HEADER    CHAPERONE                               08-MAY-09   2WI3              
TITLE     ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90        
TITLE    2 CHAPERONE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN, HSP 90-ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL ATP-BINDING DOMAIN, RESIDUES 1-236;             
COMPND   5 SYNONYM: HSP 86, RENAL CARCINOMA ANTIGEN NY-REN-38;                  
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 ORGAN: SKIN;                                                         
SOURCE   6 TISSUE: MELANOMA;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET19;                                    
SOURCE  11 OTHER_DETAILS: CLONED FROM IMAGE\:4026275                            
KEYWDS    CHAPERONE, HEAT SHOCK, STRESS RESPONSE, NUCLEOTIDE-BINDING            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.A.BROUGH,X.BARRIL,J.BORGOGNONI,P.CHENE,N.G.M.DAVIES,B.DAVIS,        
AUTHOR   2 M.J.DRYSDALE,B.DYMOCK,S.A.ECCLES,C.GARCIA-ECHEVERRIA,C.FROMONT,      
AUTHOR   3 A.HAYES,R.E.HUBBARD,A.M.JORDAN,M.RUGAARD-JENSEN,A.MASSEY,A.MERRET,   
AUTHOR   4 A.PADFIELD,R.PARSONS,T.RADIMERSKI,F.I.RAYNAUD,A.ROBERTSON,           
AUTHOR   5 S.D.ROUGHLEY,J.SCHOEPFER,H.SIMMONITE,A.SURGENOR,M.VALENTI,S.WALLS,   
AUTHOR   6 P.WEBB,M.WOOD,P.WORKMAN,L.M.WRIGHT                                   
REVDAT   3   13-DEC-23 2WI3    1       REMARK LINK                              
REVDAT   2   29-SEP-10 2WI3    1       KEYWDS AUTHOR JRNL   REMARK              
REVDAT   2 2                   1       HET    HETNAM FORMUL LINK                
REVDAT   2 3                   1       HETATM CONECT MASTER                     
REVDAT   1   28-JUL-09 2WI3    0                                                
JRNL        AUTH   P.A.BROUGH,X.BARRIL,J.BORGOGNONI,P.CHENE,N.G.M.DAVIES,       
JRNL        AUTH 2 B.DAVIS,M.J.DRYSDALE,B.DYMOCK,S.A.ECCLES,                    
JRNL        AUTH 3 C.GARCIA-ECHEVERRIA,C.FROMONT,A.HAYES,R.E.HUBBARD,           
JRNL        AUTH 4 A.M.JORDAN,M.R.JENSEN,A.MASSEY,A.MERRETT,A.PADFIELD,         
JRNL        AUTH 5 R.PARSONS,T.RADIMERSKI,F.I.RAYNAUD,A.ROBERTSON,S.D.ROUGHLEY, 
JRNL        AUTH 6 J.SCHOEPFER,H.SIMMONITE,S.Y.SHARP,A.SURGENOR,M.VALENTI,      
JRNL        AUTH 7 S.WALLS,P.WEBB,M.WOOD,P.WORKMAN,L.M.WRIGHT                   
JRNL        TITL   COMBINING HIT IDENTIFICATION STRATEGIES: FRAGMENT- BASED AND 
JRNL        TITL 2 IN SILICO APPROACHES TO ORALLY ACTIVE                        
JRNL        TITL 3 2-AMINOTHIENO[2,3-D]PYRIMIDINE INHIBITORS OF THE HSP90       
JRNL        TITL 4 MOLECULAR CHAPERONE.                                         
JRNL        REF    J.MED.CHEM.                   V.  52  4794 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19610616                                                     
JRNL        DOI    10.1021/JM900357Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 20654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1114                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 969                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 61.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.4980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1628                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 271                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.26000                                             
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -0.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.147         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.877         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1684 ; 0.028 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2277 ; 2.215 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   213 ; 6.187 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    76 ;37.862 ;25.263       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   309 ;14.116 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;20.503 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   261 ; 0.167 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1252 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1038 ; 1.398 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1679 ; 2.298 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   646 ; 3.962 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   595 ; 5.689 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2WI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290039757.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC BLUE MIRRORS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21769                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.02000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1UY6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       32.84100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.58600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.89150            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       32.84100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.58600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       49.89150            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       32.84100            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.58600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       49.89150            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       32.84100            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.58600            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.89150            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     MET A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
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     GLU A  16    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 123    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 224    CA   C    O    CB   CG   CD   CE                    
REMARK 470     LYS A 224    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   OE2  GLU A   120     O    HOH A  2165              1.61            
REMARK 500   NE   ARG A    60     O    HOH A  2086              2.01            
REMARK 500   CE   LYS A   191     O    HOH A  2222              2.10            
REMARK 500   N    GLU A    16     O    HOH A  2002              2.10            
REMARK 500   O    HOH A  2063     O    HOH A  2170              2.11            
REMARK 500   O    HOH A  2059     O    HOH A  2063              2.16            
REMARK 500   OE2  GLU A    18     O    HOH A  2006              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  42   CD    GLU A  42   OE2    -0.066                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A 147   CD  -  CE  -  NZ  ANGL. DEV. = -18.0 DEGREES          
REMARK 500    ARG A 182   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 202   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  38      105.11   -165.59                                   
REMARK 500    ILE A 110       60.83   -102.46                                   
REMARK 500    ALA A 124       28.86    -78.59                                   
REMARK 500    ALA A 166     -141.80     63.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1224  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2038   O                                                      
REMARK 620 2 HOH A2159   O   117.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1224                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZ3 A 1225                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YES   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN " CONFORMATION        
REMARK 900 RELATED ID: 1UY9   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-BENZO[1,3] DIOXOL-,5-YLMETHYL-9-BUTYL-9H-   
REMARK 900 PURIN-6- YLAMINE                                                     
REMARK 900 RELATED ID: 2CDD   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 WITH 4-(4-(2,3-DIHYDRO- BENZOL(1,4)DIOXIN-6-YL)-5-       
REMARK 900 METHYL-1H- PYRAZOL-3-YL)-6-ETHYL-BENZENE-1,3-DIOL                    
REMARK 900 RELATED ID: 1BYQ   RELATED DB: PDB                                   
REMARK 900 HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG                              
REMARK 900 RELATED ID: 1OSF   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 IN COMPLEX WITH 17-DESMETHOXY- 17-N,N-                   
REMARK 900 DIMETHYLAMINOETHYLAMINO-GELDANAMYCIN                                 
REMARK 900 RELATED ID: 2BSM   RELATED DB: PDB                                   
REMARK 900 NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE   
REMARK 900 HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN                      
REMARK 900 RELATED ID: 1UY8   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3- TRIMETHOXY-BENZYL)-9H-PURIN-    
REMARK 900 6YLAMINE                                                             
REMARK 900 RELATED ID: 2BUG   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE TPR DOMAIN FROM PROTEIN PHOSPHATASE 5 IN   
REMARK 900 COMPLEX WITH HSP90 DERIVED PEPTIDE                                   
REMARK 900 RELATED ID: 2UWD   RELATED DB: PDB                                   
REMARK 900 INHIBITION OF THE HSP90 MOLECULAR CHAPERONE IN VITRO AND IN VIVO BY  
REMARK 900 NOVEL, SYNTHETIC , POTENT RESORCINYLIC PYRAZOLE, ISOXAZOLE AMIDE     
REMARK 900 ANALOGS                                                              
REMARK 900 RELATED ID: 2BT0   RELATED DB: PDB                                   
REMARK 900 NOVEL, POTENT SMALL MOLECULE INHIBITORS OF THE MOLECULAR CHAPERONE   
REMARK 900 HSP90 DISCOVERED THROUGH STRUCTURE-BASED DESIGN                      
REMARK 900 RELATED ID: 1YER   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, " CLOSED" CONFORMATION      
REMARK 900 RELATED ID: 1UYG   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY- BENZYL)-2-FLUORO-9H-PURIN-  
REMARK 900 6-YLAMINE                                                            
REMARK 900 RELATED ID: 2CCU   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 WITH 4-CHLORO-6-(4-(4-(4- METHANESULPHONYL-BENZYL)-      
REMARK 900 PIERAZIN-1-YL)-1H- PYRAZOL-3-YL)-BENZENE-1,3-DIOL                    
REMARK 900 RELATED ID: 2BZ5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE-BASED DISCOVERY OF A NEW CLASS OF HSP90 INHIBITORS         
REMARK 900 RELATED ID: 2CCS   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 WITH 4-CHLORO-6-(4-PIPERAZIN- 1-YL-1H-PYRAZOL-3-YL)-     
REMARK 900 BENZENE-1,2-DIOL                                                     
REMARK 900 RELATED ID: 1UYF   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4, 5-TRIMETHOXY-BENZYL)-2-      
REMARK 900 FLUORO-9-PENT-4- YLNYL-9H-PURIN-6-YLAMINE                            
REMARK 900 RELATED ID: 1YC3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN HSP90ALPHA COMPLEXED                      
REMARK 900 WITHDIHYDROXYPHENYLPYRAZOLES                                         
REMARK 900 RELATED ID: 1UYI   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY- BENZYL)-2-FLUORO-9-PENT-9H- 
REMARK 900 PURIN-6- YLAMINE                                                     
REMARK 900 RELATED ID: 1UYD   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2- CHLORO-3,4,5-TRIMETHOXY-BENZYL) 
REMARK 900 -9H-PURIN- 6-YLAMINE                                                 
REMARK 900 RELATED ID: 2BYI   RELATED DB: PDB                                   
REMARK 900 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE- 4-CARBOXAMIDES AS         
REMARK 900 INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE                          
REMARK 900 RELATED ID: 1UY6   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3,4, 5-TRIMETHOXY-BENZYL)-9H-      
REMARK 900 PURIN-6-YLAMINE                                                      
REMARK 900 RELATED ID: 2VCI   RELATED DB: PDB                                   
REMARK 900 4,5 DIARYL ISOXAZOLE HSP90 CHAPERONE INHIBITORS: POTENTIAL           
REMARK 900 THERAPEUTIC AGENTS FOR THE TREATMENT OF CANCER                       
REMARK 900 RELATED ID: 2VCJ   RELATED DB: PDB                                   
REMARK 900 4,5 DIARYL ISOXAZOLE HSP90 CHAPERONE INHIBITORS: POTENTIAL           
REMARK 900 THERAPEUTIC AGENTS FOR THE TREATMENT OF CANCER                       
REMARK 900 RELATED ID: 1YC4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN HSP90ALPHA COMPLEXED                      
REMARK 900 WITHDIHYDROXYPHENYLPYRAZOLES                                         
REMARK 900 RELATED ID: 2C2L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CHIP U-BOX E3 UBIQUITIN LIGASE              
REMARK 900 RELATED ID: 1UYH   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5- DIMETHOXY-BENZYL)-2-FLUORO-   
REMARK 900 9H-PURIN-6- YLAMINE                                                  
REMARK 900 RELATED ID: 1UYK   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-BENZO[1,3] DIOXOL-,5-YLMETHYL-9-BUTYL-2-    
REMARK 900 FLUORO-9H- PURIN-6-YLAMINE                                           
REMARK 900 RELATED ID: 2CCT   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90 WITH 5-(5-CHLORO-2,4- DIHYDROXY-PHENYL)-4-PIPERAZIN-1-   
REMARK 900 YL-2H- PYRAZOLE-3-CARBOXYLIC ACID ETHYLAMIDE                         
REMARK 900 RELATED ID: 1UYL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE- BASED INHIBITOR BINDING  
REMARK 900 TO HSP90 ISOFORMS                                                    
REMARK 900 RELATED ID: 1UYE   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4, 5-TRIMETHOXY-BENZYL)-9-PENT- 
REMARK 900 4-YLNYL-9H- PURIN-6-YLAMINE                                          
REMARK 900 RELATED ID: 1YC1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURES OF HUMAN HSP90ALPHA COMPLEXED                     
REMARK 900 WITHDIHYDROXYPHENYLPYRAZOLES                                         
REMARK 900 RELATED ID: 1UY7   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(4- METHOXY-BENZYL)-9H-PURIN-6-     
REMARK 900 YLAMINE                                                              
REMARK 900 RELATED ID: 1UYC   RELATED DB: PDB                                   
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5- DIMETHOXY-BENZYL)-9H-PURIN-6- 
REMARK 900 YLAMINE                                                              
REMARK 900 RELATED ID: 1YET   RELATED DB: PDB                                   
REMARK 900 GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN- BINDING DOMAIN         
REMARK 900 RELATED ID: 2JJC   RELATED DB: PDB                                   
REMARK 900 HSP90 ALPHA ATPASE DOMAIN WITH BOUND SMALL MOLECULE FRAGMENT         
REMARK 900 RELATED ID: 2BYH   RELATED DB: PDB                                   
REMARK 900 3-(5-CHLORO-2,4-DIHYDROXYPHENYL)-PYRAZOLE- 4-CARBOXAMIDES AS         
REMARK 900 INHIBITORS OF THE HSP90 MOLECULAR CHAPERONE                          
REMARK 900 RELATED ID: 2WI1   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
REMARK 900 RELATED ID: 2WI2   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
REMARK 900 RELATED ID: 2WI4   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
REMARK 900 RELATED ID: 2WI5   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
REMARK 900 RELATED ID: 2WI6   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
REMARK 900 RELATED ID: 2WI7   RELATED DB: PDB                                   
REMARK 900 ORALLY ACTIVE 2-AMINO THIENOPYRIMIDINE INHIBITORS OF THE HSP90       
REMARK 900 CHAPERONE                                                            
DBREF  2WI3 A    1   236  UNP    P07900   HS90A_HUMAN      1    236             
SEQRES   1 A  236  MET PRO GLU GLU THR GLN THR GLN ASP GLN PRO MET GLU          
SEQRES   2 A  236  GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE          
SEQRES   3 A  236  ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE TYR SER          
SEQRES   4 A  236  ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER          
SEQRES   5 A  236  SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR          
SEQRES   6 A  236  ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE          
SEQRES   7 A  236  ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE          
SEQRES   8 A  236  VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE          
SEQRES   9 A  236  ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA          
SEQRES  10 A  236  PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET          
SEQRES  11 A  236  ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU          
SEQRES  12 A  236  VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP          
SEQRES  13 A  236  ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER          
SEQRES  14 A  236  PHE THR VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG          
SEQRES  15 A  236  GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR          
SEQRES  16 A  236  GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS          
SEQRES  17 A  236  LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE          
SEQRES  18 A  236  VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP ASP GLU          
SEQRES  19 A  236  ALA GLU                                                      
HET     MG  A1224       1                                                       
HET    ZZ3  A1225      10                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ZZ3 4-METHYL-6-(METHYLSULFANYL)-1,3,5-TRIAZIN-2-AMINE                
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ZZ3    C5 H8 N4 S                                                   
FORMUL   4  HOH   *271(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  LEU A   64  1                                  23    
HELIX    3   3 ASP A   66  ASP A   71  5                                   6    
HELIX    4   4 THR A   99  ASN A  105  1                                   7    
HELIX    5   5 ASN A  106  THR A  109  5                                   4    
HELIX    6   6 ILE A  110  ALA A  124  1                                  15    
HELIX    7   7 ASP A  127  GLY A  135  5                                   9    
HELIX    8   8 VAL A  136  LEU A  143  5                                   8    
HELIX    9   9 GLU A  192  LEU A  198  5                                   7    
HELIX   10  10 GLU A  199  SER A  211  1                                  13    
SHEET    1  AA 8 GLU A  18  ALA A  21  0                                        
SHEET    2  AA 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3  AA 8 TYR A 160  SER A 164 -1  O  ALA A 161   N  ARG A 173           
SHEET    4  AA 8 ALA A 145  LYS A 153 -1  O  VAL A 148   N  SER A 164           
SHEET    5  AA 8 GLY A 183  LEU A 190 -1  O  GLY A 183   N  LYS A 153           
SHEET    6  AA 8 THR A  88  ASP A  93 -1  O  LEU A  89   N  LEU A 188           
SHEET    7  AA 8 ILE A  78  ASN A  83 -1  O  ASN A  79   N  VAL A  92           
SHEET    8  AA 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
LINK        MG    MG A1224                 O   HOH A2038     1555   1555  2.99  
LINK        MG    MG A1224                 O   HOH A2159     1555   1555  2.84  
