ATOM   2191  C   TYR B 222      27.718 -35.978  32.849  1.00 41.44           C  
ATOM   2192  O   TYR B 222      28.663 -35.428  33.417  1.00 39.18           O  
ATOM   2193  CB  TYR B 222      25.850 -34.692  31.726  1.00 38.22           C  
ATOM   2194  CG  TYR B 222      25.817 -33.616  32.787  1.00 36.42           C  
ATOM   2195  CD1 TYR B 222      25.585 -33.935  34.119  1.00 37.11           C  
ATOM   2196  CD2 TYR B 222      25.953 -32.274  32.448  1.00 34.84           C  
ATOM   2197  CE1 TYR B 222      25.522 -32.951  35.091  1.00 38.92           C  
ATOM   2198  CE2 TYR B 222      25.893 -31.281  33.414  1.00 35.78           C  
ATOM   2199  CZ  TYR B 222      25.674 -31.627  34.733  1.00 39.38           C  
ATOM   2200  OH  TYR B 222      25.613 -30.652  35.699  1.00 40.17           O  
ATOM   2201  N   ILE B 223      27.129 -37.070  33.326  1.00 37.85           N  
ATOM   2202  CA  ILE B 223      27.583 -37.713  34.554  1.00 40.84           C  
ATOM   2203  C   ILE B 223      28.983 -38.303  34.375  1.00 43.34           C  
ATOM   2204  O   ILE B 223      29.794 -38.311  35.300  1.00 42.43           O  
ATOM   2205  CB  ILE B 223      26.608 -38.823  34.992  1.00 45.85           C  
ATOM   2206  CG1 ILE B 223      25.331 -38.209  35.572  1.00 49.16           C  
ATOM   2207  CG2 ILE B 223      27.262 -39.748  36.011  1.00 47.00           C  
ATOM   2208  CD1 ILE B 223      25.555 -37.432  36.844  1.00 47.54           C  
ATOM   2209  N   LYS B 224      29.262 -38.789  33.173  1.00 44.83           N  
ATOM   2210  CA  LYS B 224      30.563 -39.367  32.863  1.00 52.08           C  
ATOM   2211  C   LYS B 224      31.639 -38.285  32.783  1.00 49.46           C  
ATOM   2212  O   LYS B 224      32.789 -38.513  33.158  1.00 48.86           O  
ATOM   2213  CB  LYS B 224      30.484 -40.138  31.541  1.00 59.44           C  
ATOM   2214  CG  LYS B 224      31.604 -41.139  31.302  1.00 68.66           C  
ATOM   2215  CD  LYS B 224      32.843 -40.477  30.722  1.00 73.52           C  
ATOM   2216  CE  LYS B 224      33.791 -41.510  30.124  1.00 78.80           C  
ATOM   2217  NZ  LYS B 224      34.121 -42.600  31.085  1.00 79.71           N  
ATOM   2218  N   SER B 225      31.253 -37.102  32.311  1.00 44.51           N  
ATOM   2219  CA  SER B 225      32.213 -36.038  32.025  1.00 42.46           C  
ATOM   2220  C   SER B 225      32.478 -35.081  33.187  1.00 42.48           C  
ATOM   2221  O   SER B 225      33.582 -34.556  33.317  1.00 46.18           O  
ATOM   2222  CB  SER B 225      31.774 -35.239  30.793  1.00 42.40           C  
ATOM   2223  OG  SER B 225      31.994 -35.969  29.600  1.00 46.57           O  
ATOM   2224  N   PHE B 226      31.470 -34.843  34.018  1.00 43.80           N  
ATOM   2225  CA  PHE B 226      31.592 -33.862  35.093  1.00 43.33           C  
ATOM   2226  C   PHE B 226      31.539 -34.511  36.475  1.00 48.10           C  
ATOM   2227  O   PHE B 226      30.468 -34.892  36.948  1.00 52.45           O  
ATOM   2228  CB  PHE B 226      30.502 -32.795  34.968  1.00 39.83           C  
ATOM   2229  CG  PHE B 226      30.447 -32.137  33.617  1.00 40.02           C  
ATOM   2230  CD1 PHE B 226      31.445 -31.264  33.216  1.00 33.78           C  
ATOM   2231  CD2 PHE B 226      29.390 -32.382  32.752  1.00 43.17           C  
ATOM   2232  CE1 PHE B 226      31.395 -30.652  31.974  1.00 35.82           C  
ATOM   2233  CE2 PHE B 226      29.333 -31.772  31.508  1.00 39.93           C  
ATOM   2234  CZ  PHE B 226      30.338 -30.908  31.117  1.00 34.88           C  
ATOM   2235  N   PRO B 227      32.703 -34.629  37.132  1.00 51.82           N  
ATOM   2236  CA  PRO B 227      32.843 -35.293  38.434  1.00 53.32           C  
ATOM   2237  C   PRO B 227      31.936 -34.699  39.515  1.00 52.16           C  
ATOM   2238  O   PRO B 227      31.204 -35.441  40.169  1.00 52.96           O  
ATOM   2239  CB  PRO B 227      34.324 -35.065  38.781  1.00 55.17           C  
ATOM   2240  CG  PRO B 227      34.745 -33.913  37.901  1.00 60.64           C  
ATOM   2241  CD  PRO B 227      34.005 -34.164  36.631  1.00 55.72           C  
ATOM   2242  N   LEU B 228      31.983 -33.385  39.703  1.00 52.08           N  
ATOM   2243  CA  LEU B 228      31.154 -32.743  40.720  1.00 48.39           C  
ATOM   2244  C   LEU B 228      29.853 -32.231  40.117  1.00 43.36           C  
ATOM   2245  O   LEU B 228      29.813 -31.149  39.538  1.00 44.45           O  
ATOM   2246  CB  LEU B 228      31.911 -31.597  41.396  1.00 50.36           C  
ATOM   2247  CG  LEU B 228      31.195 -30.886  42.549  1.00 53.67           C  
ATOM   2248  CD1 LEU B 228      30.683 -31.885  43.579  1.00 48.64           C  
ATOM   2249  CD2 LEU B 228      32.110 -29.861  43.204  1.00 56.90           C  
ATOM   2250  N   THR B 229      28.791 -33.018  40.252  1.00 44.78           N  
ATOM   2251  CA  THR B 229      27.492 -32.664  39.694  1.00 46.64           C  
ATOM   2252  C   THR B 229      26.784 -31.662  40.598  1.00 45.64           C  
ATOM   2253  O   THR B 229      27.176 -31.480  41.750  1.00 44.70           O  
ATOM   2254  CB  THR B 229      26.598 -33.909  39.536  1.00 46.70           C  
ATOM   2255  OG1 THR B 229      26.357 -34.498  40.821  1.00 47.73           O  
ATOM   2256  CG2 THR B 229      27.261 -34.935  38.627  1.00 44.87           C  
ATOM   2257  N   LYS B 230      25.744 -31.013  40.079  1.00 37.48           N  
ATOM   2258  CA  LYS B 230      24.956 -30.099  40.902  1.00 37.18           C  
ATOM   2259  C   LYS B 230      24.343 -30.837  42.096  1.00 40.86           C  
ATOM   2260  O   LYS B 230      24.350 -30.333  43.220  1.00 42.45           O  
ATOM   2261  CB  LYS B 230      23.856 -29.410  40.089  1.00 36.32           C  
ATOM   2262  CG  LYS B 230      23.068 -28.394  40.904  1.00 37.02           C  
ATOM   2263  CD  LYS B 230      22.038 -27.645  40.071  1.00 36.54           C  
ATOM   2264  CE  LYS B 230      21.293 -26.638  40.938  1.00 34.45           C  
ATOM   2265  NZ  LYS B 230      20.306 -25.842  40.166  1.00 33.59           N  
ATOM   2266  N   ALA B 231      23.813 -32.030  41.844  1.00 39.58           N  
ATOM   2267  CA  ALA B 231      23.245 -32.856  42.906  1.00 46.31           C  
ATOM   2268  C   ALA B 231      24.243 -33.052  44.046  1.00 47.57           C  
ATOM   2269  O   ALA B 231      23.901 -32.892  45.215  1.00 49.11           O  
ATOM   2270  CB  ALA B 231      22.803 -34.202  42.353  1.00 47.40           C  
ATOM   2271  N   LYS B 232      25.480 -33.393  43.698  1.00 50.73           N  
ATOM   2272  CA  LYS B 232      26.533 -33.565  44.694  1.00 56.22           C  
ATOM   2273  C   LYS B 232      26.853 -32.245  45.385  1.00 56.02           C  
ATOM   2274  O   LYS B 232      27.028 -32.200  46.602  1.00 59.41           O  
ATOM   2275  CB  LYS B 232      27.804 -34.129  44.054  1.00 61.12           C  
ATOM   2276  CG  LYS B 232      27.673 -35.555  43.543  1.00 67.18           C  
ATOM   2277  CD  LYS B 232      28.984 -36.045  42.946  1.00 72.79           C  
ATOM   2278  CE  LYS B 232      28.805 -37.377  42.235  1.00 78.08           C  
ATOM   2279  NZ  LYS B 232      28.324 -38.445  43.155  1.00 82.38           N  
ATOM   2280  N   ALA B 233      26.932 -31.175  44.601  1.00 50.62           N  
ATOM   2281  CA  ALA B 233      27.263 -29.854  45.127  1.00 48.49           C  
ATOM   2282  C   ALA B 233      26.218 -29.346  46.118  1.00 49.17           C  
ATOM   2283  O   ALA B 233      26.566 -28.806  47.167  1.00 47.01           O  
ATOM   2284  CB  ALA B 233      27.452 -28.854  43.987  1.00 45.56           C  
ATOM   2285  N   ARG B 234      24.940 -29.514  45.784  1.00 51.68           N  
ATOM   2286  CA  ARG B 234      23.865 -29.042  46.653  1.00 50.82           C  
ATOM   2287  C   ARG B 234      23.835 -29.838  47.954  1.00 55.92           C  
ATOM   2288  O   ARG B 234      23.416 -29.330  48.993  1.00 54.49           O  
ATOM   2289  CB  ARG B 234      22.501 -29.123  45.956  1.00 52.21           C  
ATOM   2290  CG  ARG B 234      22.444 -28.511  44.561  1.00 51.62           C  
ATOM   2291  CD  ARG B 234      23.273 -27.238  44.441  1.00 53.13           C  
ATOM   2292  NE  ARG B 234      22.670 -26.097  45.124  1.00 56.61           N  
ATOM   2293  CZ  ARG B 234      23.087 -24.842  44.982  1.00 54.82           C  
ATOM   2294  NH1 ARG B 234      24.104 -24.566  44.173  1.00 46.66           N  
ATOM   2295  NH2 ARG B 234      22.486 -23.860  45.640  1.00 51.44           N  
ATOM   2296  N   ALA B 235      24.282 -31.089  47.891  1.00 57.67           N  
ATOM   2297  CA  ALA B 235      24.353 -31.930  49.080  1.00 60.66           C  
ATOM   2298  C   ALA B 235      25.411 -31.401  50.040  1.00 64.23           C  
ATOM   2299  O   ALA B 235      25.191 -31.336  51.249  1.00 66.12           O  
ATOM   2300  CB  ALA B 235      24.650 -33.370  48.698  1.00 54.65           C  
ATOM   2301  N   ILE B 236      26.560 -31.019  49.492  1.00 61.46           N  
ATOM   2302  CA  ILE B 236      27.646 -30.463  50.289  1.00 61.21           C  
ATOM   2303  C   ILE B 236      27.255 -29.112  50.879  1.00 67.65           C  
ATOM   2304  O   ILE B 236      27.515 -28.834  52.050  1.00 74.14           O  
ATOM   2305  CB  ILE B 236      28.924 -30.290  49.450  1.00 56.93           C  
ATOM   2306  CG1 ILE B 236      29.393 -31.640  48.909  1.00 56.79           C  
ATOM   2307  CG2 ILE B 236      30.022 -29.638  50.274  1.00 58.60           C  
ATOM   2308  CD1 ILE B 236      30.581 -31.540  47.978  1.00 59.49           C  
ATOM   2309  N   LEU B 237      26.638 -28.275  50.068  1.00 63.07           N  
ATOM   2310  CA  LEU B 237      26.253 -26.954  50.493  1.00 61.36           C  
ATOM   2311  C   LEU B 237      25.192 -26.927  51.578  1.00 68.18           C  
ATOM   2312  O   LEU B 237      25.125 -25.986  52.334  1.00 68.68           O  
ATOM   2313  CB  LEU B 237      25.809 -26.123  49.299  1.00 55.86           C  
ATOM   2314  CG  LEU B 237      26.901 -25.732  48.319  1.00 55.72           C  
ATOM   2315  CD1 LEU B 237      26.331 -25.267  47.053  1.00 51.27           C  
ATOM   2316  CD2 LEU B 237      27.771 -24.689  48.890  1.00 56.02           C  
ATOM   2317  N   THR B 238      24.363 -27.951  51.653  1.00 70.94           N  
ATOM   2318  CA  THR B 238      23.317 -27.981  52.653  1.00 76.47           C  
ATOM   2319  C   THR B 238      23.587 -29.024  53.713  1.00 83.47           C  
ATOM   2320  O   THR B 238      24.234 -28.747  54.693  1.00 85.16           O  
ATOM   2321  CB  THR B 238      21.980 -28.336  52.052  1.00 73.06           C  
ATOM   2322  OG1 THR B 238      22.032 -29.668  51.553  1.00 72.25           O  
ATOM   2323  CG2 THR B 238      21.618 -27.407  50.965  1.00 68.65           C  
ATOM   2324  N   GLY B 239      23.095 -30.237  53.511  1.00 87.66           N  
ATOM   2325  CA  GLY B 239      23.298 -31.290  54.489  1.00 91.96           C  
ATOM   2326  C   GLY B 239      23.801 -32.601  53.928  1.00 92.92           C  
ATOM   2327  O   GLY B 239      23.135 -33.244  53.125  1.00 93.50           O  
ATOM   2328  N   SER B 245      32.076 -32.214  56.045  1.00 95.37           N  
ATOM   2329  CA  SER B 245      31.809 -30.863  55.565  1.00 92.47           C  
ATOM   2330  C   SER B 245      33.067 -30.211  54.997  1.00 88.08           C  
ATOM   2331  O   SER B 245      34.178 -30.508  55.434  1.00 92.36           O  
ATOM   2332  CB  SER B 245      31.227 -30.000  56.686  1.00 94.77           C  
ATOM   2333  OG  SER B 245      29.896 -30.384  56.983  1.00 97.21           O  
ATOM   2334  N   PRO B 246      32.888 -29.313  54.017  1.00 76.94           N  
ATOM   2335  CA  PRO B 246      33.980 -28.609  53.336  1.00 71.48           C  
ATOM   2336  C   PRO B 246      34.698 -27.640  54.265  1.00 68.48           C  
ATOM   2337  O   PRO B 246      34.083 -27.108  55.188  1.00 70.44           O  
ATOM   2338  CB  PRO B 246      33.243 -27.815  52.252  1.00 71.57           C  
ATOM   2339  CG  PRO B 246      31.873 -27.622  52.822  1.00 73.57           C  
ATOM   2340  CD  PRO B 246      31.582 -28.949  53.443  1.00 75.50           C  
ATOM   2341  N   PHE B 247      35.984 -27.409  54.021  1.00 64.85           N  
ATOM   2342  CA  PHE B 247      36.721 -26.410  54.782  1.00 62.87           C  
ATOM   2343  C   PHE B 247      36.382 -25.021  54.263  1.00 59.31           C  
ATOM   2344  O   PHE B 247      36.471 -24.762  53.066  1.00 55.20           O  
ATOM   2345  CB  PHE B 247      38.227 -26.650  54.687  1.00 60.90           C  
ATOM   2346  CG  PHE B 247      39.046 -25.624  55.417  1.00 64.03           C  
ATOM   2347  CD1 PHE B 247      39.515 -24.497  54.762  1.00 59.94           C  
ATOM   2348  CD2 PHE B 247      39.337 -25.782  56.763  1.00 69.10           C  
ATOM   2349  CE1 PHE B 247      40.262 -23.549  55.435  1.00 63.94           C  
ATOM   2350  CE2 PHE B 247      40.086 -24.839  57.441  1.00 69.41           C  
ATOM   2351  CZ  PHE B 247      40.550 -23.721  56.776  1.00 67.99           C  
ATOM   2352  N   VAL B 248      36.000 -24.127  55.167  1.00 61.24           N  
ATOM   2353  CA  VAL B 248      35.551 -22.796  54.776  1.00 58.43           C  
ATOM   2354  C   VAL B 248      36.667 -21.760  54.819  1.00 59.22           C  
ATOM   2355  O   VAL B 248      37.327 -21.582  55.843  1.00 60.98           O  
ATOM   2356  CB  VAL B 248      34.398 -22.309  55.671  1.00 58.00           C  
ATOM   2357  CG1 VAL B 248      33.995 -20.891  55.290  1.00 54.48           C  
ATOM   2358  CG2 VAL B 248      33.214 -23.259  55.569  1.00 55.33           C  
ATOM   2359  N   ILE B 249      36.873 -21.080  53.696  1.00 58.98           N  
ATOM   2360  CA  ILE B 249      37.791 -19.952  53.640  1.00 57.97           C  
ATOM   2361  C   ILE B 249      36.977 -18.668  53.707  1.00 55.69           C  
ATOM   2362  O   ILE B 249      36.286 -18.307  52.754  1.00 51.92           O  
ATOM   2363  CB  ILE B 249      38.640 -19.966  52.356  1.00 52.31           C  
ATOM   2364  CG1 ILE B 249      39.453 -21.260  52.271  1.00 52.53           C  
ATOM   2365  CG2 ILE B 249      39.555 -18.752  52.312  1.00 50.12           C  
ATOM   2366  CD1 ILE B 249      40.266 -21.394  50.999  1.00 54.08           C  
ATOM   2367  N   TYR B 250      37.057 -17.987  54.844  1.00 55.95           N  
ATOM   2368  CA  TYR B 250      36.236 -16.811  55.095  1.00 58.68           C  
ATOM   2369  C   TYR B 250      37.084 -15.575  55.373  1.00 63.78           C  
ATOM   2370  O   TYR B 250      36.557 -14.469  55.485  1.00 65.40           O  
ATOM   2371  CB  TYR B 250      35.301 -17.071  56.276  1.00 56.36           C  
ATOM   2372  CG  TYR B 250      36.030 -17.510  57.525  1.00 58.52           C  
ATOM   2373  CD1 TYR B 250      36.513 -16.579  58.434  1.00 59.78           C  
ATOM   2374  CD2 TYR B 250      36.247 -18.858  57.787  1.00 60.29           C  
ATOM   2375  CE1 TYR B 250      37.184 -16.977  59.575  1.00 65.29           C  
ATOM   2376  CE2 TYR B 250      36.917 -19.265  58.925  1.00 65.16           C  
ATOM   2377  CZ  TYR B 250      37.384 -18.320  59.815  1.00 67.46           C  
ATOM   2378  OH  TYR B 250      38.053 -18.719  60.948  1.00 72.03           O  
ATOM   2379  N   ASP B 251      38.393 -15.768  55.501  1.00 62.03           N  
ATOM   2380  CA  ASP B 251      39.313 -14.651  55.702  1.00 62.60           C  
ATOM   2381  C   ASP B 251      40.759 -15.032  55.389  1.00 64.63           C  
ATOM   2382  O   ASP B 251      41.044 -16.155  54.970  1.00 58.73           O  
ATOM   2383  CB  ASP B 251      39.191 -14.070  57.120  1.00 61.69           C  
ATOM   2384  CG  ASP B 251      39.758 -14.989  58.187  1.00 63.20           C  
ATOM   2385  OD1 ASP B 251      39.990 -16.180  57.895  1.00 64.31           O  
ATOM   2386  OD2 ASP B 251      39.971 -14.517  59.324  1.00 65.07           O  
ATOM   2387  N   MET B 252      41.667 -14.085  55.600  1.00 69.11           N  
ATOM   2388  CA  MET B 252      43.066 -14.264  55.234  1.00 71.66           C  
ATOM   2389  C   MET B 252      43.741 -15.369  56.046  1.00 75.09           C  
ATOM   2390  O   MET B 252      44.632 -16.058  55.551  1.00 76.24           O  
ATOM   2391  CB  MET B 252      43.826 -12.946  55.397  1.00 72.64           C  
ATOM   2392  CG  MET B 252      44.923 -12.741  54.373  1.00 74.58           C  
ATOM   2393  SD  MET B 252      44.271 -12.729  52.692  1.00 81.16           S  
ATOM   2394  CE  MET B 252      43.124 -11.357  52.790  1.00 99.15           C  
ATOM   2395  N   ASN B 253      43.313 -15.532  57.294  1.00 74.37           N  
ATOM   2396  CA  ASN B 253      43.882 -16.555  58.167  1.00 74.85           C  
ATOM   2397  C   ASN B 253      43.441 -17.966  57.793  1.00 70.09           C  
ATOM   2398  O   ASN B 253      44.239 -18.904  57.825  1.00 69.01           O  
ATOM   2399  CB  ASN B 253      43.552 -16.261  59.633  1.00 81.40           C  
ATOM   2400  CG  ASN B 253      44.440 -15.181  60.224  1.00 87.54           C  
ATOM   2401  OD1 ASN B 253      45.491 -14.856  59.671  1.00 91.01           O  
ATOM   2402  ND2 ASN B 253      44.022 -14.620  61.352  1.00 88.30           N  
ATOM   2403  N   SER B 254      42.168 -18.114  57.438  1.00 64.91           N  
ATOM   2404  CA  SER B 254      41.636 -19.417  57.061  1.00 61.31           C  
ATOM   2405  C   SER B 254      42.148 -19.844  55.688  1.00 64.03           C  
ATOM   2406  O   SER B 254      42.216 -21.035  55.387  1.00 64.99           O  
ATOM   2407  CB  SER B 254      40.105 -19.412  57.092  1.00 56.66           C  
ATOM   2408  OG  SER B 254      39.578 -18.329  56.349  1.00 55.31           O  
ATOM   2409  N   LEU B 255      42.511 -18.868  54.862  1.00 63.33           N  
ATOM   2410  CA  LEU B 255      43.076 -19.155  53.546  1.00 61.85           C  
ATOM   2411  C   LEU B 255      44.408 -19.885  53.672  1.00 67.83           C  
ATOM   2412  O   LEU B 255      44.620 -20.923  53.044  1.00 65.03           O  
ATOM   2413  CB  LEU B 255      43.270 -17.867  52.744  1.00 57.06           C  
ATOM   2414  CG  LEU B 255      44.032 -18.030  51.426  1.00 62.90           C  
ATOM   2415  CD1 LEU B 255      43.245 -18.885  50.441  1.00 57.68           C  
ATOM   2416  CD2 LEU B 255      44.358 -16.677  50.817  1.00 64.45           C  
ATOM   2417  N   MET B 256      45.303 -19.332  54.485  1.00 72.17           N  
ATOM   2418  CA  MET B 256      46.612 -19.932  54.711  1.00 80.18           C  
ATOM   2419  C   MET B 256      46.471 -21.356  55.232  1.00 80.73           C  
ATOM   2420  O   MET B 256      47.174 -22.264  54.789  1.00 83.89           O  
ATOM   2421  CB  MET B 256      47.426 -19.091  55.695  1.00 87.26           C  
ATOM   2422  CG  MET B 256      47.730 -17.684  55.208  1.00 90.68           C  
ATOM   2423  SD  MET B 256      48.786 -16.771  56.350  1.00125.11           S  
ATOM   2424  CE  MET B 256      50.258 -17.791  56.344  1.00 85.97           C  
ATOM   2425  N   MET B 257      45.559 -21.544  56.178  1.00 78.73           N  
ATOM   2426  CA  MET B 257      45.282 -22.868  56.715  1.00 77.34           C  
ATOM   2427  C   MET B 257      44.665 -23.755  55.637  1.00 74.78           C  
ATOM   2428  O   MET B 257      44.978 -24.941  55.539  1.00 73.89           O  
ATOM   2429  CB  MET B 257      44.352 -22.764  57.926  1.00 76.12           C  
ATOM   2430  CG  MET B 257      43.889 -24.097  58.487  1.00 75.16           C  
ATOM   2431  SD  MET B 257      43.120 -23.922  60.111  1.00 95.31           S  
ATOM   2432  CE  MET B 257      42.360 -25.532  60.307  1.00 72.04           C  
ATOM   2433  N   GLY B 258      43.795 -23.165  54.824  1.00 74.33           N  
ATOM   2434  CA  GLY B 258      43.140 -23.888  53.749  1.00 74.46           C  
ATOM   2435  C   GLY B 258      44.131 -24.561  52.823  1.00 75.97           C  
ATOM   2436  O   GLY B 258      43.871 -25.642  52.296  1.00 72.46           O  
ATOM   2437  N   GLU B 259      45.278 -23.920  52.631  1.00 83.70           N  
ATOM   2438  CA  GLU B 259      46.313 -24.448  51.753  1.00 90.71           C  
ATOM   2439  C   GLU B 259      47.168 -25.482  52.475  1.00 98.32           C  
ATOM   2440  O   GLU B 259      48.304 -25.745  52.082  1.00102.95           O  
ATOM   2441  CB  GLU B 259      47.190 -23.311  51.230  1.00 92.06           C  
ATOM   2442  CG  GLU B 259      46.402 -22.166  50.617  1.00 90.89           C  
ATOM   2443  CD  GLU B 259      47.285 -21.016  50.178  1.00 91.94           C  
ATOM   2444  OE1 GLU B 259      46.883 -20.284  49.249  1.00 91.49           O  
ATOM   2445  OE2 GLU B 259      48.379 -20.845  50.755  1.00 94.28           O  
ATOM   2446  N   ASP B 260      46.614 -26.067  53.532  1.00101.22           N  
ATOM   2447  CA  ASP B 260      47.339 -27.043  54.334  1.00104.12           C  
ATOM   2448  C   ASP B 260      46.394 -28.113  54.869  1.00105.07           C  
ATOM   2449  O   ASP B 260      45.478 -27.818  55.637  1.00107.52           O  
ATOM   2450  CB  ASP B 260      48.058 -26.345  55.491  0.50109.13           C  
ATOM   2451  CG  ASP B 260      48.996 -27.271  56.239  0.50114.53           C  
ATOM   2452  OD1 ASP B 260      49.595 -26.827  57.241  0.50117.04           O  
ATOM   2453  OD2 ASP B 260      49.137 -28.441  55.825  0.50116.04           O  
ATOM   2454  N   PHE B 264      46.014 -27.994  47.243  1.00 74.83           N  
ATOM   2455  CA  PHE B 264      45.834 -27.381  45.931  1.00 75.47           C  
ATOM   2456  C   PHE B 264      46.963 -27.761  44.978  1.00 76.42           C  
ATOM   2457  O   PHE B 264      48.100 -27.978  45.397  1.00 77.59           O  
ATOM   2458  CB  PHE B 264      45.731 -25.860  46.059  1.00 73.53           C  
ATOM   2459  CG  PHE B 264      44.600 -25.404  46.934  1.00 74.07           C  
ATOM   2460  CD1 PHE B 264      44.760 -25.315  48.306  1.00 76.37           C  
ATOM   2461  CD2 PHE B 264      43.373 -25.071  46.385  1.00 72.77           C  
ATOM   2462  CE1 PHE B 264      43.719 -24.897  49.114  1.00 76.01           C  
ATOM   2463  CE2 PHE B 264      42.329 -24.652  47.188  1.00 71.40           C  
ATOM   2464  CZ  PHE B 264      42.503 -24.566  48.554  1.00 72.52           C  
ATOM   2465  N   LYS B 265      46.638 -27.834  43.692  1.00 75.72           N  
ATOM   2466  CA  LYS B 265      47.586 -28.286  42.681  1.00 74.72           C  
ATOM   2467  C   LYS B 265      48.278 -27.126  41.966  1.00 71.50           C  
ATOM   2468  O   LYS B 265      49.231 -27.331  41.216  1.00 70.04           O  
ATOM   2469  CB  LYS B 265      46.873 -29.187  41.671  1.00 73.20           C  
ATOM   2470  CG  LYS B 265      46.546 -30.571  42.210  1.00 76.52           C  
ATOM   2471  CD  LYS B 265      45.118 -30.981  41.876  1.00 77.00           C  
ATOM   2472  CE  LYS B 265      44.763 -30.673  40.430  1.00 76.75           C  
ATOM   2473  NZ  LYS B 265      43.382 -31.123  40.085  1.00 73.58           N  
ATOM   2474  N   HIS B 266      47.800 -25.910  42.206  1.00 72.01           N  