SITE     1 AC1  4 ILE A 110  SER A 113  HOH A2038  HOH A2159                    
SITE     1 AC2 11 LEU A  48  ASN A  51  ALA A  55  ASP A  93                    
SITE     2 AC2 11 LEU A 107  THR A 109  THR A 184  VAL A 186                    
SITE     3 AC2 11 HOH A2035  HOH A2062  HOH A2154                               
CRYST1   65.682   89.172   99.783  90.00  90.00  90.00 I 2 2 2       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      0.015225  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011214  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010022        0.00000                         
ATOM      1  N   GLU A  16      39.335  28.147  39.885  1.00 37.30           N  
ATOM      2  CA  GLU A  16      38.087  27.607  39.267  1.00 35.97           C  
ATOM      3  C   GLU A  16      38.422  26.838  37.937  1.00 34.65           C  
ATOM      4  O   GLU A  16      37.708  25.927  37.547  1.00 35.55           O  
ATOM      5  CB  GLU A  16      37.148  28.761  38.969  1.00 35.64           C  
ATOM      6  N   VAL A  17      39.469  27.222  37.212  1.00 32.54           N  
ATOM      7  CA  VAL A  17      39.721  26.570  35.881  1.00 28.96           C  
ATOM      8  C   VAL A  17      41.074  25.942  35.894  1.00 27.55           C  
ATOM      9  O   VAL A  17      42.010  26.604  36.241  1.00 26.84           O  
ATOM     10  CB  VAL A  17      39.770  27.550  34.816  1.00 28.96           C  
ATOM     11  CG1 VAL A  17      39.884  26.842  33.424  1.00 28.98           C  
ATOM     12  CG2 VAL A  17      38.557  28.425  34.895  1.00 30.25           C  
ATOM     13  N   GLU A  18      41.179  24.670  35.549  1.00 23.38           N  
ATOM     14  CA  GLU A  18      42.416  24.035  35.539  1.00 20.64           C  
ATOM     15  C   GLU A  18      42.838  23.881  34.061  1.00 20.59           C  
ATOM     16  O   GLU A  18      41.992  23.487  33.199  1.00 17.65           O  
ATOM     17  CB  GLU A  18      42.262  22.659  36.201  1.00 20.12           C  
ATOM     18  CG  GLU A  18      42.044  22.718  37.753  1.00 21.12           C  
ATOM     19  CD  GLU A  18      41.834  21.332  38.300  1.00 24.39           C  
ATOM     20  OE1 GLU A  18      40.790  20.704  38.050  1.00 26.60           O  
ATOM     21  OE2 GLU A  18      42.710  20.815  38.949  1.00 26.97           O  
ATOM     22  N   THR A  19      44.136  24.061  33.788  1.00 18.71           N  
ATOM     23  CA  THR A  19      44.645  23.957  32.441  1.00 16.91           C  
ATOM     24  C   THR A  19      45.627  22.780  32.397  1.00 18.05           C  
ATOM     25  O   THR A  19      46.517  22.622  33.245  1.00 18.25           O  
ATOM     26  CB  THR A  19      45.292  25.309  32.001  1.00 17.10           C  
ATOM     27  OG1 THR A  19      44.332  26.311  32.107  1.00 18.94           O  
ATOM     28  CG2 THR A  19      45.717  25.295  30.487  1.00 16.23           C  
ATOM     29  N   PHE A  20      45.459  21.894  31.413  1.00 17.64           N  
ATOM     30  CA  PHE A  20      46.321  20.726  31.278  1.00 15.54           C  
ATOM     31  C   PHE A  20      46.997  20.713  29.917  1.00 15.83           C  
ATOM     32  O   PHE A  20      46.417  21.208  28.954  1.00 15.61           O  
ATOM     33  CB  PHE A  20      45.419  19.457  31.302  1.00 17.56           C  
ATOM     34  CG  PHE A  20      44.634  19.316  32.539  1.00 16.14           C  
ATOM     35  CD1 PHE A  20      43.441  20.008  32.711  1.00 20.01           C  
ATOM     36  CD2 PHE A  20      45.134  18.530  33.572  1.00 18.76           C  
ATOM     37  CE1 PHE A  20      42.707  19.853  33.909  1.00 21.79           C  
ATOM     38  CE2 PHE A  20      44.406  18.362  34.806  1.00 19.60           C  
ATOM     39  CZ  PHE A  20      43.187  19.055  34.936  1.00 20.54           C  
ATOM     40  N   ALA A  21      48.172  20.064  29.823  1.00 15.23           N  
ATOM     41  CA  ALA A  21      48.782  19.868  28.518  1.00 15.66           C  
ATOM     42  C   ALA A  21      48.260  18.551  27.933  1.00 17.38           C  
ATOM     43  O   ALA A  21      48.196  17.563  28.608  1.00 16.71           O  
ATOM     44  CB  ALA A  21      50.303  19.730  28.674  1.00 16.81           C  
ATOM     45  N   PHE A  22      47.924  18.547  26.644  1.00 16.90           N  
ATOM     46  CA  PHE A  22      47.705  17.269  26.033  1.00 18.22           C  
ATOM     47  C   PHE A  22      48.956  16.398  26.110  1.00 18.05           C  
ATOM     48  O   PHE A  22      50.100  16.863  25.952  1.00 16.99           O  
ATOM     49  CB  PHE A  22      47.365  17.513  24.513  1.00 18.73           C  
ATOM     50  CG  PHE A  22      45.956  18.013  24.290  1.00 18.32           C  
ATOM     51  CD1 PHE A  22      44.869  17.204  24.661  1.00 17.81           C  
ATOM     52  CD2 PHE A  22      45.728  19.302  23.739  1.00 14.06           C  
ATOM     53  CE1 PHE A  22      43.549  17.637  24.428  1.00 14.91           C  
ATOM     54  CE2 PHE A  22      44.440  19.796  23.506  1.00 18.02           C  
ATOM     55  CZ  PHE A  22      43.293  18.938  23.872  1.00 13.67           C  
ATOM     56  N   GLN A  23      48.781  15.106  26.232  1.00 17.44           N  
ATOM     57  CA  GLN A  23      49.939  14.255  25.963  1.00 20.05           C  
ATOM     58  C   GLN A  23      50.472  14.550  24.551  1.00 19.52           C  
ATOM     59  O   GLN A  23      49.729  14.954  23.637  1.00 17.08           O  
ATOM     60  CB  GLN A  23      49.531  12.760  26.090  1.00 20.32           C  
ATOM     61  CG  GLN A  23      49.429  12.221  27.483  1.00 25.79           C  
ATOM     62  CD  GLN A  23      48.737  10.846  27.380  1.00 33.14           C  
ATOM     63  OE1 GLN A  23      47.590  10.810  27.030  1.00 28.83           O  
ATOM     64  NE2 GLN A  23      49.489   9.721  27.547  1.00 31.86           N  
ATOM     65  N   ALA A  24      51.777  14.372  24.362  1.00 19.74           N  
ATOM     66  CA  ALA A  24      52.411  14.719  23.101  1.00 19.91           C  
ATOM     67  C   ALA A  24      51.779  14.015  21.876  1.00 19.80           C  
ATOM     68  O   ALA A  24      51.656  14.624  20.830  1.00 19.20           O  
ATOM     69  CB  ALA A  24      53.937  14.406  23.156  1.00 20.43           C  
ATOM     70  N   GLU A  25      51.408  12.747  22.030  1.00 20.73           N  
ATOM     71  CA  GLU A  25      50.851  12.017  20.894  1.00 20.92           C  
ATOM     72  C   GLU A  25      49.497  12.614  20.495  1.00 18.82           C  
ATOM     73  O   GLU A  25      49.164  12.669  19.309  1.00 17.23           O  
ATOM     74  CB  GLU A  25      50.727  10.533  21.223  1.00 22.45           C  
ATOM     75  CG  GLU A  25      52.111   9.842  21.481  1.00 27.59           C  
ATOM     76  CD  GLU A  25      52.635  10.010  22.937  1.00 32.91           C  
ATOM     77  OE1 GLU A  25      52.081  10.748  23.809  1.00 27.89           O  
ATOM     78  OE2 GLU A  25      53.644   9.354  23.227  1.00 37.08           O  
ATOM     79  N   ILE A  26      48.707  13.019  21.485  1.00 17.84           N  
ATOM     80  CA  ILE A  26      47.370  13.652  21.181  1.00 14.91           C  
ATOM     81  C   ILE A  26      47.536  15.031  20.577  1.00 15.08           C  
ATOM     82  O   ILE A  26      46.859  15.415  19.645  1.00 15.96           O  
ATOM     83  CB  ILE A  26      46.541  13.723  22.496  1.00 15.07           C  
ATOM     84  CG1 ILE A  26      45.911  12.327  22.779  1.00 17.38           C  
ATOM     85  CG2 ILE A  26      45.332  14.680  22.268  1.00 11.58           C  
ATOM     86  CD1 ILE A  26      46.902  11.160  22.998  1.00 25.24           C  
ATOM     87  N   ALA A  27      48.543  15.803  21.040  1.00 15.43           N  
ATOM     88  CA  ALA A  27      48.789  17.074  20.393  1.00 17.02           C  
ATOM     89  C   ALA A  27      49.157  16.824  18.920  1.00 18.60           C  
ATOM     90  O   ALA A  27      48.710  17.585  18.026  1.00 18.05           O  
ATOM     91  CB  ALA A  27      49.941  17.806  21.093  1.00 16.38           C  
ATOM     92  N   GLN A  28      49.957  15.787  18.681  1.00 18.84           N  
ATOM     93  CA  GLN A  28      50.406  15.496  17.323  1.00 20.14           C  
ATOM     94  C   GLN A  28      49.207  15.082  16.463  1.00 19.65           C  
ATOM     95  O   GLN A  28      49.138  15.476  15.283  1.00 18.80           O  
ATOM     96  CB  GLN A  28      51.447  14.333  17.317  1.00 20.53           C  
ATOM     97  CG  GLN A  28      52.832  14.671  18.032  1.00 31.46           C  
ATOM     98  CD  GLN A  28      53.639  13.371  18.435  1.00 40.20           C  
ATOM     99  OE1 GLN A  28      53.447  12.278  17.839  1.00 42.05           O  
ATOM    100  NE2 GLN A  28      54.515  13.496  19.457  1.00 41.05           N  
ATOM    101  N   LEU A  29      48.300  14.264  17.040  1.00 19.30           N  
ATOM    102  CA  LEU A  29      47.061  13.848  16.315  1.00 20.04           C  
ATOM    103  C   LEU A  29      46.211  15.060  15.925  1.00 19.69           C  
ATOM    104  O   LEU A  29      45.766  15.230  14.784  1.00 18.69           O  
ATOM    105  CB  LEU A  29      46.245  12.880  17.186  1.00 19.35           C  
ATOM    106  CG  LEU A  29      44.830  12.512  16.683  1.00 21.72           C  
ATOM    107  CD1 LEU A  29      44.971  11.663  15.381  1.00 22.00           C  
ATOM    108  CD2 LEU A  29      44.069  11.779  17.763  1.00 21.57           C  
ATOM    109  N   MET A  30      46.020  15.968  16.883  1.00 18.16           N  
ATOM    110  CA  MET A  30      45.263  17.166  16.651  1.00 17.25           C  
ATOM    111  C   MET A  30      45.947  18.067  15.568  1.00 18.50           C  
ATOM    112  O   MET A  30      45.234  18.575  14.664  1.00 17.59           O  
ATOM    113  CB  MET A  30      44.984  17.913  17.969  1.00 16.29           C  
ATOM    114  CG  MET A  30      44.049  17.174  18.931  1.00 14.44           C  
ATOM    115  SD  MET A  30      44.021  17.913  20.598  1.00 16.84           S  
ATOM    116  CE  MET A  30      42.976  19.341  20.238  1.00 16.61           C  
ATOM    117  N   SER A  31      47.283  18.238  15.615  1.00 18.19           N  
ATOM    118  CA  SER A  31      47.951  19.075  14.578  1.00 21.09           C  
ATOM    119  C   SER A  31      47.731  18.456  13.236  1.00 19.71           C  
ATOM    120  O   SER A  31      47.551  19.192  12.262  1.00 23.19           O  
ATOM    121  CB  SER A  31      49.496  19.120  14.693  1.00 21.92           C  
ATOM    122  OG  SER A  31      49.675  19.733  15.880  1.00 28.89           O  
ATOM    123  N   LEU A  32      47.862  17.143  13.179  1.00 20.24           N  
ATOM    124  CA  LEU A  32      47.705  16.434  11.906  1.00 22.92           C  
ATOM    125  C   LEU A  32      46.266  16.631  11.342  1.00 23.09           C  
ATOM    126  O   LEU A  32      46.031  16.820  10.139  1.00 23.04           O  
ATOM    127  CB  LEU A  32      47.919  14.952  12.176  1.00 23.53           C  
ATOM    128  CG  LEU A  32      47.936  14.045  10.903  1.00 30.48           C  
ATOM    129  CD1 LEU A  32      48.824  12.812  11.160  1.00 32.66           C  
ATOM    130  CD2 LEU A  32      46.532  13.621  10.433  1.00 30.64           C  
ATOM    131  N   ILE A  33      45.293  16.583  12.236  1.00 20.45           N  
ATOM    132  CA  ILE A  33      43.901  16.750  11.839  1.00 20.68           C  
ATOM    133  C   ILE A  33      43.679  18.167  11.326  1.00 20.11           C  
ATOM    134  O   ILE A  33      42.959  18.390  10.327  1.00 19.18           O  
ATOM    135  CB  ILE A  33      42.937  16.447  12.988  1.00 18.18           C  
ATOM    136  CG1 ILE A  33      42.888  14.925  13.143  1.00 18.55           C  
ATOM    137  CG2 ILE A  33      41.542  17.135  12.681  1.00 17.93           C  
ATOM    138  CD1 ILE A  33      42.275  14.368  14.466  1.00 21.43           C  
ATOM    139  N   ILE A  34      44.293  19.117  11.991  1.00 19.70           N  
ATOM    140  CA  ILE A  34      44.048  20.523  11.652  1.00 20.90           C  
ATOM    141  C   ILE A  34      44.820  20.878  10.357  1.00 23.54           C  
ATOM    142  O   ILE A  34      44.319  21.644   9.516  1.00 22.70           O  
ATOM    143  CB  ILE A  34      44.482  21.433  12.829  1.00 22.05           C  
ATOM    144  CG1 ILE A  34      43.421  21.296  13.982  1.00 18.89           C  
ATOM    145  CG2 ILE A  34      44.699  22.877  12.379  1.00 21.39           C  
ATOM    146  CD1 ILE A  34      44.041  21.653  15.385  1.00 21.07           C  
ATOM    147  N   ASN A  35      46.041  20.345  10.250  1.00 23.24           N  
ATOM    148  CA  ASN A  35      46.990  20.781   9.199  1.00 25.78           C  
ATOM    149  C   ASN A  35      46.952  19.995   7.900  1.00 26.34           C  
ATOM    150  O   ASN A  35      47.382  20.501   6.884  1.00 29.15           O  
ATOM    151  CB  ASN A  35      48.427  20.785   9.758  1.00 26.26           C  
ATOM    152  CG  ASN A  35      48.593  21.863  10.757  1.00 26.78           C  
ATOM    153  OD1 ASN A  35      47.973  22.908  10.624  1.00 31.75           O  
ATOM    154  ND2 ASN A  35      49.388  21.635  11.777  1.00 31.87           N  
ATOM    155  N   THR A  36      46.499  18.752   7.903  1.00 24.99           N  
ATOM    156  CA  THR A  36      46.530  17.983   6.687  1.00 25.55           C  
ATOM    157  C   THR A  36      45.475  18.443   5.672  1.00 26.30           C  
ATOM    158  O   THR A  36      44.295  18.624   6.023  1.00 23.88           O  
ATOM    159  CB  THR A  36      46.269  16.521   6.990  1.00 24.41           C  
ATOM    160  OG1 THR A  36      47.293  16.046   7.844  1.00 27.58           O  
ATOM    161  CG2 THR A  36      46.263  15.649   5.713  1.00 29.13           C  
ATOM    162  N   PHE A  37      45.867  18.607   4.403  1.00 23.99           N  
ATOM    163  CA  PHE A  37      44.827  18.883   3.416  1.00 23.36           C  
ATOM    164  C   PHE A  37      43.911  17.658   3.231  1.00 22.26           C  
ATOM    165  O   PHE A  37      44.363  16.539   2.913  1.00 23.70           O  
ATOM    166  CB  PHE A  37      45.451  19.290   2.054  1.00 22.98           C  
ATOM    167  CG  PHE A  37      44.405  19.576   1.023  1.00 23.83           C  
ATOM    168  CD1 PHE A  37      43.654  20.743   1.074  1.00 26.51           C  
ATOM    169  CD2 PHE A  37      44.113  18.642   0.040  1.00 25.13           C  
ATOM    170  CE1 PHE A  37      42.625  21.021   0.101  1.00 26.85           C  
ATOM    171  CE2 PHE A  37      43.099  18.903  -0.920  1.00 21.79           C  
ATOM    172  CZ  PHE A  37      42.369  20.092  -0.866  1.00 22.49           C  
ATOM    173  N   TYR A  38      42.608  17.810   3.434  1.00 21.74           N  
ATOM    174  CA  TYR A  38      41.734  16.617   3.458  1.00 20.71           C  
ATOM    175  C   TYR A  38      40.274  17.097   3.342  1.00 20.37           C  
ATOM    176  O   TYR A  38      39.755  17.776   4.248  1.00 19.64           O  
ATOM    177  CB  TYR A  38      41.932  15.800   4.769  1.00 21.32           C  
ATOM    178  CG  TYR A  38      40.968  14.659   4.843  1.00 24.50           C  
ATOM    179  CD1 TYR A  38      41.182  13.547   4.054  1.00 27.12           C  
ATOM    180  CD2 TYR A  38      39.822  14.678   5.704  1.00 23.24           C  
ATOM    181  CE1 TYR A  38      40.309  12.481   4.038  1.00 29.86           C  
ATOM    182  CE2 TYR A  38      38.925  13.562   5.703  1.00 27.67           C  
ATOM    183  CZ  TYR A  38      39.213  12.487   4.852  1.00 28.99           C  
ATOM    184  OH  TYR A  38      38.441  11.363   4.763  1.00 34.63           O  
ATOM    185  N   SER A  39      39.680  16.914   2.160  1.00 18.15           N  
ATOM    186  CA  SER A  39      38.447  17.578   1.819  1.00 18.79           C  
ATOM    187  C   SER A  39      37.199  16.911   2.459  1.00 18.63           C  
ATOM    188  O   SER A  39      36.188  17.578   2.617  1.00 21.29           O  
ATOM    189  CB  SER A  39      38.260  17.591   0.236  1.00 18.53           C  
ATOM    190  OG  SER A  39      39.258  18.426  -0.351  1.00 19.62           O  
ATOM    191  N   ASN A  40      37.248  15.616   2.749  1.00 18.93           N  
ATOM    192  CA  ASN A  40      36.052  14.831   3.193  1.00 19.35           C  
ATOM    193  C   ASN A  40      35.819  15.089   4.740  1.00 17.44           C  
ATOM    194  O   ASN A  40      35.810  14.179   5.546  1.00 18.55           O  
ATOM    195  CB  ASN A  40      36.388  13.369   2.878  1.00 20.04           C  
ATOM    196  CG  ASN A  40      35.315  12.395   3.278  1.00 20.82           C  
ATOM    197  OD1 ASN A  40      35.615  11.254   3.626  1.00 25.54           O  
ATOM    198  ND2 ASN A  40      34.065  12.817   3.219  1.00 20.68           N  
ATOM    199  N   LYS A  41      35.614  16.354   5.106  1.00 17.67           N  
ATOM    200  CA  LYS A  41      35.518  16.763   6.493  1.00 17.01           C  
ATOM    201  C   LYS A  41      34.224  16.258   7.127  1.00 17.90           C  
ATOM    202  O   LYS A  41      34.152  16.109   8.370  1.00 18.64           O  
ATOM    203  CB  LYS A  41      35.584  18.272   6.593  1.00 17.14           C  
ATOM    204  CG  LYS A  41      37.002  18.907   6.365  1.00 16.32           C  
ATOM    205  CD  LYS A  41      36.864  20.409   6.362  1.00 15.81           C  
ATOM    206  CE  LYS A  41      38.264  21.153   6.145  1.00 16.37           C  
ATOM    207  NZ  LYS A  41      39.129  20.835   7.346  1.00 18.71           N  
ATOM    208  N   GLU A  42      33.192  16.050   6.322  1.00 17.03           N  
ATOM    209  CA  GLU A  42      31.836  15.665   6.886  1.00 18.07           C  
ATOM    210  C   GLU A  42      31.838  14.463   7.837  1.00 18.92           C  
ATOM    211  O   GLU A  42      30.905  14.292   8.640  1.00 20.36           O  
ATOM    212  CB  GLU A  42      30.841  15.414   5.742  1.00 17.73           C  
ATOM    213  CG  GLU A  42      31.004  14.060   5.058  1.00 18.96           C  
ATOM    214  CD  GLU A  42      30.086  13.982   3.806  1.00 18.91           C  
ATOM    215  OE1 GLU A  42      29.776  14.964   3.204  1.00 22.10           O  
ATOM    216  OE2 GLU A  42      29.738  12.914   3.426  1.00 24.38           O  
ATOM    217  N   ILE A  43      32.866  13.610   7.771  1.00 17.38           N  
ATOM    218  CA  ILE A  43      32.864  12.434   8.600  1.00 17.54           C  
ATOM    219  C   ILE A  43      32.938  12.804  10.093  1.00 16.62           C  
ATOM    220  O   ILE A  43      32.733  11.940  10.912  1.00 15.73           O  
ATOM    221  CB  ILE A  43      34.045  11.448   8.215  1.00 18.94           C  
ATOM    222  CG1 ILE A  43      35.396  12.125   8.388  1.00 20.96           C  
ATOM    223  CG2 ILE A  43      33.798  10.906   6.735  1.00 18.94           C  
ATOM    224  CD1 ILE A  43      36.083  11.831   9.729  1.00 24.25           C  
ATOM    225  N   PHE A  44      33.265  14.052  10.442  1.00 12.87           N  
ATOM    226  CA  PHE A  44      33.382  14.320  11.904  1.00 14.14           C  
ATOM    227  C   PHE A  44      32.024  13.989  12.528  1.00 13.98           C  
ATOM    228  O   PHE A  44      31.916  13.660  13.750  1.00 13.36           O  
ATOM    229  CB  PHE A  44      33.640  15.822  12.173  1.00 12.82           C  
ATOM    230  CG  PHE A  44      32.453  16.697  11.896  1.00 15.46           C  
ATOM    231  CD1 PHE A  44      32.183  17.152  10.635  1.00 15.24           C  
ATOM    232  CD2 PHE A  44      31.579  17.104  12.947  1.00 17.22           C  
ATOM    233  CE1 PHE A  44      31.005  18.016  10.388  1.00 15.47           C  
ATOM    234  CE2 PHE A  44      30.407  17.924  12.671  1.00 15.20           C  
ATOM    235  CZ  PHE A  44      30.151  18.376  11.407  1.00 16.71           C  
ATOM    236  N   LEU A  45      30.936  14.202  11.745  1.00 14.39           N  
ATOM    237  CA  LEU A  45      29.598  14.179  12.427  1.00 12.90           C  
ATOM    238  C   LEU A  45      29.271  12.692  12.674  1.00 15.41           C  
ATOM    239  O   LEU A  45      28.736  12.288  13.753  1.00 12.48           O  
ATOM    240  CB  LEU A  45      28.478  14.818  11.606  1.00 13.06           C  
ATOM    241  CG  LEU A  45      27.058  14.750  12.222  1.00 11.70           C  
ATOM    242  CD1 LEU A  45      27.028  15.394  13.612  1.00 11.21           C  
ATOM    243  CD2 LEU A  45      26.061  15.489  11.325  1.00 19.15           C  
ATOM    244  N   ARG A  46      29.647  11.830  11.719  1.00 14.40           N  
ATOM    245  CA  ARG A  46      29.452  10.377  11.912  1.00 13.96           C  
ATOM    246  C   ARG A  46      30.222   9.906  13.176  1.00 14.30           C  
ATOM    247  O   ARG A  46      29.771   8.995  13.942  1.00 15.77           O  
ATOM    248  CB  ARG A  46      29.965   9.552  10.700  1.00 15.23           C  
ATOM    249  CG  ARG A  46      30.041   8.072  10.968  1.00 23.41           C  
ATOM    250  CD  ARG A  46      30.778   7.368   9.753  1.00 25.91           C  
ATOM    251  NE  ARG A  46      32.263   7.604   9.826  1.00 27.38           N  
ATOM    252  CZ  ARG A  46      33.073   7.552   8.747  1.00 30.84           C  
ATOM    253  NH1 ARG A  46      32.550   7.260   7.574  1.00 27.24           N  
ATOM    254  NH2 ARG A  46      34.402   7.781   8.827  1.00 30.38           N  
ATOM    255  N   GLU A  47      31.434  10.422  13.316  1.00 13.83           N  
ATOM    256  CA  GLU A  47      32.317   9.933  14.408  1.00 13.72           C  
ATOM    257  C   GLU A  47      31.689  10.375  15.714  1.00 13.94           C  
ATOM    258  O   GLU A  47      31.759   9.672  16.714  1.00 14.54           O  
ATOM    259  CB  GLU A  47      33.723  10.587  14.292  1.00 14.38           C  
ATOM    260  CG  GLU A  47      34.459  10.083  13.072  1.00 16.59           C  
ATOM    261  CD  GLU A  47      34.474   8.544  12.933  1.00 20.34           C  
ATOM    262  OE1 GLU A  47      34.621   7.851  13.937  1.00 18.39           O  
ATOM    263  OE2 GLU A  47      34.362   8.046  11.820  1.00 22.55           O  
ATOM    264  N   LEU A  48      31.159  11.588  15.756  1.00 12.01           N  
ATOM    265  CA  LEU A  48      30.578  12.068  17.062  1.00 13.33           C  
ATOM    266  C   LEU A  48      29.278  11.316  17.455  1.00 13.18           C  
ATOM    267  O   LEU A  48      28.983  11.015  18.640  1.00 13.62           O  
ATOM    268  CB  LEU A  48      30.367  13.591  16.988  1.00 12.42           C  
ATOM    269  CG  LEU A  48      31.717  14.363  16.951  1.00 14.70           C  
ATOM    270  CD1 LEU A  48      31.316  15.842  16.822  1.00 11.92           C  
ATOM    271  CD2 LEU A  48      32.651  14.138  18.211  1.00 17.42           C  
ATOM    272  N   ILE A  49      28.432  11.124  16.475  1.00 12.51           N  
ATOM    273  CA  ILE A  49      27.237  10.404  16.696  1.00 13.17           C  
ATOM    274  C   ILE A  49      27.571   8.981  17.092  1.00 13.87           C  
ATOM    275  O   ILE A  49      26.904   8.357  17.963  1.00 15.24           O  
ATOM    276  CB  ILE A  49      26.359  10.454  15.402  1.00 12.70           C  
ATOM    277  CG1 ILE A  49      25.759  11.865  15.248  1.00 14.90           C  
ATOM    278  CG2 ILE A  49      25.250   9.265  15.473  1.00 13.14           C  
ATOM    279  CD1 ILE A  49      24.920  11.973  13.952  1.00 17.95           C  
ATOM    280  N   SER A  50      28.663   8.436  16.544  1.00 13.82           N  
ATOM    281  CA  SER A  50      29.018   7.084  16.930  1.00 14.19           C  
ATOM    282  C   SER A  50      29.492   7.027  18.374  1.00 16.31           C  
ATOM    283  O   SER A  50      29.165   6.081  19.109  1.00 13.97           O  
ATOM    284  CB  SER A  50      29.988   6.430  15.880  1.00 16.79           C  
ATOM    285  OG  SER A  50      30.633   5.354  16.484  1.00 23.53           O  
ATOM    286  N   ASN A  51      30.265   8.026  18.799  1.00 15.04           N  
ATOM    287  CA  ASN A  51      30.729   8.080  20.186  1.00 15.39           C  
ATOM    288  C   ASN A  51      29.476   8.190  21.105  1.00 13.85           C  
ATOM    289  O   ASN A  51      29.425   7.586  22.148  1.00 13.13           O  
ATOM    290  CB  ASN A  51      31.535   9.380  20.410  1.00 14.95           C  
ATOM    291  CG  ASN A  51      32.955   9.262  19.889  1.00 22.10           C  
ATOM    292  OD1 ASN A  51      33.346   8.202  19.411  1.00 20.28           O  
ATOM    293  ND2 ASN A  51      33.701  10.334  19.949  1.00 22.08           N  
ATOM    294  N   SER A  52      28.530   9.027  20.723  1.00 12.18           N  
ATOM    295  CA  SER A  52      27.275   9.166  21.522  1.00 12.28           C  
ATOM    296  C   SER A  52      26.523   7.786  21.595  1.00 14.69           C  
ATOM    297  O   SER A  52      26.052   7.406  22.655  1.00 12.21           O  
ATOM    298  CB  SER A  52      26.293  10.170  20.892  1.00 13.02           C  
ATOM    299  OG  SER A  52      26.789  11.522  20.956  1.00 14.59           O  
ATOM    300  N   SER A  53      26.350   7.120  20.443  1.00 13.80           N  
ATOM    301  CA  SER A  53      25.759   5.773  20.429  1.00 15.26           C  
ATOM    302  C   SER A  53      26.505   4.798  21.416  1.00 16.74           C  
ATOM    303  O   SER A  53      25.871   4.055  22.221  1.00 17.40           O  
ATOM    304  CB  SER A  53      25.753   5.218  18.984  1.00 15.75           C  
ATOM    305  OG  SER A  53      25.225   3.871  19.027  1.00 16.46           O  
ATOM    306  N   ASP A  54      27.846   4.757  21.356  1.00 16.03           N  
ATOM    307  CA  ASP A  54      28.615   3.990  22.357  1.00 15.95           C  
ATOM    308  C   ASP A  54      28.301   4.376  23.800  1.00 15.86           C  
ATOM    309  O   ASP A  54      28.165   3.496  24.651  1.00 15.53           O  
ATOM    310  CB  ASP A  54      30.138   4.090  22.110  1.00 14.99           C  
ATOM    311  CG  ASP A  54      30.530   3.451  20.782  1.00 20.05           C  
ATOM    312  OD1 ASP A  54      29.669   2.803  20.138  1.00 21.51           O  
ATOM    313  OD2 ASP A  54      31.642   3.711  20.307  1.00 20.20           O  
ATOM    314  N   ALA A  55      28.193   5.677  24.099  1.00 15.52           N  
ATOM    315  CA  ALA A  55      27.890   6.105  25.474  1.00 15.83           C  
ATOM    316  C   ALA A  55      26.435   5.695  25.916  1.00 14.00           C  
ATOM    317  O   ALA A  55      26.209   5.390  27.087  1.00 13.20           O  
ATOM    318  CB  ALA A  55      28.095   7.664  25.648  1.00 13.07           C  
ATOM    319  N   LEU A  56      25.498   5.715  24.979  1.00 14.47           N  
ATOM    320  CA  LEU A  56      24.118   5.386  25.244  1.00 14.63           C  
ATOM    321  C   LEU A  56      24.065   3.877  25.444  1.00 15.25           C  
ATOM    322  O   LEU A  56      23.367   3.421  26.333  1.00 15.93           O  
ATOM    323  CB  LEU A  56      23.210   5.831  24.059  1.00 15.02           C  
ATOM    324  CG  LEU A  56      23.030   7.367  24.000  1.00 17.70           C  
ATOM    325  CD1 LEU A  56      22.600   7.707  22.556  1.00 16.43           C  
ATOM    326  CD2 LEU A  56      21.860   7.727  24.972  1.00 16.25           C  
ATOM    327  N   ASP A  57      24.838   3.101  24.675  1.00 14.23           N  
ATOM    328  CA  ASP A  57      24.918   1.621  24.926  1.00 16.14           C  
ATOM    329  C   ASP A  57      25.361   1.281  26.352  1.00 17.15           C  
ATOM    330  O   ASP A  57      24.827   0.349  26.994  1.00 15.64           O  
ATOM    331  CB  ASP A  57      25.899   0.918  23.955  1.00 15.12           C  
ATOM    332  CG  ASP A  57      25.402   0.874  22.526  1.00 18.13           C  
ATOM    333  OD1 ASP A  57      24.260   1.228  22.187  1.00 18.14           O  
ATOM    334  OD2 ASP A  57      26.179   0.456  21.683  1.00 18.31           O  
ATOM    335  N   LYS A  58      26.356   2.028  26.862  1.00 16.50           N  
ATOM    336  CA  LYS A  58      26.883   1.754  28.201  1.00 17.80           C  
ATOM    337  C   LYS A  58      25.903   1.988  29.321  1.00 17.64           C  
ATOM    338  O   LYS A  58      25.814   1.172  30.250  1.00 17.92           O  
ATOM    339  CB  LYS A  58      28.172   2.578  28.458  1.00 17.24           C  
ATOM    340  CG  LYS A  58      29.351   2.151  27.543  1.00 21.18           C  
ATOM    341  CD  LYS A  58      30.523   3.227  27.691  1.00 21.94           C  
ATOM    342  CE  LYS A  58      31.720   2.811  26.757  1.00 25.55           C  
ATOM    343  NZ  LYS A  58      32.591   4.037  26.772  1.00 32.42           N  
ATOM    344  N   ILE A  59      25.219   3.120  29.304  1.00 17.10           N  
ATOM    345  CA  ILE A  59      24.153   3.351  30.276  1.00 17.36           C  
ATOM    346  C   ILE A  59      22.962   2.380  30.134  1.00 18.26           C  
ATOM    347  O   ILE A  59      22.370   1.967  31.136  1.00 17.92           O  
ATOM    348  CB  ILE A  59      23.694   4.825  30.358  1.00 15.15           C  
ATOM    349  CG1 ILE A  59      22.740   5.087  31.570  1.00 18.98           C  
ATOM    350  CG2 ILE A  59      22.916   5.309  29.109  1.00 15.79           C  
ATOM    351  CD1 ILE A  59      23.398   4.811  32.977  1.00 19.38           C  
ATOM    352  N   ARG A  60      22.598   2.021  28.922  1.00 18.32           N  
ATOM    353  CA  ARG A  60      21.528   1.008  28.776  1.00 20.27           C  
ATOM    354  C   ARG A  60      22.010  -0.296  29.409  1.00 21.04           C  
ATOM    355  O   ARG A  60      21.309  -0.899  30.214  1.00 21.22           O  
ATOM    356  CB  ARG A  60      21.169   0.711  27.329  1.00 20.07           C  
ATOM    357  CG  ARG A  60      19.805  -0.084  27.261  1.00 26.62           C  
ATOM    358  CD  ARG A  60      19.428  -0.260  25.830  1.00 32.19           C  
ATOM    359  NE  ARG A  60      18.406   0.646  25.282  1.00 35.87           N  
ATOM    360  CZ  ARG A  60      18.381   0.944  23.981  1.00 36.38           C  
ATOM    361  NH1 ARG A  60      19.368   0.470  23.199  1.00 34.02           N  
ATOM    362  NH2 ARG A  60      17.439   1.727  23.464  1.00 33.60           N  
ATOM    363  N   TYR A  61      23.237  -0.690  29.108  1.00 21.26           N  
ATOM    364  CA  TYR A  61      23.745  -1.941  29.696  1.00 21.35           C  
ATOM    365  C   TYR A  61      23.711  -1.907  31.245  1.00 22.20           C  
ATOM    366  O   TYR A  61      23.253  -2.876  31.878  1.00 21.43           O  
ATOM    367  CB  TYR A  61      25.173  -2.296  29.200  1.00 21.03           C  
ATOM    368  CG  TYR A  61      25.620  -3.679  29.710  1.00 24.82           C  
ATOM    369  CD1 TYR A  61      25.096  -4.860  29.152  1.00 23.41           C  
ATOM    370  CD2 TYR A  61      26.557  -3.793  30.730  1.00 28.89           C  
ATOM    371  CE1 TYR A  61      25.484  -6.126  29.668  1.00 29.90           C  
ATOM    372  CE2 TYR A  61      26.940  -5.017  31.227  1.00 26.30           C  
ATOM    373  CZ  TYR A  61      26.420  -6.167  30.698  1.00 26.93           C  
ATOM    374  OH  TYR A  61      26.836  -7.385  31.206  1.00 28.36           O  
ATOM    375  N   GLU A  62      24.227  -0.847  31.869  1.00 21.41           N  
ATOM    376  CA  GLU A  62      24.168  -0.759  33.372  1.00 22.80           C  
ATOM    377  C   GLU A  62      22.756  -0.804  33.859  1.00 22.34           C  
ATOM    378  O   GLU A  62      22.470  -1.461  34.859  1.00 24.25           O  
ATOM    379  CB  GLU A  62      24.785   0.532  33.874  1.00 22.86           C  
ATOM    380  CG  GLU A  62      26.295   0.488  33.565  1.00 28.42           C  
ATOM    381  CD  GLU A  62      27.017   1.558  34.314  1.00 33.82           C  
ATOM    382  OE1 GLU A  62      26.356   2.427  34.920  1.00 36.59           O  
ATOM    383  OE2 GLU A  62      28.250   1.558  34.252  1.00 36.19           O  
ATOM    384  N   SER A  63      21.854  -0.148  33.140  1.00 21.59           N  
ATOM    385  CA  SER A  63      20.447  -0.082  33.585  1.00 21.49           C  
ATOM    386  C   SER A  63      19.752  -1.467  33.537  1.00 24.10           C  
ATOM    387  O   SER A  63      18.740  -1.667  34.172  1.00 22.25           O  
ATOM    388  CB  SER A  63      19.708   0.927  32.758  1.00 21.82           C  
ATOM    389  OG  SER A  63      19.248   0.362  31.491  1.00 22.52           O  
ATOM    390  N   LEU A  64      20.291  -2.404  32.755  1.00 25.13           N  
ATOM    391  CA  LEU A  64      19.684  -3.738  32.652  1.00 27.73           C  
ATOM    392  C   LEU A  64      19.714  -4.485  33.971  1.00 29.58           C  
ATOM    393  O   LEU A  64      18.892  -5.388  34.192  1.00 30.52           O  
ATOM    394  CB  LEU A  64      20.453  -4.590  31.630  1.00 27.03           C  
ATOM    395  CG  LEU A  64      20.304  -4.146  30.150  1.00 24.48           C  
ATOM    396  CD1 LEU A  64      20.985  -5.214  29.305  1.00 23.19           C  
ATOM    397  CD2 LEU A  64      18.853  -4.021  29.756  1.00 21.64           C  
ATOM    398  N   THR A  65      20.655  -4.128  34.843  1.00 29.35           N  
ATOM    399  CA  THR A  65      20.762  -4.779  36.136  1.00 32.02           C  
ATOM    400  C   THR A  65      20.552  -3.838  37.303  1.00 33.47           C  
ATOM    401  O   THR A  65      20.382  -4.267  38.438  1.00 34.32           O  
ATOM    402  CB  THR A  65      22.123  -5.466  36.331  1.00 31.41           C  
ATOM    403  OG1 THR A  65      23.181  -4.496  36.293  1.00 34.61           O  
ATOM    404  CG2 THR A  65      22.325  -6.443  35.238  1.00 30.82           C  
ATOM    405  N   ASP A  66      20.545  -2.543  37.033  1.00 33.36           N  
ATOM    406  CA  ASP A  66      20.207  -1.585  38.056  1.00 32.91           C  
ATOM    407  C   ASP A  66      19.399  -0.467  37.422  1.00 32.82           C  
ATOM    408  O   ASP A  66      19.966   0.476  36.834  1.00 33.41           O  
ATOM    409  CB  ASP A  66      21.485  -1.101  38.715  1.00 32.82           C  
ATOM    410  CG  ASP A  66      21.220  -0.013  39.711  1.00 33.46           C  
ATOM    411  OD1 ASP A  66      20.043   0.333  39.908  1.00 36.01           O  
ATOM    412  OD2 ASP A  66      22.183   0.540  40.238  1.00 33.06           O  
ATOM    413  N   PRO A  67      18.056  -0.566  37.487  1.00 33.65           N  
ATOM    414  CA  PRO A  67      17.194   0.422  36.819  1.00 33.24           C  
ATOM    415  C   PRO A  67      17.336   1.832  37.374  1.00 31.94           C  
ATOM    416  O   PRO A  67      17.037   2.795  36.685  1.00 31.50           O  
ATOM    417  CB  PRO A  67      15.777  -0.120  37.067  1.00 33.97           C  
ATOM    418  CG  PRO A  67      16.002  -1.567  37.268  1.00 35.25           C  
ATOM    419  CD  PRO A  67      17.253  -1.638  38.096  1.00 33.49           C  
ATOM    420  N   SER A  68      17.807   1.969  38.608  1.00 30.96           N  
ATOM    421  CA  SER A  68      17.958   3.310  39.166  1.00 28.80           C  
ATOM    422  C   SER A  68      19.067   4.128  38.411  1.00 27.96           C  
ATOM    423  O   SER A  68      19.084   5.369  38.479  1.00 26.99           O  
ATOM    424  CB  SER A  68      18.240   3.252  40.659  1.00 28.48           C  
ATOM    425  OG  SER A  68      19.582   2.828  40.852  1.00 29.05           O  
ATOM    426  N   LYS A  69      19.954   3.444  37.680  1.00 27.37           N  
ATOM    427  CA  LYS A  69      20.933   4.159  36.809  1.00 26.88           C  
ATOM    428  C   LYS A  69      20.230   5.152  35.895  1.00 25.60           C  
ATOM    429  O   LYS A  69      20.834   6.126  35.403  1.00 24.21           O  
ATOM    430  CB  LYS A  69      21.693   3.165  35.966  1.00 26.04           C  
ATOM    431  CG  LYS A  69      22.524   2.218  36.812  1.00 29.93           C  
ATOM    432  CD  LYS A  69      23.812   2.868  37.184  1.00 29.10           C  
ATOM    433  CE  LYS A  69      24.715   1.881  37.913  1.00 26.47           C  
ATOM    434  NZ  LYS A  69      26.078   2.196  37.524  1.00 35.34           N  
ATOM    435  N   LEU A  70      18.959   4.908  35.614  1.00 23.98           N  
ATOM    436  CA  LEU A  70      18.222   5.814  34.760  1.00 23.13           C  
ATOM    437  C   LEU A  70      17.372   6.841  35.509  1.00 23.46           C  
ATOM    438  O   LEU A  70      16.565   7.500  34.858  1.00 20.61           O  
ATOM    439  CB  LEU A  70      17.309   5.087  33.702  1.00 23.26           C  
ATOM    440  CG  LEU A  70      17.937   4.019  32.746  1.00 25.21           C  
ATOM    441  CD1 LEU A  70      16.945   3.224  31.803  1.00 22.27           C  
ATOM    442  CD2 LEU A  70      19.006   4.725  31.901  1.00 25.61           C  
ATOM    443  N   ASP A  71      17.534   6.976  36.822  1.00 23.29           N  
ATOM    444  CA  ASP A  71      16.828   8.068  37.534  1.00 25.77           C  
ATOM    445  C   ASP A  71      17.208   9.462  36.997  1.00 26.23           C  
ATOM    446  O   ASP A  71      16.398  10.380  36.994  1.00 27.73           O  
ATOM    447  CB  ASP A  71      17.135   7.976  39.063  1.00 26.02           C  
ATOM    448  CG  ASP A  71      16.465   6.747  39.708  1.00 30.96           C  
ATOM    449  OD1 ASP A  71      15.525   6.214  39.081  1.00 34.83           O  
ATOM    450  OD2 ASP A  71      16.908   6.307  40.782  1.00 31.72           O  
ATOM    451  N   SER A  72      18.415   9.604  36.466  1.00 27.40           N  
ATOM    452  CA  SER A  72      18.906  10.892  35.988  1.00 26.03           C  
ATOM    453  C   SER A  72      18.418  11.136  34.548  1.00 27.34           C  
ATOM    454  O   SER A  72      18.790  12.142  33.893  1.00 27.20           O  
ATOM    455  CB  SER A  72      20.429  10.855  36.072  1.00 26.64           C  
ATOM    456  OG  SER A  72      20.897   9.660  35.412  1.00 24.86           O  
ATOM    457  N   GLY A  73      17.532  10.264  34.062  1.00 26.98           N  
ATOM    458  CA  GLY A  73      16.913  10.455  32.739  1.00 26.25           C  
ATOM    459  C   GLY A  73      16.661   9.113  31.996  1.00 27.07           C  
ATOM    460  O   GLY A  73      17.578   8.396  31.646  1.00 26.94           O  
ATOM    461  N   LYS A  74      15.405   8.768  31.723  1.00 27.39           N  
ATOM    462  CA  LYS A  74      15.117   7.477  31.088  1.00 27.81           C  
ATOM    463  C   LYS A  74      15.313   7.547  29.564  1.00 25.53           C  
ATOM    464  O   LYS A  74      15.563   6.524  28.951  1.00 24.19           O  
ATOM    465  CB  LYS A  74      13.655   7.024  31.360  1.00 29.09           C  
ATOM    466  CG  LYS A  74      13.366   6.851  32.831  1.00 34.91           C  
ATOM    467  CD  LYS A  74      12.008   6.219  33.039  1.00 43.06           C  
ATOM    468  CE  LYS A  74      11.767   6.178  34.531  1.00 47.67           C  
ATOM    469  NZ  LYS A  74      12.793   5.293  35.115  1.00 49.28           N  
ATOM    470  N   GLU A  75      15.146   8.705  28.946  1.00 20.98           N  
ATOM    471  CA  GLU A  75      15.108   8.680  27.479  1.00 23.38           C  