ATOM   2475  CA  HIS B 266      48.349 -24.733  41.538  1.00 74.88           C  
ATOM   2476  C   HIS B 266      49.435 -24.043  42.366  1.00 81.80           C  
ATOM   2477  O   HIS B 266      49.751 -22.874  42.138  1.00 82.85           O  
ATOM   2478  CB  HIS B 266      47.232 -23.745  41.189  1.00 70.73           C  
ATOM   2479  CG  HIS B 266      46.562 -23.144  42.383  1.00 69.89           C  
ATOM   2480  ND1 HIS B 266      45.590 -23.806  43.106  1.00 69.33           N  
ATOM   2481  CD2 HIS B 266      46.719 -21.941  42.983  1.00 69.81           C  
ATOM   2482  CE1 HIS B 266      45.183 -23.038  44.098  1.00 68.41           C  
ATOM   2483  NE2 HIS B 266      45.852 -21.899  44.047  1.00 69.51           N  
ATOM   2484  N   ILE B 267      50.002 -24.779  43.318  1.00 84.58           N  
ATOM   2485  CA  ILE B 267      51.071 -24.272  44.177  1.00 85.81           C  
ATOM   2486  C   ILE B 267      50.733 -22.897  44.740  1.00 84.41           C  
ATOM   2487  O   ILE B 267      50.418 -22.764  45.921  1.00 85.45           O  
ATOM   2488  CB  ILE B 267      52.428 -24.204  43.436  1.00 87.07           C  
ATOM   2489  CG1 ILE B 267      53.579 -24.494  44.401  1.00 92.69           C  
ATOM   2490  CG2 ILE B 267      52.615 -22.851  42.762  1.00 88.08           C  
ATOM   2491  CD1 ILE B 267      53.493 -25.856  45.055  1.00 94.77           C  
ATOM   2492  N   GLU B 276      51.461 -12.733  46.338  1.00 92.71           N  
ATOM   2493  CA  GLU B 276      50.309 -11.985  46.828  1.00 92.47           C  
ATOM   2494  C   GLU B 276      49.054 -12.853  46.865  1.00 89.00           C  
ATOM   2495  O   GLU B 276      48.894 -13.768  46.058  1.00 87.63           O  
ATOM   2496  CB  GLU B 276      50.071 -10.739  45.969  1.00 94.54           C  
ATOM   2497  CG  GLU B 276      48.868  -9.913  46.395  1.00 97.55           C  
ATOM   2498  CD  GLU B 276      48.654  -8.692  45.522  1.00101.16           C  
ATOM   2499  OE1 GLU B 276      47.576  -8.069  45.626  1.00100.80           O  
ATOM   2500  OE2 GLU B 276      49.563  -8.353  44.734  1.00104.05           O  
ATOM   2501  N   VAL B 277      48.166 -12.556  47.809  1.00 86.32           N  
ATOM   2502  CA  VAL B 277      46.952 -13.339  48.002  1.00 80.34           C  
ATOM   2503  C   VAL B 277      46.023 -13.299  46.792  1.00 78.45           C  
ATOM   2504  O   VAL B 277      45.801 -14.318  46.138  1.00 77.64           O  
ATOM   2505  CB  VAL B 277      46.174 -12.862  49.239  1.00 77.70           C  
ATOM   2506  CG1 VAL B 277      44.837 -13.579  49.332  1.00 73.77           C  
ATOM   2507  CG2 VAL B 277      46.998 -13.083  50.497  1.00 81.92           C  
ATOM   2508  N   ALA B 278      45.478 -12.119  46.508  1.00 77.37           N  
ATOM   2509  CA  ALA B 278      44.519 -11.949  45.421  1.00 74.03           C  
ATOM   2510  C   ALA B 278      44.988 -12.610  44.129  1.00 71.18           C  
ATOM   2511  O   ALA B 278      44.197 -13.228  43.416  1.00 69.84           O  
ATOM   2512  CB  ALA B 278      44.240 -10.471  45.191  1.00 75.34           C  
ATOM   2513  N   ILE B 279      46.278 -12.479  43.838  1.00 73.39           N  
ATOM   2514  CA  ILE B 279      46.854 -13.038  42.620  1.00 72.82           C  
ATOM   2515  C   ILE B 279      46.837 -14.563  42.639  1.00 68.70           C  
ATOM   2516  O   ILE B 279      46.496 -15.200  41.642  1.00 66.44           O  
ATOM   2517  CB  ILE B 279      48.298 -12.550  42.412  1.00 80.07           C  
ATOM   2518  CG1 ILE B 279      48.359 -11.023  42.498  1.00 86.42           C  
ATOM   2519  CG2 ILE B 279      48.842 -13.046  41.081  1.00 78.38           C  
ATOM   2520  CD1 ILE B 279      49.763 -10.462  42.424  1.00 91.47           C  
ATOM   2521  N   ARG B 280      47.210 -15.141  43.778  1.00 67.72           N  
ATOM   2522  CA  ARG B 280      47.209 -16.593  43.944  1.00 68.46           C  
ATOM   2523  C   ARG B 280      45.816 -17.184  43.748  1.00 62.47           C  
ATOM   2524  O   ARG B 280      45.657 -18.214  43.092  1.00 59.17           O  
ATOM   2525  CB  ARG B 280      47.773 -16.981  45.316  1.00 72.99           C  
ATOM   2526  CG  ARG B 280      49.284 -17.168  45.323  1.00 77.39           C  
ATOM   2527  CD  ARG B 280      49.911 -16.809  46.665  1.00 81.84           C  
ATOM   2528  NE  ARG B 280      49.478 -17.680  47.753  0.50 82.80           N  
ATOM   2529  CZ  ARG B 280      48.689 -17.294  48.751  0.50 83.14           C  
ATOM   2530  NH1 ARG B 280      48.244 -16.047  48.802  0.50 82.99           N  
ATOM   2531  NH2 ARG B 280      48.349 -18.151  49.702  0.50 83.88           N  
ATOM   2532  N   ILE B 281      44.812 -16.526  44.318  1.00 59.87           N  
ATOM   2533  CA  ILE B 281      43.429 -16.967  44.179  1.00 58.05           C  
ATOM   2534  C   ILE B 281      42.990 -16.931  42.718  1.00 57.16           C  
ATOM   2535  O   ILE B 281      42.329 -17.850  42.238  1.00 55.10           O  
ATOM   2536  CB  ILE B 281      42.473 -16.105  45.024  1.00 54.36           C  
ATOM   2537  CG1 ILE B 281      42.772 -16.291  46.512  1.00 57.20           C  
ATOM   2538  CG2 ILE B 281      41.025 -16.454  44.715  1.00 50.27           C  
ATOM   2539  CD1 ILE B 281      41.892 -15.466  47.426  1.00 59.61           C  
ATOM   2540  N   PHE B 282      43.364 -15.868  42.016  1.00 60.47           N  
ATOM   2541  CA  PHE B 282      43.044 -15.744  40.598  1.00 61.99           C  
ATOM   2542  C   PHE B 282      43.677 -16.866  39.782  1.00 61.27           C  
ATOM   2543  O   PHE B 282      43.030 -17.456  38.916  1.00 60.33           O  
ATOM   2544  CB  PHE B 282      43.495 -14.388  40.057  1.00 63.01           C  
ATOM   2545  CG  PHE B 282      43.295 -14.232  38.577  1.00 64.58           C  
ATOM   2546  CD1 PHE B 282      44.379 -14.215  37.714  1.00 63.80           C  
ATOM   2547  CD2 PHE B 282      42.021 -14.108  38.046  1.00 64.24           C  
ATOM   2548  CE1 PHE B 282      44.197 -14.072  36.350  1.00 58.54           C  
ATOM   2549  CE2 PHE B 282      41.834 -13.965  36.682  1.00 61.23           C  
ATOM   2550  CZ  PHE B 282      42.923 -13.947  35.834  1.00 57.26           C  
ATOM   2551  N   GLN B 283      44.945 -17.154  40.059  1.00 60.48           N  
ATOM   2552  CA  GLN B 283      45.650 -18.234  39.380  1.00 58.84           C  
ATOM   2553  C   GLN B 283      44.943 -19.564  39.614  1.00 59.17           C  
ATOM   2554  O   GLN B 283      44.872 -20.405  38.719  1.00 61.73           O  
ATOM   2555  CB  GLN B 283      47.103 -18.313  39.853  1.00 59.67           C  
ATOM   2556  N   GLY B 284      44.418 -19.749  40.821  1.00 52.86           N  
ATOM   2557  CA  GLY B 284      43.657 -20.944  41.134  1.00 49.98           C  
ATOM   2558  C   GLY B 284      42.415 -21.016  40.267  1.00 49.84           C  
ATOM   2559  O   GLY B 284      42.066 -22.075  39.746  1.00 49.47           O  
ATOM   2560  N   CYS B 285      41.751 -19.896  40.068  1.00 50.07           N  
ATOM   2561  CA  CYS B 285      40.575 -19.902  39.228  1.00 51.54           C  
ATOM   2562  C   CYS B 285      40.970 -20.290  37.820  1.00 52.98           C  
ATOM   2563  O   CYS B 285      40.259 -21.021  37.187  1.00 52.51           O  
ATOM   2564  CB  CYS B 285      39.817 -18.581  39.248  1.00 51.55           C  
ATOM   2565  SG  CYS B 285      38.162 -18.659  38.494  1.00103.16           S  
ATOM   2566  N   GLN B 286      42.111 -19.807  37.339  1.00 55.55           N  
ATOM   2567  CA AGLN B 286      42.556 -20.166  35.998  0.60 53.94           C  
ATOM   2568  CA BGLN B 286      42.580 -20.163  36.002  0.40 54.63           C  
ATOM   2569  C   GLN B 286      42.828 -21.662  35.878  1.00 52.63           C  
ATOM   2570  O   GLN B 286      42.379 -22.303  34.930  1.00 54.12           O  
ATOM   2571  CB AGLN B 286      43.796 -19.359  35.608  0.60 57.89           C  
ATOM   2572  CB BGLN B 286      43.865 -19.402  35.667  0.40 57.97           C  
ATOM   2573  CG AGLN B 286      43.548 -17.861  35.522  0.60 59.83           C  
ATOM   2574  CG BGLN B 286      43.678 -17.908  35.463  0.40 58.62           C  
ATOM   2575  CD AGLN B 286      42.379 -17.517  34.618  0.60 61.71           C  
ATOM   2576  CD BGLN B 286      44.975 -17.202  35.118  0.40 59.68           C  
ATOM   2577  OE1AGLN B 286      41.566 -16.649  34.938  0.60 65.24           O  
ATOM   2578  OE1BGLN B 286      46.021 -17.473  35.709  0.40 60.83           O  
ATOM   2579  NE2AGLN B 286      42.285 -18.201  33.484  0.60 59.08           N  
ATOM   2580  NE2BGLN B 286      44.913 -16.289  34.155  0.40 59.77           N  
ATOM   2581  N   PHE B 287      43.555 -22.214  36.844  1.00 50.60           N  
ATOM   2582  CA  PHE B 287      43.865 -23.639  36.851  1.00 49.93           C  
ATOM   2583  C   PHE B 287      42.601 -24.474  36.678  1.00 50.29           C  
ATOM   2584  O   PHE B 287      42.543 -25.362  35.827  1.00 46.51           O  
ATOM   2585  CB  PHE B 287      44.573 -24.029  38.152  1.00 52.79           C  
ATOM   2586  CG  PHE B 287      45.002 -25.471  38.202  1.00 54.09           C  
ATOM   2587  CD1 PHE B 287      44.094 -26.468  38.526  1.00 52.89           C  
ATOM   2588  CD2 PHE B 287      46.313 -25.830  37.926  1.00 57.11           C  
ATOM   2589  CE1 PHE B 287      44.485 -27.795  38.571  1.00 53.91           C  
ATOM   2590  CE2 PHE B 287      46.711 -27.156  37.971  1.00 57.73           C  
ATOM   2591  CZ  PHE B 287      45.796 -28.139  38.294  1.00 54.28           C  
ATOM   2592  N   ARG B 288      41.591 -24.183  37.491  1.00 48.71           N  
ATOM   2593  CA  ARG B 288      40.337 -24.924  37.458  1.00 43.61           C  
ATOM   2594  C   ARG B 288      39.604 -24.747  36.129  1.00 39.78           C  
ATOM   2595  O   ARG B 288      39.052 -25.704  35.585  1.00 40.27           O  
ATOM   2596  CB  ARG B 288      39.442 -24.507  38.628  1.00 47.68           C  
ATOM   2597  CG  ARG B 288      38.009 -25.003  38.532  1.00 49.05           C  
ATOM   2598  CD  ARG B 288      37.941 -26.515  38.376  1.00 48.92           C  
ATOM   2599  NE  ARG B 288      36.639 -26.945  37.871  1.00 51.53           N  
ATOM   2600  CZ  ARG B 288      36.414 -28.111  37.272  1.00 51.56           C  
ATOM   2601  NH1 ARG B 288      37.407 -28.973  37.098  1.00 50.96           N  
ATOM   2602  NH2 ARG B 288      35.197 -28.414  36.842  1.00 47.08           N  
ATOM   2603  N   SER B 289      39.599 -23.524  35.609  1.00 38.32           N  
ATOM   2604  CA  SER B 289      38.934 -23.247  34.339  1.00 43.45           C  
ATOM   2605  C   SER B 289      39.528 -24.087  33.208  1.00 45.56           C  
ATOM   2606  O   SER B 289      38.803 -24.593  32.351  1.00 41.76           O  
ATOM   2607  CB  SER B 289      39.019 -21.758  33.993  1.00 48.02           C  
ATOM   2608  OG  SER B 289      38.214 -20.983  34.869  1.00 58.23           O  
ATOM   2609  N   VAL B 290      40.850 -24.232  33.216  1.00 44.03           N  
ATOM   2610  CA  VAL B 290      41.537 -25.054  32.225  1.00 38.94           C  
ATOM   2611  C   VAL B 290      41.123 -26.517  32.358  1.00 35.24           C  
ATOM   2612  O   VAL B 290      40.927 -27.208  31.361  1.00 37.81           O  
ATOM   2613  CB  VAL B 290      43.068 -24.913  32.334  1.00 41.71           C  
ATOM   2614  CG1 VAL B 290      43.769 -26.085  31.661  1.00 33.24           C  
ATOM   2615  CG2 VAL B 290      43.514 -23.593  31.729  1.00 41.73           C  
ATOM   2616  N   GLU B 291      40.984 -26.987  33.593  1.00 38.46           N  
ATOM   2617  CA  GLU B 291      40.456 -28.324  33.830  1.00 37.76           C  
ATOM   2618  C   GLU B 291      39.053 -28.444  33.253  1.00 42.05           C  
ATOM   2619  O   GLU B 291      38.739 -29.395  32.533  1.00 46.52           O  
ATOM   2620  CB  GLU B 291      40.401 -28.622  35.325  1.00 37.78           C  
ATOM   2621  CG  GLU B 291      41.719 -29.045  35.935  1.00 44.49           C  
ATOM   2622  CD  GLU B 291      41.554 -29.506  37.364  1.00 48.47           C  
ATOM   2623  OE1 GLU B 291      40.959 -28.753  38.163  1.00 48.11           O  
ATOM   2624  OE2 GLU B 291      42.015 -30.619  37.686  1.00 49.46           O  
ATOM   2625  N   ALA B 292      38.213 -27.470  33.585  1.00 40.47           N  
ATOM   2626  CA  ALA B 292      36.822 -27.467  33.155  1.00 38.53           C  
ATOM   2627  C   ALA B 292      36.710 -27.543  31.637  1.00 33.20           C  
ATOM   2628  O   ALA B 292      35.809 -28.189  31.108  1.00 38.45           O  
ATOM   2629  CB  ALA B 292      36.102 -26.229  33.692  1.00 38.77           C  
ATOM   2630  N   VAL B 293      37.636 -26.895  30.939  1.00 30.81           N  
ATOM   2631  CA  VAL B 293      37.624 -26.905  29.479  1.00 33.31           C  
ATOM   2632  C   VAL B 293      37.719 -28.328  28.929  1.00 36.20           C  
ATOM   2633  O   VAL B 293      37.013 -28.685  27.988  1.00 36.34           O  
ATOM   2634  CB  VAL B 293      38.756 -26.034  28.895  1.00 40.67           C  
ATOM   2635  CG1 VAL B 293      38.916 -26.282  27.393  1.00 39.44           C  
ATOM   2636  CG2 VAL B 293      38.486 -24.564  29.181  1.00 34.99           C  
ATOM   2637  N   GLN B 294      38.579 -29.146  29.527  1.00 37.93           N  
ATOM   2638  CA  GLN B 294      38.748 -30.523  29.073  1.00 37.06           C  
ATOM   2639  C   GLN B 294      37.519 -31.383  29.355  1.00 38.17           C  
ATOM   2640  O   GLN B 294      37.174 -32.261  28.565  1.00 36.27           O  
ATOM   2641  CB  GLN B 294      39.993 -31.157  29.691  1.00 39.80           C  
ATOM   2642  CG  GLN B 294      41.293 -30.560  29.184  1.00 44.51           C  
ATOM   2643  CD  GLN B 294      41.332 -30.422  27.667  1.00 46.79           C  
ATOM   2644  OE1 GLN B 294      41.746 -29.388  27.141  1.00 43.35           O  
ATOM   2645  NE2 GLN B 294      40.902 -31.464  26.959  1.00 45.00           N  
ATOM   2646  N   GLU B 295      36.858 -31.130  30.479  1.00 33.82           N  
ATOM   2647  CA  GLU B 295      35.635 -31.851  30.809  1.00 30.22           C  
ATOM   2648  C   GLU B 295      34.541 -31.528  29.793  1.00 31.01           C  
ATOM   2649  O   GLU B 295      33.847 -32.421  29.304  1.00 33.75           O  
ATOM   2650  CB  GLU B 295      35.158 -31.484  32.214  1.00 36.16           C  
ATOM   2651  CG  GLU B 295      36.170 -31.754  33.315  1.00 40.41           C  
ATOM   2652  CD  GLU B 295      35.717 -31.214  34.663  1.00 44.40           C  
ATOM   2653  OE1 GLU B 295      34.573 -30.720  34.761  1.00 41.91           O  
ATOM   2654  OE2 GLU B 295      36.505 -31.280  35.626  1.00 53.09           O  
ATOM   2655  N   ILE B 296      34.393 -30.241  29.488  1.00 31.21           N  
ATOM   2656  CA  ILE B 296      33.385 -29.765  28.545  1.00 31.52           C  
ATOM   2657  C   ILE B 296      33.675 -30.277  27.138  1.00 35.54           C  
ATOM   2658  O   ILE B 296      32.768 -30.697  26.416  1.00 33.97           O  
ATOM   2659  CB  ILE B 296      33.337 -28.228  28.525  1.00 31.93           C  
ATOM   2660  CG1 ILE B 296      32.930 -27.689  29.900  1.00 29.50           C  
ATOM   2661  CG2 ILE B 296      32.389 -27.729  27.435  1.00 35.98           C  
ATOM   2662  CD1 ILE B 296      33.211 -26.206  30.076  1.00 31.18           C  
ATOM   2663  N   THR B 297      34.948 -30.243  26.757  1.00 36.00           N  
ATOM   2664  CA  THR B 297      35.382 -30.774  25.471  1.00 36.17           C  
ATOM   2665  C   THR B 297      35.007 -32.245  25.310  1.00 38.02           C  
ATOM   2666  O   THR B 297      34.498 -32.654  24.265  1.00 36.54           O  
ATOM   2667  CB  THR B 297      36.897 -30.608  25.283  1.00 37.40           C  
ATOM   2668  OG1 THR B 297      37.212 -29.214  25.185  1.00 35.97           O  
ATOM   2669  CG2 THR B 297      37.365 -31.324  24.019  1.00 39.45           C  
ATOM   2670  N   GLU B 298      35.252 -33.040  26.348  1.00 33.89           N  
ATOM   2671  CA  GLU B 298      34.880 -34.450  26.314  1.00 38.80           C  
ATOM   2672  C   GLU B 298      33.364 -34.612  26.218  1.00 40.57           C  
ATOM   2673  O   GLU B 298      32.866 -35.481  25.502  1.00 44.85           O  
ATOM   2674  CB  GLU B 298      35.406 -35.187  27.547  1.00 45.52           C  
ATOM   2675  CG  GLU B 298      35.015 -36.656  27.577  1.00 58.15           C  
ATOM   2676  CD  GLU B 298      35.335 -37.328  28.896  1.00 69.31           C  
ATOM   2677  OE1 GLU B 298      36.135 -36.773  29.678  1.00 72.87           O  
ATOM   2678  OE2 GLU B 298      34.783 -38.419  29.150  1.00 75.32           O  
ATOM   2679  N   TYR B 299      32.633 -33.774  26.944  1.00 39.18           N  
ATOM   2680  CA  TYR B 299      31.178 -33.820  26.898  1.00 40.37           C  
ATOM   2681  C   TYR B 299      30.654 -33.491  25.502  1.00 40.35           C  
ATOM   2682  O   TYR B 299      29.745 -34.149  24.999  1.00 45.61           O  
ATOM   2683  CB  TYR B 299      30.568 -32.861  27.917  1.00 37.49           C  
ATOM   2684  CG  TYR B 299      29.058 -32.836  27.878  1.00 39.89           C  
ATOM   2685  CD1 TYR B 299      28.322 -33.957  28.230  1.00 36.28           C  
ATOM   2686  CD2 TYR B 299      28.369 -31.693  27.490  1.00 36.88           C  
ATOM   2687  CE1 TYR B 299      26.945 -33.947  28.198  1.00 36.52           C  
ATOM   2688  CE2 TYR B 299      26.984 -31.673  27.454  1.00 38.09           C  
ATOM   2689  CZ  TYR B 299      26.279 -32.805  27.811  1.00 37.83           C  
ATOM   2690  OH  TYR B 299      24.904 -32.811  27.785  1.00 34.98           O  
ATOM   2691  N   ALA B 300      31.230 -32.469  24.883  1.00 32.64           N  
ATOM   2692  CA  ALA B 300      30.805 -32.043  23.553  1.00 35.41           C  
ATOM   2693  C   ALA B 300      30.886 -33.180  22.536  1.00 34.26           C  
ATOM   2694  O   ALA B 300      30.061 -33.275  21.627  1.00 39.36           O  
ATOM   2695  CB  ALA B 300      31.636 -30.856  23.089  1.00 37.34           C  
ATOM   2696  N   LYS B 301      31.881 -34.045  22.695  1.00 36.76           N  
ATOM   2697  CA  LYS B 301      32.076 -35.156  21.768  1.00 43.86           C  
ATOM   2698  C   LYS B 301      30.932 -36.168  21.808  1.00 47.60           C  
ATOM   2699  O   LYS B 301      30.685 -36.875  20.829  1.00 43.69           O  
ATOM   2700  CB  LYS B 301      33.405 -35.856  22.045  1.00 51.03           C  
ATOM   2701  CG  LYS B 301      34.623 -35.005  21.742  1.00 55.90           C  
ATOM   2702  CD  LYS B 301      35.890 -35.838  21.808  1.00 64.22           C  
ATOM   2703  CE  LYS B 301      37.117 -34.996  21.509  1.00 64.46           C  
ATOM   2704  NZ  LYS B 301      38.334 -35.839  21.405  1.00 63.85           N  
ATOM   2705  N   SER B 302      30.232 -36.231  22.937  1.00 42.78           N  
ATOM   2706  CA  SER B 302      29.132 -37.176  23.100  1.00 38.93           C  
ATOM   2707  C   SER B 302      27.821 -36.655  22.505  1.00 41.85           C  
ATOM   2708  O   SER B 302      26.847 -37.396  22.381  1.00 44.48           O  
ATOM   2709  CB  SER B 302      28.925 -37.499  24.577  1.00 40.02           C  
ATOM   2710  OG  SER B 302      28.139 -36.498  25.197  1.00 42.58           O  
ATOM   2711  N   ILE B 303      27.789 -35.376  22.153  1.00 41.17           N  
ATOM   2712  CA  ILE B 303      26.593 -34.797  21.557  1.00 42.91           C  
ATOM   2713  C   ILE B 303      26.424 -35.289  20.121  1.00 43.44           C  
ATOM   2714  O   ILE B 303      27.273 -35.029  19.270  1.00 46.69           O  
ATOM   2715  CB  ILE B 303      26.642 -33.260  21.577  1.00 36.84           C  
ATOM   2716  CG1 ILE B 303      26.701 -32.749  23.019  1.00 36.09           C  
ATOM   2717  CG2 ILE B 303      25.437 -32.684  20.853  1.00 32.90           C  
ATOM   2718  CD1 ILE B 303      26.986 -31.264  23.138  1.00 30.08           C  
ATOM   2719  N   PRO B 304      25.324 -36.011  19.850  1.00 41.39           N  
ATOM   2720  CA  PRO B 304      25.086 -36.602  18.529  1.00 43.74           C  
ATOM   2721  C   PRO B 304      25.260 -35.579  17.414  1.00 44.29           C  
ATOM   2722  O   PRO B 304      24.604 -34.536  17.424  1.00 40.64           O  
ATOM   2723  CB  PRO B 304      23.628 -37.061  18.611  1.00 46.15           C  
ATOM   2724  CG  PRO B 304      23.411 -37.334  20.061  1.00 45.57           C  
ATOM   2725  CD  PRO B 304      24.231 -36.306  20.792  1.00 43.77           C  
ATOM   2726  N   GLY B 305      26.155 -35.875  16.476  1.00 43.28           N  
ATOM   2727  CA  GLY B 305      26.416 -34.994  15.355  1.00 41.63           C  
ATOM   2728  C   GLY B 305      27.685 -34.170  15.497  1.00 43.17           C  
ATOM   2729  O   GLY B 305      28.330 -33.846  14.502  1.00 41.25           O  
ATOM   2730  N   PHE B 306      28.047 -33.828  16.730  1.00 41.16           N  
ATOM   2731  CA  PHE B 306      29.177 -32.931  16.968  1.00 34.92           C  
ATOM   2732  C   PHE B 306      30.473 -33.392  16.296  1.00 37.54           C  
ATOM   2733  O   PHE B 306      31.142 -32.610  15.619  1.00 39.76           O  
ATOM   2734  CB  PHE B 306      29.409 -32.725  18.467  1.00 34.58           C  
ATOM   2735  CG  PHE B 306      30.433 -31.669  18.775  1.00 35.00           C  
ATOM   2736  CD1 PHE B 306      30.073 -30.333  18.835  1.00 31.00           C  
ATOM   2737  CD2 PHE B 306      31.758 -32.010  18.992  1.00 34.58           C  
ATOM   2738  CE1 PHE B 306      31.014 -29.359  19.112  1.00 32.52           C  
ATOM   2739  CE2 PHE B 306      32.703 -31.041  19.271  1.00 33.14           C  
ATOM   2740  CZ  PHE B 306      32.332 -29.715  19.328  1.00 31.93           C  
ATOM   2741  N   VAL B 307      30.827 -34.658  16.487  1.00 39.24           N  
ATOM   2742  CA  VAL B 307      32.065 -35.191  15.924  1.00 44.69           C  
ATOM   2743  C   VAL B 307      32.046 -35.186  14.395  1.00 49.08           C  
ATOM   2744  O   VAL B 307      33.094 -35.098  13.753  1.00 50.10           O  
ATOM   2745  CB  VAL B 307      32.362 -36.614  16.444  1.00 45.76           C  
ATOM   2746  CG1 VAL B 307      33.572 -37.196  15.741  1.00 56.39           C  
ATOM   2747  CG2 VAL B 307      32.591 -36.583  17.949  1.00 46.42           C  
ATOM   2748  N   ASN B 308      30.853 -35.265  13.814  1.00 46.66           N  
ATOM   2749  CA  ASN B 308      30.716 -35.296  12.361  1.00 48.71           C  
ATOM   2750  C   ASN B 308      30.880 -33.916  11.730  1.00 47.57           C  
ATOM   2751  O   ASN B 308      30.929 -33.781  10.506  1.00 46.16           O  
ATOM   2752  CB  ASN B 308      29.367 -35.900  11.962  1.00 53.71           C  
ATOM   2753  CG  ASN B 308      29.177 -37.309  12.495  1.00 62.20           C  
ATOM   2754  OD1 ASN B 308      28.089 -37.673  12.948  1.00 68.64           O  
ATOM   2755  ND2 ASN B 308      30.237 -38.108  12.450  1.00 57.46           N  
ATOM   2756  N   LEU B 309      30.959 -32.890  12.570  1.00 40.00           N  
ATOM   2757  CA  LEU B 309      31.092 -31.521  12.090  1.00 36.95           C  
ATOM   2758  C   LEU B 309      32.507 -31.244  11.603  1.00 42.57           C  