ATOM    472  C   GLU A  75      16.541   8.584  26.920  1.00 21.45           C  
ATOM    473  O   GLU A  75      17.405   9.322  27.389  1.00 24.21           O  
ATOM    474  CB  GLU A  75      14.599  10.002  26.941  1.00 23.53           C  
ATOM    475  CG  GLU A  75      13.093  10.313  26.957  1.00 32.54           C  
ATOM    476  CD  GLU A  75      12.842  11.705  26.314  1.00 42.75           C  
ATOM    477  OE1 GLU A  75      11.840  11.889  25.535  1.00 51.72           O  
ATOM    478  OE2 GLU A  75      13.682  12.618  26.576  1.00 45.21           O  
ATOM    479  N   LEU A  76      16.812   7.678  25.993  1.00 19.77           N  
ATOM    480  CA  LEU A  76      18.174   7.483  25.433  1.00 18.79           C  
ATOM    481  C   LEU A  76      18.092   7.970  24.036  1.00 18.65           C  
ATOM    482  O   LEU A  76      17.451   7.290  23.158  1.00 16.82           O  
ATOM    483  CB  LEU A  76      18.574   6.024  25.479  1.00 18.69           C  
ATOM    484  CG  LEU A  76      18.633   5.380  26.867  1.00 20.51           C  
ATOM    485  CD1 LEU A  76      19.183   3.929  26.817  1.00 23.20           C  
ATOM    486  CD2 LEU A  76      19.424   6.273  27.790  1.00 17.43           C  
ATOM    487  N   HIS A  77      18.711   9.146  23.780  1.00 17.88           N  
ATOM    488  CA  HIS A  77      18.621   9.796  22.472  1.00 16.92           C  
ATOM    489  C   HIS A  77      19.790  10.714  22.161  1.00 14.32           C  
ATOM    490  O   HIS A  77      20.607  11.018  23.039  1.00 13.26           O  
ATOM    491  CB  HIS A  77      17.328  10.624  22.319  1.00 20.72           C  
ATOM    492  CG  HIS A  77      17.246  11.775  23.269  1.00 22.37           C  
ATOM    493  ND1 HIS A  77      16.178  11.987  24.099  1.00 29.01           N  
ATOM    494  CD2 HIS A  77      18.129  12.769  23.541  1.00 25.95           C  
ATOM    495  CE1 HIS A  77      16.365  13.091  24.788  1.00 20.69           C  
ATOM    496  NE2 HIS A  77      17.559  13.558  24.497  1.00 24.35           N  
ATOM    497  N   ILE A  78      19.862  11.101  20.900  1.00 11.77           N  
ATOM    498  CA  ILE A  78      20.804  12.101  20.373  1.00 13.58           C  
ATOM    499  C   ILE A  78      20.122  13.279  19.681  1.00 14.97           C  
ATOM    500  O   ILE A  78      19.238  13.082  18.832  1.00 15.86           O  
ATOM    501  CB  ILE A  78      21.669  11.391  19.300  1.00 14.93           C  
ATOM    502  CG1 ILE A  78      22.327  10.195  19.970  1.00 10.88           C  
ATOM    503  CG2 ILE A  78      22.614  12.396  18.615  1.00 11.44           C  
ATOM    504  CD1 ILE A  78      23.025   9.217  18.969  1.00 18.41           C  
ATOM    505  N   ASN A  79      20.477  14.501  20.072  1.00 15.11           N  
ATOM    506  CA  ASN A  79      19.965  15.678  19.419  1.00 15.18           C  
ATOM    507  C   ASN A  79      21.131  16.400  18.731  1.00 15.67           C  
ATOM    508  O   ASN A  79      22.241  16.497  19.291  1.00 14.62           O  
ATOM    509  CB  ASN A  79      19.352  16.659  20.472  1.00 15.44           C  
ATOM    510  CG  ASN A  79      18.146  16.071  21.220  1.00 17.54           C  
ATOM    511  OD1 ASN A  79      17.894  16.408  22.392  1.00 20.68           O  
ATOM    512  ND2 ASN A  79      17.430  15.196  20.568  1.00 10.69           N  
ATOM    513  N   LEU A  80      20.820  16.968  17.556  1.00 13.92           N  
ATOM    514  CA  LEU A  80      21.743  17.777  16.798  1.00 13.75           C  
ATOM    515  C   LEU A  80      21.166  19.170  16.790  1.00 15.80           C  
ATOM    516  O   LEU A  80      20.069  19.375  16.258  1.00 15.08           O  
ATOM    517  CB  LEU A  80      21.784  17.250  15.384  1.00 12.56           C  
ATOM    518  CG  LEU A  80      22.133  15.690  15.315  1.00 11.60           C  
ATOM    519  CD1 LEU A  80      22.313  15.392  13.873  1.00 13.44           C  
ATOM    520  CD2 LEU A  80      23.463  15.389  15.965  1.00 11.77           C  
ATOM    521  N   ILE A  81      21.912  20.141  17.314  1.00 13.95           N  
ATOM    522  CA  ILE A  81      21.368  21.491  17.420  1.00 14.76           C  
ATOM    523  C   ILE A  81      22.253  22.536  16.742  1.00 15.08           C  
ATOM    524  O   ILE A  81      23.246  22.943  17.312  1.00 15.22           O  
ATOM    525  CB  ILE A  81      21.148  21.883  18.914  1.00 14.04           C  
ATOM    526  CG1 ILE A  81      20.454  20.716  19.662  1.00 13.98           C  
ATOM    527  CG2 ILE A  81      20.435  23.287  19.004  1.00 14.04           C  
ATOM    528  CD1 ILE A  81      20.262  20.954  21.238  1.00 18.24           C  
ATOM    529  N   PRO A  82      21.870  22.966  15.534  1.00 16.11           N  
ATOM    530  CA  PRO A  82      22.626  24.006  14.873  1.00 16.18           C  
ATOM    531  C   PRO A  82      22.128  25.371  15.431  1.00 18.82           C  
ATOM    532  O   PRO A  82      20.897  25.543  15.736  1.00 17.80           O  
ATOM    533  CB  PRO A  82      22.261  23.813  13.384  1.00 15.75           C  
ATOM    534  CG  PRO A  82      20.812  23.189  13.412  1.00 15.81           C  
ATOM    535  CD  PRO A  82      20.674  22.542  14.775  1.00 15.34           C  
ATOM    536  N   ASN A  83      23.065  26.307  15.548  1.00 20.06           N  
ATOM    537  CA  ASN A  83      22.763  27.672  15.945  1.00 22.14           C  
ATOM    538  C   ASN A  83      23.592  28.645  15.121  1.00 22.88           C  
ATOM    539  O   ASN A  83      24.807  28.826  15.340  1.00 23.19           O  
ATOM    540  CB  ASN A  83      23.026  27.877  17.430  1.00 20.40           C  
ATOM    541  CG  ASN A  83      22.508  29.232  17.880  1.00 26.55           C  
ATOM    542  OD1 ASN A  83      22.899  30.255  17.318  1.00 26.75           O  
ATOM    543  ND2 ASN A  83      21.625  29.246  18.857  1.00 27.42           N  
ATOM    544  N   LYS A  84      22.966  29.222  14.115  1.00 26.22           N  
ATOM    545  CA  LYS A  84      23.708  30.109  13.209  1.00 28.17           C  
ATOM    546  C   LYS A  84      24.191  31.405  13.847  1.00 28.18           C  
ATOM    547  O   LYS A  84      25.229  31.912  13.454  1.00 26.94           O  
ATOM    548  CB  LYS A  84      22.923  30.379  11.917  1.00 28.45           C  
ATOM    549  CG  LYS A  84      22.762  29.126  11.095  1.00 28.95           C  
ATOM    550  CD  LYS A  84      22.024  29.298   9.758  1.00 31.25           C  
ATOM    551  CE  LYS A  84      21.290  28.043   9.380  1.00 30.69           C  
ATOM    552  NZ  LYS A  84      21.000  28.143   7.942  1.00 39.05           N  
ATOM    553  N   GLN A  85      23.497  31.907  14.870  1.00 29.58           N  
ATOM    554  CA  GLN A  85      23.946  33.156  15.502  1.00 30.95           C  
ATOM    555  C   GLN A  85      25.286  32.967  16.209  1.00 30.38           C  
ATOM    556  O   GLN A  85      26.174  33.794  16.065  1.00 31.42           O  
ATOM    557  CB  GLN A  85      22.872  33.752  16.461  1.00 32.16           C  
ATOM    558  CG  GLN A  85      21.640  34.313  15.708  1.00 36.43           C  
ATOM    559  CD  GLN A  85      20.777  33.207  15.072  1.00 42.64           C  
ATOM    560  OE1 GLN A  85      20.508  32.169  15.709  1.00 49.32           O  
ATOM    561  NE2 GLN A  85      20.344  33.416  13.824  1.00 41.46           N  
ATOM    562  N   ASP A  86      25.438  31.867  16.931  1.00 27.56           N  
ATOM    563  CA  ASP A  86      26.631  31.579  17.707  1.00 25.68           C  
ATOM    564  C   ASP A  86      27.633  30.780  16.866  1.00 21.75           C  
ATOM    565  O   ASP A  86      28.724  30.541  17.315  1.00 21.74           O  
ATOM    566  CB  ASP A  86      26.297  30.668  18.870  1.00 25.78           C  
ATOM    567  CG  ASP A  86      25.248  31.246  19.754  1.00 34.22           C  
ATOM    568  OD1 ASP A  86      25.019  32.477  19.653  1.00 33.01           O  
ATOM    569  OD2 ASP A  86      24.674  30.482  20.549  1.00 34.12           O  
ATOM    570  N   ARG A  87      27.237  30.389  15.671  1.00 21.67           N  
ATOM    571  CA  ARG A  87      28.061  29.556  14.782  1.00 18.81           C  
ATOM    572  C   ARG A  87      28.469  28.238  15.474  1.00 19.09           C  
ATOM    573  O   ARG A  87      29.645  27.831  15.445  1.00 18.93           O  
ATOM    574  CB  ARG A  87      29.296  30.331  14.245  1.00 21.67           C  
ATOM    575  CG  ARG A  87      29.742  29.690  12.950  1.00 18.92           C  
ATOM    576  CD  ARG A  87      31.189  29.929  12.547  1.00 29.26           C  
ATOM    577  NE  ARG A  87      31.443  31.323  12.484  1.00 35.20           N  
ATOM    578  CZ  ARG A  87      32.631  31.879  12.692  1.00 34.60           C  
ATOM    579  NH1 ARG A  87      33.704  31.182  12.989  1.00 30.46           N  
ATOM    580  NH2 ARG A  87      32.720  33.160  12.597  1.00 33.38           N  
ATOM    581  N   THR A  88      27.488  27.515  16.038  1.00 17.08           N  
ATOM    582  CA  THR A  88      27.782  26.284  16.746  1.00 17.24           C  
ATOM    583  C   THR A  88      26.900  25.172  16.241  1.00 16.18           C  
ATOM    584  O   THR A  88      25.706  25.388  15.882  1.00 17.97           O  
ATOM    585  CB  THR A  88      27.536  26.385  18.328  1.00 18.10           C  
ATOM    586  OG1 THR A  88      26.214  26.862  18.545  1.00 18.27           O  
ATOM    587  CG2 THR A  88      28.603  27.264  19.016  1.00 18.68           C  
ATOM    588  N   LEU A  89      27.493  23.976  16.202  1.00 16.48           N  
ATOM    589  CA  LEU A  89      26.710  22.758  16.028  1.00 16.19           C  
ATOM    590  C   LEU A  89      26.897  21.979  17.329  1.00 16.71           C  
ATOM    591  O   LEU A  89      28.031  21.614  17.696  1.00 14.65           O  
ATOM    592  CB  LEU A  89      27.202  21.930  14.821  1.00 15.34           C  
ATOM    593  CG  LEU A  89      26.388  20.584  14.705  1.00 14.66           C  
ATOM    594  CD1 LEU A  89      24.876  20.926  14.522  1.00 15.43           C  
ATOM    595  CD2 LEU A  89      27.010  19.902  13.426  1.00 14.84           C  
ATOM    596  N   THR A  90      25.786  21.668  18.032  1.00 16.05           N  
ATOM    597  CA  THR A  90      25.950  20.946  19.260  1.00 15.50           C  
ATOM    598  C   THR A  90      25.337  19.574  19.096  1.00 15.70           C  
ATOM    599  O   THR A  90      24.232  19.456  18.576  1.00 15.77           O  
ATOM    600  CB  THR A  90      25.197  21.671  20.430  1.00 15.69           C  
ATOM    601  OG1 THR A  90      25.762  22.987  20.520  1.00 16.23           O  
ATOM    602  CG2 THR A  90      25.276  20.887  21.776  1.00 18.13           C  
ATOM    603  N   ILE A  91      26.069  18.564  19.535  1.00 14.63           N  
ATOM    604  CA  ILE A  91      25.550  17.205  19.590  1.00 15.43           C  
ATOM    605  C   ILE A  91      25.329  16.840  21.087  1.00 15.79           C  
ATOM    606  O   ILE A  91      26.300  16.782  21.896  1.00 14.17           O  
ATOM    607  CB  ILE A  91      26.522  16.233  18.921  1.00 15.28           C  
ATOM    608  CG1 ILE A  91      26.782  16.619  17.431  1.00 17.35           C  
ATOM    609  CG2 ILE A  91      26.061  14.780  19.065  1.00 13.53           C  
ATOM    610  CD1 ILE A  91      27.982  17.481  17.187  1.00 24.14           C  
ATOM    611  N   VAL A  92      24.108  16.443  21.397  1.00 13.07           N  
ATOM    612  CA  VAL A  92      23.810  16.087  22.779  1.00 14.23           C  
ATOM    613  C   VAL A  92      23.359  14.701  22.799  1.00 15.27           C  
ATOM    614  O   VAL A  92      22.481  14.316  21.960  1.00 16.90           O  
ATOM    615  CB  VAL A  92      22.538  16.915  23.321  1.00 13.63           C  
ATOM    616  CG1 VAL A  92      22.348  16.682  24.814  1.00 14.72           C  
ATOM    617  CG2 VAL A  92      22.715  18.458  23.036  1.00 16.73           C  
ATOM    618  N   ASP A  93      23.805  13.953  23.830  1.00 15.10           N  
ATOM    619  CA  ASP A  93      23.312  12.580  24.023  1.00 15.65           C  
ATOM    620  C   ASP A  93      22.957  12.424  25.503  1.00 16.07           C  
ATOM    621  O   ASP A  93      23.421  13.231  26.338  1.00 15.53           O  
ATOM    622  CB  ASP A  93      24.301  11.477  23.539  1.00 15.30           C  
ATOM    623  CG  ASP A  93      25.567  11.413  24.380  1.00 15.87           C  
ATOM    624  OD1 ASP A  93      25.548  11.082  25.590  1.00 17.58           O  
ATOM    625  OD2 ASP A  93      26.610  11.673  23.792  1.00 15.53           O  
ATOM    626  N   THR A  94      22.122  11.431  25.821  1.00 14.13           N  
ATOM    627  CA  THR A  94      21.833  11.132  27.258  1.00 14.07           C  
ATOM    628  C   THR A  94      22.481   9.787  27.610  1.00 15.95           C  
ATOM    629  O   THR A  94      21.877   8.940  28.276  1.00 15.78           O  
ATOM    630  CB  THR A  94      20.273  11.019  27.471  1.00 15.53           C  
ATOM    631  OG1 THR A  94      19.732  10.234  26.422  1.00 15.60           O  
ATOM    632  CG2 THR A  94      19.652  12.477  27.381  1.00 15.55           C  
ATOM    633  N   GLY A  95      23.728   9.600  27.131  1.00 16.47           N  
ATOM    634  CA  GLY A  95      24.481   8.411  27.406  1.00 13.43           C  
ATOM    635  C   GLY A  95      25.050   8.495  28.822  1.00 15.20           C  
ATOM    636  O   GLY A  95      24.589   9.245  29.740  1.00 14.93           O  
ATOM    637  N   ILE A  96      26.034   7.661  29.026  1.00 14.99           N  
ATOM    638  CA  ILE A  96      26.573   7.466  30.376  1.00 16.59           C  
ATOM    639  C   ILE A  96      27.337   8.671  30.890  1.00 17.08           C  
ATOM    640  O   ILE A  96      27.471   8.823  32.109  1.00 18.22           O  
ATOM    641  CB  ILE A  96      27.381   6.133  30.455  1.00 16.42           C  
ATOM    642  CG1 ILE A  96      27.569   5.668  31.925  1.00 18.63           C  
ATOM    643  CG2 ILE A  96      28.761   6.208  29.708  1.00 12.31           C  
ATOM    644  CD1 ILE A  96      28.163   4.253  31.954  1.00 24.30           C  
ATOM    645  N   GLY A  97      27.795   9.586  30.009  1.00 15.79           N  
ATOM    646  CA  GLY A  97      28.529  10.756  30.561  1.00 14.02           C  
ATOM    647  C   GLY A  97      29.932  10.376  30.945  1.00 14.39           C  
ATOM    648  O   GLY A  97      30.383   9.237  30.761  1.00 14.93           O  
ATOM    649  N   MET A  98      30.682  11.347  31.436  1.00 15.97           N  
ATOM    650  CA  MET A  98      32.079  11.086  31.799  1.00 15.11           C  
ATOM    651  C   MET A  98      32.372  11.755  33.149  1.00 15.30           C  
ATOM    652  O   MET A  98      31.850  12.859  33.459  1.00 15.22           O  
ATOM    653  CB  MET A  98      33.032  11.693  30.736  1.00 15.90           C  
ATOM    654  CG  MET A  98      33.004  10.982  29.393  1.00 18.93           C  
ATOM    655  SD  MET A  98      34.108  11.812  28.194  1.00 18.57           S  
ATOM    656  CE  MET A  98      32.926  13.076  27.570  1.00 13.92           C  
ATOM    657  N   THR A  99      33.222  11.073  33.921  1.00 18.13           N  
ATOM    658  CA  THR A  99      33.704  11.620  35.183  1.00 18.84           C  
ATOM    659  C   THR A  99      34.810  12.641  34.852  1.00 19.65           C  
ATOM    660  O   THR A  99      35.327  12.705  33.734  1.00 15.81           O  
ATOM    661  CB  THR A  99      34.344  10.536  36.018  1.00 19.36           C  
ATOM    662  OG1 THR A  99      35.452   9.972  35.297  1.00 18.57           O  
ATOM    663  CG2 THR A  99      33.284   9.348  36.342  1.00 20.45           C  
ATOM    664  N   LYS A 100      35.179  13.424  35.859  1.00 21.52           N  
ATOM    665  CA  LYS A 100      36.245  14.396  35.685  1.00 21.44           C  
ATOM    666  C   LYS A 100      37.511  13.664  35.247  1.00 21.08           C  
ATOM    667  O   LYS A 100      38.239  14.121  34.357  1.00 20.91           O  
ATOM    668  CB  LYS A 100      36.448  15.174  37.013  1.00 21.81           C  
ATOM    669  CG  LYS A 100      37.510  16.322  36.836  1.00 25.24           C  
ATOM    670  CD  LYS A 100      37.864  16.989  38.179  1.00 24.82           C  
ATOM    671  CE  LYS A 100      38.744  18.222  37.887  1.00 22.69           C  
ATOM    672  NZ  LYS A 100      39.527  18.466  39.111  1.00 26.42           N  
ATOM    673  N   ALA A 101      37.784  12.517  35.875  1.00 20.97           N  
ATOM    674  CA  ALA A 101      38.947  11.678  35.603  1.00 21.60           C  
ATOM    675  C   ALA A 101      38.909  11.200  34.141  1.00 21.68           C  
ATOM    676  O   ALA A 101      39.917  11.225  33.463  1.00 21.88           O  
ATOM    677  CB  ALA A 101      38.996  10.468  36.557  1.00 22.16           C  
ATOM    678  N   ASP A 102      37.745  10.760  33.668  1.00 21.31           N  
ATOM    679  CA  ASP A 102      37.609  10.320  32.261  1.00 22.28           C  
ATOM    680  C   ASP A 102      37.941  11.520  31.346  1.00 19.99           C  
ATOM    681  O   ASP A 102      38.672  11.368  30.349  1.00 20.91           O  
ATOM    682  CB  ASP A 102      36.153   9.903  31.950  1.00 23.25           C  
ATOM    683  CG  ASP A 102      35.753   8.528  32.510  1.00 25.73           C  
ATOM    684  OD1 ASP A 102      36.651   7.647  32.634  1.00 26.27           O  
ATOM    685  OD2 ASP A 102      34.488   8.384  32.765  1.00 25.72           O  
ATOM    686  N   LEU A 103      37.394  12.699  31.648  1.00 20.64           N  
ATOM    687  CA  LEU A 103      37.577  13.882  30.780  1.00 20.64           C  
ATOM    688  C   LEU A 103      39.050  14.185  30.623  1.00 20.86           C  
ATOM    689  O   LEU A 103      39.593  14.369  29.487  1.00 17.51           O  
ATOM    690  CB  LEU A 103      36.967  15.137  31.381  1.00 20.51           C  
ATOM    691  CG  LEU A 103      35.539  15.471  31.064  1.00 20.03           C  
ATOM    692  CD1 LEU A 103      35.123  16.803  31.825  1.00 17.05           C  
ATOM    693  CD2 LEU A 103      35.080  15.480  29.518  1.00 16.64           C  
ATOM    694  N   ILE A 104      39.731  14.164  31.764  1.00 20.00           N  
ATOM    695  CA  ILE A 104      41.177  14.485  31.723  1.00 21.42           C  
ATOM    696  C   ILE A 104      41.989  13.425  30.987  1.00 20.95           C  
ATOM    697  O   ILE A 104      42.950  13.736  30.256  1.00 22.49           O  
ATOM    698  CB  ILE A 104      41.729  14.636  33.149  1.00 22.78           C  
ATOM    699  CG1 ILE A 104      41.158  15.893  33.759  1.00 23.22           C  
ATOM    700  CG2 ILE A 104      43.333  14.568  33.147  1.00 19.35           C  
ATOM    701  CD1 ILE A 104      41.399  16.021  35.376  1.00 23.01           C  
ATOM    702  N   ASN A 105      41.625  12.171  31.208  1.00 18.89           N  
ATOM    703  CA AASN A 105      42.268  11.059  30.546  0.50 19.53           C  
ATOM    704  CA BASN A 105      42.265  11.075  30.532  0.50 19.73           C  
ATOM    705  C   ASN A 105      41.734  10.874  29.111  1.00 19.47           C  
ATOM    706  O   ASN A 105      41.153   9.809  28.761  1.00 18.59           O  
ATOM    707  CB AASN A 105      42.008   9.795  31.375  0.50 19.78           C  
ATOM    708  CB BASN A 105      42.081   9.801  31.347  0.50 20.16           C  
ATOM    709  CG AASN A 105      42.870   8.618  30.974  0.50 20.70           C  
ATOM    710  CG BASN A 105      42.968   9.775  32.560  0.50 22.05           C  
ATOM    711  OD1AASN A 105      43.792   8.724  30.161  0.50 24.81           O  
ATOM    712  OD1BASN A 105      44.081   9.276  32.480  0.50 27.18           O  
ATOM    713  ND2AASN A 105      42.558   7.469  31.558  0.50 24.43           N  
ATOM    714  ND2BASN A 105      42.500  10.330  33.679  0.50 26.35           N  
ATOM    715  N   ASN A 106      41.874  11.914  28.305  1.00 18.58           N  
ATOM    716  CA  ASN A 106      41.474  11.855  26.889  1.00 16.65           C  
ATOM    717  C   ASN A 106      40.009  11.493  26.651  1.00 18.43           C  
ATOM    718  O   ASN A 106      39.710  10.729  25.748  1.00 16.09           O  
ATOM    719  CB  ASN A 106      42.484  10.961  26.087  1.00 17.14           C  
ATOM    720  CG  ASN A 106      43.909  11.460  26.240  1.00 17.71           C  
ATOM    721  OD1 ASN A 106      44.176  12.634  26.041  1.00 19.60           O  
ATOM    722  ND2 ASN A 106      44.835  10.562  26.547  1.00 17.64           N  
ATOM    723  N   LEU A 107      39.094  12.076  27.437  1.00 15.51           N  
ATOM    724  CA  LEU A 107      37.672  11.836  27.246  1.00 18.11           C  
ATOM    725  C   LEU A 107      37.360  10.315  27.218  1.00 19.02           C  
ATOM    726  O   LEU A 107      36.602   9.842  26.382  1.00 16.72           O  
ATOM    727  CB  LEU A 107      37.121  12.614  25.988  1.00 16.53           C  
ATOM    728  CG  LEU A 107      37.384  14.173  26.078  1.00 17.61           C  
ATOM    729  CD1 LEU A 107      38.664  14.559  25.310  1.00 15.96           C  
ATOM    730  CD2 LEU A 107      36.260  14.894  25.469  1.00 22.13           C  
ATOM    731  N   GLY A 108      37.958   9.591  28.164  1.00 19.47           N  
ATOM    732  CA  GLY A 108      37.717   8.143  28.351  1.00 22.63           C  
ATOM    733  C   GLY A 108      38.219   7.254  27.206  1.00 23.63           C  
ATOM    734  O   GLY A 108      37.662   6.159  26.962  1.00 24.79           O  
ATOM    735  N   THR A 109      39.223   7.695  26.464  1.00 21.50           N  
ATOM    736  CA  THR A 109      39.610   6.905  25.274  1.00 23.02           C  
ATOM    737  C   THR A 109      40.997   6.375  25.568  1.00 22.08           C  
ATOM    738  O   THR A 109      41.617   6.804  26.573  1.00 21.84           O  
ATOM    739  CB  THR A 109      39.658   7.761  23.971  1.00 22.82           C  
ATOM    740  OG1 THR A 109      40.700   8.751  24.055  1.00 23.05           O  
ATOM    741  CG2 THR A 109      38.312   8.467  23.749  1.00 22.95           C  
ATOM    742  N   ILE A 110      41.505   5.494  24.720  1.00 21.21           N  
ATOM    743  CA  ILE A 110      42.902   5.069  24.854  1.00 21.80           C  
ATOM    744  C   ILE A 110      43.716   5.806  23.788  1.00 22.02           C  
ATOM    745  O   ILE A 110      44.319   5.222  22.870  1.00 20.45           O  
ATOM    746  CB  ILE A 110      43.104   3.498  24.817  1.00 23.82           C  
ATOM    747  CG1 ILE A 110      42.338   2.807  23.652  1.00 24.22           C  
ATOM    748  CG2 ILE A 110      42.737   2.855  26.167  1.00 23.44           C  
ATOM    749  CD1 ILE A 110      42.895   1.333  23.549  1.00 25.51           C  
ATOM    750  N   ALA A 111      43.692   7.119  23.899  1.00 20.97           N  
ATOM    751  CA  ALA A 111      44.065   7.930  22.799  1.00 21.72           C  
ATOM    752  C   ALA A 111      45.535   7.781  22.511  1.00 21.73           C  
ATOM    753  O   ALA A 111      45.949   7.808  21.355  1.00 21.08           O  
ATOM    754  CB  ALA A 111      43.685   9.420  23.067  1.00 22.89           C  
ATOM    755  N   LYS A 112      46.342   7.529  23.517  1.00 22.23           N  
ATOM    756  CA  LYS A 112      47.759   7.321  23.163  1.00 24.98           C  
ATOM    757  C   LYS A 112      48.062   6.099  22.201  1.00 25.18           C  
ATOM    758  O   LYS A 112      48.674   6.259  21.143  1.00 23.22           O  
ATOM    759  CB  LYS A 112      48.674   7.391  24.390  1.00 24.62           C  
ATOM    760  CG  LYS A 112      50.083   7.124  24.068  1.00 29.43           C  
ATOM    761  CD  LYS A 112      50.927   7.356  25.329  1.00 32.08           C  
ATOM    762  CE  LYS A 112      52.004   6.313  25.368  1.00 39.12           C  
ATOM    763  NZ  LYS A 112      53.017   6.720  26.402  1.00 45.32           N  
ATOM    764  N   SER A 113      47.593   4.915  22.549  1.00 24.19           N  
ATOM    765  CA  SER A 113      47.776   3.779  21.701  1.00 24.96           C  
ATOM    766  C   SER A 113      46.879   3.885  20.464  1.00 24.23           C  
ATOM    767  O   SER A 113      47.281   3.414  19.446  1.00 23.80           O  
ATOM    768  CB  SER A 113      47.550   2.450  22.450  1.00 25.27           C  
ATOM    769  OG  SER A 113      46.217   2.395  22.957  1.00 29.69           O  
ATOM    770  N   GLY A 114      45.687   4.495  20.522  1.00 22.20           N  
ATOM    771  CA  GLY A 114      44.914   4.576  19.255  1.00 23.03           C  
ATOM    772  C   GLY A 114      45.590   5.525  18.293  1.00 22.65           C  
ATOM    773  O   GLY A 114      45.673   5.278  17.069  1.00 21.08           O  
ATOM    774  N   THR A 115      46.125   6.636  18.807  1.00 22.73           N  
ATOM    775  CA  THR A 115      46.869   7.506  17.930  1.00 23.97           C  
ATOM    776  C   THR A 115      48.067   6.772  17.270  1.00 25.74           C  
ATOM    777  O   THR A 115      48.295   6.890  16.036  1.00 24.79           O  
ATOM    778  CB  THR A 115      47.401   8.782  18.639  1.00 24.56           C  
ATOM    779  OG1 THR A 115      46.290   9.529  19.130  1.00 25.87           O  
ATOM    780  CG2 THR A 115      48.171   9.641  17.635  1.00 23.18           C  
ATOM    781  N   LYS A 116      48.797   6.008  18.048  1.00 26.03           N  
ATOM    782  CA  LYS A 116      49.861   5.217  17.493  1.00 27.43           C  
ATOM    783  C   LYS A 116      49.371   4.328  16.367  1.00 26.95           C  
ATOM    784  O   LYS A 116      49.891   4.345  15.325  1.00 28.63           O  
ATOM    785  CB  LYS A 116      50.545   4.397  18.566  1.00 28.33           C  
ATOM    786  CG  LYS A 116      51.799   3.723  18.068  1.00 34.65           C  
ATOM    787  CD  LYS A 116      52.225   2.655  18.976  1.00 42.47           C  
ATOM    788  CE  LYS A 116      53.371   1.883  18.447  1.00 45.78           C  
ATOM    789  NZ  LYS A 116      52.970   0.520  18.626  1.00 47.57           N  
ATOM    790  N   ALA A 117      48.366   3.532  16.600  1.00 27.66           N  
ATOM    791  CA  ALA A 117      47.932   2.674  15.524  1.00 28.22           C  
ATOM    792  C   ALA A 117      47.393   3.528  14.344  1.00 28.44           C  
ATOM    793  O   ALA A 117      47.585   3.207  13.150  1.00 27.27           O  
ATOM    794  CB  ALA A 117      46.916   1.716  16.030  1.00 27.26           C  
ATOM    795  N   PHE A 118      46.725   4.654  14.633  1.00 27.47           N  
ATOM    796  CA  PHE A 118      46.120   5.401  13.510  1.00 26.13           C  
ATOM    797  C   PHE A 118      47.270   5.911  12.665  1.00 28.75           C  
ATOM    798  O   PHE A 118      47.241   5.902  11.419  1.00 27.84           O  
ATOM    799  CB  PHE A 118      45.287   6.570  14.044  1.00 25.06           C  
ATOM    800  CG  PHE A 118      44.679   7.456  13.015  1.00 24.15           C  
ATOM    801  CD1 PHE A 118      44.057   6.935  11.867  1.00 24.36           C  
ATOM    802  CD2 PHE A 118      44.640   8.856  13.246  1.00 23.29           C  
ATOM    803  CE1 PHE A 118      43.409   7.779  10.985  1.00 26.92           C  
ATOM    804  CE2 PHE A 118      43.985   9.691  12.397  1.00 27.05           C  
ATOM    805  CZ  PHE A 118      43.367   9.149  11.223  1.00 23.48           C  
ATOM    806  N   MET A 119      48.333   6.352  13.320  1.00 30.18           N  
ATOM    807  CA  MET A 119      49.309   7.025  12.502  1.00 32.99           C  
ATOM    808  C   MET A 119      50.116   5.996  11.635  1.00 35.97           C  
ATOM    809  O   MET A 119      50.430   6.242  10.460  1.00 38.62           O  
ATOM    810  CB  MET A 119      50.102   8.125  13.267  1.00 32.59           C  
ATOM    811  CG  MET A 119      49.533   9.599  13.038  1.00 22.40           C  
ATOM    812  SD  MET A 119      50.507  10.369  14.230  1.00 50.26           S  
ATOM    813  CE  MET A 119      49.580  11.772  14.832  1.00 32.77           C  
ATOM    814  N   GLU A 120      50.365   4.828  12.157  1.00 37.78           N  
ATOM    815  CA  GLU A 120      50.962   3.803  11.307  1.00 40.60           C  
ATOM    816  C   GLU A 120      50.009   3.484  10.110  1.00 41.18           C  
ATOM    817  O   GLU A 120      50.447   3.434   8.899  1.00 41.27           O  
ATOM    818  CB  GLU A 120      51.250   2.556  12.138  1.00 40.72           C  
ATOM    819  CG  GLU A 120      52.325   2.785  13.192  1.00 45.91           C  
ATOM    820  CD  GLU A 120      52.417   1.653  14.217  1.00 50.80           C  
ATOM    821  OE1 GLU A 120      51.487   0.848  14.367  1.00 52.34           O  
ATOM    822  OE2 GLU A 120      53.438   1.566  14.915  1.00 56.24           O  
ATOM    823  N   ALA A 121      48.718   3.288  10.425  1.00 39.86           N  
ATOM    824  CA  ALA A 121      47.729   3.055   9.379  1.00 38.70           C  
ATOM    825  C   ALA A 121      47.820   4.079   8.275  1.00 39.25           C  
ATOM    826  O   ALA A 121      47.739   3.690   7.083  1.00 40.17           O  
ATOM    827  CB  ALA A 121      46.353   2.982   9.949  1.00 38.97           C  
ATOM    828  N   LEU A 122      47.989   5.360   8.632  1.00 38.73           N  
ATOM    829  CA  LEU A 122      48.114   6.453   7.663  1.00 40.32           C  
ATOM    830  C   LEU A 122      49.357   6.350   6.748  1.00 43.16           C  
ATOM    831  O   LEU A 122      49.232   6.359   5.499  1.00 42.82           O  
ATOM    832  CB  LEU A 122      48.105   7.825   8.335  1.00 38.88           C  
ATOM    833  CG  LEU A 122      46.785   8.323   8.989  1.00 37.93           C  
ATOM    834  CD1 LEU A 122      46.879   9.797   9.516  1.00 33.66           C  
ATOM    835  CD2 LEU A 122      45.603   8.131   8.025  1.00 34.35           C  
ATOM    836  N   GLN A 123      50.537   6.325   7.371  1.00 44.72           N  
ATOM    837  CA  GLN A 123      51.798   5.978   6.690  1.00 46.57           C  
ATOM    838  C   GLN A 123      51.569   4.848   5.644  1.00 47.47           C  
ATOM    839  O   GLN A 123      51.925   5.024   4.476  1.00 48.82           O  
ATOM    840  CB  GLN A 123      52.886   5.609   7.731  1.00 46.70           C  
ATOM    841  N   ALA A 124      50.932   3.739   6.066  1.00 47.80           N  
ATOM    842  CA  ALA A 124      50.518   2.595   5.225  1.00 47.73           C  
ATOM    843  C   ALA A 124      49.228   2.751   4.364  1.00 48.50           C  
ATOM    844  O   ALA A 124      48.520   1.742   4.102  1.00 48.91           O  
ATOM    845  CB  ALA A 124      50.358   1.370   6.092  1.00 47.56           C  
ATOM    846  N   GLY A 125      48.908   3.987   3.956  1.00 48.02           N  
ATOM    847  CA  GLY A 125      47.851   4.256   2.962  1.00 45.97           C  
ATOM    848  C   GLY A 125      46.405   4.518   3.384  1.00 44.69           C  
ATOM    849  O   GLY A 125      45.558   4.806   2.518  1.00 44.68           O  
ATOM    850  N   ALA A 126      46.108   4.372   4.685  1.00 42.22           N  
ATOM    851  CA  ALA A 126      44.795   4.669   5.278  1.00 39.44           C  
ATOM    852  C   ALA A 126      44.513   6.116   5.040  1.00 36.81           C  
ATOM    853  O   ALA A 126      45.416   6.842   4.643  1.00 36.90           O  
ATOM    854  CB  ALA A 126      44.852   4.406   6.778  1.00 39.93           C  
ATOM    855  N   ASP A 127      43.271   6.570   5.267  1.00 35.05           N  
ATOM    856  CA  ASP A 127      43.006   7.998   5.204  1.00 32.27           C  
ATOM    857  C   ASP A 127      42.280   8.439   6.494  1.00 29.01           C  
ATOM    858  O   ASP A 127      41.884   7.609   7.284  1.00 26.33           O  
ATOM    859  CB  ASP A 127      42.222   8.380   3.955  1.00 33.29           C  
ATOM    860  CG  ASP A 127      40.833   7.857   4.003  1.00 36.03           C  
ATOM    861  OD1 ASP A 127      40.650   6.683   3.682  1.00 44.45           O  
ATOM    862  OD2 ASP A 127      39.931   8.573   4.444  1.00 36.88           O  
ATOM    863  N   ILE A 128      42.119   9.749   6.656  1.00 27.70           N  
ATOM    864  CA  ILE A 128      41.606  10.311   7.917  1.00 26.93           C  
ATOM    865  C   ILE A 128      40.223   9.837   8.284  1.00 26.39           C  
ATOM    866  O   ILE A 128      39.864   9.775   9.456  1.00 25.48           O  
ATOM    867  CB  ILE A 128      41.767  11.818   7.900  1.00 26.75           C  
ATOM    868  CG1 ILE A 128      43.225  12.130   8.301  1.00 28.93           C  
ATOM    869  CG2 ILE A 128      40.812  12.560   8.875  1.00 24.31           C  
ATOM    870  CD1 ILE A 128      43.724  13.493   7.680  1.00 24.01           C  
ATOM    871  N   SER A 129      39.457   9.423   7.270  1.00 25.86           N  
ATOM    872  CA  SER A 129      38.083   8.925   7.512  1.00 25.75           C  
ATOM    873  C   SER A 129      38.056   7.637   8.315  1.00 25.55           C  
ATOM    874  O   SER A 129      37.027   7.295   8.918  1.00 24.28           O  
ATOM    875  CB  SER A 129      37.312   8.774   6.172  1.00 26.41           C  
ATOM    876  OG  SER A 129      37.649   7.547   5.551  1.00 24.89           O  
ATOM    877  N   MET A 130      39.160   6.915   8.387  1.00 22.47           N  
ATOM    878  CA  MET A 130      39.169   5.674   9.177  1.00 22.51           C  
ATOM    879  C   MET A 130      39.577   5.908  10.628  1.00 20.73           C  
ATOM    880  O   MET A 130      39.657   4.989  11.435  1.00 18.98           O  
ATOM    881  CB  MET A 130      40.144   4.692   8.557  1.00 25.20           C  
ATOM    882  CG  MET A 130      39.666   4.352   7.078  1.00 27.52           C  
ATOM    883  SD  MET A 130      41.110   3.817   6.119  1.00 39.99           S  
ATOM    884  CE  MET A 130      41.377   2.279   7.064  1.00 31.05           C  
ATOM    885  N   ILE A 131      39.746   7.173  10.983  1.00 20.46           N  
ATOM    886  CA  ILE A 131      40.090   7.529  12.411  1.00 18.32           C  
ATOM    887  C   ILE A 131      39.263   6.847  13.484  1.00 18.71           C  
ATOM    888  O   ILE A 131      39.786   6.466  14.552  1.00 16.82           O  
ATOM    889  CB  ILE A 131      39.949   9.097  12.621  1.00 19.21           C  
ATOM    890  CG1 ILE A 131      40.492   9.534  14.027  1.00 18.91           C  
ATOM    891  CG2 ILE A 131      38.418   9.538  12.378  1.00 16.54           C  
ATOM    892  CD1 ILE A 131      40.690  11.061  14.117  1.00 16.98           C  
ATOM    893  N   GLY A 132      37.959   6.671  13.231  1.00 20.05           N  
ATOM    894  CA  GLY A 132      37.091   6.045  14.217  1.00 21.53           C  
ATOM    895  C   GLY A 132      37.442   4.577  14.513  1.00 23.38           C  
ATOM    896  O   GLY A 132      37.084   4.057  15.559  1.00 22.76           O  
ATOM    897  N   GLN A 133      38.099   3.892  13.586  1.00 24.73           N  
ATOM    898  CA  GLN A 133      38.516   2.483  13.835  1.00 26.70           C  
ATOM    899  C   GLN A 133      39.667   2.409  14.867  1.00 28.69           C  
ATOM    900  O   GLN A 133      39.915   1.321  15.475  1.00 28.14           O  
ATOM    901  CB  GLN A 133      38.958   1.862  12.530  1.00 28.72           C  
ATOM    902  CG  GLN A 133      37.821   1.961  11.502  1.00 30.05           C  
ATOM    903  CD  GLN A 133      38.230   1.476  10.131  1.00 37.73           C  
ATOM    904  OE1 GLN A 133      37.834   2.066   9.101  1.00 41.04           O  
ATOM    905  NE2 GLN A 133      39.036   0.403  10.096  1.00 32.92           N  
ATOM    906  N   PHE A 134      40.293   3.577  15.134  1.00 26.40           N  
ATOM    907  CA  PHE A 134      41.406   3.637  16.110  1.00 24.73           C  
ATOM    908  C   PHE A 134      40.964   4.208  17.462  1.00 24.20           C  
ATOM    909  O   PHE A 134      41.803   4.465  18.307  1.00 25.84           O  
ATOM    910  CB  PHE A 134      42.610   4.374  15.493  1.00 23.88           C  
ATOM    911  CG  PHE A 134      42.972   3.852  14.121  1.00 24.33           C  
ATOM    912  CD1 PHE A 134      43.688   2.630  13.992  1.00 33.92           C  
ATOM    913  CD2 PHE A 134      42.525   4.475  12.984  1.00 26.87           C  
ATOM    914  CE1 PHE A 134      44.018   2.088  12.692  1.00 35.98           C  
ATOM    915  CE2 PHE A 134      42.836   3.969  11.673  1.00 36.26           C  
ATOM    916  CZ  PHE A 134      43.604   2.788  11.534  1.00 35.47           C  
ATOM    917  N   GLY A 135      39.656   4.396  17.702  1.00 21.42           N  
ATOM    918  CA  GLY A 135      39.237   4.799  19.077  1.00 18.63           C  
ATOM    919  C   GLY A 135      39.456   6.310  19.403  1.00 18.51           C  
ATOM    920  O   GLY A 135      39.244   6.733  20.549  1.00 21.13           O  
ATOM    921  N   VAL A 136      39.793   7.099  18.397  1.00 16.50           N  
ATOM    922  CA  VAL A 136      40.077   8.551  18.536  1.00 16.73           C  
ATOM    923  C   VAL A 136      39.242   9.434  17.608  1.00 16.02           C  
ATOM    924  O   VAL A 136      39.645  10.548  17.262  1.00 14.12           O  
ATOM    925  CB  VAL A 136      41.603   8.841  18.372  1.00 16.70           C  
ATOM    926  CG1 VAL A 136      42.385   8.203  19.649  1.00 16.37           C  
ATOM    927  CG2 VAL A 136      42.136   8.336  17.118  1.00 18.06           C  
ATOM    928  N   GLY A 137      38.051   8.963  17.278  1.00 14.22           N  
ATOM    929  CA  GLY A 137      37.214   9.715  16.365  1.00 13.31           C  
ATOM    930  C   GLY A 137      36.735  11.054  16.936  1.00 14.50           C  
ATOM    931  O   GLY A 137      36.427  11.995  16.184  1.00 14.88           O  
ATOM    932  N   PHE A 138      36.618  11.144  18.248  1.00 14.25           N  
ATOM    933  CA  PHE A 138      36.379  12.479  18.850  1.00 14.07           C  
ATOM    934  C   PHE A 138      37.167  13.594  18.205  1.00 14.53           C  
ATOM    935  O   PHE A 138      36.627  14.705  17.958  1.00 13.44           O  
ATOM    936  CB  PHE A 138      36.616  12.491  20.419  1.00 15.21           C  
ATOM    937  CG  PHE A 138      36.543  13.886  21.011  1.00 18.74           C  
ATOM    938  CD1 PHE A 138      35.291  14.465  21.233  1.00 16.99           C  
ATOM    939  CD2 PHE A 138      37.730  14.628  21.326  1.00 14.89           C  
ATOM    940  CE1 PHE A 138      35.199  15.794  21.730  1.00 13.47           C  
ATOM    941  CE2 PHE A 138      37.643  15.922  21.866  1.00 15.59           C  
ATOM    942  CZ  PHE A 138      36.394  16.510  22.032  1.00 16.91           C  
ATOM    943  N   TYR A 139      38.481  13.377  18.013  1.00 13.76           N  
ATOM    944  CA  TYR A 139      39.352  14.491  17.620  1.00 14.05           C  
ATOM    945  C   TYR A 139      39.083  14.960  16.198  1.00 14.53           C  
ATOM    946  O   TYR A 139      39.552  16.015  15.819  1.00 13.99           O  
ATOM    947  CB  TYR A 139      40.865  14.088  17.792  1.00 14.01           C  
ATOM    948  CG  TYR A 139      41.120  13.828  19.272  1.00 15.24           C  
ATOM    949  CD1 TYR A 139      41.354  14.867  20.129  1.00 15.42           C  
ATOM    950  CD2 TYR A 139      41.010  12.532  19.809  1.00 14.65           C  