ATOM   2759  O   LEU B 309      33.461 -31.876  12.050  1.00 44.55           O  
ATOM   2760  CB  LEU B 309      30.742 -30.527  13.196  1.00 34.89           C  
ATOM   2761  CG  LEU B 309      29.337 -30.553  13.792  1.00 35.02           C  
ATOM   2762  CD1 LEU B 309      29.236 -29.514  14.916  1.00 31.45           C  
ATOM   2763  CD2 LEU B 309      28.283 -30.306  12.709  1.00 35.22           C  
ATOM   2764  N   ASP B 310      32.630 -30.293  10.684  1.00 42.18           N  
ATOM   2765  CA  ASP B 310      33.927 -29.786  10.258  1.00 44.95           C  
ATOM   2766  C   ASP B 310      34.826 -29.578  11.474  1.00 45.29           C  
ATOM   2767  O   ASP B 310      34.393 -29.029  12.487  1.00 38.70           O  
ATOM   2768  CB  ASP B 310      33.737 -28.465   9.517  1.00 44.40           C  
ATOM   2769  CG  ASP B 310      35.040 -27.862   9.055  1.00 45.75           C  
ATOM   2770  OD1 ASP B 310      35.226 -27.750   7.829  1.00 44.94           O  
ATOM   2771  OD2 ASP B 310      35.874 -27.493   9.908  1.00 52.64           O  
ATOM   2772  N   LEU B 311      36.078 -30.008  11.371  1.00 43.13           N  
ATOM   2773  CA  LEU B 311      36.976 -29.997  12.521  1.00 43.68           C  
ATOM   2774  C   LEU B 311      37.223 -28.578  13.037  1.00 36.21           C  
ATOM   2775  O   LEU B 311      37.320 -28.353  14.241  1.00 31.79           O  
ATOM   2776  CB  LEU B 311      38.298 -30.680  12.170  1.00 49.13           C  
ATOM   2777  CG  LEU B 311      38.758 -31.757  13.152  1.00 60.22           C  
ATOM   2778  CD1 LEU B 311      37.805 -32.941  13.120  1.00 60.01           C  
ATOM   2779  CD2 LEU B 311      40.174 -32.208  12.835  1.00 66.27           C  
ATOM   2780  N   ASN B 312      37.328 -27.623  12.118  1.00 40.37           N  
ATOM   2781  CA  ASN B 312      37.514 -26.223  12.489  1.00 38.94           C  
ATOM   2782  C   ASN B 312      36.300 -25.666  13.226  1.00 37.21           C  
ATOM   2783  O   ASN B 312      36.434 -24.844  14.130  1.00 34.06           O  
ATOM   2784  CB  ASN B 312      37.804 -25.371  11.251  1.00 37.59           C  
ATOM   2785  CG  ASN B 312      39.145 -25.695  10.618  1.00 41.24           C  
ATOM   2786  OD1 ASN B 312      40.196 -25.524  11.233  1.00 45.34           O  
ATOM   2787  ND2 ASN B 312      39.113 -26.151   9.374  1.00 40.26           N  
ATOM   2788  N   ASP B 313      35.115 -26.118  12.831  1.00 37.78           N  
ATOM   2789  CA  ASP B 313      33.882 -25.669  13.463  1.00 37.44           C  
ATOM   2790  C   ASP B 313      33.759 -26.215  14.885  1.00 38.22           C  
ATOM   2791  O   ASP B 313      33.310 -25.510  15.788  1.00 39.05           O  
ATOM   2792  CB  ASP B 313      32.668 -26.058  12.618  1.00 32.43           C  
ATOM   2793  CG  ASP B 313      32.494 -25.162  11.403  1.00 36.30           C  
ATOM   2794  OD1 ASP B 313      33.296 -24.220  11.232  1.00 39.54           O  
ATOM   2795  OD2 ASP B 313      31.551 -25.395  10.618  1.00 40.25           O  
ATOM   2796  N   GLN B 314      34.165 -27.468  15.079  1.00 37.90           N  
ATOM   2797  CA  GLN B 314      34.195 -28.059  16.414  1.00 34.72           C  
ATOM   2798  C   GLN B 314      35.059 -27.214  17.345  1.00 31.93           C  
ATOM   2799  O   GLN B 314      34.664 -26.905  18.467  1.00 31.37           O  
ATOM   2800  CB  GLN B 314      34.738 -29.491  16.368  1.00 33.66           C  
ATOM   2801  CG  GLN B 314      33.876 -30.471  15.587  1.00 36.08           C  
ATOM   2802  CD  GLN B 314      34.488 -31.863  15.532  1.00 39.56           C  
ATOM   2803  OE1 GLN B 314      34.431 -32.543  14.503  1.00 44.68           O  
ATOM   2804  NE2 GLN B 314      35.089 -32.287  16.638  1.00 33.59           N  
ATOM   2805  N   VAL B 315      36.247 -26.852  16.871  1.00 32.86           N  
ATOM   2806  CA  VAL B 315      37.165 -26.028  17.648  1.00 34.80           C  
ATOM   2807  C   VAL B 315      36.561 -24.653  17.914  1.00 35.21           C  
ATOM   2808  O   VAL B 315      36.668 -24.118  19.017  1.00 36.40           O  
ATOM   2809  CB  VAL B 315      38.520 -25.864  16.930  1.00 37.63           C  
ATOM   2810  CG1 VAL B 315      39.360 -24.789  17.610  1.00 36.91           C  
ATOM   2811  CG2 VAL B 315      39.268 -27.194  16.890  1.00 35.78           C  
ATOM   2812  N   THR B 316      35.920 -24.086  16.899  1.00 33.55           N  
ATOM   2813  CA  THR B 316      35.287 -22.781  17.040  1.00 34.39           C  
ATOM   2814  C   THR B 316      34.145 -22.803  18.058  1.00 34.16           C  
ATOM   2815  O   THR B 316      34.051 -21.922  18.915  1.00 35.69           O  
ATOM   2816  CB  THR B 316      34.767 -22.260  15.689  1.00 36.65           C  
ATOM   2817  OG1 THR B 316      35.879 -21.959  14.835  1.00 39.65           O  
ATOM   2818  CG2 THR B 316      33.926 -21.005  15.889  1.00 34.21           C  
ATOM   2819  N   LEU B 317      33.279 -23.808  17.960  1.00 30.25           N  
ATOM   2820  CA  LEU B 317      32.163 -23.939  18.892  1.00 32.09           C  
ATOM   2821  C   LEU B 317      32.672 -24.031  20.326  1.00 35.49           C  
ATOM   2822  O   LEU B 317      32.116 -23.415  21.233  1.00 34.56           O  
ATOM   2823  CB  LEU B 317      31.312 -25.169  18.560  1.00 31.00           C  
ATOM   2824  CG  LEU B 317      30.516 -25.144  17.251  1.00 31.88           C  
ATOM   2825  CD1 LEU B 317      29.752 -26.443  17.074  1.00 28.35           C  
ATOM   2826  CD2 LEU B 317      29.563 -23.957  17.237  1.00 31.75           C  
ATOM   2827  N   LEU B 318      33.735 -24.803  20.529  1.00 29.69           N  
ATOM   2828  CA  LEU B 318      34.304 -24.950  21.864  1.00 30.27           C  
ATOM   2829  C   LEU B 318      34.947 -23.653  22.339  1.00 28.76           C  
ATOM   2830  O   LEU B 318      34.709 -23.209  23.459  1.00 32.14           O  
ATOM   2831  CB  LEU B 318      35.311 -26.104  21.908  1.00 30.20           C  
ATOM   2832  CG  LEU B 318      34.650 -27.485  21.887  1.00 34.16           C  
ATOM   2833  CD1 LEU B 318      35.670 -28.596  21.725  1.00 34.87           C  
ATOM   2834  CD2 LEU B 318      33.805 -27.694  23.145  1.00 34.29           C  
ATOM   2835  N   LYS B 319      35.756 -23.048  21.476  1.00 30.80           N  
ATOM   2836  CA  LYS B 319      36.463 -21.817  21.813  1.00 37.72           C  
ATOM   2837  C   LYS B 319      35.532 -20.741  22.360  1.00 37.67           C  
ATOM   2838  O   LYS B 319      35.849 -20.081  23.353  1.00 34.86           O  
ATOM   2839  CB  LYS B 319      37.201 -21.276  20.588  1.00 41.39           C  
ATOM   2840  CG  LYS B 319      37.809 -19.900  20.794  1.00 47.76           C  
ATOM   2841  CD  LYS B 319      38.516 -19.408  19.536  1.00 53.18           C  
ATOM   2842  CE  LYS B 319      38.997 -17.972  19.700  1.00 61.48           C  
ATOM   2843  NZ  LYS B 319      39.727 -17.480  18.496  1.00 69.06           N  
ATOM   2844  N   TYR B 320      34.392 -20.559  21.702  1.00 33.00           N  
ATOM   2845  CA  TYR B 320      33.458 -19.510  22.091  1.00 38.61           C  
ATOM   2846  C   TYR B 320      32.407 -20.001  23.077  1.00 41.54           C  
ATOM   2847  O   TYR B 320      31.687 -19.199  23.665  1.00 50.57           O  
ATOM   2848  CB  TYR B 320      32.781 -18.898  20.860  1.00 40.05           C  
ATOM   2849  CG  TYR B 320      33.713 -18.067  20.009  1.00 42.16           C  
ATOM   2850  CD1 TYR B 320      34.010 -16.753  20.350  1.00 43.42           C  
ATOM   2851  CD2 TYR B 320      34.297 -18.597  18.868  1.00 41.82           C  
ATOM   2852  CE1 TYR B 320      34.865 -15.991  19.577  1.00 45.90           C  
ATOM   2853  CE2 TYR B 320      35.155 -17.846  18.091  1.00 46.37           C  
ATOM   2854  CZ  TYR B 320      35.434 -16.544  18.448  1.00 51.46           C  
ATOM   2855  OH  TYR B 320      36.288 -15.795  17.671  1.00 54.68           O  
ATOM   2856  N   GLY B 321      32.324 -21.314  23.267  1.00 36.72           N  
ATOM   2857  CA  GLY B 321      31.285 -21.878  24.110  1.00 36.35           C  
ATOM   2858  C   GLY B 321      31.685 -22.159  25.550  1.00 35.20           C  
ATOM   2859  O   GLY B 321      30.849 -22.095  26.453  1.00 31.15           O  
ATOM   2860  N   VAL B 322      32.958 -22.478  25.767  1.00 38.73           N  
ATOM   2861  CA  VAL B 322      33.417 -22.919  27.084  1.00 37.33           C  
ATOM   2862  C   VAL B 322      33.163 -21.898  28.190  1.00 34.37           C  
ATOM   2863  O   VAL B 322      32.789 -22.267  29.300  1.00 33.42           O  
ATOM   2864  CB  VAL B 322      34.912 -23.326  27.080  1.00 39.14           C  
ATOM   2865  CG1 VAL B 322      35.095 -24.649  26.360  1.00 38.20           C  
ATOM   2866  CG2 VAL B 322      35.766 -22.243  26.441  1.00 39.94           C  
ATOM   2867  N   HIS B 323      33.360 -20.619  27.892  1.00 32.07           N  
ATOM   2868  CA  HIS B 323      33.157 -19.582  28.898  1.00 36.70           C  
ATOM   2869  C   HIS B 323      31.722 -19.558  29.423  1.00 35.31           C  
ATOM   2870  O   HIS B 323      31.499 -19.512  30.630  1.00 35.28           O  
ATOM   2871  CB  HIS B 323      33.549 -18.207  28.357  1.00 49.78           C  
ATOM   2872  CG  HIS B 323      34.997 -17.875  28.541  1.00 62.61           C  
ATOM   2873  ND1 HIS B 323      35.949 -18.135  27.578  1.00 67.38           N  
ATOM   2874  CD2 HIS B 323      35.656 -17.301  29.575  1.00 67.90           C  
ATOM   2875  CE1 HIS B 323      37.132 -17.736  28.012  1.00 70.57           C  
ATOM   2876  NE2 HIS B 323      36.981 -17.225  29.221  1.00 71.73           N  
ATOM   2877  N   GLU B 324      30.752 -19.587  28.514  1.00 34.09           N  
ATOM   2878  CA  GLU B 324      29.346 -19.588  28.904  1.00 33.98           C  
ATOM   2879  C   GLU B 324      29.012 -20.815  29.743  1.00 30.74           C  
ATOM   2880  O   GLU B 324      28.271 -20.726  30.721  1.00 33.40           O  
ATOM   2881  CB  GLU B 324      28.443 -19.528  27.668  1.00 34.78           C  
ATOM   2882  CG  GLU B 324      28.425 -18.166  26.992  1.00 35.82           C  
ATOM   2883  CD  GLU B 324      27.979 -18.228  25.544  1.00 39.98           C  
ATOM   2884  OE1 GLU B 324      27.105 -19.056  25.210  1.00 41.16           O  
ATOM   2885  OE2 GLU B 324      28.508 -17.441  24.735  1.00 46.25           O  
ATOM   2886  N   ILE B 325      29.565 -21.960  29.359  1.00 32.87           N  
ATOM   2887  CA  ILE B 325      29.309 -23.204  30.074  1.00 35.32           C  
ATOM   2888  C   ILE B 325      29.975 -23.207  31.447  1.00 36.93           C  
ATOM   2889  O   ILE B 325      29.418 -23.724  32.411  1.00 33.10           O  
ATOM   2890  CB  ILE B 325      29.772 -24.427  29.273  1.00 36.17           C  
ATOM   2891  CG1 ILE B 325      28.975 -24.533  27.975  1.00 43.34           C  
ATOM   2892  CG2 ILE B 325      29.610 -25.701  30.101  1.00 27.07           C  
ATOM   2893  CD1 ILE B 325      29.369 -25.716  27.130  1.00 49.70           C  
ATOM   2894  N   ILE B 326      31.164 -22.620  31.533  1.00 34.96           N  
ATOM   2895  CA  ILE B 326      31.869 -22.525  32.808  1.00 32.01           C  
ATOM   2896  C   ILE B 326      31.066 -21.758  33.863  1.00 32.67           C  
ATOM   2897  O   ILE B 326      30.982 -22.176  35.015  1.00 34.55           O  
ATOM   2898  CB  ILE B 326      33.257 -21.886  32.633  1.00 31.40           C  
ATOM   2899  CG1 ILE B 326      34.214 -22.889  31.977  1.00 33.74           C  
ATOM   2900  CG2 ILE B 326      33.798 -21.411  33.978  1.00 35.70           C  
ATOM   2901  CD1 ILE B 326      35.564 -22.310  31.612  1.00 35.48           C  
ATOM   2902  N   TYR B 327      30.460 -20.644  33.465  1.00 33.90           N  
ATOM   2903  CA  TYR B 327      29.676 -19.848  34.405  1.00 36.00           C  
ATOM   2904  C   TYR B 327      28.328 -20.493  34.692  1.00 38.88           C  
ATOM   2905  O   TYR B 327      27.780 -20.353  35.784  1.00 37.04           O  
ATOM   2906  CB  TYR B 327      29.514 -18.418  33.893  1.00 39.60           C  
ATOM   2907  CG  TYR B 327      30.846 -17.763  33.631  1.00 49.25           C  
ATOM   2908  CD1 TYR B 327      31.876 -17.859  34.559  1.00 57.33           C  
ATOM   2909  CD2 TYR B 327      31.083 -17.060  32.459  1.00 53.93           C  
ATOM   2910  CE1 TYR B 327      33.105 -17.274  34.327  1.00 63.44           C  
ATOM   2911  CE2 TYR B 327      32.309 -16.465  32.219  1.00 60.31           C  
ATOM   2912  CZ  TYR B 327      33.316 -16.576  33.157  1.00 64.86           C  
ATOM   2913  OH  TYR B 327      34.536 -15.986  32.924  1.00 71.81           O  
ATOM   2914  N   THR B 328      27.803 -21.214  33.710  1.00 35.82           N  
ATOM   2915  CA  THR B 328      26.584 -21.976  33.914  1.00 37.96           C  
ATOM   2916  C   THR B 328      26.799 -23.013  35.011  1.00 40.17           C  
ATOM   2917  O   THR B 328      26.013 -23.114  35.957  1.00 38.20           O  
ATOM   2918  CB  THR B 328      26.150 -22.688  32.624  1.00 35.59           C  
ATOM   2919  OG1 THR B 328      25.749 -21.711  31.657  1.00 35.10           O  
ATOM   2920  CG2 THR B 328      24.990 -23.634  32.899  1.00 31.68           C  
ATOM   2921  N   MET B 329      27.879 -23.774  34.886  1.00 35.61           N  
ATOM   2922  CA  MET B 329      28.150 -24.858  35.818  1.00 41.00           C  
ATOM   2923  C   MET B 329      28.701 -24.348  37.149  1.00 39.74           C  
ATOM   2924  O   MET B 329      28.523 -24.986  38.186  1.00 38.66           O  
ATOM   2925  CB  MET B 329      29.077 -25.894  35.179  1.00 42.08           C  
ATOM   2926  CG  MET B 329      28.519 -26.462  33.880  1.00 43.63           C  
ATOM   2927  SD  MET B 329      29.356 -27.955  33.328  1.00 50.40           S  
ATOM   2928  CE  MET B 329      28.977 -29.073  34.677  1.00 41.00           C  
ATOM   2929  N   LEU B 330      29.351 -23.189  37.118  1.00 38.12           N  
ATOM   2930  CA  LEU B 330      29.832 -22.556  38.343  1.00 38.88           C  
ATOM   2931  C   LEU B 330      28.658 -22.190  39.252  1.00 38.32           C  
ATOM   2932  O   LEU B 330      28.776 -22.200  40.476  1.00 35.90           O  
ATOM   2933  CB  LEU B 330      30.656 -21.308  38.017  1.00 36.79           C  
ATOM   2934  CG  LEU B 330      31.237 -20.530  39.200  1.00 39.52           C  
ATOM   2935  CD1 LEU B 330      32.225 -21.393  39.982  1.00 41.31           C  
ATOM   2936  CD2 LEU B 330      31.897 -19.242  38.726  1.00 38.92           C  
ATOM   2937  N   ALA B 331      27.524 -21.865  38.642  1.00 38.01           N  
ATOM   2938  CA  ALA B 331      26.320 -21.542  39.398  1.00 37.27           C  
ATOM   2939  C   ALA B 331      25.898 -22.725  40.262  1.00 39.62           C  
ATOM   2940  O   ALA B 331      25.360 -22.544  41.354  1.00 40.07           O  
ATOM   2941  CB  ALA B 331      25.195 -21.139  38.459  1.00 34.08           C  
ATOM   2942  N   SER B 332      26.150 -23.933  39.765  1.00 36.64           N  
ATOM   2943  CA  SER B 332      25.826 -25.153  40.498  1.00 39.35           C  
ATOM   2944  C   SER B 332      26.620 -25.255  41.794  1.00 41.42           C  
ATOM   2945  O   SER B 332      26.182 -25.901  42.744  1.00 40.88           O  
ATOM   2946  CB  SER B 332      26.105 -26.391  39.642  1.00 38.30           C  
ATOM   2947  OG  SER B 332      25.292 -26.419  38.486  1.00 36.61           O  
ATOM   2948  N   LEU B 333      27.792 -24.628  41.823  1.00 39.15           N  
ATOM   2949  CA  LEU B 333      28.669 -24.701  42.988  1.00 41.50           C  
ATOM   2950  C   LEU B 333      28.495 -23.500  43.914  1.00 41.42           C  
ATOM   2951  O   LEU B 333      29.225 -23.352  44.896  1.00 42.68           O  
ATOM   2952  CB  LEU B 333      30.131 -24.807  42.550  1.00 45.42           C  
ATOM   2953  CG  LEU B 333      30.464 -25.833  41.464  1.00 48.30           C  
ATOM   2954  CD1 LEU B 333      31.970 -25.911  41.251  1.00 48.09           C  
ATOM   2955  CD2 LEU B 333      29.900 -27.200  41.808  1.00 45.94           C  
ATOM   2956  N   MET B 334      27.520 -22.651  43.603  1.00 39.65           N  
ATOM   2957  CA  MET B 334      27.343 -21.396  44.323  1.00 40.56           C  
ATOM   2958  C   MET B 334      26.015 -21.295  45.065  1.00 43.43           C  
ATOM   2959  O   MET B 334      24.992 -21.817  44.620  1.00 43.12           O  
ATOM   2960  CB  MET B 334      27.425 -20.211  43.354  1.00 41.25           C  
ATOM   2961  CG  MET B 334      28.818 -19.848  42.864  1.00 43.54           C  
ATOM   2962  SD  MET B 334      28.738 -18.505  41.657  1.00 44.23           S  
ATOM   2963  CE  MET B 334      30.406 -17.863  41.747  1.00 44.74           C  
ATOM   2964  N   ASN B 335      26.049 -20.606  46.199  1.00 42.67           N  
ATOM   2965  CA  ASN B 335      24.849 -20.020  46.776  1.00 44.85           C  
ATOM   2966  C   ASN B 335      25.115 -18.538  47.024  1.00 48.67           C  
ATOM   2967  O   ASN B 335      26.139 -18.014  46.586  1.00 48.34           O  
ATOM   2968  CB  ASN B 335      24.396 -20.752  48.044  1.00 41.77           C  
ATOM   2969  CG  ASN B 335      25.446 -20.754  49.140  1.00 45.25           C  
ATOM   2970  OD1 ASN B 335      26.331 -19.901  49.182  1.00 48.26           O  
ATOM   2971  ND2 ASN B 335      25.341 -21.718  50.044  1.00 45.71           N  
ATOM   2972  N   LYS B 336      24.209 -17.858  47.714  1.00 49.00           N  
ATOM   2973  CA  LYS B 336      24.362 -16.420  47.910  1.00 50.39           C  
ATOM   2974  C   LYS B 336      25.533 -16.077  48.829  1.00 50.96           C  
ATOM   2975  O   LYS B 336      25.946 -14.921  48.909  1.00 49.36           O  
ATOM   2976  CB  LYS B 336      23.068 -15.801  48.444  1.00 50.90           C  
ATOM   2977  CG  LYS B 336      22.630 -16.328  49.800  1.00 52.62           C  
ATOM   2978  CD  LYS B 336      21.293 -15.732  50.205  1.00 57.49           C  
ATOM   2979  CE  LYS B 336      20.839 -16.252  51.561  1.00 62.85           C  
ATOM   2980  NZ  LYS B 336      21.834 -15.961  52.629  1.00 64.27           N  
ATOM   2981  N   ASP B 337      26.078 -17.084  49.503  1.00 48.28           N  
ATOM   2982  CA  ASP B 337      27.104 -16.851  50.515  1.00 51.55           C  
ATOM   2983  C   ASP B 337      28.509 -17.303  50.112  1.00 50.49           C  
ATOM   2984  O   ASP B 337      29.484 -16.964  50.783  1.00 48.33           O  
ATOM   2985  CB  ASP B 337      26.705 -17.508  51.839  1.00 54.23           C  
ATOM   2986  CG  ASP B 337      25.512 -16.836  52.487  1.00 58.38           C  
ATOM   2987  OD1 ASP B 337      25.539 -15.597  52.643  1.00 57.02           O  
ATOM   2988  OD2 ASP B 337      24.550 -17.548  52.843  1.00 61.08           O  
ATOM   2989  N   GLY B 338      28.620 -18.070  49.032  1.00 47.65           N  
ATOM   2990  CA  GLY B 338      29.927 -18.518  48.584  1.00 44.59           C  
ATOM   2991  C   GLY B 338      29.928 -19.554  47.478  1.00 45.60           C  
ATOM   2992  O   GLY B 338      28.891 -19.852  46.886  1.00 45.26           O  
ATOM   2993  N   VAL B 339      31.106 -20.109  47.206  1.00 46.28           N  
ATOM   2994  CA  VAL B 339      31.282 -21.047  46.104  1.00 44.79           C  
ATOM   2995  C   VAL B 339      32.162 -22.234  46.496  1.00 47.27           C  
ATOM   2996  O   VAL B 339      33.192 -22.069  47.148  1.00 47.67           O  
ATOM   2997  CB  VAL B 339      31.895 -20.345  44.872  1.00 42.36           C  
ATOM   2998  CG1 VAL B 339      33.238 -19.724  45.228  1.00 40.56           C  
ATOM   2999  CG2 VAL B 339      32.041 -21.321  43.712  1.00 41.94           C  
ATOM   3000  N   LEU B 340      31.740 -23.431  46.100  1.00 49.79           N  
ATOM   3001  CA  LEU B 340      32.537 -24.638  46.297  1.00 48.09           C  
ATOM   3002  C   LEU B 340      33.823 -24.566  45.483  1.00 50.55           C  
ATOM   3003  O   LEU B 340      33.807 -24.169  44.318  1.00 49.58           O  
ATOM   3004  CB  LEU B 340      31.740 -25.872  45.872  1.00 47.20           C  
ATOM   3005  CG  LEU B 340      30.992 -26.664  46.943  1.00 52.40           C  
ATOM   3006  CD1 LEU B 340      30.565 -25.770  48.089  1.00 61.89           C  
ATOM   3007  CD2 LEU B 340      29.803 -27.392  46.336  1.00 47.24           C  
ATOM   3008  N   ILE B 341      34.936 -24.952  46.097  1.00 50.77           N  
ATOM   3009  CA  ILE B 341      36.213 -24.995  45.392  1.00 53.61           C  
ATOM   3010  C   ILE B 341      36.912 -26.332  45.610  1.00 54.85           C  
ATOM   3011  O   ILE B 341      36.521 -27.115  46.478  1.00 49.81           O  
ATOM   3012  CB  ILE B 341      37.161 -23.865  45.845  1.00 54.25           C  
ATOM   3013  CG1 ILE B 341      37.636 -24.111  47.280  1.00 51.82           C  
ATOM   3014  CG2 ILE B 341      36.490 -22.505  45.698  1.00 51.44           C  
ATOM   3015  CD1 ILE B 341      38.782 -23.218  47.711  1.00 53.24           C  
ATOM   3016  N   SER B 342      37.947 -26.581  44.812  1.00 52.91           N  
ATOM   3017  CA  SER B 342      38.776 -27.772  44.958  1.00 53.24           C  
ATOM   3018  C   SER B 342      37.944 -29.044  45.078  1.00 52.70           C  
ATOM   3019  O   SER B 342      38.033 -29.760  46.075  1.00 51.63           O  
ATOM   3020  CB  SER B 342      39.692 -27.635  46.174  1.00 58.91           C  
ATOM   3021  OG  SER B 342      40.635 -28.691  46.215  1.00 64.67           O  
ATOM   3022  N   GLU B 343      37.130 -29.310  44.062  1.00 51.39           N  
ATOM   3023  CA  GLU B 343      36.303 -30.511  44.031  1.00 54.09           C  
ATOM   3024  C   GLU B 343      35.367 -30.600  45.232  1.00 57.91           C  
ATOM   3025  O   GLU B 343      35.037 -31.693  45.691  1.00 61.20           O  
ATOM   3026  CB  GLU B 343      37.179 -31.764  43.953  1.00 59.06           C  
ATOM   3027  N   GLY B 344      34.945 -29.445  45.740  1.00 54.13           N  
ATOM   3028  CA  GLY B 344      33.985 -29.394  46.827  1.00 52.96           C  
ATOM   3029  C   GLY B 344      34.577 -29.621  48.207  1.00 55.40           C  
ATOM   3030  O   GLY B 344      33.848 -29.692  49.196  1.00 59.28           O  
ATOM   3031  N   GLN B 345      35.899 -29.737  48.280  1.00 53.54           N  
ATOM   3032  CA  GLN B 345      36.570 -29.920  49.563  1.00 60.75           C  
ATOM   3033  C   GLN B 345      36.578 -28.618  50.348  1.00 58.25           C  
ATOM   3034  O   GLN B 345      36.627 -28.623  51.575  1.00 57.89           O  
ATOM   3035  CB  GLN B 345      38.004 -30.414  49.364  1.00 64.86           C  
ATOM   3036  CG  GLN B 345      38.102 -31.819  48.803  1.00 72.57           C  
ATOM   3037  CD  GLN B 345      39.529 -32.219  48.486  1.00 82.65           C  
ATOM   3038  OE1 GLN B 345      39.780 -32.961  47.536  1.00 88.33           O  
ATOM   3039  NE2 GLN B 345      40.475 -31.722  49.277  1.00 83.81           N  
ATOM   3040  N   GLY B 346      36.528 -27.500  49.632  1.00 52.44           N  
ATOM   3041  CA  GLY B 346      36.539 -26.199  50.270  1.00 49.59           C  
ATOM   3042  C   GLY B 346      35.325 -25.365  49.915  1.00 50.57           C  