ATOM    951  CE1 TYR A 139      41.544  14.653  21.549  1.00 15.45           C  
ATOM    952  CE2 TYR A 139      41.188  12.297  21.135  1.00 19.14           C  
ATOM    953  CZ  TYR A 139      41.456  13.342  22.007  1.00 18.78           C  
ATOM    954  OH  TYR A 139      41.578  13.041  23.326  1.00 16.74           O  
ATOM    955  N   SER A 140      38.359  14.173  15.410  1.00 13.84           N  
ATOM    956  CA  SER A 140      37.896  14.635  14.081  1.00 13.40           C  
ATOM    957  C   SER A 140      36.981  15.855  14.168  1.00 13.87           C  
ATOM    958  O   SER A 140      36.755  16.545  13.147  1.00 13.95           O  
ATOM    959  CB  SER A 140      37.168  13.491  13.331  1.00 14.91           C  
ATOM    960  OG  SER A 140      35.889  13.247  13.925  1.00 14.70           O  
ATOM    961  N   ALA A 141      36.516  16.200  15.392  1.00 12.30           N  
ATOM    962  CA  ALA A 141      35.812  17.481  15.539  1.00 13.34           C  
ATOM    963  C   ALA A 141      36.657  18.616  15.001  1.00 13.94           C  
ATOM    964  O   ALA A 141      36.131  19.594  14.477  1.00 13.76           O  
ATOM    965  CB  ALA A 141      35.507  17.751  17.031  1.00 11.41           C  
ATOM    966  N   TYR A 142      37.984  18.499  15.210  1.00 14.18           N  
ATOM    967  CA  TYR A 142      38.863  19.570  14.776  1.00 13.92           C  
ATOM    968  C   TYR A 142      39.001  19.711  13.228  1.00 15.18           C  
ATOM    969  O   TYR A 142      39.616  20.673  12.762  1.00 14.58           O  
ATOM    970  CB  TYR A 142      40.226  19.518  15.488  1.00 12.69           C  
ATOM    971  CG  TYR A 142      40.002  19.844  16.973  1.00 14.90           C  
ATOM    972  CD1 TYR A 142      40.010  21.173  17.419  1.00 13.60           C  
ATOM    973  CD2 TYR A 142      39.711  18.838  17.871  1.00 12.99           C  
ATOM    974  CE1 TYR A 142      39.783  21.540  18.752  1.00 14.45           C  
ATOM    975  CE2 TYR A 142      39.415  19.168  19.256  1.00 14.04           C  
ATOM    976  CZ  TYR A 142      39.477  20.503  19.666  1.00 15.77           C  
ATOM    977  OH  TYR A 142      39.228  20.799  20.962  1.00 16.20           O  
ATOM    978  N   LEU A 143      38.379  18.818  12.463  1.00 14.54           N  
ATOM    979  CA  LEU A 143      38.240  19.062  10.980  1.00 14.78           C  
ATOM    980  C   LEU A 143      37.394  20.303  10.712  1.00 16.67           C  
ATOM    981  O   LEU A 143      37.611  21.012   9.751  1.00 16.20           O  
ATOM    982  CB  LEU A 143      37.571  17.877  10.263  1.00 15.42           C  
ATOM    983  CG  LEU A 143      38.449  16.615  10.264  1.00 12.97           C  
ATOM    984  CD1 LEU A 143      37.663  15.341   9.856  1.00 17.60           C  
ATOM    985  CD2 LEU A 143      39.752  16.820   9.361  1.00 14.05           C  
ATOM    986  N   VAL A 144      36.437  20.587  11.590  1.00 16.00           N  
ATOM    987  CA  VAL A 144      35.491  21.698  11.308  1.00 16.79           C  
ATOM    988  C   VAL A 144      35.448  22.765  12.407  1.00 17.53           C  
ATOM    989  O   VAL A 144      34.981  23.854  12.163  1.00 21.43           O  
ATOM    990  CB  VAL A 144      34.059  21.107  10.984  1.00 16.05           C  
ATOM    991  CG1 VAL A 144      34.109  20.154   9.752  1.00 15.37           C  
ATOM    992  CG2 VAL A 144      33.558  20.268  12.169  1.00 14.32           C  
ATOM    993  N   ALA A 145      35.886  22.478  13.624  1.00 17.18           N  
ATOM    994  CA  ALA A 145      35.738  23.408  14.753  1.00 14.84           C  
ATOM    995  C   ALA A 145      37.075  24.048  15.090  1.00 16.08           C  
ATOM    996  O   ALA A 145      38.113  23.303  15.174  1.00 15.42           O  
ATOM    997  CB  ALA A 145      35.239  22.639  16.023  1.00 12.85           C  
ATOM    998  N   GLU A 146      37.043  25.361  15.303  1.00 14.50           N  
ATOM    999  CA  GLU A 146      38.164  26.118  15.855  1.00 17.23           C  
ATOM   1000  C   GLU A 146      38.291  25.898  17.382  1.00 17.26           C  
ATOM   1001  O   GLU A 146      39.397  25.913  17.951  1.00 17.33           O  
ATOM   1002  CB  GLU A 146      37.979  27.583  15.531  1.00 17.87           C  
ATOM   1003  CG  GLU A 146      37.044  28.284  16.498  1.00 25.34           C  
ATOM   1004  CD  GLU A 146      36.675  29.657  15.930  1.00 33.55           C  
ATOM   1005  OE1 GLU A 146      37.356  30.066  14.986  1.00 30.93           O  
ATOM   1006  OE2 GLU A 146      35.731  30.319  16.421  1.00 32.73           O  
ATOM   1007  N   LYS A 147      37.160  25.611  18.035  1.00 17.71           N  
ATOM   1008  CA  LYS A 147      37.184  25.338  19.478  1.00 16.25           C  
ATOM   1009  C   LYS A 147      36.119  24.293  19.766  1.00 15.75           C  
ATOM   1010  O   LYS A 147      35.055  24.312  19.100  1.00 14.81           O  
ATOM   1011  CB  LYS A 147      36.836  26.595  20.211  1.00 16.85           C  
ATOM   1012  CG  LYS A 147      36.698  26.428  21.754  1.00 17.16           C  
ATOM   1013  CD  LYS A 147      36.540  27.882  22.267  1.00 21.48           C  
ATOM   1014  CE  LYS A 147      35.852  28.039  23.532  1.00 27.10           C  
ATOM   1015  NZ  LYS A 147      35.476  29.494  23.260  1.00 28.36           N  
ATOM   1016  N   VAL A 148      36.370  23.393  20.725  1.00 14.33           N  
ATOM   1017  CA  VAL A 148      35.333  22.416  21.062  1.00 13.36           C  
ATOM   1018  C   VAL A 148      35.147  22.470  22.570  1.00 15.10           C  
ATOM   1019  O   VAL A 148      36.143  22.487  23.304  1.00 13.87           O  
ATOM   1020  CB  VAL A 148      35.714  20.965  20.687  1.00 14.49           C  
ATOM   1021  CG1 VAL A 148      34.657  19.929  21.233  1.00 12.67           C  
ATOM   1022  CG2 VAL A 148      35.938  20.785  19.124  1.00 11.68           C  
ATOM   1023  N   THR A 149      33.865  22.544  22.991  1.00 13.64           N  
ATOM   1024  CA  THR A 149      33.481  22.558  24.354  1.00 15.68           C  
ATOM   1025  C   THR A 149      32.659  21.266  24.675  1.00 14.13           C  
ATOM   1026  O   THR A 149      31.657  20.980  24.005  1.00 16.21           O  
ATOM   1027  CB  THR A 149      32.621  23.802  24.722  1.00 14.26           C  
ATOM   1028  OG1 THR A 149      33.288  24.972  24.282  1.00 17.70           O  
ATOM   1029  CG2 THR A 149      32.404  23.843  26.325  1.00 15.70           C  
ATOM   1030  N   VAL A 150      33.071  20.491  25.693  1.00 13.02           N  
ATOM   1031  CA  VAL A 150      32.315  19.254  26.038  1.00 13.22           C  
ATOM   1032  C   VAL A 150      31.744  19.381  27.434  1.00 14.64           C  
ATOM   1033  O   VAL A 150      32.532  19.550  28.415  1.00 16.36           O  
ATOM   1034  CB  VAL A 150      33.235  18.048  26.023  1.00 12.76           C  
ATOM   1035  CG1 VAL A 150      32.456  16.733  26.482  1.00 13.70           C  
ATOM   1036  CG2 VAL A 150      33.849  17.845  24.604  1.00 14.17           C  
ATOM   1037  N   ILE A 151      30.427  19.351  27.557  1.00 12.20           N  
ATOM   1038  CA  ILE A 151      29.860  19.443  28.898  1.00 16.01           C  
ATOM   1039  C   ILE A 151      29.383  18.041  29.182  1.00 14.73           C  
ATOM   1040  O   ILE A 151      28.825  17.408  28.300  1.00 14.85           O  
ATOM   1041  CB  ILE A 151      28.649  20.347  28.902  1.00 14.97           C  
ATOM   1042  CG1 ILE A 151      28.876  21.718  28.166  1.00 19.28           C  
ATOM   1043  CG2 ILE A 151      28.037  20.551  30.356  1.00 16.39           C  
ATOM   1044  CD1 ILE A 151      29.859  22.621  28.782  1.00 17.27           C  
ATOM   1045  N   THR A 152      29.649  17.514  30.373  1.00 14.52           N  
ATOM   1046  CA  THR A 152      29.340  16.116  30.603  1.00 14.72           C  
ATOM   1047  C   THR A 152      28.861  15.923  32.060  1.00 17.46           C  
ATOM   1048  O   THR A 152      29.313  16.636  32.961  1.00 15.28           O  
ATOM   1049  CB  THR A 152      30.544  15.189  30.269  1.00 14.66           C  
ATOM   1050  OG1 THR A 152      30.137  13.817  30.172  1.00 15.06           O  
ATOM   1051  CG2 THR A 152      31.705  15.355  31.196  1.00 13.42           C  
ATOM   1052  N   LYS A 153      28.016  14.919  32.270  1.00 16.15           N  
ATOM   1053  CA  LYS A 153      27.547  14.597  33.622  1.00 15.78           C  
ATOM   1054  C   LYS A 153      27.427  13.135  33.715  1.00 16.57           C  
ATOM   1055  O   LYS A 153      26.580  12.499  32.994  1.00 19.03           O  
ATOM   1056  CB  LYS A 153      26.144  15.205  33.815  1.00 14.59           C  
ATOM   1057  CG  LYS A 153      25.437  14.743  35.214  1.00 15.55           C  
ATOM   1058  CD  LYS A 153      26.198  15.335  36.388  1.00 16.50           C  
ATOM   1059  CE  LYS A 153      25.418  15.085  37.777  1.00 17.34           C  
ATOM   1060  NZ  LYS A 153      25.437  13.648  38.052  1.00 16.64           N  
ATOM   1061  N   HIS A 154      28.216  12.541  34.578  1.00 18.27           N  
ATOM   1062  CA  HIS A 154      28.088  11.069  34.816  1.00 16.96           C  
ATOM   1063  C   HIS A 154      27.312  10.865  36.153  1.00 19.97           C  
ATOM   1064  O   HIS A 154      27.394  11.734  37.023  1.00 19.90           O  
ATOM   1065  CB  HIS A 154      29.509  10.529  34.888  1.00 17.47           C  
ATOM   1066  CG  HIS A 154      29.633   9.030  34.994  1.00 19.78           C  
ATOM   1067  ND1 HIS A 154      29.393   8.334  36.163  1.00 19.30           N  
ATOM   1068  CD2 HIS A 154      30.059   8.124  34.098  1.00 17.70           C  
ATOM   1069  CE1 HIS A 154      29.573   7.049  35.953  1.00 20.48           C  
ATOM   1070  NE2 HIS A 154      30.014   6.893  34.712  1.00 18.55           N  
ATOM   1071  N   ASN A 155      26.537   9.779  36.305  1.00 21.08           N  
ATOM   1072  CA  ASN A 155      25.866   9.531  37.601  1.00 21.89           C  
ATOM   1073  C   ASN A 155      26.866   9.637  38.762  1.00 23.56           C  
ATOM   1074  O   ASN A 155      26.461  10.076  39.833  1.00 25.13           O  
ATOM   1075  CB  ASN A 155      25.214   8.121  37.644  1.00 21.34           C  
ATOM   1076  CG  ASN A 155      23.943   8.054  36.809  1.00 20.85           C  
ATOM   1077  OD1 ASN A 155      23.276   9.090  36.584  1.00 23.73           O  
ATOM   1078  ND2 ASN A 155      23.585   6.842  36.350  1.00 22.23           N  
ATOM   1079  N   ASP A 156      28.121   9.203  38.595  1.00 25.41           N  
ATOM   1080  CA  ASP A 156      29.059   9.165  39.753  1.00 29.56           C  
ATOM   1081  C   ASP A 156      29.831  10.470  40.053  1.00 30.53           C  
ATOM   1082  O   ASP A 156      30.808  10.411  40.832  1.00 31.80           O  
ATOM   1083  CB  ASP A 156      30.040   7.944  39.745  1.00 29.57           C  
ATOM   1084  CG  ASP A 156      29.298   6.599  39.635  1.00 29.58           C  
ATOM   1085  OD1 ASP A 156      28.149   6.488  40.101  1.00 28.54           O  
ATOM   1086  OD2 ASP A 156      29.852   5.680  39.039  1.00 31.81           O  
ATOM   1087  N   ASP A 157      29.376  11.639  39.551  1.00 29.60           N  
ATOM   1088  CA  ASP A 157      30.253  12.827  39.573  1.00 26.69           C  
ATOM   1089  C   ASP A 157      29.422  14.095  39.306  1.00 26.30           C  
ATOM   1090  O   ASP A 157      28.236  14.009  38.979  1.00 26.65           O  
ATOM   1091  CB  ASP A 157      31.467  12.631  38.586  1.00 27.20           C  
ATOM   1092  CG  ASP A 157      32.762  13.391  39.025  1.00 26.07           C  
ATOM   1093  OD1 ASP A 157      32.617  14.271  39.881  1.00 27.62           O  
ATOM   1094  OD2 ASP A 157      33.902  13.173  38.478  1.00 29.49           O  
ATOM   1095  N   GLU A 158      30.036  15.270  39.445  1.00 24.15           N  
ATOM   1096  CA AGLU A 158      29.422  16.553  39.176  0.50 23.06           C  
ATOM   1097  CA BGLU A 158      29.338  16.526  39.179  0.50 22.96           C  
ATOM   1098  C   GLU A 158      29.430  16.839  37.666  1.00 21.55           C  
ATOM   1099  O   GLU A 158      30.103  16.142  36.942  1.00 19.98           O  
ATOM   1100  CB AGLU A 158      30.313  17.587  39.856  0.50 24.30           C  
ATOM   1101  CB BGLU A 158      29.994  17.687  39.949  0.50 24.43           C  
ATOM   1102  CG AGLU A 158      30.456  17.223  41.306  0.50 28.91           C  
ATOM   1103  CG BGLU A 158      30.433  17.353  41.396  0.50 28.46           C  
ATOM   1104  CD AGLU A 158      29.101  17.248  41.939  0.50 32.34           C  
ATOM   1105  CD BGLU A 158      31.285  18.458  42.020  0.50 30.55           C  
ATOM   1106  OE1AGLU A 158      28.563  18.354  42.060  0.50 34.24           O  
ATOM   1107  OE1BGLU A 158      31.049  19.645  41.716  0.50 32.39           O  
ATOM   1108  OE2AGLU A 158      28.560  16.187  42.274  0.50 34.66           O  
ATOM   1109  OE2BGLU A 158      32.206  18.122  42.795  0.50 32.24           O  
ATOM   1110  N   GLN A 159      28.778  17.909  37.234  1.00 18.98           N  
ATOM   1111  CA  GLN A 159      28.809  18.364  35.843  1.00 18.85           C  
ATOM   1112  C   GLN A 159      30.107  19.176  35.538  1.00 19.70           C  
ATOM   1113  O   GLN A 159      30.399  20.162  36.208  1.00 17.91           O  
ATOM   1114  CB  GLN A 159      27.612  19.246  35.548  1.00 21.21           C  
ATOM   1115  CG  GLN A 159      27.438  19.499  34.066  1.00 22.11           C  
ATOM   1116  CD  GLN A 159      25.995  19.878  33.720  1.00 25.84           C  
ATOM   1117  OE1 GLN A 159      25.058  19.129  33.991  1.00 23.29           O  
ATOM   1118  NE2 GLN A 159      25.824  21.017  33.128  1.00 20.32           N  
ATOM   1119  N   TYR A 160      30.836  18.797  34.482  1.00 17.74           N  
ATOM   1120  CA  TYR A 160      32.089  19.446  34.171  1.00 18.00           C  
ATOM   1121  C   TYR A 160      32.056  19.968  32.756  1.00 17.58           C  
ATOM   1122  O   TYR A 160      31.356  19.362  31.912  1.00 16.51           O  
ATOM   1123  CB  TYR A 160      33.201  18.420  34.265  1.00 18.66           C  
ATOM   1124  CG  TYR A 160      33.504  18.074  35.707  1.00 26.06           C  
ATOM   1125  CD1 TYR A 160      34.284  18.933  36.494  1.00 30.18           C  
ATOM   1126  CD2 TYR A 160      33.007  16.881  36.290  1.00 27.42           C  
ATOM   1127  CE1 TYR A 160      34.560  18.634  37.811  1.00 33.04           C  
ATOM   1128  CE2 TYR A 160      33.260  16.612  37.610  1.00 34.76           C  
ATOM   1129  CZ  TYR A 160      34.032  17.485  38.339  1.00 35.56           C  
ATOM   1130  OH  TYR A 160      34.307  17.181  39.633  1.00 45.17           O  
ATOM   1131  N   ALA A 161      32.855  21.012  32.471  1.00 15.32           N  
ATOM   1132  CA  ALA A 161      33.040  21.506  31.117  1.00 16.26           C  
ATOM   1133  C   ALA A 161      34.545  21.368  30.749  1.00 16.68           C  
ATOM   1134  O   ALA A 161      35.438  21.838  31.524  1.00 17.54           O  
ATOM   1135  CB  ALA A 161      32.572  23.043  31.005  1.00 17.42           C  
ATOM   1136  N   TRP A 162      34.834  20.671  29.641  1.00 15.38           N  
ATOM   1137  CA  TRP A 162      36.175  20.563  29.061  1.00 15.81           C  
ATOM   1138  C   TRP A 162      36.197  21.436  27.844  1.00 15.82           C  
ATOM   1139  O   TRP A 162      35.158  21.572  27.121  1.00 15.52           O  
ATOM   1140  CB  TRP A 162      36.346  19.070  28.612  1.00 16.30           C  
ATOM   1141  CG  TRP A 162      37.615  18.656  27.870  1.00 16.26           C  
ATOM   1142  CD1 TRP A 162      38.681  17.947  28.386  1.00 14.22           C  
ATOM   1143  CD2 TRP A 162      37.880  18.838  26.460  1.00 13.52           C  
ATOM   1144  NE1 TRP A 162      39.600  17.691  27.368  1.00 13.95           N  
ATOM   1145  CE2 TRP A 162      39.120  18.250  26.193  1.00 15.65           C  
ATOM   1146  CE3 TRP A 162      37.164  19.462  25.392  1.00 12.07           C  
ATOM   1147  CZ2 TRP A 162      39.686  18.245  24.906  1.00 13.87           C  
ATOM   1148  CZ3 TRP A 162      37.782  19.472  24.087  1.00 13.60           C  
ATOM   1149  CH2 TRP A 162      39.004  18.821  23.877  1.00 13.36           C  
ATOM   1150  N   GLU A 163      37.330  22.068  27.562  1.00 15.48           N  
ATOM   1151  CA  GLU A 163      37.360  22.909  26.407  1.00 15.22           C  
ATOM   1152  C   GLU A 163      38.749  22.979  25.797  1.00 14.23           C  
ATOM   1153  O   GLU A 163      39.721  22.914  26.506  1.00 13.53           O  
ATOM   1154  CB  GLU A 163      36.980  24.347  26.786  1.00 18.23           C  
ATOM   1155  CG  GLU A 163      36.617  25.231  25.552  1.00 20.24           C  
ATOM   1156  CD  GLU A 163      35.882  26.498  25.998  1.00 28.92           C  
ATOM   1157  OE1 GLU A 163      36.422  27.221  26.880  1.00 27.75           O  
ATOM   1158  OE2 GLU A 163      34.749  26.671  25.536  1.00 25.61           O  
ATOM   1159  N   SER A 164      38.846  23.152  24.465  1.00 14.42           N  
ATOM   1160  CA  SER A 164      40.170  23.197  23.861  1.00 13.16           C  
ATOM   1161  C   SER A 164      40.060  23.817  22.471  1.00 14.36           C  
ATOM   1162  O   SER A 164      39.152  23.466  21.679  1.00 14.09           O  
ATOM   1163  CB  SER A 164      40.829  21.819  23.740  1.00 12.05           C  
ATOM   1164  OG  SER A 164      42.148  22.055  23.087  1.00 14.31           O  
ATOM   1165  N   SER A 165      40.911  24.783  22.192  1.00 15.57           N  
ATOM   1166  CA  SER A 165      41.096  25.272  20.834  1.00 15.35           C  
ATOM   1167  C   SER A 165      42.364  24.678  20.300  1.00 15.75           C  
ATOM   1168  O   SER A 165      43.043  25.316  19.450  1.00 18.00           O  
ATOM   1169  CB  SER A 165      41.245  26.790  20.850  1.00 17.59           C  
ATOM   1170  OG  SER A 165      40.035  27.320  21.334  1.00 17.38           O  
ATOM   1171  N   ALA A 166      42.707  23.476  20.755  1.00 15.78           N  
ATOM   1172  CA  ALA A 166      43.940  22.807  20.307  1.00 16.62           C  
ATOM   1173  C   ALA A 166      45.187  23.614  20.733  1.00 19.38           C  
ATOM   1174  O   ALA A 166      45.160  24.108  21.867  1.00 19.01           O  
ATOM   1175  CB  ALA A 166      43.844  22.439  18.714  1.00 18.40           C  
ATOM   1176  N   GLY A 167      46.273  23.741  19.947  1.00 18.62           N  
ATOM   1177  CA  GLY A 167      47.546  24.441  20.429  1.00 19.80           C  
ATOM   1178  C   GLY A 167      48.178  23.815  21.736  1.00 18.57           C  
ATOM   1179  O   GLY A 167      48.974  24.424  22.427  1.00 21.46           O  
ATOM   1180  N   GLY A 168      47.824  22.602  22.082  1.00 16.86           N  
ATOM   1181  CA  GLY A 168      48.553  21.814  23.026  1.00 17.15           C  
ATOM   1182  C   GLY A 168      47.961  21.710  24.422  1.00 17.61           C  
ATOM   1183  O   GLY A 168      48.559  21.031  25.292  1.00 17.20           O  
ATOM   1184  N   SER A 169      46.875  22.457  24.658  1.00 19.57           N  
ATOM   1185  CA  SER A 169      46.268  22.500  26.052  1.00 16.87           C  
ATOM   1186  C   SER A 169      44.711  22.421  26.057  1.00 15.45           C  
ATOM   1187  O   SER A 169      44.062  22.767  25.048  1.00 18.68           O  
ATOM   1188  CB  SER A 169      46.741  23.751  26.780  1.00 17.41           C  
ATOM   1189  OG  SER A 169      46.065  24.866  26.280  1.00 17.76           O  
ATOM   1190  N   PHE A 170      44.131  21.995  27.174  1.00 15.50           N  
ATOM   1191  CA  PHE A 170      42.700  21.987  27.316  1.00 15.29           C  
ATOM   1192  C   PHE A 170      42.419  22.437  28.774  1.00 15.66           C  
ATOM   1193  O   PHE A 170      43.304  22.366  29.609  1.00 16.14           O  
ATOM   1194  CB  PHE A 170      42.119  20.572  27.054  1.00 15.02           C  
ATOM   1195  CG  PHE A 170      42.665  19.470  27.971  1.00 16.33           C  
ATOM   1196  CD1 PHE A 170      41.992  19.148  29.173  1.00 17.36           C  
ATOM   1197  CD2 PHE A 170      43.772  18.708  27.620  1.00 15.35           C  
ATOM   1198  CE1 PHE A 170      42.407  18.093  29.991  1.00 14.15           C  
ATOM   1199  CE2 PHE A 170      44.222  17.620  28.467  1.00 16.77           C  
ATOM   1200  CZ  PHE A 170      43.546  17.336  29.670  1.00 14.96           C  
ATOM   1201  N   THR A 171      41.212  22.927  29.016  1.00 14.47           N  
ATOM   1202  CA  THR A 171      40.818  23.285  30.347  1.00 14.40           C  
ATOM   1203  C   THR A 171      39.742  22.383  30.855  1.00 15.11           C  
ATOM   1204  O   THR A 171      38.973  21.833  30.055  1.00 15.87           O  
ATOM   1205  CB  THR A 171      40.334  24.768  30.393  1.00 13.65           C  
ATOM   1206  OG1 THR A 171      39.165  24.940  29.538  1.00 15.92           O  
ATOM   1207  CG2 THR A 171      41.523  25.766  30.022  1.00 14.24           C  
ATOM   1208  N   VAL A 172      39.603  22.308  32.207  1.00 15.29           N  
ATOM   1209  CA  VAL A 172      38.481  21.616  32.780  1.00 16.61           C  
ATOM   1210  C   VAL A 172      38.020  22.504  33.971  1.00 18.84           C  
ATOM   1211  O   VAL A 172      38.866  22.956  34.785  1.00 16.52           O  
ATOM   1212  CB  VAL A 172      38.836  20.186  33.309  1.00 16.39           C  
ATOM   1213  CG1 VAL A 172      37.624  19.527  34.141  1.00 18.53           C  
ATOM   1214  CG2 VAL A 172      39.396  19.256  32.204  1.00 15.54           C  
ATOM   1215  N   ARG A 173      36.706  22.723  34.051  1.00 18.28           N  
ATOM   1216  CA  ARG A 173      36.086  23.445  35.166  1.00 21.15           C  
ATOM   1217  C   ARG A 173      34.757  22.727  35.554  1.00 22.30           C  
ATOM   1218  O   ARG A 173      34.157  22.010  34.728  1.00 19.34           O  
ATOM   1219  CB  ARG A 173      35.776  24.917  34.814  1.00 20.75           C  
ATOM   1220  CG  ARG A 173      34.779  25.141  33.665  1.00 25.65           C  
ATOM   1221  CD  ARG A 173      34.816  26.563  33.010  1.00 34.78           C  
ATOM   1222  NE  ARG A 173      36.044  26.664  32.192  1.00 40.31           N  
ATOM   1223  CZ  ARG A 173      36.623  27.778  31.684  1.00 43.14           C  
ATOM   1224  NH1 ARG A 173      36.107  29.000  31.844  1.00 40.76           N  
ATOM   1225  NH2 ARG A 173      37.757  27.664  30.977  1.00 40.79           N  
ATOM   1226  N   THR A 174      34.336  22.884  36.815  1.00 23.79           N  
ATOM   1227  CA  THR A 174      32.969  22.523  37.230  1.00 26.07           C  
ATOM   1228  C   THR A 174      32.033  23.373  36.438  1.00 26.80           C  
ATOM   1229  O   THR A 174      32.296  24.525  36.257  1.00 28.82           O  
ATOM   1230  CB  THR A 174      32.808  22.764  38.771  1.00 25.60           C  
ATOM   1231  OG1 THR A 174      33.834  22.001  39.378  1.00 27.98           O  
ATOM   1232  CG2 THR A 174      31.517  22.200  39.245  1.00 30.72           C  
ATOM   1233  N   ASP A 175      30.990  22.805  35.844  1.00 26.83           N  
ATOM   1234  CA  ASP A 175      30.156  23.564  35.012  1.00 28.68           C  
ATOM   1235  C   ASP A 175      28.967  23.948  35.886  1.00 32.81           C  
ATOM   1236  O   ASP A 175      28.313  23.084  36.473  1.00 33.26           O  
ATOM   1237  CB  ASP A 175      29.616  22.686  33.874  1.00 27.57           C  
ATOM   1238  CG  ASP A 175      28.687  23.429  32.953  1.00 28.93           C  
ATOM   1239  OD1 ASP A 175      28.972  24.586  32.632  1.00 31.77           O  
ATOM   1240  OD2 ASP A 175      27.660  22.876  32.538  1.00 27.89           O  
ATOM   1241  N   THR A 176      28.626  25.224  35.877  1.00 36.81           N  
ATOM   1242  CA  THR A 176      27.367  25.658  36.512  1.00 41.77           C  
ATOM   1243  C   THR A 176      26.328  26.217  35.473  1.00 42.08           C  
ATOM   1244  O   THR A 176      25.305  26.793  35.855  1.00 43.67           O  
ATOM   1245  CB  THR A 176      27.651  26.619  37.736  1.00 41.73           C  
ATOM   1246  OG1 THR A 176      26.431  27.285  38.101  1.00 48.54           O  
ATOM   1247  CG2 THR A 176      28.716  27.683  37.363  1.00 41.72           C  
ATOM   1248  N   GLY A 177      26.594  26.038  34.165  1.00 42.01           N  
ATOM   1249  CA  GLY A 177      25.565  26.229  33.107  1.00 38.96           C  
ATOM   1250  C   GLY A 177      24.352  25.331  33.383  1.00 36.81           C  
ATOM   1251  O   GLY A 177      24.186  24.803  34.483  1.00 35.63           O  
ATOM   1252  N   GLU A 178      23.510  25.150  32.373  1.00 34.91           N  
ATOM   1253  CA  GLU A 178      22.231  24.498  32.516  1.00 32.64           C  
ATOM   1254  C   GLU A 178      22.520  23.053  32.923  1.00 30.81           C  
ATOM   1255  O   GLU A 178      23.263  22.397  32.233  1.00 26.91           O  
ATOM   1256  CB  GLU A 178      21.595  24.484  31.119  1.00 32.31           C  
ATOM   1257  CG  GLU A 178      20.130  24.521  31.053  1.00 36.29           C  
ATOM   1258  CD  GLU A 178      19.531  25.500  32.081  1.00 39.73           C  
ATOM   1259  OE1 GLU A 178      18.970  25.003  33.066  1.00 40.97           O  
ATOM   1260  OE2 GLU A 178      19.684  26.739  31.954  1.00 39.34           O  
ATOM   1261  N   PRO A 179      21.908  22.549  34.015  1.00 30.77           N  
ATOM   1262  CA  PRO A 179      22.155  21.138  34.341  1.00 30.34           C  
ATOM   1263  C   PRO A 179      21.703  20.193  33.241  1.00 31.28           C  
ATOM   1264  O   PRO A 179      20.713  20.430  32.552  1.00 30.35           O  
ATOM   1265  CB  PRO A 179      21.294  20.863  35.609  1.00 31.22           C  
ATOM   1266  CG  PRO A 179      20.568  22.249  35.932  1.00 31.04           C  
ATOM   1267  CD  PRO A 179      21.343  23.315  35.166  1.00 31.11           C  
ATOM   1268  N   MET A 180      22.422  19.114  33.054  1.00 30.03           N  
ATOM   1269  CA  MET A 180      21.922  18.253  32.048  1.00 31.80           C  
ATOM   1270  C   MET A 180      21.364  16.927  32.454  1.00 29.45           C  
ATOM   1271  O   MET A 180      20.994  16.140  31.564  1.00 30.40           O  
ATOM   1272  CB  MET A 180      22.948  18.026  30.970  1.00 32.64           C  
ATOM   1273  CG  MET A 180      24.262  17.594  31.387  1.00 38.11           C  
ATOM   1274  SD  MET A 180      25.268  18.020  29.940  1.00 45.79           S  
ATOM   1275  CE  MET A 180      24.870  16.697  28.813  1.00 39.19           C  
ATOM   1276  N   GLY A 181      21.369  16.585  33.718  1.00 24.64           N  
ATOM   1277  CA  GLY A 181      20.732  15.295  34.031  1.00 22.78           C  
ATOM   1278  C   GLY A 181      21.702  14.158  33.947  1.00 20.55           C  
ATOM   1279  O   GLY A 181      22.210  13.667  34.960  1.00 19.97           O  
ATOM   1280  N   ARG A 182      22.040  13.752  32.712  1.00 19.31           N  
ATOM   1281  CA  ARG A 182      23.052  12.734  32.514  1.00 17.72           C  
ATOM   1282  C   ARG A 182      23.397  12.777  31.027  1.00 17.49           C  
ATOM   1283  O   ARG A 182      22.501  12.857  30.183  1.00 16.58           O  
ATOM   1284  CB  ARG A 182      22.526  11.297  32.836  1.00 16.24           C  
ATOM   1285  CG  ARG A 182      23.682  10.242  32.889  1.00 18.78           C  
ATOM   1286  CD  ARG A 182      23.224   8.749  32.616  1.00 15.63           C  
ATOM   1287  NE  ARG A 182      22.283   8.630  31.461  1.00 16.99           N  
ATOM   1288  CZ  ARG A 182      20.953   8.507  31.543  1.00 21.35           C  
ATOM   1289  NH1 ARG A 182      20.259   8.574  32.707  1.00 17.15           N  
ATOM   1290  NH2 ARG A 182      20.277   8.399  30.430  1.00 15.69           N  
ATOM   1291  N   GLY A 183      24.667  12.683  30.700  1.00 17.57           N  
ATOM   1292  CA  GLY A 183      25.060  12.506  29.278  1.00 15.92           C  
ATOM   1293  C   GLY A 183      26.125  13.523  28.895  1.00 16.80           C  
ATOM   1294  O   GLY A 183      26.880  13.985  29.761  1.00 16.00           O  
ATOM   1295  N   THR A 184      26.302  13.727  27.587  1.00 15.66           N  
ATOM   1296  CA  THR A 184      27.388  14.578  27.097  1.00 15.00           C  
ATOM   1297  C   THR A 184      26.852  15.488  26.012  1.00 16.37           C  
ATOM   1298  O   THR A 184      26.042  15.063  25.145  1.00 13.94           O  
ATOM   1299  CB  THR A 184      28.582  13.708  26.583  1.00 16.26           C  
ATOM   1300  OG1 THR A 184      29.072  12.973  27.694  1.00 17.51           O  
ATOM   1301  CG2 THR A 184      29.747  14.542  25.860  1.00 15.11           C  
ATOM   1302  N   LYS A 185      27.391  16.701  26.013  1.00 15.44           N  
ATOM   1303  CA  LYS A 185      27.088  17.666  25.009  1.00 16.91           C  
ATOM   1304  C   LYS A 185      28.391  18.151  24.421  1.00 17.25           C  
ATOM   1305  O   LYS A 185      29.285  18.682  25.146  1.00 16.27           O  
ATOM   1306  CB  LYS A 185      26.400  18.809  25.731  1.00 18.11           C  
ATOM   1307  CG  LYS A 185      26.008  19.944  24.985  1.00 21.12           C  
ATOM   1308  CD  LYS A 185      24.778  20.598  25.798  1.00 31.89           C  
ATOM   1309  CE  LYS A 185      25.254  21.765  26.594  1.00 34.81           C  
ATOM   1310  NZ  LYS A 185      24.307  22.239  27.657  1.00 38.38           N  
ATOM   1311  N   VAL A 186      28.529  17.964  23.109  1.00 16.15           N  
ATOM   1312  CA  VAL A 186      29.732  18.451  22.397  1.00 14.90           C  
ATOM   1313  C   VAL A 186      29.358  19.704  21.572  1.00 15.73           C  
ATOM   1314  O   VAL A 186      28.502  19.658  20.623  1.00 13.90           O  
ATOM   1315  CB  VAL A 186      30.296  17.307  21.412  1.00 13.73           C  
ATOM   1316  CG1 VAL A 186      31.501  17.867  20.564  1.00 12.27           C  
ATOM   1317  CG2 VAL A 186      30.691  16.070  22.221  1.00 15.43           C  
ATOM   1318  N   ILE A 187      29.934  20.849  21.940  1.00 15.56           N  
ATOM   1319  CA  ILE A 187      29.605  22.077  21.233  1.00 14.31           C  
ATOM   1320  C   ILE A 187      30.748  22.434  20.262  1.00 14.65           C  
ATOM   1321  O   ILE A 187      31.865  22.689  20.733  1.00 13.79           O  
ATOM   1322  CB  ILE A 187      29.411  23.230  22.220  1.00 15.65           C  
ATOM   1323  CG1 ILE A 187      28.382  22.786  23.285  1.00 15.83           C  
ATOM   1324  CG2 ILE A 187      29.091  24.634  21.470  1.00 14.88           C  
ATOM   1325  CD1 ILE A 187      28.285  23.820  24.429  1.00 22.61           C  
ATOM   1326  N   LEU A 188      30.447  22.456  18.975  1.00 14.07           N  
ATOM   1327  CA  LEU A 188      31.476  22.701  17.965  1.00 15.24           C  
ATOM   1328  C   LEU A 188      31.354  24.157  17.602  1.00 16.24           C  
ATOM   1329  O   LEU A 188      30.369  24.532  17.021  1.00 16.56           O  
ATOM   1330  CB  LEU A 188      31.199  21.795  16.734  1.00 12.99           C  
ATOM   1331  CG  LEU A 188      31.176  20.268  17.011  1.00 11.36           C  
ATOM   1332  CD1 LEU A 188      30.875  19.438  15.765  1.00 15.52           C  
ATOM   1333  CD2 LEU A 188      32.525  19.759  17.567  1.00 10.65           C  
ATOM   1334  N   HIS A 189      32.347  24.984  17.966  1.00 16.59           N  
ATOM   1335  CA  HIS A 189      32.423  26.358  17.479  1.00 17.31           C  
ATOM   1336  C   HIS A 189      33.077  26.305  16.105  1.00 15.79           C  
ATOM   1337  O   HIS A 189      34.211  26.042  15.995  1.00 17.46           O  
ATOM   1338  CB  HIS A 189      33.252  27.215  18.469  1.00 17.03           C  
ATOM   1339  CG  HIS A 189      32.726  27.134  19.879  1.00 20.17           C  
ATOM   1340  ND1 HIS A 189      31.784  28.027  20.368  1.00 23.83           N  
ATOM   1341  CD2 HIS A 189      32.957  26.228  20.882  1.00 19.16           C  
ATOM   1342  CE1 HIS A 189      31.466  27.693  21.614  1.00 18.49           C  
ATOM   1343  NE2 HIS A 189      32.185  26.625  21.967  1.00 24.89           N  
ATOM   1344  N   LEU A 190      32.306  26.455  15.053  1.00 16.37           N  
ATOM   1345  CA  LEU A 190      32.790  26.056  13.747  1.00 16.12           C  
ATOM   1346  C   LEU A 190      33.734  27.114  13.188  1.00 19.02           C  
ATOM   1347  O   LEU A 190      33.553  28.317  13.429  1.00 19.05           O  
ATOM   1348  CB  LEU A 190      31.586  25.964  12.799  1.00 15.95           C  
ATOM   1349  CG  LEU A 190      30.624  24.796  13.074  1.00 12.07           C  
ATOM   1350  CD1 LEU A 190      29.365  24.671  12.108  1.00 15.12           C  
ATOM   1351  CD2 LEU A 190      31.389  23.531  13.075  1.00 17.16           C  
ATOM   1352  N   LYS A 191      34.704  26.665  12.405  1.00 19.33           N  
ATOM   1353  CA  LYS A 191      35.535  27.563  11.577  1.00 22.44           C  
ATOM   1354  C   LYS A 191      34.689  28.334  10.616  1.00 23.20           C  
ATOM   1355  O   LYS A 191      33.657  27.863  10.120  1.00 22.80           O  
ATOM   1356  CB  LYS A 191      36.554  26.772  10.742  1.00 20.28           C  
ATOM   1357  CG  LYS A 191      37.556  26.029  11.618  1.00 24.77           C  
ATOM   1358  CD  LYS A 191      37.962  24.742  10.876  1.00 28.50           C  
ATOM   1359  CE  LYS A 191      39.412  24.523  10.879  1.00 40.32           C  
ATOM   1360  NZ  LYS A 191      40.041  25.359   9.783  1.00 44.16           N  
ATOM   1361  N   GLU A 192      35.127  29.552  10.327  1.00 25.41           N  
ATOM   1362  CA  GLU A 192      34.301  30.401   9.499  1.00 27.03           C  
ATOM   1363  C   GLU A 192      33.996  29.871   8.136  1.00 25.55           C  
ATOM   1364  O   GLU A 192      32.967  30.169   7.623  1.00 25.83           O  
ATOM   1365  CB  GLU A 192      34.811  31.870   9.446  1.00 28.28           C  
ATOM   1366  CG  GLU A 192      36.058  32.100   8.674  1.00 35.76           C  
ATOM   1367  CD  GLU A 192      36.367  33.582   8.629  1.00 43.27           C  
ATOM   1368  OE1 GLU A 192      35.596  34.354   7.978  1.00 48.85           O  
ATOM   1369  OE2 GLU A 192      37.339  33.991   9.313  1.00 49.40           O  
ATOM   1370  N   ASP A 193      34.834  29.021   7.574  1.00 25.91           N  
ATOM   1371  CA  ASP A 193      34.541  28.445   6.286  1.00 25.03           C  
ATOM   1372  C   ASP A 193      33.815  27.081   6.350  1.00 23.92           C  
ATOM   1373  O   ASP A 193      33.767  26.365   5.353  1.00 21.16           O  
ATOM   1374  CB  ASP A 193      35.808  28.366   5.438  1.00 26.94           C  
ATOM   1375  CG  ASP A 193      36.836  27.456   6.027  1.00 29.28           C  
ATOM   1376  OD1 ASP A 193      36.741  27.047   7.203  1.00 30.81           O  
ATOM   1377  OD2 ASP A 193      37.779  27.146   5.307  1.00 32.50           O  
ATOM   1378  N   GLN A 194      33.320  26.686   7.535  1.00 21.92           N  
ATOM   1379  CA  GLN A 194      32.663  25.372   7.679  1.00 21.31           C  
ATOM   1380  C   GLN A 194      31.196  25.538   8.113  1.00 21.75           C  
ATOM   1381  O   GLN A 194      30.641  24.657   8.755  1.00 21.05           O  
ATOM   1382  CB  GLN A 194      33.407  24.487   8.722  1.00 21.62           C  
ATOM   1383  CG  GLN A 194      34.880  24.319   8.301  1.00 20.99           C  
ATOM   1384  CD  GLN A 194      34.999  23.609   6.960  1.00 25.30           C  
ATOM   1385  OE1 GLN A 194      34.278  22.645   6.686  1.00 24.73           O  
ATOM   1386  NE2 GLN A 194      35.952  24.047   6.132  1.00 25.94           N  
ATOM   1387  N   THR A 195      30.563  26.660   7.771  1.00 22.30           N  
ATOM   1388  CA  THR A 195      29.187  26.855   8.237  1.00 23.70           C  
ATOM   1389  C   THR A 195      28.138  26.095   7.439  1.00 22.46           C  
ATOM   1390  O   THR A 195      26.953  26.104   7.805  1.00 22.56           O  
ATOM   1391  CB  THR A 195      28.775  28.394   8.266  1.00 23.95           C  
ATOM   1392  OG1 THR A 195      28.904  28.864   6.930  1.00 25.46           O  
ATOM   1393  CG2 THR A 195      29.677  29.194   9.150  1.00 24.60           C  
ATOM   1394  N   GLU A 196      28.531  25.396   6.389  1.00 21.65           N  
ATOM   1395  CA  GLU A 196      27.556  24.472   5.743  1.00 21.53           C  
ATOM   1396  C   GLU A 196      26.964  23.440   6.716  1.00 20.14           C  
ATOM   1397  O   GLU A 196      25.880  22.870   6.469  1.00 18.43           O  
ATOM   1398  CB  GLU A 196      28.199  23.686   4.562  1.00 19.65           C  
ATOM   1399  CG  GLU A 196      29.215  22.669   4.959  1.00 22.01           C  
ATOM   1400  CD  GLU A 196      30.050  22.172   3.786  1.00 22.96           C  
ATOM   1401  OE1 GLU A 196      30.988  22.901   3.427  1.00 23.09           O  
ATOM   1402  OE2 GLU A 196      29.792  21.096   3.257  1.00 21.87           O  
ATOM   1403  N   TYR A 197      27.713  23.128   7.772  1.00 19.56           N  
ATOM   1404  CA  TYR A 197      27.280  22.079   8.741  1.00 18.84           C  
ATOM   1405  C   TYR A 197      26.248  22.649   9.733  1.00 19.53           C  
ATOM   1406  O   TYR A 197      25.836  21.955  10.631  1.00 18.96           O  
ATOM   1407  CB  TYR A 197      28.484  21.404   9.500  1.00 17.94           C  
ATOM   1408  CG  TYR A 197      29.432  20.764   8.476  1.00 14.21           C  
ATOM   1409  CD1 TYR A 197      29.038  19.674   7.774  1.00 17.13           C  
ATOM   1410  CD2 TYR A 197      30.672  21.336   8.193  1.00 13.85           C  
ATOM   1411  CE1 TYR A 197      29.834  19.143   6.755  1.00 17.41           C  
ATOM   1412  CE2 TYR A 197      31.500  20.810   7.204  1.00 17.51           C  
ATOM   1413  CZ  TYR A 197      31.061  19.717   6.497  1.00 16.07           C  
ATOM   1414  OH  TYR A 197      31.841  19.154   5.509  1.00 18.58           O  
ATOM   1415  N   LEU A 198      25.856  23.904   9.553  1.00 20.19           N  
ATOM   1416  CA  LEU A 198      24.675  24.420  10.235  1.00 20.63           C  
ATOM   1417  C   LEU A 198      23.451  24.395   9.340  1.00 21.46           C  
ATOM   1418  O   LEU A 198      22.412  24.815   9.788  1.00 21.53           O  
ATOM   1419  CB  LEU A 198      24.941  25.850  10.704  1.00 20.69           C  
ATOM   1420  CG  LEU A 198      26.176  25.949  11.602  1.00 20.31           C  
ATOM   1421  CD1 LEU A 198      26.509  27.404  11.791  1.00 24.50           C  
ATOM   1422  CD2 LEU A 198      25.963  25.231  12.949  1.00 25.49           C  
ATOM   1423  N   GLU A 199      23.578  23.986   8.075  1.00 21.36           N  
ATOM   1424  CA  GLU A 199      22.424  24.007   7.164  1.00 23.39           C  
ATOM   1425  C   GLU A 199      21.644  22.719   7.342  1.00 22.13           C  
ATOM   1426  O   GLU A 199      22.224  21.604   7.321  1.00 21.59           O  
ATOM   1427  CB  GLU A 199      22.872  24.104   5.681  1.00 24.33           C  
ATOM   1428  CG  GLU A 199      23.541  25.406   5.376  1.00 29.85           C  
ATOM   1429  CD  GLU A 199      22.584  26.589   5.547  1.00 39.49           C  