ATOM   3043  O   GLY B 346      34.513 -25.747  49.074  1.00 50.11           O  
ATOM   3044  N   PHE B 347      35.208 -24.216  50.569  1.00 52.13           N  
ATOM   3045  CA  PHE B 347      34.124 -23.279  50.311  1.00 51.68           C  
ATOM   3046  C   PHE B 347      34.636 -21.872  50.579  1.00 50.22           C  
ATOM   3047  O   PHE B 347      34.981 -21.533  51.709  1.00 48.15           O  
ATOM   3048  CB  PHE B 347      32.924 -23.595  51.207  1.00 56.74           C  
ATOM   3049  CG  PHE B 347      31.785 -22.621  51.072  1.00 55.98           C  
ATOM   3050  CD1 PHE B 347      30.897 -22.714  50.013  1.00 54.66           C  
ATOM   3051  CD2 PHE B 347      31.593 -21.624  52.014  1.00 56.87           C  
ATOM   3052  CE1 PHE B 347      29.845 -21.823  49.890  1.00 52.03           C  
ATOM   3053  CE2 PHE B 347      30.544 -20.730  51.897  1.00 56.42           C  
ATOM   3054  CZ  PHE B 347      29.669 -20.831  50.834  1.00 54.98           C  
ATOM   3055  N   MET B 348      34.710 -21.057  49.534  1.00 51.05           N  
ATOM   3056  CA  MET B 348      35.218 -19.701  49.684  1.00 54.52           C  
ATOM   3057  C   MET B 348      34.056 -18.725  49.744  1.00 52.20           C  
ATOM   3058  O   MET B 348      33.265 -18.634  48.807  1.00 51.69           O  
ATOM   3059  CB  MET B 348      36.161 -19.341  48.534  1.00 56.52           C  
ATOM   3060  CG  MET B 348      36.953 -18.062  48.762  1.00 58.27           C  
ATOM   3061  SD  MET B 348      38.264 -17.831  47.547  1.00 69.69           S  
ATOM   3062  CE  MET B 348      39.366 -19.177  47.974  1.00 67.97           C  
ATOM   3063  N   THR B 349      33.956 -18.001  50.854  1.00 53.18           N  
ATOM   3064  CA  THR B 349      32.833 -17.099  51.071  1.00 54.29           C  
ATOM   3065  C   THR B 349      32.792 -15.984  50.035  1.00 53.46           C  
ATOM   3066  O   THR B 349      33.827 -15.542  49.536  1.00 47.65           O  
ATOM   3067  CB  THR B 349      32.857 -16.481  52.485  1.00 53.72           C  
ATOM   3068  OG1 THR B 349      33.973 -15.591  52.606  1.00 54.60           O  
ATOM   3069  CG2 THR B 349      32.968 -17.570  53.535  1.00 54.79           C  
ATOM   3070  N   ARG B 350      31.580 -15.545  49.716  1.00 56.88           N  
ATOM   3071  CA  ARG B 350      31.367 -14.433  48.804  1.00 54.91           C  
ATOM   3072  C   ARG B 350      32.021 -13.174  49.354  1.00 56.89           C  
ATOM   3073  O   ARG B 350      32.570 -12.368  48.603  1.00 53.18           O  
ATOM   3074  CB  ARG B 350      29.868 -14.201  48.627  1.00 53.86           C  
ATOM   3075  CG  ARG B 350      29.497 -13.085  47.674  1.00 54.79           C  
ATOM   3076  CD  ARG B 350      27.993 -13.065  47.470  1.00 55.48           C  
ATOM   3077  NE  ARG B 350      27.579 -12.125  46.435  1.00 57.67           N  
ATOM   3078  CZ  ARG B 350      26.333 -12.017  45.987  1.00 58.67           C  
ATOM   3079  NH1 ARG B 350      25.379 -12.798  46.480  1.00 57.18           N  
ATOM   3080  NH2 ARG B 350      26.040 -11.132  45.044  1.00 57.61           N  
ATOM   3081  N   GLU B 351      31.959 -13.019  50.674  1.00 59.34           N  
ATOM   3082  CA  GLU B 351      32.499 -11.840  51.343  1.00 62.57           C  
ATOM   3083  C   GLU B 351      34.022 -11.766  51.294  1.00 63.69           C  
ATOM   3084  O   GLU B 351      34.587 -10.684  51.140  1.00 65.54           O  
ATOM   3085  CB  GLU B 351      32.009 -11.774  52.791  1.00 67.62           C  
ATOM   3086  CG  GLU B 351      30.594 -11.245  52.928  1.00 75.09           C  
ATOM   3087  CD  GLU B 351      30.451  -9.837  52.380  1.00 84.62           C  
ATOM   3088  OE1 GLU B 351      31.316  -8.990  52.688  1.00 89.24           O  
ATOM   3089  OE2 GLU B 351      29.475  -9.577  51.643  1.00 85.89           O  
ATOM   3090  N   PHE B 352      34.687 -12.908  51.433  1.00 63.25           N  
ATOM   3091  CA  PHE B 352      36.144 -12.929  51.370  1.00 64.75           C  
ATOM   3092  C   PHE B 352      36.635 -12.559  49.978  1.00 63.92           C  
ATOM   3093  O   PHE B 352      37.557 -11.760  49.830  1.00 67.38           O  
ATOM   3094  CB  PHE B 352      36.705 -14.293  51.774  1.00 63.97           C  
ATOM   3095  CG  PHE B 352      38.184 -14.423  51.544  1.00 64.13           C  
ATOM   3096  CD1 PHE B 352      39.076 -13.602  52.215  1.00 67.74           C  
ATOM   3097  CD2 PHE B 352      38.683 -15.355  50.650  1.00 63.16           C  
ATOM   3098  CE1 PHE B 352      40.437 -13.712  52.004  1.00 68.23           C  
ATOM   3099  CE2 PHE B 352      40.044 -15.470  50.435  1.00 63.71           C  
ATOM   3100  CZ  PHE B 352      40.921 -14.648  51.113  1.00 66.00           C  
ATOM   3101  N   LEU B 353      36.019 -13.150  48.960  1.00 63.19           N  
ATOM   3102  CA  LEU B 353      36.351 -12.832  47.577  1.00 62.90           C  
ATOM   3103  C   LEU B 353      36.105 -11.355  47.295  1.00 67.49           C  
ATOM   3104  O   LEU B 353      36.907 -10.692  46.637  1.00 68.60           O  
ATOM   3105  CB  LEU B 353      35.527 -13.692  46.618  1.00 57.32           C  
ATOM   3106  CG  LEU B 353      35.973 -15.148  46.480  1.00 53.81           C  
ATOM   3107  CD1 LEU B 353      34.848 -16.018  45.926  1.00 53.46           C  
ATOM   3108  CD2 LEU B 353      37.220 -15.236  45.608  1.00 52.71           C  
ATOM   3109  N   LYS B 354      34.985 -10.851  47.801  1.00 67.12           N  
ATOM   3110  CA  LYS B 354      34.596  -9.462  47.596  1.00 74.48           C  
ATOM   3111  C   LYS B 354      35.560  -8.506  48.300  1.00 77.36           C  
ATOM   3112  O   LYS B 354      35.681  -7.342  47.920  1.00 80.43           O  
ATOM   3113  CB  LYS B 354      33.171  -9.246  48.110  1.00 79.60           C  
ATOM   3114  CG  LYS B 354      32.443  -8.062  47.500  1.00 82.29           C  
ATOM   3115  CD  LYS B 354      31.020  -7.977  48.034  1.00 84.53           C  
ATOM   3116  CE  LYS B 354      30.237  -6.861  47.363  1.00 88.29           C  
ATOM   3117  NZ  LYS B 354      28.887  -6.700  47.970  1.00 91.99           N  
ATOM   3118  N   SER B 355      36.250  -9.006  49.321  1.00 75.47           N  
ATOM   3119  CA  SER B 355      37.139  -8.174  50.127  1.00 74.35           C  
ATOM   3120  C   SER B 355      38.525  -8.024  49.508  1.00 74.80           C  
ATOM   3121  O   SER B 355      39.375  -7.314  50.044  1.00 76.56           O  
ATOM   3122  CB  SER B 355      37.267  -8.740  51.542  1.00 76.24           C  
ATOM   3123  OG  SER B 355      38.162  -9.838  51.574  1.00 75.34           O  
ATOM   3124  N   LEU B 356      38.753  -8.692  48.383  1.00 75.06           N  
ATOM   3125  CA  LEU B 356      40.050  -8.638  47.720  1.00 78.38           C  
ATOM   3126  C   LEU B 356      40.314  -7.260  47.120  1.00 82.13           C  
ATOM   3127  O   LEU B 356      39.390  -6.578  46.675  1.00 81.40           O  
ATOM   3128  CB  LEU B 356      40.150  -9.719  46.642  1.00 76.49           C  
ATOM   3129  CG  LEU B 356      40.049 -11.164  47.136  1.00 74.54           C  
ATOM   3130  CD1 LEU B 356      40.237 -12.142  45.986  1.00 71.19           C  
ATOM   3131  CD2 LEU B 356      41.067 -11.425  48.233  1.00 75.92           C  
ATOM   3132  N   ARG B 357      41.581  -6.856  47.116  1.00 86.09           N  
ATOM   3133  CA  ARG B 357      41.972  -5.550  46.596  1.00 89.57           C  
ATOM   3134  C   ARG B 357      41.667  -5.425  45.109  1.00 90.17           C  
ATOM   3135  O   ARG B 357      41.825  -6.383  44.351  1.00 86.55           O  
ATOM   3136  CB  ARG B 357      43.461  -5.298  46.845  1.00 89.95           C  
ATOM   3137  N   LYS B 358      41.231  -4.238  44.699  1.00 93.77           N  
ATOM   3138  CA  LYS B 358      40.900  -3.976  43.304  1.00 92.10           C  
ATOM   3139  C   LYS B 358      42.069  -4.322  42.391  1.00 91.44           C  
ATOM   3140  O   LYS B 358      43.229  -4.166  42.773  1.00 91.90           O  
ATOM   3141  CB  LYS B 358      40.505  -2.509  43.114  1.00 92.27           C  
ATOM   3142  N   PRO B 359      41.764  -4.798  41.175  1.00 90.08           N  
ATOM   3143  CA  PRO B 359      40.403  -5.047  40.696  1.00 90.30           C  
ATOM   3144  C   PRO B 359      39.960  -6.486  40.954  1.00 87.92           C  
ATOM   3145  O   PRO B 359      38.980  -6.941  40.363  1.00 85.45           O  
ATOM   3146  CB  PRO B 359      40.560  -4.831  39.196  1.00 89.69           C  
ATOM   3147  CG  PRO B 359      41.880  -5.480  38.942  1.00 87.09           C  
ATOM   3148  CD  PRO B 359      42.735  -4.927  40.073  1.00 89.05           C  
ATOM   3149  N   PHE B 360      40.675  -7.188  41.827  1.00 87.09           N  
ATOM   3150  CA  PHE B 360      40.425  -8.609  42.059  1.00 80.49           C  
ATOM   3151  C   PHE B 360      39.209  -8.881  42.938  1.00 79.48           C  
ATOM   3152  O   PHE B 360      38.658  -9.979  42.922  1.00 81.11           O  
ATOM   3153  CB  PHE B 360      41.665  -9.281  42.655  1.00 78.18           C  
ATOM   3154  CG  PHE B 360      42.801  -9.421  41.683  1.00 77.29           C  
ATOM   3155  CD1 PHE B 360      43.778  -8.445  41.593  1.00 78.96           C  
ATOM   3156  CD2 PHE B 360      42.887 -10.527  40.854  1.00 75.80           C  
ATOM   3157  CE1 PHE B 360      44.823  -8.572  40.698  1.00 78.02           C  
ATOM   3158  CE2 PHE B 360      43.928 -10.658  39.957  1.00 75.87           C  
ATOM   3159  CZ  PHE B 360      44.898  -9.680  39.879  1.00 77.02           C  
ATOM   3160  N   GLY B 361      38.788  -7.884  43.706  1.00 78.70           N  
ATOM   3161  CA  GLY B 361      37.658  -8.063  44.596  1.00 78.67           C  
ATOM   3162  C   GLY B 361      36.328  -8.006  43.871  1.00 77.76           C  
ATOM   3163  O   GLY B 361      35.272  -8.099  44.496  1.00 77.55           O  
ATOM   3164  N   ASP B 362      36.375  -7.868  42.550  1.00 80.26           N  
ATOM   3165  CA  ASP B 362      35.159  -7.638  41.780  1.00 84.65           C  
ATOM   3166  C   ASP B 362      35.056  -8.503  40.522  1.00 81.35           C  
ATOM   3167  O   ASP B 362      34.444  -8.093  39.536  1.00 84.39           O  
ATOM   3168  CB  ASP B 362      35.060  -6.156  41.403  1.00 92.32           C  
ATOM   3169  CG  ASP B 362      33.627  -5.690  41.222  1.00 99.19           C  
ATOM   3170  OD1 ASP B 362      32.818  -6.437  40.631  1.00 99.32           O  
ATOM   3171  OD2 ASP B 362      33.313  -4.567  41.671  1.00103.28           O  
ATOM   3172  N   PHE B 363      35.645  -9.695  40.545  1.00 75.60           N  
ATOM   3173  CA  PHE B 363      35.544 -10.581  39.388  1.00 70.64           C  
ATOM   3174  C   PHE B 363      34.514 -11.694  39.585  1.00 61.64           C  
ATOM   3175  O   PHE B 363      33.899 -12.152  38.624  1.00 58.90           O  
ATOM   3176  CB  PHE B 363      36.916 -11.139  38.970  1.00 76.43           C  
ATOM   3177  CG  PHE B 363      37.426 -12.255  39.843  1.00 83.87           C  
ATOM   3178  CD1 PHE B 363      37.314 -13.578  39.439  1.00 85.60           C  
ATOM   3179  CD2 PHE B 363      38.041 -11.983  41.054  1.00 87.11           C  
ATOM   3180  CE1 PHE B 363      37.793 -14.607  40.236  1.00 86.44           C  
ATOM   3181  CE2 PHE B 363      38.521 -13.007  41.855  1.00 87.19           C  
ATOM   3182  CZ  PHE B 363      38.396 -14.321  41.446  1.00 86.63           C  
ATOM   3183  N   MET B 364      34.313 -12.108  40.832  1.00 58.43           N  
ATOM   3184  CA  MET B 364      33.359 -13.174  41.132  1.00 59.04           C  
ATOM   3185  C   MET B 364      31.957 -12.642  41.420  1.00 59.43           C  
ATOM   3186  O   MET B 364      30.968 -13.353  41.239  1.00 57.82           O  
ATOM   3187  CB  MET B 364      33.842 -14.024  42.312  1.00 63.04           C  
ATOM   3188  CG  MET B 364      34.927 -15.033  41.973  1.00 65.59           C  
ATOM   3189  SD  MET B 364      34.350 -16.368  40.905  1.00 68.16           S  
ATOM   3190  CE  MET B 364      34.585 -15.646  39.283  1.00 87.55           C  
ATOM   3191  N   GLU B 365      31.876 -11.395  41.871  1.00 58.88           N  
ATOM   3192  CA  GLU B 365      30.595 -10.807  42.250  1.00 61.84           C  
ATOM   3193  C   GLU B 365      29.543 -10.908  41.142  1.00 61.36           C  
ATOM   3194  O   GLU B 365      28.421 -11.353  41.391  1.00 62.47           O  
ATOM   3195  CB  GLU B 365      30.772  -9.356  42.712  1.00 65.21           C  
ATOM   3196  CG  GLU B 365      29.546  -8.765  43.390  1.00 67.49           C  
ATOM   3197  CD  GLU B 365      29.110  -9.551  44.615  1.00 69.74           C  
ATOM   3198  OE1 GLU B 365      29.814 -10.506  45.006  1.00 71.51           O  
ATOM   3199  OE2 GLU B 365      28.055  -9.210  45.189  1.00 72.31           O  
ATOM   3200  N   PRO B 366      29.900 -10.500  39.913  1.00 59.88           N  
ATOM   3201  CA  PRO B 366      28.956 -10.618  38.796  1.00 57.50           C  
ATOM   3202  C   PRO B 366      28.503 -12.060  38.581  1.00 56.00           C  
ATOM   3203  O   PRO B 366      27.372 -12.294  38.158  1.00 58.45           O  
ATOM   3204  CB  PRO B 366      29.777 -10.144  37.595  1.00 57.30           C  
ATOM   3205  CG  PRO B 366      30.815  -9.253  38.177  1.00 60.99           C  
ATOM   3206  CD  PRO B 366      31.159  -9.852  39.503  1.00 61.62           C  
ATOM   3207  N   LYS B 367      29.384 -13.014  38.865  1.00 49.50           N  
ATOM   3208  CA  LYS B 367      29.046 -14.426  38.731  1.00 48.89           C  
ATOM   3209  C   LYS B 367      28.038 -14.847  39.799  1.00 45.34           C  
ATOM   3210  O   LYS B 367      27.109 -15.606  39.523  1.00 47.56           O  
ATOM   3211  CB  LYS B 367      30.304 -15.290  38.826  1.00 49.90           C  
ATOM   3212  CG  LYS B 367      31.487 -14.754  38.035  1.00 51.88           C  
ATOM   3213  CD  LYS B 367      31.200 -14.714  36.550  1.00 57.97           C  
ATOM   3214  CE  LYS B 367      32.461 -14.405  35.749  1.00 63.59           C  
ATOM   3215  NZ  LYS B 367      33.042 -13.076  36.079  1.00 65.71           N  
ATOM   3216  N   PHE B 368      28.230 -14.351  41.018  1.00 40.48           N  
ATOM   3217  CA  PHE B 368      27.312 -14.636  42.117  1.00 43.94           C  
ATOM   3218  C   PHE B 368      25.915 -14.114  41.811  1.00 48.28           C  
ATOM   3219  O   PHE B 368      24.918 -14.803  42.033  1.00 48.47           O  
ATOM   3220  CB  PHE B 368      27.819 -14.011  43.420  1.00 48.63           C  
ATOM   3221  CG  PHE B 368      28.862 -14.832  44.124  1.00 47.93           C  
ATOM   3222  CD1 PHE B 368      28.521 -16.026  44.738  1.00 46.77           C  
ATOM   3223  CD2 PHE B 368      30.178 -14.404  44.185  1.00 46.00           C  
ATOM   3224  CE1 PHE B 368      29.473 -16.783  45.391  1.00 46.81           C  
ATOM   3225  CE2 PHE B 368      31.136 -15.156  44.840  1.00 48.48           C  
ATOM   3226  CZ  PHE B 368      30.782 -16.347  45.443  1.00 47.96           C  
ATOM   3227  N   GLU B 369      25.851 -12.889  41.301  1.00 50.16           N  
ATOM   3228  CA  GLU B 369      24.578 -12.259  40.981  1.00 56.02           C  
ATOM   3229  C   GLU B 369      23.821 -13.087  39.955  1.00 48.45           C  
ATOM   3230  O   GLU B 369      22.612 -13.287  40.067  1.00 48.68           O  
ATOM   3231  CB  GLU B 369      24.801 -10.840  40.458  1.00 61.81           C  
ATOM   3232  CG  GLU B 369      25.519  -9.929  41.440  1.00 68.47           C  
ATOM   3233  CD  GLU B 369      25.541  -8.482  40.987  1.00 74.92           C  
ATOM   3234  OE1 GLU B 369      25.772  -7.595  41.837  1.00 77.74           O  
ATOM   3235  OE2 GLU B 369      25.323  -8.230  39.782  1.00 76.21           O  
ATOM   3236  N   PHE B 370      24.540 -13.572  38.951  1.00 46.05           N  
ATOM   3237  CA  PHE B 370      23.936 -14.427  37.945  1.00 43.08           C  
ATOM   3238  C   PHE B 370      23.467 -15.743  38.552  1.00 42.05           C  
ATOM   3239  O   PHE B 370      22.356 -16.195  38.291  1.00 44.24           O  
ATOM   3240  CB  PHE B 370      24.915 -14.709  36.806  1.00 43.33           C  
ATOM   3241  CG  PHE B 370      24.510 -15.867  35.952  1.00 46.25           C  
ATOM   3242  CD1 PHE B 370      23.463 -15.746  35.055  1.00 46.48           C  
ATOM   3243  CD2 PHE B 370      25.154 -17.087  36.064  1.00 41.15           C  
ATOM   3244  CE1 PHE B 370      23.077 -16.814  34.276  1.00 47.46           C  
ATOM   3245  CE2 PHE B 370      24.772 -18.160  35.286  1.00 42.95           C  
ATOM   3246  CZ  PHE B 370      23.731 -18.024  34.393  1.00 42.49           C  
ATOM   3247  N   ALA B 371      24.325 -16.354  39.361  1.00 42.42           N  
ATOM   3248  CA  ALA B 371      24.051 -17.670  39.927  1.00 37.14           C  
ATOM   3249  C   ALA B 371      22.821 -17.679  40.829  1.00 44.14           C  
ATOM   3250  O   ALA B 371      21.998 -18.592  40.756  1.00 44.96           O  
ATOM   3251  CB  ALA B 371      25.265 -18.178  40.686  1.00 38.43           C  
ATOM   3252  N   VAL B 372      22.705 -16.675  41.692  1.00 43.49           N  
ATOM   3253  CA  VAL B 372      21.549 -16.574  42.572  1.00 48.75           C  
ATOM   3254  C   VAL B 372      20.262 -16.593  41.753  1.00 48.38           C  
ATOM   3255  O   VAL B 372      19.316 -17.305  42.084  1.00 53.33           O  
ATOM   3256  CB  VAL B 372      21.601 -15.301  43.439  1.00 53.58           C  
ATOM   3257  CG1 VAL B 372      20.239 -15.024  44.060  1.00 54.85           C  
ATOM   3258  CG2 VAL B 372      22.667 -15.438  44.513  1.00 52.25           C  
ATOM   3259  N   LYS B 373      20.239 -15.817  40.677  1.00 48.58           N  
ATOM   3260  CA  LYS B 373      19.075 -15.762  39.802  1.00 53.93           C  
ATOM   3261  C   LYS B 373      18.907 -17.064  39.026  1.00 53.40           C  
ATOM   3262  O   LYS B 373      17.807 -17.611  38.944  1.00 58.71           O  
ATOM   3263  CB  LYS B 373      19.190 -14.582  38.837  1.00 57.89           C  
ATOM   3264  N   PHE B 374      20.004 -17.563  38.465  1.00 44.29           N  
ATOM   3265  CA  PHE B 374      19.966 -18.790  37.677  1.00 38.91           C  
ATOM   3266  C   PHE B 374      19.491 -19.965  38.524  1.00 38.90           C  
ATOM   3267  O   PHE B 374      18.671 -20.770  38.080  1.00 38.28           O  
ATOM   3268  CB  PHE B 374      21.340 -19.083  37.067  1.00 39.50           C  
ATOM   3269  CG  PHE B 374      21.325 -20.172  36.034  1.00 37.93           C  
ATOM   3270  CD1 PHE B 374      20.780 -19.947  34.780  1.00 38.05           C  
ATOM   3271  CD2 PHE B 374      21.856 -21.420  36.313  1.00 37.91           C  
ATOM   3272  CE1 PHE B 374      20.766 -20.947  33.820  1.00 36.18           C  
ATOM   3273  CE2 PHE B 374      21.844 -22.425  35.358  1.00 36.41           C  
ATOM   3274  CZ  PHE B 374      21.297 -22.187  34.110  1.00 34.05           C  
ATOM   3275  N   ASN B 375      20.000 -20.047  39.749  1.00 39.23           N  
ATOM   3276  CA  ASN B 375      19.656 -21.132  40.661  1.00 42.07           C  
ATOM   3277  C   ASN B 375      18.192 -21.117  41.091  1.00 45.58           C  
ATOM   3278  O   ASN B 375      17.653 -22.144  41.501  1.00 46.61           O  
ATOM   3279  CB  ASN B 375      20.570 -21.113  41.890  1.00 37.36           C  
ATOM   3280  CG  ASN B 375      21.993 -21.517  41.559  1.00 39.89           C  
ATOM   3281  OD1 ASN B 375      22.265 -22.022  40.470  1.00 38.87           O  
ATOM   3282  ND2 ASN B 375      22.908 -21.300  42.497  1.00 39.59           N  
ATOM   3283  N   ALA B 376      17.553 -19.953  40.999  1.00 45.81           N  
ATOM   3284  CA  ALA B 376      16.145 -19.831  41.364  1.00 50.36           C  
ATOM   3285  C   ALA B 376      15.268 -20.620  40.398  1.00 52.36           C  
ATOM   3286  O   ALA B 376      14.118 -20.932  40.702  1.00 53.47           O  
ATOM   3287  CB  ALA B 376      15.722 -18.364  41.405  1.00 53.30           C  
ATOM   3288  N   LEU B 377      15.820 -20.937  39.231  1.00 49.02           N  
ATOM   3289  CA  LEU B 377      15.125 -21.758  38.247  1.00 46.07           C  
ATOM   3290  C   LEU B 377      15.047 -23.204  38.723  1.00 42.68           C  
ATOM   3291  O   LEU B 377      14.226 -23.982  38.242  1.00 47.03           O  
ATOM   3292  CB  LEU B 377      15.834 -21.689  36.893  1.00 46.67           C  
ATOM   3293  CG  LEU B 377      15.458 -20.546  35.946  1.00 53.70           C  
ATOM   3294  CD1 LEU B 377      15.328 -19.223  36.682  1.00 60.13           C  
ATOM   3295  CD2 LEU B 377      16.466 -20.434  34.814  1.00 53.33           C  
ATOM   3296  N   GLU B 378      15.914 -23.555  39.667  1.00 39.33           N  
ATOM   3297  CA  GLU B 378      15.913 -24.888  40.266  1.00 44.32           C  
ATOM   3298  C   GLU B 378      16.076 -26.012  39.245  1.00 44.07           C  
ATOM   3299  O   GLU B 378      15.408 -27.043  39.332  1.00 43.21           O  
ATOM   3300  CB  GLU B 378      14.636 -25.105  41.080  1.00 50.28           C  
ATOM   3301  CG  GLU B 378      14.479 -24.141  42.239  1.00 54.46           C  
ATOM   3302  CD  GLU B 378      13.286 -24.472  43.112  1.00 58.72           C  
ATOM   3303  OE1 GLU B 378      12.244 -24.890  42.566  1.00 60.42           O  
ATOM   3304  OE2 GLU B 378      13.392 -24.311  44.346  1.00 61.38           O  
ATOM   3305  N   LEU B 379      16.964 -25.811  38.280  1.00 39.08           N  
ATOM   3306  CA  LEU B 379      17.267 -26.849  37.308  1.00 36.85           C  
ATOM   3307  C   LEU B 379      18.076 -27.951  37.984  1.00 39.99           C  
ATOM   3308  O   LEU B 379      18.835 -27.683  38.914  1.00 39.75           O  
ATOM   3309  CB  LEU B 379      18.062 -26.265  36.138  1.00 38.55           C  
ATOM   3310  CG  LEU B 379      17.435 -25.082  35.396  1.00 39.20           C  
ATOM   3311  CD1 LEU B 379      18.354 -24.615  34.269  1.00 37.47           C  
ATOM   3312  CD2 LEU B 379      16.065 -25.456  34.860  1.00 35.67           C  
ATOM   3313  N   ASP B 380      17.907 -29.188  37.530  1.00 41.24           N  
ATOM   3314  CA  ASP B 380      18.760 -30.277  37.998  1.00 44.21           C  
ATOM   3315  C   ASP B 380      19.743 -30.704  36.904  1.00 40.46           C  
ATOM   3316  O   ASP B 380      19.776 -30.112  35.824  1.00 39.70           O  
ATOM   3317  CB  ASP B 380      17.931 -31.464  38.502  1.00 47.80           C  
ATOM   3318  CG  ASP B 380      17.102 -32.107  37.411  1.00 52.45           C  
ATOM   3319  OD1 ASP B 380      17.528 -32.071  36.238  1.00 52.69           O  
ATOM   3320  OD2 ASP B 380      16.024 -32.655  37.729  1.00 52.33           O  
ATOM   3321  N   ASP B 381      20.538 -31.728  37.191  1.00 38.92           N  
ATOM   3322  CA  ASP B 381      21.584 -32.172  36.275  1.00 38.07           C  
ATOM   3323  C   ASP B 381      21.045 -32.615  34.917  1.00 40.51           C  
ATOM   3324  O   ASP B 381      21.663 -32.352  33.887  1.00 38.34           O  
ATOM   3325  CB  ASP B 381      22.408 -33.294  36.909  1.00 36.87           C  
ATOM   3326  CG  ASP B 381      23.278 -32.802  38.044  1.00 41.00           C  
ATOM   3327  OD1 ASP B 381      24.041 -31.837  37.827  1.00 38.68           O  
ATOM   3328  OD2 ASP B 381      23.202 -33.379  39.150  1.00 45.47           O  
ATOM   3329  N   SER B 382      19.896 -33.284  34.914  1.00 38.92           N  
ATOM   3330  CA  SER B 382      19.307 -33.751  33.662  1.00 43.68           C  
ATOM   3331  C   SER B 382      18.861 -32.587  32.776  1.00 43.46           C  
ATOM   3332  O   SER B 382      18.937 -32.671  31.550  1.00 44.73           O  
ATOM   3333  CB  SER B 382      18.153 -34.727  33.917  1.00 45.91           C  
ATOM   3334  OG  SER B 382      17.141 -34.145  34.718  1.00 48.82           O  
ATOM   3335  N   ASP B 383      18.401 -31.505  33.401  1.00 39.14           N  
ATOM   3336  CA  ASP B 383      18.050 -30.290  32.671  1.00 36.20           C  
ATOM   3337  C   ASP B 383      19.313 -29.639  32.117  1.00 35.10           C  
ATOM   3338  O   ASP B 383      19.390 -29.312  30.933  1.00 34.35           O  
ATOM   3339  CB  ASP B 383      17.348 -29.281  33.584  1.00 33.96           C  
ATOM   3340  CG  ASP B 383      16.091 -29.836  34.226  1.00 37.05           C  
ATOM   3341  OD1 ASP B 383      15.316 -30.541  33.544  1.00 40.72           O  
ATOM   3342  OD2 ASP B 383      15.873 -29.548  35.421  1.00 38.97           O  
ATOM   3343  N   LEU B 384      20.293 -29.445  32.997  1.00 30.56           N  
ATOM   3344  CA  LEU B 384      21.550 -28.778  32.659  1.00 34.66           C  
ATOM   3345  C   LEU B 384      22.286 -29.442  31.496  1.00 35.86           C  
ATOM   3346  O   LEU B 384      22.883 -28.762  30.658  1.00 34.11           O  
ATOM   3347  CB  LEU B 384      22.462 -28.740  33.888  1.00 36.98           C  
ATOM   3348  CG  LEU B 384      22.503 -27.462  34.732  1.00 40.62           C  
ATOM   3349  CD1 LEU B 384      21.335 -26.547  34.439  1.00 42.97           C  
ATOM   3350  CD2 LEU B 384      22.592 -27.795  36.216  1.00 34.78           C  
ATOM   3351  N   ALA B 385      22.245 -30.770  31.455  1.00 35.74           N  
ATOM   3352  CA  ALA B 385      22.945 -31.527  30.422  1.00 37.21           C  
ATOM   3353  C   ALA B 385      22.493 -31.113  29.023  1.00 38.24           C  
ATOM   3354  O   ALA B 385      23.316 -30.912  28.129  1.00 36.82           O  
ATOM   3355  CB  ALA B 385      22.751 -33.022  30.631  1.00 35.04           C  
ATOM   3356  N   ILE B 386      21.184 -30.973  28.837  1.00 35.58           N  
ATOM   3357  CA  ILE B 386      20.654 -30.542  27.547  1.00 35.11           C  
ATOM   3358  C   ILE B 386      20.913 -29.055  27.304  1.00 34.73           C  
ATOM   3359  O   ILE B 386      21.264 -28.653  26.196  1.00 36.09           O  
ATOM   3360  CB  ILE B 386      19.147 -30.823  27.425  1.00 37.42           C  
ATOM   3361  CG1 ILE B 386      18.829 -32.248  27.885  1.00 33.05           C  
ATOM   3362  CG2 ILE B 386      18.683 -30.603  25.995  1.00 38.30           C  
ATOM   3363  CD1 ILE B 386      17.359 -32.595  27.803  1.00 32.43           C  
ATOM   3364  N   PHE B 387      20.744 -28.241  28.340  1.00 31.14           N  
ATOM   3365  CA  PHE B 387      20.991 -26.807  28.227  1.00 29.70           C  
ATOM   3366  C   PHE B 387      22.416 -26.515  27.757  1.00 31.12           C  
ATOM   3367  O   PHE B 387      22.633 -25.692  26.871  1.00 34.81           O  
ATOM   3368  CB  PHE B 387      20.751 -26.123  29.572  1.00 32.97           C  
ATOM   3369  CG  PHE B 387      21.007 -24.644  29.554  1.00 40.62           C  
ATOM   3370  CD1 PHE B 387      20.332 -23.821  28.669  1.00 45.38           C  
ATOM   3371  CD2 PHE B 387      21.916 -24.075  30.430  1.00 38.08           C  
ATOM   3372  CE1 PHE B 387      20.562 -22.459  28.655  1.00 46.54           C  
ATOM   3373  CE2 PHE B 387      22.149 -22.716  30.423  1.00 36.77           C  
ATOM   3374  CZ  PHE B 387      21.471 -21.907  29.536  1.00 43.99           C  
ATOM   3375  N   ILE B 388      23.383 -27.184  28.372  1.00 29.91           N  
ATOM   3376  CA  ILE B 388      24.790 -26.998  28.030  1.00 32.16           C  
ATOM   3377  C   ILE B 388      25.086 -27.426  26.596  1.00 30.70           C  
ATOM   3378  O   ILE B 388      25.867 -26.782  25.899  1.00 31.97           O  
ATOM   3379  CB  ILE B 388      25.696 -27.765  29.011  1.00 33.00           C  
ATOM   3380  CG1 ILE B 388      25.836 -26.979  30.314  1.00 36.36           C  
ATOM   3381  CG2 ILE B 388      27.053 -28.045  28.391  1.00 35.84           C  
ATOM   3382  CD1 ILE B 388      26.288 -27.827  31.481  1.00 43.74           C  
ATOM   3383  N   ALA B 389      24.455 -28.511  26.160  1.00 31.91           N  
ATOM   3384  CA  ALA B 389      24.594 -28.974  24.786  1.00 34.36           C  
ATOM   3385  C   ALA B 389      24.057 -27.921  23.818  1.00 36.46           C  
ATOM   3386  O   ALA B 389      24.651 -27.671  22.768  1.00 34.33           O  
ATOM   3387  CB  ALA B 389      23.868 -30.304  24.593  1.00 31.31           C  
ATOM   3388  N   VAL B 390      22.934 -27.306  24.181  1.00 36.01           N  
ATOM   3389  CA  VAL B 390      22.352 -26.236  23.374  1.00 34.44           C  
ATOM   3390  C   VAL B 390      23.337 -25.080  23.182  1.00 32.94           C  
ATOM   3391  O   VAL B 390      23.508 -24.571  22.074  1.00 36.19           O  
ATOM   3392  CB  VAL B 390      21.041 -25.689  23.995  1.00 32.57           C  
ATOM   3393  CG1 VAL B 390      20.625 -24.408  23.300  1.00 34.27           C  
ATOM   3394  CG2 VAL B 390      19.927 -26.723  23.907  1.00 30.04           C  
ATOM   3395  N   ILE B 391      23.982 -24.668  24.269  1.00 36.73           N  
ATOM   3396  CA  ILE B 391      24.941 -23.571  24.221  1.00 34.59           C  
ATOM   3397  C   ILE B 391      26.089 -23.884  23.265  1.00 33.39           C  
ATOM   3398  O   ILE B 391      26.515 -23.029  22.489  1.00 30.72           O  
ATOM   3399  CB  ILE B 391      25.522 -23.277  25.615  1.00 36.40           C  
ATOM   3400  CG1 ILE B 391      24.435 -22.729  26.548  1.00 37.42           C  
ATOM   3401  CG2 ILE B 391      26.684 -22.296  25.512  1.00 33.23           C  
ATOM   3402  CD1 ILE B 391      24.934 -22.402  27.943  1.00 34.20           C  
ATOM   3403  N   ILE B 392      26.583 -25.117  23.321  1.00 28.68           N  
ATOM   3404  CA  ILE B 392      27.714 -25.520  22.492  1.00 33.06           C  
ATOM   3405  C   ILE B 392      27.387 -25.426  21.005  1.00 35.08           C  
ATOM   3406  O   ILE B 392      28.188 -24.926  20.212  1.00 33.08           O  
ATOM   3407  CB  ILE B 392      28.177 -26.949  22.819  1.00 32.60           C  
ATOM   3408  CG1 ILE B 392      28.659 -27.026  24.266  1.00 36.98           C  
ATOM   3409  CG2 ILE B 392      29.289 -27.376  21.873  1.00 31.34           C  
ATOM   3410  CD1 ILE B 392      29.102 -28.414  24.695  1.00 35.28           C  
ATOM   3411  N   LEU B 393      26.203 -25.902  20.638  1.00 34.81           N  
ATOM   3412  CA  LEU B 393      25.791 -25.941  19.240  1.00 30.87           C  
ATOM   3413  C   LEU B 393      25.150 -24.625  18.802  1.00 31.51           C  
ATOM   3414  O   LEU B 393      24.047 -24.618  18.262  1.00 35.44           O  
ATOM   3415  CB  LEU B 393      24.826 -27.110  19.000  1.00 29.26           C  
ATOM   3416  CG  LEU B 393      25.458 -28.502  18.858  1.00 32.09           C  
ATOM   3417  CD1 LEU B 393      26.199 -28.634  17.531  1.00 35.85           C  
ATOM   3418  CD2 LEU B 393      26.386 -28.807  20.009  1.00 28.29           C  
ATOM   3419  N   SER B 394      25.848 -23.517  19.040  1.00 32.16           N  
ATOM   3420  CA  SER B 394      25.368 -22.195  18.638  1.00 36.18           C  
ATOM   3421  C   SER B 394      25.904 -21.808  17.259  1.00 40.17           C  
ATOM   3422  O   SER B 394      27.115 -21.691  17.056  1.00 38.03           O  
ATOM   3423  CB  SER B 394      25.768 -21.134  19.668  1.00 35.95           C  
ATOM   3424  OG  SER B 394      25.173 -21.391  20.931  1.00 37.68           O  
ATOM   3425  N   GLY B 395      24.994 -21.604  16.316  1.00 42.47           N  
ATOM   3426  CA  GLY B 395      25.375 -21.329  14.943  1.00 41.20           C  
ATOM   3427  C   GLY B 395      25.844 -19.913  14.663  1.00 40.59           C  
ATOM   3428  O   GLY B 395      26.160 -19.584  13.520  1.00 39.88           O  
ATOM   3429  N   ASP B 396      25.901 -19.072  15.693  1.00 39.25           N  
ATOM   3430  CA  ASP B 396      26.276 -17.673  15.493  1.00 39.06           C  
ATOM   3431  C   ASP B 396      27.696 -17.332  15.959  1.00 41.96           C  
ATOM   3432  O   ASP B 396      28.068 -16.160  16.019  1.00 44.75           O  
ATOM   3433  CB  ASP B 396      25.253 -16.731  16.143  1.00 45.02           C  
ATOM   3434  CG  ASP B 396      25.295 -16.774  17.659  1.00 49.35           C  
ATOM   3435  OD1 ASP B 396      25.929 -17.692  18.215  1.00 48.15           O  
ATOM   3436  OD2 ASP B 396      24.690 -15.886  18.296  1.00 54.96           O  
ATOM   3437  N   ARG B 397      28.488 -18.350  16.283  1.00 40.22           N  
ATOM   3438  CA  ARG B 397      29.888 -18.129  16.638  1.00 40.03           C  
ATOM   3439  C   ARG B 397      30.647 -17.606  15.423  1.00 43.45           C  
ATOM   3440  O   ARG B 397      30.423 -18.066  14.304  1.00 42.98           O  
ATOM   3441  CB  ARG B 397      30.540 -19.420  17.139  1.00 34.62           C  
ATOM   3442  CG  ARG B 397      29.773 -20.130  18.245  1.00 35.21           C  
ATOM   3443  CD  ARG B 397      29.531 -19.224  19.448  1.00 31.53           C  
ATOM   3444  NE  ARG B 397      29.070 -19.990  20.603  1.00 34.59           N  
ATOM   3445  CZ  ARG B 397      28.688 -19.458  21.759  1.00 35.22           C  
ATOM   3446  NH1 ARG B 397      28.703 -18.141  21.926  1.00 27.81           N  
ATOM   3447  NH2 ARG B 397      28.287 -20.246  22.749  1.00 33.35           N  
ATOM   3448  N   PRO B 398      31.555 -16.644  15.638  1.00 43.38           N  
ATOM   3449  CA  PRO B 398      32.326 -16.083  14.523  1.00 46.72           C  
ATOM   3450  C   PRO B 398      33.205 -17.140  13.858  1.00 44.32           C  
ATOM   3451  O   PRO B 398      33.775 -17.984  14.550  1.00 43.60           O  
ATOM   3452  CB  PRO B 398      33.207 -15.023  15.199  1.00 46.19           C  
ATOM   3453  CG  PRO B 398      32.543 -14.737  16.513  1.00 44.96           C  
ATOM   3454  CD  PRO B 398      31.904 -16.023  16.926  1.00 42.65           C  
ATOM   3455  N   GLY B 399      33.295 -17.097  12.532  1.00 43.01           N  
ATOM   3456  CA  GLY B 399      34.226 -17.935  11.795  1.00 42.43           C  
ATOM   3457  C   GLY B 399      33.755 -19.344  11.479  1.00 44.21           C  
ATOM   3458  O   GLY B 399      34.536 -20.161  10.993  1.00 47.35           O  
ATOM   3459  N   LEU B 400      32.490 -19.638  11.761  1.00 37.72           N  
ATOM   3460  CA  LEU B 400      31.914 -20.934  11.410  1.00 39.26           C  
ATOM   3461  C   LEU B 400      31.917 -21.128   9.895  1.00 42.72           C  
ATOM   3462  O   LEU B 400      31.613 -20.202   9.145  1.00 46.05           O  
ATOM   3463  CB  LEU B 400      30.485 -21.048  11.950  1.00 39.94           C  
ATOM   3464  CG  LEU B 400      30.226 -21.936  13.174  1.00 42.48           C  
ATOM   3465  CD1 LEU B 400      31.485 -22.202  13.984  1.00 39.55           C  
ATOM   3466  CD2 LEU B 400      29.125 -21.361  14.051  1.00 36.12           C  
ATOM   3467  N   LEU B 401      32.254 -22.335   9.451  1.00 43.76           N  
ATOM   3468  CA  LEU B 401      32.306 -22.640   8.023  1.00 43.39           C  
ATOM   3469  C   LEU B 401      30.995 -23.223   7.491  1.00 39.96           C  
ATOM   3470  O   LEU B 401      30.589 -22.936   6.366  1.00 41.24           O  
ATOM   3471  CB  LEU B 401      33.464 -23.595   7.715  1.00 48.31           C  
ATOM   3472  CG  LEU B 401      34.872 -22.997   7.602  1.00 53.62           C  
ATOM   3473  CD1 LEU B 401      34.857 -21.770   6.702  1.00 54.17           C  
ATOM   3474  CD2 LEU B 401      35.443 -22.650   8.966  1.00 56.43           C  
ATOM   3475  N   ASN B 402      30.339 -24.052   8.296  1.00 39.92           N  
ATOM   3476  CA  ASN B 402      29.092 -24.678   7.872  1.00 41.53           C  
ATOM   3477  C   ASN B 402      28.040 -24.635   8.972  1.00 42.37           C  
ATOM   3478  O   ASN B 402      27.929 -25.564   9.769  1.00 40.84           O  
ATOM   3479  CB  ASN B 402      29.335 -26.124   7.430  1.00 42.30           C  
ATOM   3480  CG  ASN B 402      28.109 -26.748   6.786  1.00 45.15           C  
ATOM   3481  OD1 ASN B 402      27.095 -26.077   6.571  1.00 40.69           O  
ATOM   3482  ND2 ASN B 402      28.196 -28.037   6.472  1.00 43.03           N  
ATOM   3483  N   VAL B 403      27.274 -23.550   9.008  1.00 39.47           N  
ATOM   3484  CA  VAL B 403      26.297 -23.322  10.069  1.00 41.50           C  
ATOM   3485  C   VAL B 403      25.139 -24.320  10.040  1.00 42.83           C  
ATOM   3486  O   VAL B 403      24.551 -24.635  11.076  1.00 42.04           O  
ATOM   3487  CB  VAL B 403      25.738 -21.882  10.006  1.00 44.35           C  
ATOM   3488  CG1 VAL B 403      24.638 -21.678  11.045  1.00 42.96           C  
ATOM   3489  CG2 VAL B 403      26.864 -20.868  10.191  1.00 44.00           C  
ATOM   3490  N   LYS B 404      24.822 -24.823   8.851  1.00 43.46           N  
ATOM   3491  CA  LYS B 404      23.649 -25.676   8.667  1.00 48.30           C  
ATOM   3492  C   LYS B 404      23.546 -26.858   9.639  1.00 48.20           C  
ATOM   3493  O   LYS B 404      22.549 -26.984  10.350  1.00 45.85           O  
ATOM   3494  CB  LYS B 404      23.548 -26.164   7.217  1.00 51.00           C  
ATOM   3495  CG  LYS B 404      22.379 -27.103   6.971  1.00 53.29           C  
ATOM   3496  CD  LYS B 404      22.071 -27.244   5.487  1.00 56.58           C  
ATOM   3497  CE  LYS B 404      21.063 -28.354   5.246  1.00 56.73           C  
ATOM   3498  NZ  LYS B 404      19.982 -28.331   6.268  1.00 55.77           N  
ATOM   3499  N   PRO B 405      24.571 -27.730   9.671  1.00 46.42           N  
ATOM   3500  CA  PRO B 405      24.499 -28.926  10.519  1.00 44.23           C  
ATOM   3501  C   PRO B 405      24.458 -28.551  11.993  1.00 41.94           C  
ATOM   3502  O   PRO B 405      23.876 -29.271  12.803  1.00 42.82           O  
ATOM   3503  CB  PRO B 405      25.812 -29.663  10.214  1.00 41.72           C  
ATOM   3504  CG  PRO B 405      26.353 -29.033   8.980  1.00 46.50           C  
ATOM   3505  CD  PRO B 405      25.870 -27.623   8.989  1.00 45.42           C  
ATOM   3506  N   ILE B 406      25.081 -27.428  12.329  1.00 38.89           N  
ATOM   3507  CA  ILE B 406      25.117 -26.949  13.706  1.00 35.77           C  
ATOM   3508  C   ILE B 406      23.730 -26.530  14.194  1.00 40.73           C  
ATOM   3509  O   ILE B 406      23.288 -26.943  15.266  1.00 40.12           O  
ATOM   3510  CB  ILE B 406      26.105 -25.779  13.852  1.00 35.25           C  
ATOM   3511  CG1 ILE B 406      27.514 -26.239  13.465  1.00 34.23           C  
ATOM   3512  CG2 ILE B 406      26.075 -25.220  15.272  1.00 33.26           C  
ATOM   3513  CD1 ILE B 406      28.532 -25.128  13.408  1.00 36.33           C  
ATOM   3514  N   GLU B 407      23.043 -25.712  13.402  1.00 42.21           N  
ATOM   3515  CA  GLU B 407      21.694 -25.280  13.747  1.00 42.40           C  
ATOM   3516  C   GLU B 407      20.728 -26.458  13.722  1.00 45.83           C  
ATOM   3517  O   GLU B 407      19.803 -26.528  14.528  1.00 43.01           O  
ATOM   3518  CB  GLU B 407      21.212 -24.188  12.793  1.00 47.20           C  
ATOM   3519  CG  GLU B 407      21.774 -22.811  13.087  1.00 53.72           C  
ATOM   3520  CD  GLU B 407      21.303 -21.767  12.092  1.00 66.05           C  
ATOM   3521  OE1 GLU B 407      20.532 -22.122  11.174  1.00 70.40           O  
ATOM   3522  OE2 GLU B 407      21.705 -20.591  12.224  1.00 68.88           O  
ATOM   3523  N   ASP B 408      20.947 -27.384  12.794  1.00 45.20           N  
ATOM   3524  CA  ASP B 408      20.109 -28.573  12.700  1.00 45.00           C  
ATOM   3525  C   ASP B 408      20.191 -29.396  13.982  1.00 45.13           C  
ATOM   3526  O   ASP B 408      19.177 -29.877  14.490  1.00 46.45           O  
ATOM   3527  CB  ASP B 408      20.506 -29.428  11.495  1.00 45.75           C  
ATOM   3528  CG  ASP B 408      19.999 -28.861  10.177  1.00 54.57           C  
ATOM   3529  OD1 ASP B 408      19.164 -27.930  10.197  1.00 56.66           O  
ATOM   3530  OD2 ASP B 408      20.436 -29.353   9.117  1.00 55.94           O  
ATOM   3531  N   ILE B 409      21.402 -29.554  14.506  1.00 40.67           N  
ATOM   3532  CA  ILE B 409      21.597 -30.286  15.752  1.00 38.77           C  
ATOM   3533  C   ILE B 409      21.009 -29.522  16.940  1.00 38.09           C  
ATOM   3534  O   ILE B 409      20.362 -30.110  17.806  1.00 44.06           O  
ATOM   3535  CB  ILE B 409      23.087 -30.587  16.006  1.00 40.12           C  
ATOM   3536  CG1 ILE B 409      23.640 -31.496  14.903  1.00 42.45           C  
ATOM   3537  CG2 ILE B 409      23.279 -31.227  17.376  1.00 29.66           C  
ATOM   3538  CD1 ILE B 409      25.137 -31.724  14.987  1.00 45.14           C  
ATOM   3539  N   GLN B 410      21.227 -28.211  16.977  1.00 33.20           N  
ATOM   3540  CA  GLN B 410      20.698 -27.397  18.067  1.00 35.25           C  
ATOM   3541  C   GLN B 410      19.171 -27.414  18.080  1.00 36.41           C  
ATOM   3542  O   GLN B 410      18.551 -27.404  19.140  1.00 37.59           O  
ATOM   3543  CB  GLN B 410      21.205 -25.956  17.987  1.00 36.47           C  
ATOM   3544  CG  GLN B 410      21.060 -25.206  19.306  1.00 37.50           C  
ATOM   3545  CD  GLN B 410      21.268 -23.712  19.173  1.00 33.44           C  
ATOM   3546  OE1 GLN B 410      21.959 -23.100  19.983  1.00 42.04           O  
ATOM   3547  NE2 GLN B 410      20.670 -23.118  18.151  1.00 32.23           N  
ATOM   3548  N   ASP B 411      18.568 -27.435  16.898  1.00 37.36           N  
ATOM   3549  CA  ASP B 411      17.118 -27.546  16.797  1.00 43.51           C  
ATOM   3550  C   ASP B 411      16.611 -28.793  17.516  1.00 41.56           C  
ATOM   3551  O   ASP B 411      15.625 -28.734  18.249  1.00 39.39           O  
ATOM   3552  CB  ASP B 411      16.674 -27.548  15.333  1.00 53.67           C  
ATOM   3553  CG  ASP B 411      16.607 -26.151  14.746  1.00 68.22           C  
ATOM   3554  OD1 ASP B 411      16.868 -25.181  15.492  1.00 67.60           O  
ATOM   3555  OD2 ASP B 411      16.291 -26.019  13.544  1.00 77.48           O  
ATOM   3556  N   ASN B 412      17.296 -29.914  17.311  1.00 42.46           N  
ATOM   3557  CA  ASN B 412      16.938 -31.169  17.966  1.00 43.56           C  
ATOM   3558  C   ASN B 412      17.182 -31.119  19.471  1.00 41.23           C  
ATOM   3559  O   ASN B 412      16.409 -31.671  20.254  1.00 42.16           O  
ATOM   3560  CB  ASN B 412      17.713 -32.336  17.349  1.00 43.87           C  
ATOM   3561  CG  ASN B 412      17.393 -32.534  15.881  1.00 59.75           C  
ATOM   3562  OD1 ASN B 412      18.245 -32.960  15.100  1.00 71.70           O  
ATOM   3563  ND2 ASN B 412      16.161 -32.219  15.495  1.00 60.97           N  
ATOM   3564  N   LEU B 413      18.267 -30.462  19.869  1.00 34.60           N  
ATOM   3565  CA  LEU B 413      18.584 -30.310  21.282  1.00 35.71           C  
ATOM   3566  C   LEU B 413      17.565 -29.410  21.974  1.00 38.95           C  
ATOM   3567  O   LEU B 413      17.173 -29.665  23.113  1.00 36.95           O  
ATOM   3568  CB  LEU B 413      19.999 -29.754  21.459  1.00 36.07           C  
ATOM   3569  CG  LEU B 413      21.130 -30.698  21.032  1.00 37.58           C  
ATOM   3570  CD1 LEU B 413      22.464 -29.967  20.950  1.00 31.27           C  
ATOM   3571  CD2 LEU B 413      21.218 -31.902  21.963  1.00 33.73           C  
ATOM   3572  N   LEU B 414      17.139 -28.360  21.279  1.00 38.03           N  
ATOM   3573  CA  LEU B 414      16.126 -27.452  21.804  1.00 38.87           C  
ATOM   3574  C   LEU B 414      14.803 -28.185  21.995  1.00 43.08           C  
ATOM   3575  O   LEU B 414      14.120 -27.995  23.002  1.00 40.05           O  
ATOM   3576  CB  LEU B 414      15.946 -26.247  20.875  1.00 40.99           C  
ATOM   3577  CG  LEU B 414      17.064 -25.200  20.933  1.00 40.42           C  
ATOM   3578  CD1 LEU B 414      16.983 -24.251  19.753  1.00 39.99           C  
ATOM   3579  CD2 LEU B 414      17.021 -24.432  22.251  1.00 39.14           C  
ATOM   3580  N   GLN B 415      14.447 -29.026  21.026  1.00 44.33           N  
ATOM   3581  CA  GLN B 415      13.253 -29.858  21.141  1.00 45.90           C  
ATOM   3582  C   GLN B 415      13.356 -30.751  22.367  1.00 45.53           C  
ATOM   3583  O   GLN B 415      12.399 -30.895  23.126  1.00 45.68           O  
ATOM   3584  CB  GLN B 415      13.064 -30.723  19.894  1.00 47.30           C  
ATOM   3585  CG  GLN B 415      12.653 -29.960  18.650  1.00 55.67           C  
ATOM   3586  CD  GLN B 415      12.370 -30.879  17.475  1.00 63.34           C  
ATOM   3587  OE1 GLN B 415      12.935 -30.712  16.392  1.00 66.66           O  
ATOM   3588  NE2 GLN B 415      11.498 -31.860  17.685  1.00 61.99           N  
ATOM   3589  N   ALA B 416      14.526 -31.351  22.552  1.00 41.32           N  
ATOM   3590  CA  ALA B 416      14.758 -32.238  23.682  1.00 39.09           C  
ATOM   3591  C   ALA B 416      14.662 -31.475  24.999  1.00 41.63           C  
ATOM   3592  O   ALA B 416      14.072 -31.958  25.965  1.00 41.84           O  
ATOM   3593  CB  ALA B 416      16.111 -32.920  23.553  1.00 37.47           C  
ATOM   3594  N   LEU B 417      15.239 -30.279  25.026  1.00 39.46           N  
ATOM   3595  CA  LEU B 417      15.212 -29.444  26.220  1.00 39.95           C  
ATOM   3596  C   LEU B 417      13.780 -29.053  26.572  1.00 41.34           C  
ATOM   3597  O   LEU B 417      13.373 -29.112  27.733  1.00 40.26           O  
ATOM   3598  CB  LEU B 417      16.061 -28.189  26.008  1.00 38.70           C  
ATOM   3599  CG  LEU B 417      16.109 -27.184  27.162  1.00 37.28           C  
ATOM   3600  CD1 LEU B 417      16.684 -27.836  28.418  1.00 30.19           C  
ATOM   3601  CD2 LEU B 417      16.916 -25.945  26.766  1.00 30.71           C  
ATOM   3602  N   GLU B 418      13.021 -28.656  25.557  1.00 44.21           N  
ATOM   3603  CA  GLU B 418      11.643 -28.229  25.749  1.00 46.56           C  
ATOM   3604  C   GLU B 418      10.812 -29.326  26.406  1.00 47.63           C  
ATOM   3605  O   GLU B 418      10.123 -29.084  27.397  1.00 49.01           O  
ATOM   3606  CB  GLU B 418      11.020 -27.814  24.414  1.00 53.18           C  
ATOM   3607  CG  GLU B 418       9.623 -27.236  24.542  1.00 58.33           C  
ATOM   3608  CD  GLU B 418       9.119 -26.631  23.247  1.00 62.87           C  
ATOM   3609  OE1 GLU B 418       9.574 -27.061  22.166  1.00 59.43           O  
ATOM   3610  OE2 GLU B 418       8.263 -25.724  23.313  1.00 68.66           O  
ATOM   3611  N   LEU B 419      10.884 -30.532  25.851  1.00 47.47           N  
ATOM   3612  CA  LEU B 419      10.152 -31.669  26.395  1.00 46.76           C  
ATOM   3613  C   LEU B 419      10.636 -31.988  27.805  1.00 47.65           C  
ATOM   3614  O   LEU B 419       9.837 -32.243  28.705  1.00 50.50           O  
ATOM   3615  CB  LEU B 419      10.306 -32.894  25.488  1.00 45.89           C  
ATOM   3616  CG  LEU B 419       9.529 -34.150  25.891  1.00 48.23           C  
ATOM   3617  CD1 LEU B 419       8.035 -33.863  25.936  1.00 51.59           C  
ATOM   3618  CD2 LEU B 419       9.822 -35.303  24.943  1.00 45.32           C  
ATOM   3619  N   GLN B 420      11.952 -31.967  27.990  1.00 47.05           N  
ATOM   3620  CA  GLN B 420      12.552 -32.237  29.292  1.00 43.98           C  
ATOM   3621  C   GLN B 420      11.960 -31.351  30.386  1.00 44.05           C  
ATOM   3622  O   GLN B 420      11.549 -31.837  31.437  1.00 45.78           O  
ATOM   3623  CB  GLN B 420      14.067 -32.034  29.223  1.00 41.77           C  
ATOM   3624  CG  GLN B 420      14.756 -31.986  30.578  1.00 43.37           C  
ATOM   3625  CD  GLN B 420      14.771 -33.328  31.287  1.00 44.35           C  
ATOM   3626  OE1 GLN B 420      14.546 -34.373  30.675  1.00 45.93           O  
ATOM   3627  NE2 GLN B 420      15.047 -33.304  32.587  1.00 41.30           N  
ATOM   3628  N   LEU B 421      11.919 -30.048  30.129  1.00 42.96           N  
ATOM   3629  CA  LEU B 421      11.435 -29.085  31.111  1.00 44.47           C  
ATOM   3630  C   LEU B 421       9.942 -29.243  31.391  1.00 46.51           C  
ATOM   3631  O   LEU B 421       9.503 -29.104  32.531  1.00 45.83           O  
ATOM   3632  CB  LEU B 421      11.746 -27.659  30.655  1.00 45.71           C  
ATOM   3633  CG  LEU B 421      13.235 -27.338  30.496  1.00 43.37           C  
ATOM   3634  CD1 LEU B 421      13.420 -25.937  29.936  1.00 38.52           C  
ATOM   3635  CD2 LEU B 421      13.973 -27.500  31.825  1.00 39.89           C  
ATOM   3636  N   LYS B 422       9.165 -29.532  30.352  1.00 44.35           N  
ATOM   3637  CA  LYS B 422       7.729 -29.735  30.513  1.00 51.18           C  
ATOM   3638  C   LYS B 422       7.425 -30.983  31.337  1.00 52.10           C  
ATOM   3639  O   LYS B 422       6.468 -31.007  32.106  1.00 56.56           O  
ATOM   3640  CB  LYS B 422       7.034 -29.805  29.150  1.00 57.73           C  
ATOM   3641  CG  LYS B 422       6.869 -28.451  28.480  1.00 64.04           C  
ATOM   3642  CD  LYS B 422       6.202 -28.568  27.116  1.00 70.58           C  
ATOM   3643  CE  LYS B 422       6.041 -27.202  26.465  1.00 71.51           C  
ATOM   3644  NZ  LYS B 422       5.576 -27.304  25.055  1.00 74.81           N  
ATOM   3645  N   LEU B 423       8.247 -32.015  31.176  1.00 50.11           N  
ATOM   3646  CA  LEU B 423       8.073 -33.255  31.923  1.00 50.79           C  
ATOM   3647  C   LEU B 423       8.639 -33.152  33.337  1.00 51.49           C  
ATOM   3648  O   LEU B 423       8.074 -33.701  34.281  1.00 53.43           O  
ATOM   3649  CB  LEU B 423       8.742 -34.419  31.190  1.00 51.26           C  
ATOM   3650  CG  LEU B 423       8.112 -34.901  29.885  1.00 50.06           C  
ATOM   3651  CD1 LEU B 423       8.949 -36.018  29.281  1.00 51.15           C  
ATOM   3652  CD2 LEU B 423       6.692 -35.371  30.129  1.00 50.68           C  
ATOM   3653  N   ASN B 424       9.757 -32.446  33.476  1.00 48.18           N  
ATOM   3654  CA  ASN B 424      10.470 -32.383  34.747  1.00 44.96           C  
ATOM   3655  C   ASN B 424      10.000 -31.240  35.644  1.00 47.06           C  
ATOM   3656  O   ASN B 424      10.170 -31.292  36.861  1.00 49.27           O  
ATOM   3657  CB  ASN B 424      11.977 -32.267  34.503  1.00 44.05           C  
ATOM   3658  CG  ASN B 424      12.801 -32.753  35.682  1.00 49.50           C  
ATOM   3659  OD1 ASN B 424      12.394 -33.662  36.407  1.00 49.40           O  
ATOM   3660  ND2 ASN B 424      13.972 -32.155  35.872  1.00 48.62           N  
ATOM   3661  N   HIS B 425       9.419 -30.210  35.038  1.00 47.04           N  
ATOM   3662  CA  HIS B 425       8.915 -29.057  35.782  1.00 48.99           C  
ATOM   3663  C   HIS B 425       7.525 -28.677  35.284  1.00 52.46           C  
ATOM   3664  O   HIS B 425       7.328 -27.580  34.761  1.00 49.53           O  
ATOM   3665  CB  HIS B 425       9.855 -27.856  35.633  1.00 46.00           C  
ATOM   3666  CG  HIS B 425      11.269 -28.132  36.042  1.00 47.20           C  
ATOM   3667  ND1 HIS B 425      11.731 -27.915  37.323  1.00 48.47           N  
ATOM   3668  CD2 HIS B 425      12.328 -28.593  35.334  1.00 44.03           C  
ATOM   3669  CE1 HIS B 425      13.010 -28.239  37.389  1.00 49.48           C  
ATOM   3670  NE2 HIS B 425      13.397 -28.653  36.195  1.00 43.81           N  
ATOM   3671  N   PRO B 426       6.553 -29.584  35.452  1.00 56.35           N  
ATOM   3672  CA  PRO B 426       5.207 -29.406  34.901  1.00 56.50           C  
ATOM   3673  C   PRO B 426       4.545 -28.111  35.356  1.00 58.22           C  
ATOM   3674  O   PRO B 426       3.726 -27.558  34.623  1.00 60.53           O  
ATOM   3675  CB  PRO B 426       4.443 -30.615  35.465  1.00 59.46           C  
ATOM   3676  CG  PRO B 426       5.260 -31.057  36.649  1.00 58.13           C  
ATOM   3677  CD  PRO B 426       6.661 -30.855  36.185  1.00 56.07           C  
ATOM   3678  N   GLU B 427       4.899 -27.630  36.543  1.00 59.26           N  
ATOM   3679  CA  GLU B 427       4.237 -26.460  37.112  1.00 64.34           C  
ATOM   3680  C   GLU B 427       4.986 -25.154  36.853  1.00 62.20           C  
ATOM   3681  O   GLU B 427       4.556 -24.091  37.297  1.00 60.44           O  
ATOM   3682  CB  GLU B 427       4.011 -26.651  38.614  1.00 70.17           C  
ATOM   3683  CG  GLU B 427       3.189 -27.880  38.962  1.00 79.68           C  
ATOM   3684  CD  GLU B 427       2.675 -27.855  40.391  1.00 89.75           C  
ATOM   3685  OE1 GLU B 427       2.905 -26.845  41.091  1.00 91.10           O  
ATOM   3686  OE2 GLU B 427       2.037 -28.844  40.811  1.00 93.60           O  
ATOM   3687  N   SER B 428       6.098 -25.235  36.130  1.00 58.02           N  
ATOM   3688  CA  SER B 428       6.899 -24.053  35.828  1.00 56.89           C  
ATOM   3689  C   SER B 428       6.602 -23.524  34.430  1.00 56.92           C  
ATOM   3690  O   SER B 428       7.281 -23.875  33.464  1.00 55.12           O  
ATOM   3691  CB  SER B 428       8.390 -24.367  35.962  1.00 61.24           C  
ATOM   3692  OG  SER B 428       8.705 -24.799  37.273  1.00 68.51           O  
ATOM   3693  N   SER B 429       5.588 -22.672  34.328  1.00 57.25           N  
ATOM   3694  CA  SER B 429       5.186 -22.115  33.043  1.00 58.06           C  
ATOM   3695  C   SER B 429       6.334 -21.380  32.352  1.00 50.37           C  
ATOM   3696  O   SER B 429       7.049 -20.593  32.976  1.00 45.00           O  
ATOM   3697  CB  SER B 429       3.991 -21.175  33.222  1.00 64.39           C  
ATOM   3698  OG  SER B 429       3.563 -20.651  31.977  1.00 65.61           O  
ATOM   3699  N   GLN B 430       6.499 -21.646  31.060  1.00 48.62           N  
ATOM   3700  CA  GLN B 430       7.499 -20.964  30.241  1.00 47.70           C  
ATOM   3701  C   GLN B 430       8.913 -21.055  30.814  1.00 47.42           C  
ATOM   3702  O   GLN B 430       9.716 -20.138  30.643  1.00 47.74           O  
ATOM   3703  CB  GLN B 430       7.112 -19.498  30.020  1.00 46.26           C  
ATOM   3704  CG  GLN B 430       5.834 -19.308  29.213  1.00 45.26           C  
ATOM   3705  CD  GLN B 430       5.899 -19.966  27.845  1.00 50.48           C  
ATOM   3706  OE1 GLN B 430       5.100 -20.846  27.528  1.00 57.55           O  
ATOM   3707  NE2 GLN B 430       6.860 -19.547  27.031  1.00 44.83           N  
ATOM   3708  N   LEU B 431       9.217 -22.161  31.486  1.00 43.22           N  
ATOM   3709  CA  LEU B 431      10.570 -22.386  31.985  1.00 40.60           C  
ATOM   3710  C   LEU B 431      11.536 -22.387  30.804  1.00 36.64           C  
ATOM   3711  O   LEU B 431      12.616 -21.804  30.868  1.00 38.13           O  
ATOM   3712  CB  LEU B 431      10.662 -23.723  32.719  1.00 40.66           C  
ATOM   3713  CG  LEU B 431      11.568 -23.785  33.955  1.00 44.43           C  
ATOM   3714  CD1 LEU B 431      12.032 -25.216  34.213  1.00 36.59           C  
ATOM   3715  CD2 LEU B 431      12.754 -22.848  33.849  1.00 41.63           C  
ATOM   3716  N   PHE B 432      11.129 -23.052  29.729  1.00 36.69           N  
ATOM   3717  CA  PHE B 432      11.906 -23.103  28.495  1.00 37.34           C  
ATOM   3718  C   PHE B 432      12.349 -21.705  28.072  1.00 40.37           C  
ATOM   3719  O   PHE B 432      13.541 -21.447  27.896  1.00 40.91           O  
ATOM   3720  CB  PHE B 432      11.077 -23.767  27.392  1.00 36.56           C  
ATOM   3721  CG  PHE B 432      11.810 -23.942  26.092  1.00 41.28           C  
ATOM   3722  CD1 PHE B 432      13.004 -24.643  26.043  1.00 36.06           C  
ATOM   3723  CD2 PHE B 432      11.291 -23.428  24.913  1.00 45.08           C  
ATOM   3724  CE1 PHE B 432      13.676 -24.813  24.846  1.00 41.04           C  
ATOM   3725  CE2 PHE B 432      11.958 -23.595  23.711  1.00 44.61           C  
ATOM   3726  CZ  PHE B 432      13.152 -24.290  23.678  1.00 42.65           C  
ATOM   3727  N   ALA B 433      11.383 -20.802  27.930  1.00 39.54           N  
ATOM   3728  CA  ALA B 433      11.666 -19.426  27.534  1.00 39.78           C  
ATOM   3729  C   ALA B 433      12.584 -18.717  28.529  1.00 39.34           C  
ATOM   3730  O   ALA B 433      13.525 -18.028  28.134  1.00 39.11           O  
ATOM   3731  CB  ALA B 433      10.368 -18.645  27.361  1.00 39.41           C  
ATOM   3732  N   LYS B 434      12.303 -18.883  29.817  1.00 38.59           N  
ATOM   3733  CA  LYS B 434      13.112 -18.260  30.863  1.00 46.06           C  
ATOM   3734  C   LYS B 434      14.573 -18.685  30.752  1.00 42.59           C  
ATOM   3735  O   LYS B 434      15.484 -17.867  30.880  1.00 43.11           O  
ATOM   3736  CB  LYS B 434      12.574 -18.618  32.251  1.00 50.45           C  
ATOM   3737  CG  LYS B 434      11.212 -18.023  32.580  1.00 58.10           C  
ATOM   3738  CD  LYS B 434      10.748 -18.468  33.962  1.00 61.65           C  
ATOM   3739  CE  LYS B 434       9.365 -17.928  34.299  1.00 68.86           C  
ATOM   3740  NZ  LYS B 434       9.385 -16.467  34.589  1.00 70.22           N  
ATOM   3741  N   LEU B 435      14.784 -19.972  30.512  1.00 43.07           N  
ATOM   3742  CA  LEU B 435      16.125 -20.523  30.385  1.00 44.17           C  
ATOM   3743  C   LEU B 435      16.861 -19.915  29.193  1.00 42.10           C  
ATOM   3744  O   LEU B 435      18.030 -19.534  29.301  1.00 41.01           O  
ATOM   3745  CB  LEU B 435      16.049 -22.043  30.252  1.00 47.26           C  
ATOM   3746  CG  LEU B 435      17.355 -22.823  30.366  1.00 52.09           C  
ATOM   3747  CD1 LEU B 435      18.210 -22.273  31.504  1.00 55.90           C  
ATOM   3748  CD2 LEU B 435      17.058 -24.302  30.566  1.00 50.72           C  
ATOM   3749  N   LEU B 436      16.169 -19.815  28.061  1.00 38.48           N  
ATOM   3750  CA  LEU B 436      16.755 -19.229  26.860  1.00 39.96           C  
ATOM   3751  C   LEU B 436      17.168 -17.786  27.108  1.00 39.38           C  
ATOM   3752  O   LEU B 436      18.181 -17.324  26.584  1.00 38.96           O  
ATOM   3753  CB  LEU B 436      15.783 -19.298  25.683  1.00 40.95           C  
ATOM   3754  CG  LEU B 436      15.415 -20.704  25.210  1.00 41.37           C  
ATOM   3755  CD1 LEU B 436      14.698 -20.628  23.884  1.00 45.47           C  
ATOM   3756  CD2 LEU B 436      16.655 -21.581  25.096  1.00 41.10           C  
ATOM   3757  N   GLN B 437      16.379 -17.081  27.913  1.00 39.00           N  
ATOM   3758  CA  GLN B 437      16.683 -15.700  28.270  1.00 42.32           C  
ATOM   3759  C   GLN B 437      17.980 -15.614  29.067  1.00 45.36           C  
ATOM   3760  O   GLN B 437      18.726 -14.644  28.947  1.00 51.59           O  
ATOM   3761  CB  GLN B 437      15.532 -15.081  29.069  1.00 44.88           C  
ATOM   3762  CG  GLN B 437      14.275 -14.818  28.247  1.00 47.68           C  
ATOM   3763  CD  GLN B 437      13.136 -14.252  29.078  1.00 55.13           C  
ATOM   3764  OE1 GLN B 437      12.376 -13.403  28.612  1.00 57.68           O  
ATOM   3765  NE2 GLN B 437      13.018 -14.717  30.316  1.00 57.64           N  
ATOM   3766  N   LYS B 438      18.244 -16.628  29.885  1.00 35.28           N  
ATOM   3767  CA  LYS B 438      19.471 -16.662  30.677  1.00 42.89           C  
ATOM   3768  C   LYS B 438      20.716 -16.797  29.802  1.00 50.17           C  
ATOM   3769  O   LYS B 438      21.767 -16.241  30.123  1.00 50.43           O  
ATOM   3770  CB  LYS B 438      19.423 -17.775  31.727  1.00 46.25           C  
ATOM   3771  CG  LYS B 438      18.996 -17.297  33.108  1.00 50.43           C  
ATOM   3772  CD  LYS B 438      17.531 -16.911  33.137  1.00 60.11           C  
ATOM   3773  CE  LYS B 438      17.252 -15.879  34.217  1.00 65.88           C  
ATOM   3774  NZ  LYS B 438      17.917 -16.209  35.504  1.00 68.52           N  
ATOM   3775  N   MET B 439      20.598 -17.539  28.703  1.00 52.45           N  
ATOM   3776  CA  MET B 439      21.697 -17.664  27.751  1.00 59.22           C  
ATOM   3777  C   MET B 439      22.177 -16.281  27.348  1.00 56.53           C  
ATOM   3778  O   MET B 439      23.372 -16.055  27.157  1.00 56.73           O  
ATOM   3779  CB  MET B 439      21.261 -18.448  26.513  1.00 61.10           C  
ATOM   3780  CG  MET B 439      21.250 -19.952  26.706  1.00 61.27           C  
ATOM   3781  SD  MET B 439      20.424 -20.834  25.366  1.00 75.72           S  
ATOM   3782  CE  MET B 439      21.360 -20.259  23.952  1.00139.59           C  
ATOM   3783  N   THR B 440      21.230 -15.356  27.234  1.00 54.74           N  
ATOM   3784  CA  THR B 440      21.540 -13.967  26.926  1.00 60.10           C  
ATOM   3785  C   THR B 440      22.370 -13.334  28.037  1.00 65.43           C  
ATOM   3786  O   THR B 440      23.309 -12.583  27.773  1.00 71.95           O  
ATOM   3787  CB  THR B 440      20.251 -13.143  26.708  1.00 64.14           C  
ATOM   3788  OG1 THR B 440      19.648 -13.521  25.464  1.00 66.53           O  
ATOM   3789  CG2 THR B 440      20.558 -11.650  26.686  1.00 62.08           C  
ATOM   3790  N   ASP B 441      22.023 -13.646  29.280  1.00 62.06           N  
ATOM   3791  CA  ASP B 441      22.734 -13.104  30.432  1.00 59.50           C  
ATOM   3792  C   ASP B 441      24.125 -13.714  30.580  1.00 57.36           C  
ATOM   3793  O   ASP B 441      25.002 -13.134  31.222  1.00 62.38           O  
ATOM   3794  CB  ASP B 441      21.925 -13.333  31.707  1.00 62.06           C  
ATOM   3795  CG  ASP B 441      20.521 -12.772  31.613  1.00 67.17           C  
ATOM   3796  OD1 ASP B 441      20.282 -11.891  30.758  1.00 69.71           O  
ATOM   3797  OD2 ASP B 441      19.659 -13.216  32.398  1.00 66.47           O  
ATOM   3798  N   LEU B 442      24.319 -14.893  29.996  1.00 48.48           N  
ATOM   3799  CA  LEU B 442      25.633 -15.525  29.981  1.00 46.81           C  
ATOM   3800  C   LEU B 442      26.553 -14.767  29.038  1.00 46.75           C  
ATOM   3801  O   LEU B 442      27.702 -14.485  29.374  1.00 47.03           O  
ATOM   3802  CB  LEU B 442      25.533 -16.986  29.539  1.00 46.12           C  
ATOM   3803  CG  LEU B 442      25.166 -18.024  30.596  1.00 50.75           C  
ATOM   3804  CD1 LEU B 442      23.971 -17.561  31.364  1.00 63.43           C  
ATOM   3805  CD2 LEU B 442      24.874 -19.355  29.937  1.00 51.22           C  
ATOM   3806  N   ARG B 443      26.034 -14.444  27.855  1.00 42.48           N  
ATOM   3807  CA  ARG B 443      26.786 -13.696  26.854  1.00 45.94           C  
ATOM   3808  C   ARG B 443      27.283 -12.378  27.433  1.00 50.04           C  
ATOM   3809  O   ARG B 443      28.416 -11.968  27.180  1.00 51.99           O  
ATOM   3810  CB  ARG B 443      25.922 -13.431  25.618  1.00 49.61           C  
ATOM   3811  CG  ARG B 443      25.452 -14.682  24.885  1.00 54.81           C  
ATOM   3812  CD  ARG B 443      26.541 -15.254  23.992  1.00 60.36           C  
ATOM   3813  NE  ARG B 443      26.061 -16.365  23.172  1.00 58.98           N  
ATOM   3814  CZ  ARG B 443      25.765 -16.267  21.879  1.00 57.35           C  
ATOM   3815  NH1 ARG B 443      25.902 -15.107  21.252  1.00 59.24           N  
ATOM   3816  NH2 ARG B 443      25.336 -17.329  21.211  1.00 52.07           N  
ATOM   3817  N   GLN B 444      26.431 -11.720  28.214  1.00 54.69           N  
ATOM   3818  CA  GLN B 444      26.787 -10.455  28.851  1.00 60.39           C  
ATOM   3819  C   GLN B 444      27.867 -10.656  29.909  1.00 59.19           C  
ATOM   3820  O   GLN B 444      28.818  -9.880  29.992  1.00 65.29           O  
ATOM   3821  CB  GLN B 444      25.553  -9.802  29.478  1.00 72.07           C  
ATOM   3822  CG  GLN B 444      25.858  -8.563  30.308  1.00 81.25           C  
ATOM   3823  CD  GLN B 444      26.379  -7.408  29.471  1.00 88.65           C  
ATOM   3824  OE1 GLN B 444      27.183  -6.601  29.938  1.00 91.21           O  
ATOM   3825  NE2 GLN B 444      25.921  -7.325  28.226  1.00 90.29           N  
ATOM   3826  N   ILE B 445      27.708 -11.698  30.719  1.00 56.46           N  
ATOM   3827  CA  ILE B 445      28.691 -12.042  31.741  1.00 56.42           C  
ATOM   3828  C   ILE B 445      30.069 -12.259  31.123  1.00 52.72           C  
ATOM   3829  O   ILE B 445      31.069 -11.726  31.603  1.00 50.57           O  
ATOM   3830  CB  ILE B 445      28.282 -13.317  32.507  1.00 60.17           C  
ATOM   3831  CG1 ILE B 445      27.189 -12.999  33.528  1.00 64.72           C  
ATOM   3832  CG2 ILE B 445      29.485 -13.935  33.203  1.00 58.82           C  
ATOM   3833  CD1 ILE B 445      27.676 -12.175  34.697  1.00 68.45           C  
ATOM   3834  N   VAL B 446      30.113 -13.042  30.053  1.00 48.94           N  
ATOM   3835  CA  VAL B 446      31.371 -13.346  29.384  1.00 48.83           C  
ATOM   3836  C   VAL B 446      31.995 -12.092  28.787  1.00 51.16           C  
ATOM   3837  O   VAL B 446      33.174 -11.811  29.007  1.00 50.69           O  
ATOM   3838  CB  VAL B 446      31.179 -14.400  28.285  1.00 44.19           C  
ATOM   3839  CG1 VAL B 446      32.441 -14.534  27.451  1.00 45.02           C  
ATOM   3840  CG2 VAL B 446      30.793 -15.729  28.906  1.00 42.78           C  
ATOM   3841  N   THR B 447      31.197 -11.337  28.036  1.00 52.01           N  
ATOM   3842  CA  THR B 447      31.667 -10.097  27.433  1.00 54.88           C  
ATOM   3843  C   THR B 447      32.241  -9.165  28.496  1.00 59.27           C  
ATOM   3844  O   THR B 447      33.239  -8.482  28.267  1.00 62.36           O  
ATOM   3845  CB  THR B 447      30.535  -9.369  26.680  1.00 59.30           C  
ATOM   3846  OG1 THR B 447      29.956 -10.250  25.710  1.00 59.07           O  
ATOM   3847  CG2 THR B 447      31.074  -8.136  25.975  1.00 61.24           C  
ATOM   3848  N   GLU B 448      31.605  -9.147  29.663  1.00 61.88           N  
ATOM   3849  CA  GLU B 448      32.047  -8.299  30.764  1.00 69.01           C  
ATOM   3850  C   GLU B 448      33.313  -8.849  31.416  1.00 67.71           C  
ATOM   3851  O   GLU B 448      34.187  -8.090  31.830  1.00 69.58           O  
ATOM   3852  CB  GLU B 448      30.938  -8.153  31.808  1.00 75.89           C  
ATOM   3853  CG  GLU B 448      31.341  -7.343  33.028  1.00 86.99           C  
ATOM   3854  CD  GLU B 448      30.196  -7.138  34.003  1.00 95.49           C  
ATOM   3855  OE1 GLU B 448      29.214  -7.910  33.945  1.00 97.60           O  
ATOM   3856  OE2 GLU B 448      30.279  -6.204  34.830  1.00 98.35           O  
ATOM   3857  N   HIS B 449      33.405 -10.172  31.505  1.00 63.43           N  
ATOM   3858  CA  HIS B 449      34.564 -10.813  32.116  1.00 63.74           C  
ATOM   3859  C   HIS B 449      35.820 -10.581  31.281  1.00 63.83           C  
ATOM   3860  O   HIS B 449      36.897 -10.331  31.819  1.00 65.10           O  
ATOM   3861  CB  HIS B 449      34.316 -12.312  32.299  1.00 62.36           C  
ATOM   3862  CG  HIS B 449      35.408 -13.018  33.041  1.00 64.08           C  
ATOM   3863  ND1 HIS B 449      35.522 -12.976  34.414  1.00 66.08           N  
ATOM   3864  CD2 HIS B 449      36.435 -13.782  32.601  1.00 66.24           C  
ATOM   3865  CE1 HIS B 449      36.572 -13.685  34.788  1.00 67.92           C  
ATOM   3866  NE2 HIS B 449      37.144 -14.185  33.707  1.00 68.28           N  
ATOM   3867  N   VAL B 450      35.672 -10.665  29.963  1.00 64.82           N  
ATOM   3868  CA  VAL B 450      36.786 -10.448  29.049  1.00 68.36           C  
ATOM   3869  C   VAL B 450      37.402  -9.066  29.240  1.00 73.02           C  
ATOM   3870  O   VAL B 450      38.624  -8.922  29.288  1.00 73.05           O  
ATOM   3871  CB  VAL B 450      36.344 -10.610  27.585  1.00 68.92           C  
ATOM   3872  CG1 VAL B 450      37.369  -9.992  26.647  1.00 71.02           C  
ATOM   3873  CG2 VAL B 450      36.119 -12.080  27.260  1.00 66.13           C  
ATOM   3874  N   GLN B 451      36.549  -8.053  29.351  1.00 76.70           N  
ATOM   3875  CA  GLN B 451      37.009  -6.683  29.542  1.00 83.32           C  
ATOM   3876  C   GLN B 451      37.785  -6.538  30.848  1.00 89.82           C  
ATOM   3877  O   GLN B 451      38.613  -5.639  30.992  1.00 94.10           O  
ATOM   3878  CB  GLN B 451      35.827  -5.712  29.522  1.00 84.57           C  
ATOM   3879  N   LEU B 452      37.511  -7.428  31.796  1.00 89.71           N  
ATOM   3880  CA  LEU B 452      38.193  -7.410  33.084  1.00 89.64           C  
ATOM   3881  C   LEU B 452      39.617  -7.938  32.945  1.00 87.20           C  
ATOM   3882  O   LEU B 452      40.542  -7.430  33.580  1.00 87.61           O  
ATOM   3883  CB  LEU B 452      37.411  -8.233  34.112  1.00 91.23           C  
ATOM   3884  CG  LEU B 452      37.808  -8.106  35.585  1.00 95.60           C  
ATOM   3885  CD1 LEU B 452      36.628  -8.442  36.486  1.00 95.46           C  
ATOM   3886  CD2 LEU B 452      39.009  -8.984  35.914  1.00 97.54           C  
ATOM   3887  N   LEU B 453      39.787  -8.958  32.111  1.00 86.36           N  
ATOM   3888  CA  LEU B 453      41.106  -9.523  31.852  1.00 88.58           C  
ATOM   3889  C   LEU B 453      41.991  -8.510  31.133  1.00 97.36           C  
ATOM   3890  O   LEU B 453      41.814  -8.251  29.942  1.00 98.96           O  
ATOM   3891  CB  LEU B 453      40.990 -10.803  31.025  1.00 81.28           C  
ATOM   3892  CG  LEU B 453      40.167 -11.936  31.640  1.00 75.90           C  
ATOM   3893  CD1 LEU B 453      40.167 -13.150  30.725  1.00 71.53           C  
ATOM   3894  CD2 LEU B 453      40.698 -12.301  33.015  1.00 77.34           C  
ATOM   3895  N   GLN B 454      42.944  -7.942  31.865  1.00101.23           N  
ATOM   3896  CA  GLN B 454      43.810  -6.904  31.323  1.00103.75           C  
ATOM   3897  C   GLN B 454      44.988  -6.644  32.257  1.00109.19           C  
ATOM   3898  O   GLN B 454      44.967  -7.040  33.422  1.00110.12           O  
ATOM   3899  CB  GLN B 454      43.015  -5.615  31.118  1.00101.39           C  
ATOM   3900  CG  GLN B 454      42.404  -5.070  32.398  1.00100.79           C  
ATOM   3901  CD  GLN B 454      41.357  -4.007  32.140  1.00101.78           C  
ATOM   3902  OE1 GLN B 454      40.801  -3.429  33.073  1.00101.63           O  
ATOM   3903  NE2 GLN B 454      41.080  -3.745  30.868  1.00102.85           N  
ATOM   3904  N   VAL B 455      46.013  -5.975  31.741  1.00112.54           N  
ATOM   3905  CA  VAL B 455      47.194  -5.658  32.536  1.00115.14           C  
ATOM   3906  C   VAL B 455      47.456  -4.156  32.559  1.00116.03           C  
ATOM   3907  O   VAL B 455      46.969  -3.445  33.438  1.00115.99           O  
ATOM   3908  CB  VAL B 455      48.443  -6.380  32.002  1.00116.66           C  
ATOM   3909  CG1 VAL B 455      49.619  -6.169  32.943  1.00119.00           C  
ATOM   3910  CG2 VAL B 455      48.158  -7.862  31.814  1.00115.24           C  
ATOM   3911  N   LEU B 465      53.362 -16.211  35.827  1.00 96.37           N  
ATOM   3912  CA  LEU B 465      54.039 -14.950  35.558  1.00 99.02           C  
ATOM   3913  C   LEU B 465      55.172 -15.150  34.555  1.00101.20           C  
ATOM   3914  O   LEU B 465      55.584 -14.209  33.877  1.00104.46           O  
ATOM   3915  CB  LEU B 465      54.578 -14.347  36.857  1.00101.77           C  
ATOM   3916  CG  LEU B 465      54.993 -12.875  36.819  1.00104.77           C  
ATOM   3917  CD1 LEU B 465      53.795 -11.989  36.515  1.00104.41           C  
ATOM   3918  CD2 LEU B 465      55.647 -12.469  38.132  1.00104.95           C  
ATOM   3919  N   HIS B 466      55.673 -16.379  34.465  1.00 98.02           N  
ATOM   3920  CA  HIS B 466      56.734 -16.698  33.516  1.00 96.95           C  
ATOM   3921  C   HIS B 466      56.156 -17.316  32.242  1.00 88.58           C  
ATOM   3922  O   HIS B 466      55.115 -17.972  32.284  1.00 85.14           O  
ATOM   3923  CB  HIS B 466      57.790 -17.612  34.151  1.00103.07           C  
ATOM   3924  CG  HIS B 466      57.356 -19.037  34.296  1.00106.48           C  
ATOM   3925  ND1 HIS B 466      57.472 -19.958  33.277  1.00107.93           N  
ATOM   3926  CD2 HIS B 466      56.823 -19.704  35.347  1.00107.46           C  
ATOM   3927  CE1 HIS B 466      57.020 -21.128  33.690  1.00107.74           C  
ATOM   3928  NE2 HIS B 466      56.621 -21.002  34.943  1.00107.54           N  
ATOM   3929  N   PRO B 467      56.840 -17.105  31.107  1.00 83.58           N  
ATOM   3930  CA  PRO B 467      56.367 -17.448  29.760  1.00 76.00           C  
ATOM   3931  C   PRO B 467      55.631 -18.783  29.653  1.00 67.32           C  
ATOM   3932  O   PRO B 467      54.572 -18.843  29.030  1.00 65.66           O  
ATOM   3933  CB  PRO B 467      57.662 -17.503  28.949  1.00 77.97           C  
ATOM   3934  CG  PRO B 467      58.547 -16.518  29.613  1.00 83.59           C  
ATOM   3935  CD  PRO B 467      58.209 -16.557  31.082  1.00 84.88           C  
ATOM   3936  N   LEU B 468      56.182 -19.835  30.248  1.00 65.31           N  
ATOM   3937  CA  LEU B 468      55.650 -21.178  30.037  1.00 68.46           C  
ATOM   3938  C   LEU B 468      54.217 -21.354  30.548  1.00 70.34           C  
ATOM   3939  O   LEU B 468      53.325 -21.724  29.786  1.00 69.16           O  
ATOM   3940  CB  LEU B 468      56.585 -22.229  30.638  1.00 73.96           C  
ATOM   3941  CG  LEU B 468      56.641 -23.555  29.876  1.00 75.79           C  
ATOM   3942  CD1 LEU B 468      57.983 -24.243  30.078  1.00 73.80           C  
ATOM   3943  CD2 LEU B 468      55.488 -24.465  30.279  1.00 77.47           C  
ATOM   3944  N   LEU B 469      53.988 -21.092  31.831  1.00 71.38           N  
ATOM   3945  CA  LEU B 469      52.633 -21.199  32.365  1.00 71.26           C  
ATOM   3946  C   LEU B 469      51.739 -20.100  31.793  1.00 65.23           C  
ATOM   3947  O   LEU B 469      50.515 -20.236  31.756  1.00 64.02           O  
ATOM   3948  CB  LEU B 469      52.625 -21.198  33.898  1.00 75.40           C  
ATOM   3949  CG  LEU B 469      53.258 -20.036  34.663  1.00 80.04           C  
ATOM   3950  CD1 LEU B 469      52.391 -18.792  34.565  1.00 82.04           C  
ATOM   3951  CD2 LEU B 469      53.466 -20.426  36.119  1.00 81.00           C  
ATOM   3952  N   GLN B 470      52.360 -19.016  31.339  1.00 64.42           N  
ATOM   3953  CA  GLN B 470      51.635 -17.964  30.638  1.00 68.85           C  
ATOM   3954  C   GLN B 470      51.043 -18.520  29.347  1.00 65.00           C  
ATOM   3955  O   GLN B 470      49.965 -18.108  28.917  1.00 64.32           O  
ATOM   3956  CB  GLN B 470      52.555 -16.780  30.334  1.00 77.83           C  
ATOM   3957  CG  GLN B 470      51.876 -15.648  29.579  1.00 85.79           C  
ATOM   3958  CD  GLN B 470      52.827 -14.516  29.238  1.00 95.93           C  
ATOM   3959  OE1 GLN B 470      54.047 -14.666  29.320  1.00 99.22           O  
ATOM   3960  NE2 GLN B 470      52.271 -13.373  28.851  1.00 97.52           N  
ATOM   3961  N   GLU B 471      51.756 -19.461  28.733  1.00 60.26           N  
ATOM   3962  CA  GLU B 471      51.257 -20.146  27.546  1.00 56.39           C  
ATOM   3963  C   GLU B 471      50.070 -21.033  27.901  1.00 52.39           C  
ATOM   3964  O   GLU B 471      49.054 -21.037  27.206  1.00 53.64           O  
ATOM   3965  CB  GLU B 471      52.364 -20.976  26.889  1.00 58.72           C  
ATOM   3966  CG  GLU B 471      53.277 -20.171  25.982  1.00 60.22           C  
ATOM   3967  CD  GLU B 471      52.521 -19.506  24.847  1.00 63.65           C  
ATOM   3968  OE1 GLU B 471      51.616 -20.151  24.275  1.00 56.99           O  
ATOM   3969  OE2 GLU B 471      52.832 -18.341  24.523  1.00 72.54           O  
ATOM   3970  N   ILE B 472      50.204 -21.782  28.991  1.00 51.92           N  
ATOM   3971  CA  ILE B 472      49.143 -22.674  29.441  1.00 53.10           C  
ATOM   3972  C   ILE B 472      47.816 -21.939  29.617  1.00 56.77           C  
ATOM   3973  O   ILE B 472      46.755 -22.477  29.301  1.00 60.13           O  
ATOM   3974  CB  ILE B 472      49.524 -23.381  30.755  1.00 55.34           C  
ATOM   3975  CG1 ILE B 472      50.720 -24.310  30.531  1.00 51.49           C  
ATOM   3976  CG2 ILE B 472      48.343 -24.162  31.298  1.00 57.81           C  
ATOM   3977  CD1 ILE B 472      51.197 -25.010  31.787  1.00 49.99           C  
ATOM   3978  N   TYR B 473      47.879 -20.706  30.112  1.00 62.79           N  
ATOM   3979  CA  TYR B 473      46.673 -19.910  30.331  1.00 65.52           C  
ATOM   3980  C   TYR B 473      46.571 -18.749  29.347  1.00 69.85           C  
ATOM   3981  O   TYR B 473      46.160 -17.647  29.715  1.00 71.46           O  
ATOM   3982  CB  TYR B 473      46.625 -19.385  31.769  1.00 61.91           C  
ATOM   3983  CG  TYR B 473      46.776 -20.466  32.815  1.00 62.78           C  
ATOM   3984  CD1 TYR B 473      45.897 -21.538  32.861  1.00 61.91           C  
ATOM   3985  CD2 TYR B 473      47.793 -20.412  33.760  1.00 66.30           C  
ATOM   3986  CE1 TYR B 473      46.029 -22.531  33.812  1.00 63.97           C  
ATOM   3987  CE2 TYR B 473      47.931 -21.400  34.718  1.00 67.02           C  
ATOM   3988  CZ  TYR B 473      47.046 -22.457  34.737  1.00 65.94           C  
ATOM   3989  OH  TYR B 473      47.173 -23.446  35.683  1.00 68.60           O  
ATOM   3990  N   LYS B 474      46.945 -19.002  28.097  1.00 68.75           N  
ATOM   3991  CA  LYS B 474      46.904 -17.978  27.058  1.00 70.31           C  
ATOM   3992  C   LYS B 474      45.509 -17.372  26.918  1.00 71.48           C  
ATOM   3993  O   LYS B 474      44.508 -18.004  27.259  1.00 72.28           O  
ATOM   3994  CB  LYS B 474      47.360 -18.556  25.717  1.00 69.75           C  
TER    3995      LYS B 474                                                      
HETATM 3996  C1  KNA A 501      12.461   3.522  13.740  1.00 69.61           C  
HETATM 3997  O1  KNA A 501      12.201   3.864  12.575  1.00 74.89           O  
HETATM 3998  C2  KNA A 501      13.177   4.551  14.576  1.00 66.73           C  
HETATM 3999  O2  KNA A 501      12.204   2.421  14.263  1.00 64.75           O  
HETATM 4000  C3  KNA A 501      14.334   5.097  13.792  1.00 71.92           C  
HETATM 4001  C4  KNA A 501      15.622   5.218  14.587  1.00 75.45           C  
HETATM 4002  C5  KNA A 501      16.489   6.343  14.027  1.00 78.38           C  
HETATM 4003  C6  KNA A 501      17.416   5.863  12.908  1.00 80.31           C  
HETATM 4004  C7  KNA A 501      16.778   6.013  11.531  1.00 77.79           C  
HETATM 4005  C8  KNA A 501      17.615   6.918  10.657  1.00 76.11           C  
HETATM 4006  C9  KNA A 501      18.788   6.141  10.135  1.00 76.14           C  
HETATM 4007  C1  KNA A 502      19.290   7.496  19.759  1.00 74.68           C  
HETATM 4008  O1  KNA A 502      20.115   7.107  20.514  1.00 77.00           O  
HETATM 4009  C2  KNA A 502      19.606   8.670  18.834  1.00 70.96           C  
HETATM 4010  O2  KNA A 502      17.968   7.055  19.900  1.00 75.25           O  
HETATM 4011  C3  KNA A 502      20.826   8.556  17.923  1.00 65.24           C  
HETATM 4012  C4  KNA A 502      20.616   8.010  16.511  1.00 61.21           C  
HETATM 4013  C5  KNA A 502      21.865   7.711  15.685  1.00 59.15           C  
HETATM 4014  C6  KNA A 502      21.752   7.756  14.163  1.00 58.14           C  
HETATM 4015  C7  KNA A 502      23.051   7.864  13.366  1.00 54.77           C  
HETATM 4016  C8  KNA A 502      22.947   8.139  11.868  1.00 52.22           C  
HETATM 4017  C9  KNA A 502      24.172   8.724  11.168  1.00 48.53           C  
HETATM 4018  C1  KNA A 503      13.562   6.239   9.636  1.00 74.73           C  
HETATM 4019  O1  KNA A 503      12.408   6.067   9.852  1.00 81.08           O  
HETATM 4020  C2  KNA A 503      14.072   7.639   9.303  1.00 69.26           C  
HETATM 4021  O2  KNA A 503      14.475   5.197   9.846  1.00 72.44           O  
HETATM 4022  C3  KNA A 503      13.119   8.816   9.493  1.00 60.85           C  
HETATM 4023  C4  KNA A 503      13.663  10.192   9.122  1.00 63.42           C  
HETATM 4024  C5  KNA A 503      15.162  10.403   9.330  1.00 66.47           C  
HETATM 4025  C6  KNA A 503      15.865  11.438   8.456  1.00 66.87           C  
HETATM 4026  C7  KNA A 503      17.346  11.213   8.162  1.00 64.17           C  
HETATM 4027  C8  KNA A 503      18.167  12.414   7.696  1.00 66.45           C  
HETATM 4028  C9  KNA A 503      17.646  13.220   6.508  1.00 65.18           C  
HETATM 4029  C1  GOL A 504       6.825   2.366  13.119  1.00 71.37           C  
HETATM 4030  O1  GOL A 504       6.659   3.548  12.384  1.00 69.91           O  
HETATM 4031  C2  GOL A 504       8.038   1.540  12.700  1.00 69.03           C  
HETATM 4032  O2  GOL A 504       9.070   2.365  12.308  1.00 68.88           O  
HETATM 4033  C3  GOL A 504       7.704   0.577  11.574  1.00 64.09           C  
HETATM 4034  O3  GOL A 504       8.349  -0.651  11.696  1.00 53.26           O  
HETATM 4035  C1  KNA B 501      33.877 -24.771  36.957  0.80 64.26           C  
HETATM 4036  O1  KNA B 501      32.802 -24.809  36.320  0.80 62.86           O  
HETATM 4037  C2  KNA B 501      35.026 -23.976  36.334  0.80 60.52           C  
HETATM 4038  O2  KNA B 501      34.099 -25.323  38.057  0.80 69.61           O  
HETATM 4039  C3  KNA B 501      35.648 -23.020  37.354  0.80 60.15           C  
HETATM 4040  C4  KNA B 501      36.213 -21.776  36.665  0.80 63.45           C  
HETATM 4041  C5  KNA B 501      36.086 -20.545  37.566  0.80 67.23           C  
HETATM 4042  C6  KNA B 501      35.346 -19.415  36.848  0.80 71.24           C  
HETATM 4043  C7  KNA B 501      36.168 -18.125  36.862  0.80 76.57           C  
HETATM 4044  C8  KNA B 501      35.434 -16.998  36.132  0.80 78.92           C  
HETATM 4045  C9  KNA B 501      35.865 -15.629  36.662  0.80 80.76           C  
HETATM 4046  O16 TCE B 502      44.407 -20.297  46.524  1.00 85.43           O  
HETATM 4047  C14 TCE B 502      43.302 -20.730  46.389  0.84 85.06           C  
HETATM 4048  O15 TCE B 502      42.689 -21.422  47.448  0.86 86.54           O  
HETATM 4049  C5  TCE B 502      42.666 -20.788  44.986  0.74 82.24           C  
HETATM 4050  C2  TCE B 502      41.151 -21.050  45.110  1.00 80.99           C  
HETATM 4051  P   TCE B 502      40.580 -22.103  43.661  0.51 87.68           P  
HETATM 4052  C3  TCE B 502      39.042 -21.345  42.917  1.00 94.29           C  
HETATM 4053  C6  TCE B 502      39.100 -19.824  43.060  1.00 95.22           C  
HETATM 4054  C8  TCE B 502      38.218 -19.175  41.984  1.00 94.79           C  
HETATM 4055  O10 TCE B 502      37.080 -19.500  41.868  1.00 94.61           O  
HETATM 4056  O9  TCE B 502      38.784 -18.271  41.077  1.00 93.21           O  
HETATM 4057  C1  TCE B 502      40.198 -23.855  44.259  1.00102.86           C  
HETATM 4058  C4  TCE B 502      40.021 -24.798  43.036  1.00 71.40           C  
HETATM 4059  C11 TCE B 502      38.612 -24.601  42.429  0.90 69.48           C  
HETATM 4060  O12 TCE B 502      37.922 -25.545  42.193  1.00 67.57           O  
HETATM 4061  O13 TCE B 502      38.178 -23.305  42.080  0.92 71.32           O  
HETATM 4062  C1  GOL B 503      41.420 -27.430   7.963  1.00 59.97           C  
HETATM 4063  O1  GOL B 503      42.173 -26.255   8.170  1.00 52.85           O  
HETATM 4064  C2  GOL B 503      41.671 -28.412   9.103  1.00 66.06           C  
HETATM 4065  O2  GOL B 503      42.702 -27.931   9.941  1.00 65.30           O  
HETATM 4066  C3  GOL B 503      42.050 -29.779   8.542  1.00 64.39           C  
HETATM 4067  O3  GOL B 503      40.896 -30.436   8.061  1.00 66.74           O  
HETATM 4068  C1  GOL B 504      30.230 -28.057  37.652  1.00 70.58           C  
HETATM 4069  O1  GOL B 504      28.984 -28.535  38.123  1.00 62.92           O  
HETATM 4070  C2  GOL B 504      31.444 -28.810  38.193  1.00 75.96           C  
HETATM 4071  O2  GOL B 504      32.481 -27.887  38.171  1.00 77.70           O  
HETATM 4072  C3  GOL B 504      31.830 -30.001  37.326  1.00 78.89           C  
HETATM 4073  O3  GOL B 504      32.848 -30.782  37.913  1.00 79.31           O  
HETATM 4074  O   HOH A 601      -1.955  -1.576  30.148  1.00 37.60           O  
HETATM 4075  O   HOH A 602      11.968 -11.129  10.692  1.00 40.14           O  
HETATM 4076  O   HOH A 603      11.389  -6.238  12.309  1.00 30.90           O  
HETATM 4077  O   HOH A 604      11.920  -8.279  10.591  1.00 37.77           O  
HETATM 4078  O   HOH A 605      -1.384 -16.366  20.530  1.00 37.33           O  
HETATM 4079  O   HOH A 606      16.589   2.195  25.810  1.00 39.32           O  
HETATM 4080  O   HOH A 607      11.401   0.961  38.714  1.00 47.24           O  
HETATM 4081  O   HOH A 608      18.153  -4.986  30.821  1.00 44.00           O  
HETATM 4082  O   HOH A 609      11.772 -10.520   6.612  1.00 38.65           O  
HETATM 4083  O   HOH A 610      24.383   0.408   0.099  1.00 45.57           O  
HETATM 4084  O   HOH A 611      -0.258   1.086  11.205  1.00 36.59           O  
HETATM 4085  O   HOH A 612      -0.535 -10.922  16.968  1.00 35.27           O  
HETATM 4086  O   HOH A 613      -8.434   0.695  20.122  1.00 46.61           O  
HETATM 4087  O   HOH A 614       6.081  -3.826  38.820  1.00 44.94           O  
HETATM 4088  O   HOH A 615       0.819  -8.733  36.735  1.00 49.27           O  
HETATM 4089  O   HOH A 616       4.044  -2.784  40.183  1.00 43.80           O  
HETATM 4090  O   HOH A 617       3.905  -6.239   2.217  1.00 45.92           O  
HETATM 4091  O   HOH A 618     -10.175  -3.851  16.027  1.00 54.77           O  
HETATM 4092  O   HOH A 619      25.986   5.253  10.396  1.00 49.09           O  
HETATM 4093  O   HOH A 620       8.163 -21.732  17.199  1.00 41.76           O  
HETATM 4094  O   HOH A 621       1.383   6.292  17.831  1.00 44.30           O  
HETATM 4095  O   HOH A 622       0.416  -5.257   9.074  1.00 40.13           O  
HETATM 4096  O   HOH A 623      -4.339  -3.024  31.349  1.00 51.45           O  
HETATM 4097  O   HOH A 624      10.729 -18.474   9.662  1.00 52.84           O  
HETATM 4098  O   HOH A 625      18.157  -2.620  13.489  1.00 50.09           O  
HETATM 4099  O   HOH A 626       4.749  -8.161   3.801  1.00 45.27           O  
HETATM 4100  O   HOH A 627      -0.473  -5.541  36.268  1.00 45.70           O  
HETATM 4101  O   HOH A 628      11.642   5.260  37.552  1.00 53.41           O  
HETATM 4102  O   HOH A 629      26.945   3.019   9.334  1.00 48.22           O  
HETATM 4103  O   HOH A 630      27.793  20.793  25.462  1.00 61.80           O  
HETATM 4104  O   HOH A 631       7.109 -22.114  14.332  1.00 53.30           O  
HETATM 4105  O   HOH A 632       9.630  -8.407  43.271  1.00 60.11           O  
HETATM 4106  O   HOH A 633       8.814   1.028  -4.625  1.00 55.93           O  
HETATM 4107  O   HOH A 634       8.197 -15.176  38.252  1.00 56.17           O  
HETATM 4108  O   HOH A 635       7.630 -24.324  25.573  1.00 61.05           O  
HETATM 4109  O   HOH A 636      -7.261   3.086  20.986  1.00 45.47           O  
HETATM 4110  O   HOH A 637       8.188  -3.234  12.577  1.00 36.94           O  
HETATM 4111  O   HOH A 638       5.685  -8.271   6.295  1.00 44.28           O  
HETATM 4112  O   HOH A 639       3.667  -8.045   8.108  1.00 39.33           O  
HETATM 4113  O   HOH A 640      17.633 -11.010   5.465  1.00 62.56           O  
HETATM 4114  O   HOH A 641      11.802  -3.108  29.366  1.00 39.41           O  
HETATM 4115  O   HOH A 642      11.152 -22.913  20.010  1.00 51.93           O  
HETATM 4116  O   HOH A 643      25.259   4.383  -1.906  1.00 58.95           O  
HETATM 4117  O   HOH A 644      15.116  -6.254  37.773  1.00 55.91           O  
HETATM 4118  O   HOH A 645      18.299  -7.773   2.078  1.00 56.42           O  
HETATM 4119  O   HOH A 646      15.938 -12.193  36.002  1.00 61.57           O  
HETATM 4120  O   HOH A 647       6.764 -10.897   6.620  1.00 43.98           O  
HETATM 4121  O   HOH A 648       1.845  -4.413  40.758  1.00 66.48           O  
HETATM 4122  O   HOH A 649       3.346   5.185   6.612  1.00 53.36           O  
HETATM 4123  O   HOH A 650      -9.142  -9.863  21.318  1.00 61.82           O  
HETATM 4124  O   HOH A 651      -2.430 -12.483  15.484  1.00 58.87           O  
HETATM 4125  O   HOH A 652      16.359  -7.988   4.484  1.00 51.09           O  
HETATM 4126  O   HOH A 653      24.539   1.223  -2.539  1.00 66.64           O  
HETATM 4127  O   HOH A 654      24.648  -7.585   4.744  1.00 62.02           O  
HETATM 4128  O   HOH A 655       1.423   8.041  15.338  1.00 61.12           O  
HETATM 4129  O   HOH A 656       1.788 -21.401  24.277  1.00 54.21           O  
HETATM 4130  O   HOH A 657       8.885 -11.693   4.961  1.00 70.71           O  
HETATM 4131  O   HOH A 658      -7.268  -4.750  13.659  1.00 59.05           O  
HETATM 4132  O   HOH A 659      -7.298   3.302  23.581  1.00 44.43           O  
HETATM 4133  O   HOH A 660       0.516 -22.465  26.550  1.00 73.57           O  
HETATM 4134  O   HOH A 661      12.497  -8.587   4.892  1.00 66.85           O  
HETATM 4135  O   HOH A 662       3.964   8.821  15.005  1.00 55.46           O  
HETATM 4136  O   HOH A 663      25.226  -0.502  17.688  1.00 61.89           O  
HETATM 4137  O   HOH A 664       0.741  -9.551  10.012  1.00 35.22           O  
HETATM 4138  O   HOH A 665      13.162   3.884  -5.931  1.00 41.60           O  
HETATM 4139  O   HOH A 666       7.202   5.609  -0.556  1.00 44.00           O  
HETATM 4140  O   HOH A 667      -1.243 -14.028  12.188  1.00 57.00           O  
HETATM 4141  O   HOH A 668       4.433   6.541   3.129  1.00 64.70           O  
HETATM 4142  O   HOH A 669      27.638  18.192  25.017  1.00 70.65           O  
HETATM 4143  O   HOH A 670       3.864   9.144   3.637  1.00 67.84           O  
HETATM 4144  O   HOH A 671       4.675   5.457   0.819  1.00 62.09           O  
HETATM 4145  O   HOH A 672       2.711   8.426  18.813  1.00 66.77           O  
HETATM 4146  O   HOH A 673      19.332 -20.860  15.731  1.00 64.31           O  
HETATM 4147  O   HOH A 674       6.659   8.058  -1.909  1.00 61.45           O  
HETATM 4148  O   HOH A 675      -6.191  -8.013  15.301  1.00 57.15           O  
HETATM 4149  O   HOH A 676       1.143  -9.238   6.949  1.00 58.42           O  
HETATM 4150  O   HOH A 677       1.088   2.989  -5.170  1.00 50.53           O  
HETATM 4151  O   HOH A 678      15.256   2.179  -6.700  1.00 40.95           O  
HETATM 4152  O   HOH A 679      19.172  -2.865  26.916  1.00 59.76           O  
HETATM 4153  O   HOH A 680      15.479 -12.012   4.320  1.00 64.16           O  
HETATM 4154  O   HOH A 681      14.058  -6.329   0.170  1.00 59.17           O  
HETATM 4155  O   HOH A 682      18.839  -0.351  27.444  1.00 72.97           O  
HETATM 4156  O   HOH A 683      -9.660  -6.466  17.256  1.00 70.32           O  
HETATM 4157  O   HOH A 684      35.089  18.608  25.440  1.00 65.33           O  
HETATM 4158  O   HOH A 685      11.609  -6.747  43.316  1.00 67.74           O  
HETATM 4159  O   HOH A 686       8.425 -18.850   8.165  1.00 69.25           O  
HETATM 4160  O   HOH A 687      36.717  17.035  26.779  1.00 64.89           O  
HETATM 4161  O   HOH A 688      28.877  -3.064   4.752  1.00 51.57           O  
HETATM 4162  O   HOH A 689       6.646 -23.964  28.137  1.00 73.41           O  
HETATM 4163  O   HOH A 690       5.647  -7.062  -0.153  1.00 60.64           O  
HETATM 4164  O   HOH A 691      14.931 -10.542  37.887  1.00 66.85           O  
HETATM 4165  O   HOH A 692      18.704 -21.209  18.323  1.00 68.30           O  
HETATM 4166  O   HOH A 693      17.527 -12.950  33.824  1.00 60.24           O  
HETATM 4167  O   HOH A 694      29.053  11.093  -1.082  1.00 61.77           O  
HETATM 4168  O   HOH A 695      33.506  19.552  27.367  1.00 70.43           O  
HETATM 4169  O   HOH A 696      26.150   1.514   7.212  1.00 46.47           O  
HETATM 4170  O   HOH A 697      12.200  -7.622   1.349  1.00 58.68           O  
HETATM 4171  O   HOH A 698       0.745 -20.269  34.079  1.00 73.83           O  
HETATM 4172  O   HOH A 699      12.535 -11.562  32.267  1.00 75.77           O  
HETATM 4173  O   HOH A 700       4.371   9.924  17.435  1.00 57.26           O  
HETATM 4174  O   HOH A 701      24.717  -9.989   8.858  1.00 65.88           O  
HETATM 4175  O   HOH A 702      15.368  -5.282  41.093  1.00 71.68           O  
HETATM 4176  O   HOH A 703      -0.644   4.689   8.904  1.00 50.39           O  
HETATM 4177  O   HOH A 704      -3.186  -6.370  36.340  1.00 62.43           O  
HETATM 4178  O   HOH A 705      23.906  -9.615   3.349  1.00 66.01           O  
HETATM 4179  O   HOH A 706      10.562   8.014  38.363  1.00 71.63           O  
HETATM 4180  O   HOH A 707      15.019   8.039  33.857  1.00 62.99           O  
HETATM 4181  O   HOH A 708      21.764 -10.677   2.613  1.00 60.46           O  
HETATM 4182  O   HOH A 709      12.807 -11.570  35.135  1.00 73.10           O  
HETATM 4183  O   HOH A 710      -4.748   3.332  19.935  1.00 58.88           O  
HETATM 4184  O   HOH A 711      21.635  18.865  27.294  1.00 63.36           O  
HETATM 4185  O   HOH A 712      29.585  -5.230  24.134  1.00 68.11           O  
HETATM 4186  O   HOH A 713      30.657  -8.853  22.744  1.00 78.30           O  
HETATM 4187  O   HOH A 714       1.864   1.101   7.611  1.00 41.72           O  
HETATM 4188  O   HOH A 715       3.122   9.042  23.332  1.00 46.42           O  
HETATM 4189  O   HOH A 716       7.508  14.101  17.872  1.00 69.76           O  
HETATM 4190  O   HOH A 717      33.615  14.610  16.492  1.00 74.14           O  
HETATM 4191  O   HOH A 718      29.117  -4.815  19.032  1.00 72.69           O  
HETATM 4192  O   HOH A 719      12.563 -11.957   2.133  1.00 65.03           O  
HETATM 4193  O   HOH A 720      25.032  -6.431  15.061  1.00 66.74           O  
HETATM 4194  O   HOH A 721      19.671  19.210  25.468  1.00 74.89           O  
HETATM 4195  O   HOH A 722      -2.361 -16.817  12.348  1.00 63.59           O  
HETATM 4196  O   HOH A 723      36.222  18.624  19.224  1.00 76.39           O  
HETATM 4197  O   HOH A 724      13.655 -13.556   3.961  1.00 72.87           O  
HETATM 4198  O   HOH A 725      -7.090 -10.660  25.150  1.00 61.28           O  
HETATM 4199  O   HOH A 726      30.388  13.020   6.810  1.00 67.86           O  
HETATM 4200  O   HOH A 727      -3.456  -6.742   8.701  1.00 68.39           O  
HETATM 4201  O   HOH A 728       6.369  -0.036  -4.626  1.00 45.35           O  
HETATM 4202  O   HOH A 729      26.710  14.108  -4.867  1.00 78.18           O  
HETATM 4203  O   HOH A 730       1.502  -5.329  -6.400  1.00 63.00           O  
HETATM 4204  O   HOH A 731      15.798   2.049  36.988  1.00 64.74           O  
HETATM 4205  O   HOH A 732      31.625   4.680  -0.023  1.00 71.91           O  
HETATM 4206  O   HOH A 733       9.449   5.748   9.833  1.00 59.07           O  
HETATM 4207  O   HOH A 734      23.354  18.875   4.477  1.00 65.45           O  
HETATM 4208  O   HOH A 735      23.156  18.400  24.631  1.00 58.00           O  
HETATM 4209  O   HOH A 736       9.754   1.753  16.366  1.00 52.37           O  
HETATM 4210  O   HOH A 737      27.428  -7.235  25.643  1.00 93.20           O  
HETATM 4211  O   HOH A 738       5.481  12.984  11.601  1.00 82.89           O  
HETATM 4212  O   HOH A 739      -9.224 -23.097  23.822  1.00 63.43           O  
HETATM 4213  O   HOH A 740       8.974  10.450  -2.398  1.00 67.61           O  
HETATM 4214  O   HOH A 741      28.809   3.404  29.850  1.00 90.85           O  
HETATM 4215  O   HOH A 742       7.057  12.668  -3.645  1.00 74.77           O  
HETATM 4216  O   HOH A 743       1.069   9.619  21.917  1.00 73.79           O  
HETATM 4217  O   HOH A 744      -5.649  -4.710  34.004  1.00 85.08           O  
HETATM 4218  O   HOH A 745       3.076  12.058  21.631  1.00 68.24           O  
HETATM 4219  O   HOH A 746      -6.100 -17.510  14.600  1.00 83.28           O  
HETATM 4220  O   HOH A 747       9.852  12.590   8.223  1.00 80.17           O  
HETATM 4221  O   HOH A 748      21.562 -16.946  22.584  1.00 72.23           O  
HETATM 4222  O   HOH A 749      11.581  -5.492  -6.885  1.00 80.10           O  
HETATM 4223  O   HOH A 750      10.120 -18.708   2.552  1.00 81.14           O  
HETATM 4224  O   HOH A 751      23.731  15.175  25.795  1.00 76.19           O  
HETATM 4225  O   HOH A 752      -1.215 -19.273  32.768  1.00 78.22           O  
HETATM 4226  O   HOH A 753      13.136 -12.958  39.286  1.00 78.15           O  
HETATM 4227  O   HOH A 754      33.633   5.155   8.556  1.00 96.24           O  
HETATM 4228  O   HOH A 755      26.387 -11.288  15.414  1.00 75.96           O  
HETATM 4229  O   HOH A 756      -5.769 -20.561  14.318  1.00 67.70           O  
HETATM 4230  O   HOH A 757      26.158   4.572  35.370  1.00 91.97           O  
HETATM 4231  O   HOH A 758      -1.869  -1.643  41.075  1.00 84.71           O  
HETATM 4232  O   HOH A 759      -0.389 -12.694   9.665  1.00 72.72           O  
HETATM 4233  O   HOH A 760      25.410  17.134  25.827  1.00 72.44           O  
HETATM 4234  O   HOH A 761      34.152   3.308   6.855  1.00 98.78           O  
HETATM 4235  O   HOH A 762      29.245  -4.279  16.319  1.00 82.08           O  
HETATM 4236  O   HOH A 763      32.297  21.985  19.548  1.00 88.20           O  
HETATM 4237  O   HOH A 764      20.528  21.595   0.806  1.00103.87           O  
HETATM 4238  O   HOH A 765      -1.961 -14.959  34.768  1.00 85.09           O  
HETATM 4239  O   HOH A 766      -4.106 -13.218  33.361  1.00 74.63           O  
HETATM 4240  O   HOH A 767      -1.315 -12.112  35.020  1.00 78.51           O  
HETATM 4241  O   HOH A 768      -2.256 -10.568   8.747  1.00 82.26           O  
HETATM 4242  O   HOH A 769      18.516  22.278  -0.946  1.00 87.18           O  
HETATM 4243  O   HOH A 770      24.053  -9.533  15.074  1.00 87.87           O  
HETATM 4244  O   HOH A 771      -4.809  -0.935  40.029  1.00 68.65           O  
HETATM 4245  O   HOH B 601      29.523 -22.700  20.991  1.00 29.35           O  
HETATM 4246  O   HOH B 602      21.681 -24.132  38.575  1.00 33.77           O  
HETATM 4247  O   HOH B 603      35.284 -22.493  12.140  1.00 38.75           O  
HETATM 4248  O   HOH B 604       8.725 -21.453  27.165  1.00 42.11           O  
HETATM 4249  O   HOH B 605       9.005 -24.794  29.919  1.00 37.42           O  
HETATM 4250  O   HOH B 606      18.829 -23.508  38.123  1.00 38.31           O  
HETATM 4251  O   HOH B 607      23.995 -24.503  37.155  1.00 34.04           O  
HETATM 4252  O   HOH B 608      38.801 -33.724  26.563  1.00 53.62           O  
HETATM 4253  O   HOH B 609      27.934 -21.564   6.490  1.00 40.53           O  
HETATM 4254  O   HOH B 610      44.589 -27.063  35.046  1.00 39.14           O  
HETATM 4255  O   HOH B 611      21.594 -20.176  45.143  1.00 44.73           O  
HETATM 4256  O   HOH B 612      46.937 -25.817  34.084  1.00 45.72           O  
HETATM 4257  O   HOH B 613      26.376 -28.269  36.828  1.00 38.67           O  
HETATM 4258  O   HOH B 614      42.153 -27.062  28.758  1.00 43.51           O  
HETATM 4259  O   HOH B 615      20.672 -32.456  39.996  1.00 45.24           O  
HETATM 4260  O   HOH B 616      11.659 -23.676  38.132  1.00 56.71           O  
HETATM 4261  O   HOH B 617      36.210 -35.354  31.895  1.00 56.66           O  
HETATM 4262  O   HOH B 618       9.694 -30.652  22.006  1.00 55.59           O  
HETATM 4263  O   HOH B 619      38.716 -24.724  20.987  1.00 50.78           O  
HETATM 4264  O   HOH B 620      30.080 -15.452  24.861  1.00 42.63           O  
HETATM 4265  O   HOH B 621      18.644 -35.115  30.494  1.00 42.53           O  
HETATM 4266  O   HOH B 622      19.078 -34.788  37.351  1.00 47.13           O  
HETATM 4267  O   HOH B 623      38.773 -22.952  14.424  1.00 49.21           O  
HETATM 4268  O   HOH B 624      36.671 -19.051  14.600  1.00 51.41           O  
HETATM 4269  O   HOH B 625      29.701 -12.906  24.932  1.00 46.69           O  
HETATM 4270  O   HOH B 626      29.566 -37.383  37.630  1.00 49.59           O  
HETATM 4271  O   HOH B 627      25.793 -41.412  27.140  1.00 53.21           O  
HETATM 4272  O   HOH B 628      38.404 -25.020  23.562  1.00 44.67           O  
HETATM 4273  O   HOH B 629      27.035 -42.365  32.958  1.00 52.63           O  
HETATM 4274  O   HOH B 630      20.518 -30.672  41.992  1.00 50.29           O  
HETATM 4275  O   HOH B 631      13.616 -34.646  26.217  1.00 46.26           O  
HETATM 4276  O   HOH B 632      24.407 -18.453  26.108  1.00 50.25           O  
HETATM 4277  O   HOH B 633      40.751 -24.826  13.989  1.00 53.04           O  
HETATM 4278  O   HOH B 634      38.232 -20.146  24.891  1.00 55.71           O  
HETATM 4279  O   HOH B 635      18.908 -23.617  15.610  1.00 59.97           O  
HETATM 4280  O   HOH B 636      47.701 -22.607  25.753  1.00 56.27           O  
HETATM 4281  O   HOH B 637      19.707 -31.819  44.301  1.00 46.67           O  
HETATM 4282  O   HOH B 638      21.469 -32.910  46.189  1.00 60.22           O  
HETATM 4283  O   HOH B 639      34.405 -19.014  25.435  1.00 45.12           O  
HETATM 4284  O   HOH B 640       9.107 -14.462  32.621  1.00 61.50           O  
HETATM 4285  O   HOH B 641       7.116 -34.173  22.042  1.00 70.95           O  
HETATM 4286  O   HOH B 642      22.403 -36.455  39.180  1.00 53.45           O  
HETATM 4287  O   HOH B 643      21.392 -18.745  47.670  1.00 57.82           O  
HETATM 4288  O   HOH B 644      28.689 -17.706  12.430  1.00 53.85           O  
HETATM 4289  O   HOH B 645      41.448 -34.293  27.944  1.00 61.46           O  
HETATM 4290  O   HOH B 646      39.781 -20.973  16.165  1.00 70.67           O  
HETATM 4291  O   HOH B 647      33.027 -38.221  24.436  1.00 61.84           O  
HETATM 4292  O   HOH B 648      37.255 -19.828  10.248  1.00 58.90           O  
HETATM 4293  O   HOH B 649      20.215 -26.145  46.664  1.00 58.63           O  
HETATM 4294  O   HOH B 650       7.951 -23.886  21.485  1.00 62.13           O  
HETATM 4295  O   HOH B 651      37.594 -38.448  20.277  1.00 61.88           O  
HETATM 4296  O   HOH B 652       5.777 -35.383  34.245  1.00 72.06           O  
HETATM 4297  O   HOH B 653      18.224 -29.115  41.617  1.00 53.74           O  
HETATM 4298  O   HOH B 654      30.054 -14.537  52.412  1.00 55.83           O  
HETATM 4299  O   HOH B 655      41.469 -21.956  18.521  1.00 59.11           O  
HETATM 4300  O   HOH B 656      22.038 -20.741  16.809  1.00 61.33           O  
HETATM 4301  O   HOH B 657      10.533 -25.887  39.409  1.00 68.37           O  
HETATM 4302  O   HOH B 658      38.250 -33.135  35.678  1.00 60.28           O  
HETATM 4303  O   HOH B 659      40.354 -34.563  20.334  1.00 56.14           O  
HETATM 4304  O   HOH B 660      39.857 -32.126  33.599  1.00 51.27           O  
HETATM 4305  O   HOH B 661      31.622 -10.987  34.679  1.00 61.90           O  
HETATM 4306  O   HOH B 662      29.603 -18.131   9.571  1.00 59.79           O  
HETATM 4307  O   HOH B 663      31.970 -26.734  33.584  1.00 50.95           O  
HETATM 4308  O   HOH B 664      35.281 -24.122  41.723  1.00 55.72           O  
HETATM 4309  O   HOH B 665      38.860 -20.290  29.471  1.00 78.01           O  
HETATM 4310  O   HOH B 666      40.626 -21.838  28.045  1.00 70.03           O  
HETATM 4311  O   HOH B 667      22.598 -20.247  20.300  1.00 58.79           O  
HETATM 4312  O   HOH B 668      36.727 -30.904   8.585  1.00 54.37           O  
HETATM 4313  O   HOH B 669      18.993 -18.461  44.432  1.00 64.62           O  
HETATM 4314  O   HOH B 670      43.363 -23.548  17.195  1.00 70.85           O  
HETATM 4315  O   HOH B 671      37.703 -35.726  34.518  1.00 61.01           O  
HETATM 4316  O   HOH B 672      38.906 -21.338  12.107  1.00 60.86           O  
HETATM 4317  O   HOH B 673      17.875 -25.623  11.162  1.00 56.57           O  
HETATM 4318  O   HOH B 674      29.820 -27.275  10.769  1.00 37.04           O  
HETATM 4319  O   HOH B 675      38.686 -34.068  31.742  1.00 71.24           O  
HETATM 4320  O   HOH B 676      30.502 -29.326   9.220  1.00 40.99           O  
HETATM 4321  O   HOH B 677      28.538 -18.110  37.647  1.00 57.58           O  
HETATM 4322  O   HOH B 678      28.966 -31.679   8.774  1.00 58.42           O  
HETATM 4323  O   HOH B 679      47.306 -21.398  37.884  1.00 66.63           O  
HETATM 4324  O   HOH B 680      39.977 -32.527  21.918  1.00 63.22           O  
HETATM 4325  O   HOH B 681      40.979 -31.262  24.039  1.00 59.12           O  
HETATM 4326  O   HOH B 682      16.783 -37.132  31.476  1.00 70.68           O  
HETATM 4327  O   HOH B 683      29.564 -36.313  18.386  1.00 44.75           O  
HETATM 4328  O   HOH B 684      10.856 -33.408  38.816  1.00 73.66           O  
HETATM 4329  O   HOH B 685      40.956 -28.458  40.811  1.00 67.50           O  
HETATM 4330  O   HOH B 686      27.473 -18.981   7.258  1.00 54.99           O  
HETATM 4331  O   HOH B 687      44.386 -14.444  31.880  1.00 64.94           O  
HETATM 4332  O   HOH B 688      27.824 -11.754  50.410  1.00 74.97           O  
HETATM 4333  O   HOH B 689      24.733 -18.914  23.327  1.00 55.27           O  
HETATM 4334  O   HOH B 690      27.636 -38.474  39.556  1.00 62.43           O  
HETATM 4335  O   HOH B 691      14.332 -35.884  34.892  1.00 72.26           O  
HETATM 4336  O   HOH B 692      11.250 -36.206  34.626  1.00 71.87           O  
HETATM 4337  O   HOH B 693      33.460 -14.178  54.764  1.00 55.53           O  
HETATM 4338  O   HOH B 694      37.604 -22.634  58.476  1.00 57.29           O  
HETATM 4339  O   HOH B 695      43.927  -9.125  35.052  1.00 74.59           O  
HETATM 4340  O   HOH B 696      39.519 -22.149  60.267  1.00 74.88           O  
HETATM 4341  O   HOH B 697      45.151 -22.446  18.813  1.00 68.98           O  
HETATM 4342  O   HOH B 698      11.711 -14.997  33.375  1.00 66.62           O  
HETATM 4343  O   HOH B 699      24.986 -11.052  36.520  1.00 65.55           O  
HETATM 4344  O   HOH B 700      45.358 -28.798  50.211  1.00 65.70           O  
HETATM 4345  O   HOH B 701      42.794 -28.200  50.728  1.00 70.79           O  
HETATM 4346  O   HOH B 702      22.365 -12.557  46.538  1.00 57.39           O  
HETATM 4347  O   HOH B 703       6.563 -41.087  21.267  1.00 74.01           O  
HETATM 4348  O   HOH B 704       7.496 -33.998  19.010  1.00 72.39           O  
HETATM 4349  O   HOH B 705      49.800 -20.085  39.324  1.00 64.99           O  
HETATM 4350  O   HOH B 706      20.128 -13.541  47.623  1.00 68.12           O  
HETATM 4351  O   HOH B 707      40.112 -27.277  50.583  1.00 66.19           O  
HETATM 4352  O   HOH B 708      39.502 -24.832  61.967  1.00 73.89           O  
HETATM 4353  O   HOH B 709      35.427 -39.387  32.229  1.00 70.13           O  
HETATM 4354  O   HOH B 710      17.112 -20.475  44.514  1.00 68.01           O  
HETATM 4355  O   HOH B 711      35.034 -30.247   6.327  1.00 71.36           O  
HETATM 4356  O   HOH B 712      29.996 -15.540  20.384  1.00 59.97           O  
HETATM 4357  O   HOH B 713      50.920 -17.010  36.163  1.00 78.19           O  
HETATM 4358  O   HOH B 714      31.788 -44.707  32.040  1.00 73.40           O  
HETATM 4359  O   HOH B 715       7.267 -42.026  19.227  1.00 78.58           O  
HETATM 4360  O   HOH B 716      17.409 -12.111  28.174  1.00 73.95           O  
HETATM 4361  O   HOH B 717      23.896 -12.635  50.220  1.00 80.62           O  
HETATM 4362  O   HOH B 718      35.220 -34.176  10.588  1.00 78.90           O  
HETATM 4363  O   HOH B 719      49.939 -20.070  53.438  1.00 92.56           O  
HETATM 4364  O   HOH B 720      49.611 -30.676  53.508  1.00 87.90           O  
HETATM 4365  O   HOH B 721      29.490  -4.002  46.957  1.00 87.32           O  
HETATM 4366  O   HOH B 722      10.653 -35.550  37.985  1.00 85.77           O  
HETATM 4367  O   HOH B 723      49.188 -29.540  50.811  1.00 73.07           O  
HETATM 4368  O   HOH B 724       7.079 -28.424  38.782  1.00 60.27           O  
HETATM 4369  O   HOH B 725      42.088 -22.957   8.162  1.00 83.90           O  
HETATM 4370  O   HOH B 726      31.748  -5.801  44.044  1.00 83.62           O  
HETATM 4371  O   HOH B 727      20.920 -11.638  42.212  1.00 83.14           O  
HETATM 4372  O   HOH B 728      14.825 -39.230  29.639  1.00 73.37           O  
HETATM 4373  O   HOH B 729      42.896 -31.031  45.295  1.00 92.79           O  
HETATM 4374  O   HOH B 730       2.415 -28.639  31.983  1.00 69.50           O  
HETATM 4375  O   HOH B 731      20.097  -9.863  32.372  1.00 76.07           O  
HETATM 4376  O   HOH B 732      32.071 -16.091  22.937  1.00 66.85           O  
HETATM 4377  O   HOH B 733      43.466  -8.299  48.352  1.00 84.84           O  
HETATM 4378  O   HOH B 734      18.114 -22.182  11.407  1.00 83.63           O  
HETATM 4379  O   HOH B 735      33.174 -13.219  23.934  1.00 85.56           O  
HETATM 4380  O   HOH B 736      53.353 -14.589  31.522  1.00 78.31           O  
HETATM 4381  O   HOH B 737      35.693 -36.772  13.305  1.00 88.16           O  
HETATM 4382  O   HOH B 738      39.818 -23.236   6.490  1.00 76.98           O  
HETATM 4383  O   HOH B 739       4.951 -26.703  31.153  1.00 71.43           O  
HETATM 4384  O   HOH B 740      22.317  -8.942  31.963  1.00 76.91           O  
CONECT 3996 3997 3998 3999                                                      
CONECT 3997 3996                                                                
CONECT 3998 3996 4000                                                           
CONECT 3999 3996                                                                
CONECT 4000 3998 4001                                                           
CONECT 4001 4000 4002                                                           
CONECT 4002 4001 4003                                                           
CONECT 4003 4002 4004                                                           
CONECT 4004 4003 4005                                                           
CONECT 4005 4004 4006                                                           
CONECT 4006 4005                                                                
CONECT 4007 4008 4009 4010                                                      
CONECT 4008 4007                                                                
CONECT 4009 4007 4011                                                           
CONECT 4010 4007                                                                
CONECT 4011 4009 4012                                                           
CONECT 4012 4011 4013                                                           
CONECT 4013 4012 4014                                                           
CONECT 4014 4013 4015                                                           
CONECT 4015 4014 4016                                                           
CONECT 4016 4015 4017                                                           
CONECT 4017 4016                                                                
CONECT 4018 4019 4020 4021                                                      
CONECT 4019 4018                                                                
CONECT 4020 4018 4022                                                           
CONECT 4021 4018                                                                
CONECT 4022 4020 4023                                                           
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4026                                                           
CONECT 4026 4025 4027                                                           
CONECT 4027 4026 4028                                                           
CONECT 4028 4027                                                                
CONECT 4029 4030 4031                                                           
CONECT 4030 4029                                                                
CONECT 4031 4029 4032 4033                                                      
CONECT 4032 4031                                                                
CONECT 4033 4031 4034                                                           
CONECT 4034 4033                                                                
CONECT 4035 4036 4037 4038                                                      
CONECT 4036 4035                                                                
CONECT 4037 4035 4039                                                           
CONECT 4038 4035                                                                
CONECT 4039 4037 4040                                                           
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4042                                                           
CONECT 4042 4041 4043                                                           
CONECT 4043 4042 4044                                                           
CONECT 4044 4043 4045                                                           
CONECT 4045 4044                                                                
CONECT 4046 4047                                                                
CONECT 4047 4046 4048 4049                                                      
CONECT 4048 4047                                                                
CONECT 4049 4047 4050                                                           
CONECT 4050 4049 4051                                                           
CONECT 4051 4050 4052 4057                                                      
CONECT 4052 4051 4053                                                           
CONECT 4053 4052 4054                                                           
CONECT 4054 4053 4055 4056                                                      
CONECT 4055 4054                                                                
CONECT 4056 4054                                                                
CONECT 4057 4051 4058                                                           
CONECT 4058 4057 4059                                                           
CONECT 4059 4058 4060 4061                                                      
CONECT 4060 4059                                                                
CONECT 4061 4059                                                                
CONECT 4062 4063 4064                                                           
CONECT 4063 4062                                                                
CONECT 4064 4062 4065 4066                                                      
CONECT 4065 4064                                                                
CONECT 4066 4064 4067                                                           
CONECT 4067 4066                                                                
CONECT 4068 4069 4070                                                           
CONECT 4069 4068                                                                
CONECT 4070 4068 4071 4072                                                      
CONECT 4071 4070                                                                
CONECT 4072 4070 4073                                                           
CONECT 4073 4072                                                                
MASTER      449    0    8   27    8    0   16    6 4352    2   78   44          
END                                                                             