ATOM   1430  OE1 GLU A 199      21.396  26.501   5.128  1.00 44.59           O  
ATOM   1431  OE2 GLU A 199      23.025  27.620   6.114  1.00 45.12           O  
ATOM   1432  N   GLU A 200      20.335  22.861   7.543  1.00 22.83           N  
ATOM   1433  CA  GLU A 200      19.494  21.713   7.772  1.00 22.10           C  
ATOM   1434  C   GLU A 200      19.618  20.610   6.685  1.00 21.41           C  
ATOM   1435  O   GLU A 200      19.728  19.402   6.970  1.00 18.42           O  
ATOM   1436  CB  GLU A 200      18.007  22.172   7.909  1.00 23.80           C  
ATOM   1437  CG  GLU A 200      17.190  20.968   8.028  1.00 23.13           C  
ATOM   1438  CD  GLU A 200      15.683  21.196   8.207  1.00 36.16           C  
ATOM   1439  OE1 GLU A 200      15.188  22.296   7.882  1.00 33.60           O  
ATOM   1440  OE2 GLU A 200      15.018  20.248   8.696  1.00 38.61           O  
ATOM   1441  N   ARG A 201      19.590  20.977   5.408  1.00 21.61           N  
ATOM   1442  CA  ARG A 201      19.650  19.912   4.426  1.00 21.50           C  
ATOM   1443  C   ARG A 201      21.023  19.213   4.381  1.00 20.36           C  
ATOM   1444  O   ARG A 201      21.112  18.049   4.052  1.00 19.14           O  
ATOM   1445  CB  ARG A 201      19.368  20.499   3.050  1.00 22.80           C  
ATOM   1446  CG  ARG A 201      20.356  21.533   2.632  1.00 28.70           C  
ATOM   1447  CD  ARG A 201      19.718  22.196   1.370  1.00 34.92           C  
ATOM   1448  NE  ARG A 201      20.558  23.274   0.906  1.00 39.36           N  
ATOM   1449  CZ  ARG A 201      20.384  23.830  -0.286  1.00 42.98           C  
ATOM   1450  NH1 ARG A 201      19.409  23.373  -1.090  1.00 41.71           N  
ATOM   1451  NH2 ARG A 201      21.177  24.804  -0.664  1.00 44.06           N  
ATOM   1452  N   ARG A 202      22.092  19.966   4.650  1.00 20.11           N  
ATOM   1453  CA  ARG A 202      23.443  19.360   4.733  1.00 19.56           C  
ATOM   1454  C   ARG A 202      23.508  18.400   5.906  1.00 19.03           C  
ATOM   1455  O   ARG A 202      24.041  17.301   5.776  1.00 17.35           O  
ATOM   1456  CB  ARG A 202      24.474  20.441   4.877  1.00 18.25           C  
ATOM   1457  CG  ARG A 202      25.960  19.940   4.830  1.00 19.48           C  
ATOM   1458  CD  ARG A 202      26.381  19.533   3.367  1.00 20.26           C  
ATOM   1459  NE  ARG A 202      27.783  19.178   3.405  1.00 17.85           N  
ATOM   1460  CZ  ARG A 202      28.318  17.959   3.300  1.00 19.40           C  
ATOM   1461  NH1 ARG A 202      27.625  16.873   3.012  1.00 16.85           N  
ATOM   1462  NH2 ARG A 202      29.642  17.856   3.399  1.00 22.61           N  
ATOM   1463  N   ILE A 203      23.056  18.827   7.091  1.00 18.72           N  
ATOM   1464  CA  ILE A 203      23.093  17.897   8.192  1.00 18.09           C  
ATOM   1465  C   ILE A 203      22.273  16.639   7.887  1.00 18.50           C  
ATOM   1466  O   ILE A 203      22.731  15.537   8.181  1.00 17.42           O  
ATOM   1467  CB  ILE A 203      22.599  18.516   9.545  1.00 18.58           C  
ATOM   1468  CG1 ILE A 203      23.474  19.709   9.960  1.00 15.78           C  
ATOM   1469  CG2 ILE A 203      22.512  17.420  10.624  1.00 19.12           C  
ATOM   1470  CD1 ILE A 203      22.708  20.744  10.872  1.00 15.73           C  
ATOM   1471  N   LYS A 204      21.075  16.779   7.281  1.00 19.02           N  
ATOM   1472  CA  LYS A 204      20.193  15.612   7.050  1.00 18.25           C  
ATOM   1473  C   LYS A 204      20.884  14.675   6.081  1.00 17.52           C  
ATOM   1474  O   LYS A 204      20.851  13.449   6.215  1.00 16.87           O  
ATOM   1475  CB  LYS A 204      18.865  16.039   6.334  1.00 17.00           C  
ATOM   1476  CG  LYS A 204      17.809  16.610   7.187  1.00 26.57           C  
ATOM   1477  CD  LYS A 204      16.539  17.012   6.307  1.00 32.25           C  
ATOM   1478  CE  LYS A 204      15.729  18.056   7.121  1.00 38.65           C  
ATOM   1479  NZ  LYS A 204      14.559  18.719   6.416  1.00 40.01           N  
ATOM   1480  N   GLU A 205      21.520  15.262   5.051  1.00 17.07           N  
ATOM   1481  CA  GLU A 205      22.247  14.431   4.077  1.00 16.21           C  
ATOM   1482  C   GLU A 205      23.310  13.583   4.743  1.00 15.06           C  
ATOM   1483  O   GLU A 205      23.464  12.421   4.441  1.00 15.24           O  
ATOM   1484  CB  GLU A 205      22.927  15.383   3.072  1.00 16.53           C  
ATOM   1485  CG  GLU A 205      23.862  14.674   2.110  1.00 19.60           C  
ATOM   1486  CD  GLU A 205      24.581  15.631   1.186  1.00 16.84           C  
ATOM   1487  OE1 GLU A 205      25.107  16.706   1.642  1.00 20.68           O  
ATOM   1488  OE2 GLU A 205      24.532  15.384  -0.052  1.00 20.10           O  
ATOM   1489  N   ILE A 206      24.086  14.165   5.629  1.00 16.00           N  
ATOM   1490  CA  ILE A 206      25.217  13.426   6.296  1.00 16.34           C  
ATOM   1491  C   ILE A 206      24.715  12.351   7.259  1.00 18.15           C  
ATOM   1492  O   ILE A 206      25.273  11.247   7.301  1.00 18.11           O  
ATOM   1493  CB  ILE A 206      26.082  14.422   7.007  1.00 17.77           C  
ATOM   1494  CG1 ILE A 206      26.690  15.377   5.980  1.00 19.73           C  
ATOM   1495  CG2 ILE A 206      27.203  13.770   7.831  1.00 16.48           C  
ATOM   1496  CD1 ILE A 206      27.268  16.621   6.662  1.00 18.64           C  
ATOM   1497  N   VAL A 207      23.625  12.628   8.009  1.00 16.78           N  
ATOM   1498  CA  VAL A 207      23.084  11.630   8.916  1.00 16.65           C  
ATOM   1499  C   VAL A 207      22.587  10.469   8.111  1.00 17.35           C  
ATOM   1500  O   VAL A 207      22.819   9.317   8.447  1.00 18.18           O  
ATOM   1501  CB  VAL A 207      21.927  12.277   9.807  1.00 17.64           C  
ATOM   1502  CG1 VAL A 207      21.087  11.221  10.602  1.00 17.49           C  
ATOM   1503  CG2 VAL A 207      22.524  13.440  10.744  1.00 16.35           C  
ATOM   1504  N   LYS A 208      21.890  10.752   7.023  1.00 18.81           N  
ATOM   1505  CA  LYS A 208      21.316   9.660   6.192  1.00 20.14           C  
ATOM   1506  C   LYS A 208      22.431   8.862   5.530  1.00 20.14           C  
ATOM   1507  O   LYS A 208      22.405   7.613   5.527  1.00 20.50           O  
ATOM   1508  CB  LYS A 208      20.376  10.295   5.164  1.00 21.61           C  
ATOM   1509  CG  LYS A 208      19.661   9.270   4.226  1.00 27.25           C  
ATOM   1510  CD  LYS A 208      18.794   9.999   3.187  1.00 30.91           C  
ATOM   1511  CE  LYS A 208      18.517   9.004   2.036  1.00 37.20           C  
ATOM   1512  NZ  LYS A 208      17.519   9.675   1.156  1.00 42.61           N  
ATOM   1513  N   LYS A 209      23.486   9.558   5.098  1.00 20.61           N  
ATOM   1514  CA  LYS A 209      24.671   8.909   4.414  1.00 22.86           C  
ATOM   1515  C   LYS A 209      25.490   8.002   5.327  1.00 22.96           C  
ATOM   1516  O   LYS A 209      25.865   6.892   4.958  1.00 21.73           O  
ATOM   1517  CB  LYS A 209      25.611  10.009   3.890  1.00 21.50           C  
ATOM   1518  CG  LYS A 209      26.893   9.448   3.326  1.00 28.15           C  
ATOM   1519  CD  LYS A 209      27.610  10.494   2.481  1.00 34.47           C  
ATOM   1520  CE  LYS A 209      28.538   9.743   1.524  1.00 41.61           C  
ATOM   1521  NZ  LYS A 209      29.581  10.664   0.874  1.00 47.46           N  
ATOM   1522  N   HIS A 210      25.732   8.447   6.564  1.00 23.12           N  
ATOM   1523  CA  HIS A 210      26.740   7.799   7.450  1.00 24.06           C  
ATOM   1524  C   HIS A 210      26.221   7.258   8.804  1.00 23.38           C  
ATOM   1525  O   HIS A 210      26.905   6.493   9.460  1.00 22.99           O  
ATOM   1526  CB  HIS A 210      27.826   8.825   7.815  1.00 22.87           C  
ATOM   1527  CG  HIS A 210      28.646   9.256   6.664  1.00 28.99           C  
ATOM   1528  ND1 HIS A 210      29.504   8.392   6.000  1.00 27.16           N  
ATOM   1529  CD2 HIS A 210      28.773  10.465   6.060  1.00 30.34           C  
ATOM   1530  CE1 HIS A 210      30.123   9.060   5.040  1.00 27.15           C  
ATOM   1531  NE2 HIS A 210      29.695  10.312   5.050  1.00 32.02           N  
ATOM   1532  N   SER A 211      25.019   7.631   9.189  1.00 22.22           N  
ATOM   1533  CA  SER A 211      24.507   7.301  10.539  1.00 23.40           C  
ATOM   1534  C   SER A 211      23.095   6.669  10.453  1.00 24.05           C  
ATOM   1535  O   SER A 211      22.321   6.713  11.402  1.00 22.07           O  
ATOM   1536  CB  SER A 211      24.493   8.600  11.381  1.00 23.01           C  
ATOM   1537  OG  SER A 211      25.849   9.130  11.484  1.00 21.49           O  
ATOM   1538  N   GLN A 212      22.769   6.016   9.326  1.00 26.54           N  
ATOM   1539  CA AGLN A 212      21.385   5.556   9.115  0.50 26.93           C  
ATOM   1540  CA BGLN A 212      21.396   5.506   9.085  0.50 27.80           C  
ATOM   1541  C   GLN A 212      20.963   4.410  10.026  1.00 27.88           C  
ATOM   1542  O   GLN A 212      19.769   4.246  10.284  1.00 29.09           O  
ATOM   1543  CB AGLN A 212      21.151   5.129   7.659  0.50 27.66           C  
ATOM   1544  CB BGLN A 212      21.211   4.971   7.647  0.50 28.80           C  
ATOM   1545  CG AGLN A 212      22.017   3.974   7.250  0.50 26.11           C  
ATOM   1546  CG BGLN A 212      20.204   5.753   6.827  0.50 31.64           C  
ATOM   1547  CD AGLN A 212      23.336   4.387   6.568  0.50 25.43           C  
ATOM   1548  CD BGLN A 212      19.591   4.914   5.745  0.50 35.60           C  
ATOM   1549  OE1AGLN A 212      24.142   5.144   7.103  0.50 20.50           O  
ATOM   1550  OE1BGLN A 212      20.200   3.941   5.274  0.50 37.53           O  
ATOM   1551  NE2AGLN A 212      23.560   3.834   5.373  0.50 28.21           N  
ATOM   1552  NE2BGLN A 212      18.363   5.272   5.339  0.50 36.46           N  
ATOM   1553  N   PHE A 213      21.919   3.626  10.512  1.00 26.90           N  
ATOM   1554  CA  PHE A 213      21.583   2.513  11.364  1.00 27.55           C  
ATOM   1555  C   PHE A 213      21.970   2.720  12.802  1.00 27.48           C  
ATOM   1556  O   PHE A 213      22.212   1.765  13.490  1.00 30.23           O  
ATOM   1557  CB  PHE A 213      22.341   1.257  10.900  1.00 28.76           C  
ATOM   1558  CG  PHE A 213      21.952   0.855   9.481  1.00 31.99           C  
ATOM   1559  CD1 PHE A 213      20.632   0.552   9.194  1.00 35.35           C  
ATOM   1560  CD2 PHE A 213      22.869   0.908   8.441  1.00 35.53           C  
ATOM   1561  CE1 PHE A 213      20.223   0.256   7.866  1.00 38.20           C  
ATOM   1562  CE2 PHE A 213      22.478   0.602   7.132  1.00 35.89           C  
ATOM   1563  CZ  PHE A 213      21.150   0.291   6.845  1.00 36.67           C  
ATOM   1564  N   ILE A 214      22.093   3.938  13.250  1.00 23.53           N  
ATOM   1565  CA  ILE A 214      22.324   4.137  14.658  1.00 22.20           C  
ATOM   1566  C   ILE A 214      21.018   3.769  15.436  1.00 22.44           C  
ATOM   1567  O   ILE A 214      19.940   4.160  15.011  1.00 22.81           O  
ATOM   1568  CB  ILE A 214      22.699   5.662  14.863  1.00 21.09           C  
ATOM   1569  CG1 ILE A 214      24.098   5.913  14.239  1.00 16.79           C  
ATOM   1570  CG2 ILE A 214      22.647   6.032  16.391  1.00 19.77           C  
ATOM   1571  CD1 ILE A 214      25.266   5.211  15.046  1.00 20.51           C  
ATOM   1572  N   GLY A 215      21.121   3.090  16.566  1.00 19.66           N  
ATOM   1573  CA  GLY A 215      19.966   2.540  17.262  1.00 20.08           C  
ATOM   1574  C   GLY A 215      19.252   3.428  18.278  1.00 20.31           C  
ATOM   1575  O   GLY A 215      18.602   2.932  19.179  1.00 21.40           O  
ATOM   1576  N   TYR A 216      19.336   4.742  18.113  1.00 18.25           N  
ATOM   1577  CA  TYR A 216      18.704   5.663  19.065  1.00 19.53           C  
ATOM   1578  C   TYR A 216      18.141   6.737  18.158  1.00 18.72           C  
ATOM   1579  O   TYR A 216      18.734   7.018  17.091  1.00 18.91           O  
ATOM   1580  CB  TYR A 216      19.768   6.264  20.041  1.00 16.90           C  
ATOM   1581  CG  TYR A 216      20.407   5.214  20.885  1.00 18.81           C  
ATOM   1582  CD1 TYR A 216      19.782   4.765  22.057  1.00 18.97           C  
ATOM   1583  CD2 TYR A 216      21.619   4.610  20.506  1.00 17.18           C  
ATOM   1584  CE1 TYR A 216      20.309   3.738  22.760  1.00 17.86           C  
ATOM   1585  CE2 TYR A 216      22.161   3.597  21.255  1.00 15.69           C  
ATOM   1586  CZ  TYR A 216      21.502   3.211  22.413  1.00 15.99           C  
ATOM   1587  OH  TYR A 216      22.019   2.215  23.168  1.00 15.62           O  
ATOM   1588  N   PRO A 217      17.040   7.365  18.577  1.00 18.51           N  
ATOM   1589  CA  PRO A 217      16.510   8.445  17.790  1.00 17.58           C  
ATOM   1590  C   PRO A 217      17.457   9.639  17.709  1.00 18.41           C  
ATOM   1591  O   PRO A 217      18.093  10.022  18.715  1.00 18.12           O  
ATOM   1592  CB  PRO A 217      15.168   8.806  18.504  1.00 19.66           C  
ATOM   1593  CG  PRO A 217      15.329   8.339  19.911  1.00 22.72           C  
ATOM   1594  CD  PRO A 217      16.317   7.119  19.855  1.00 17.56           C  
ATOM   1595  N   ILE A 218      17.606  10.200  16.519  1.00 19.22           N  
ATOM   1596  CA  ILE A 218      18.510  11.358  16.276  1.00 17.61           C  
ATOM   1597  C   ILE A 218      17.567  12.447  15.829  1.00 17.29           C  
ATOM   1598  O   ILE A 218      16.899  12.286  14.766  1.00 17.53           O  
ATOM   1599  CB  ILE A 218      19.483  11.078  15.148  1.00 17.60           C  
ATOM   1600  CG1 ILE A 218      20.492   9.940  15.588  1.00 17.45           C  
ATOM   1601  CG2 ILE A 218      20.215  12.376  14.797  1.00 15.97           C  
ATOM   1602  CD1 ILE A 218      21.410   9.477  14.455  1.00 16.78           C  
ATOM   1603  N   THR A 219      17.463  13.524  16.622  1.00 14.71           N  
ATOM   1604  CA  THR A 219      16.553  14.593  16.312  1.00 14.13           C  
ATOM   1605  C   THR A 219      17.337  15.803  15.874  1.00 14.45           C  
ATOM   1606  O   THR A 219      18.188  16.322  16.608  1.00 13.83           O  
ATOM   1607  CB  THR A 219      15.699  14.975  17.548  1.00 13.35           C  
ATOM   1608  OG1 THR A 219      14.981  13.825  17.925  1.00 15.23           O  
ATOM   1609  CG2 THR A 219      14.689  16.101  17.184  1.00 19.65           C  
ATOM   1610  N   LEU A 220      17.066  16.238  14.666  1.00 14.80           N  
ATOM   1611  CA  LEU A 220      17.745  17.431  14.136  1.00 16.86           C  
ATOM   1612  C   LEU A 220      16.849  18.619  14.436  1.00 17.00           C  
ATOM   1613  O   LEU A 220      15.718  18.719  13.832  1.00 16.44           O  
ATOM   1614  CB  LEU A 220      17.951  17.281  12.576  1.00 14.90           C  
ATOM   1615  CG  LEU A 220      18.434  18.536  11.872  1.00 17.33           C  
ATOM   1616  CD1 LEU A 220      19.621  19.219  12.510  1.00 17.61           C  
ATOM   1617  CD2 LEU A 220      18.750  18.245  10.289  1.00 17.34           C  
ATOM   1618  N   PHE A 221      17.311  19.491  15.337  1.00 15.53           N  
ATOM   1619  CA  PHE A 221      16.517  20.703  15.721  1.00 17.53           C  
ATOM   1620  C   PHE A 221      16.534  21.727  14.545  1.00 19.57           C  
ATOM   1621  O   PHE A 221      17.529  21.814  13.771  1.00 17.94           O  
ATOM   1622  CB  PHE A 221      17.130  21.387  16.953  1.00 15.03           C  
ATOM   1623  CG  PHE A 221      16.835  20.704  18.247  1.00 15.98           C  
ATOM   1624  CD1 PHE A 221      16.733  19.304  18.315  1.00 12.80           C  
ATOM   1625  CD2 PHE A 221      16.706  21.457  19.432  1.00 14.39           C  
ATOM   1626  CE1 PHE A 221      16.529  18.614  19.535  1.00 12.83           C  
ATOM   1627  CE2 PHE A 221      16.436  20.804  20.626  1.00 14.86           C  
ATOM   1628  CZ  PHE A 221      16.331  19.354  20.683  1.00 13.74           C  
ATOM   1629  N   VAL A 222      15.441  22.504  14.449  1.00 19.03           N  
ATOM   1630  CA  VAL A 222      15.191  23.565  13.464  1.00 23.02           C  
ATOM   1631  C   VAL A 222      15.570  24.908  14.087  1.00 22.74           C  
ATOM   1632  O   VAL A 222      15.557  25.052  15.317  1.00 20.43           O  
ATOM   1633  CB  VAL A 222      13.606  23.670  13.212  1.00 21.64           C  
ATOM   1634  CG1 VAL A 222      13.323  24.635  12.070  1.00 29.35           C  
ATOM   1635  CG2 VAL A 222      13.029  22.351  12.894  1.00 29.88           C  
ATOM   1636  N   GLU A 223      15.912  25.895  13.297  1.00 24.14           N  
ATOM   1637  CA  GLU A 223      16.121  27.221  13.902  1.00 28.09           C  
ATOM   1638  C   GLU A 223      14.926  28.236  13.757  1.00 30.41           C  
ATOM   1639  O   GLU A 223      14.397  28.207  12.673  1.00 29.98           O  
ATOM   1640  CB  GLU A 223      17.415  27.805  13.361  1.00 30.12           C  
ATOM   1641  CG  GLU A 223      18.620  27.034  13.863  1.00 28.42           C  
ATOM   1642  CD  GLU A 223      19.865  27.501  13.213  1.00 31.65           C  
ATOM   1643  OE1 GLU A 223      20.332  28.559  13.699  1.00 24.92           O  
ATOM   1644  OE2 GLU A 223      20.354  26.801  12.250  1.00 34.33           O  
ATOM   1645  N   LYS A 224      14.450  29.097  14.612  1.00 31.40           N  
TER    1646      LYS A 224                                                      
HETATM 1647 MG    MG A1224      46.565   4.031  25.677  1.00 15.50          MG  
HETATM 1648  N5  ZZ3 A1225      29.038  10.758  24.543  1.00 20.32           N  
HETATM 1649  C2  ZZ3 A1225      30.205  11.105  23.949  1.00 29.90           C  
HETATM 1650  N4  ZZ3 A1225      31.380  10.747  24.509  1.00 34.73           N  
HETATM 1651  N1  ZZ3 A1225      30.194  11.809  22.797  1.00 32.44           N  
HETATM 1652  C3  ZZ3 A1225      31.357  12.155  22.205  1.00 26.18           C  
HETATM 1653  C8  ZZ3 A1225      31.344  12.940  20.921  1.00 26.11           C  
HETATM 1654  N3  ZZ3 A1225      32.532  11.797  22.766  1.00 37.73           N  
HETATM 1655  C4  ZZ3 A1225      32.543  11.092  23.917  1.00 35.69           C  
HETATM 1656  S1  ZZ3 A1225      34.018  10.642  24.621  1.00 43.64           S  
HETATM 1657  C6  ZZ3 A1225      35.207  10.347  23.354  1.00 32.24           C  
HETATM 1658  O   HOH A2001      35.754  24.690  38.520  1.00 35.04           O  
HETATM 1659  O   HOH A2002      40.071  26.219  40.284  1.00 60.10           O  
HETATM 1660  O   HOH A2003      44.823  25.555  38.234  1.00 28.75           O  
HETATM 1661  O   HOH A2004      40.680  30.360  37.517  1.00 49.43           O  
HETATM 1662  O   HOH A2005      43.841  22.414  40.349  1.00 44.92           O  
HETATM 1663  O   HOH A2006      43.013  18.655  39.107  1.00 51.30           O  
HETATM 1664  O   HOH A2007      41.359  19.913  41.249  1.00 46.40           O  
HETATM 1665  O   HOH A2008      44.339  27.490  34.541  1.00 28.46           O  
HETATM 1666  O   HOH A2009      43.933  28.290  30.366  1.00 26.69           O  
HETATM 1667  O   HOH A2010      46.926  16.061  30.732  1.00 28.86           O  
HETATM 1668  O   HOH A2011      50.245  15.071  29.766  1.00 41.31           O  
HETATM 1669  O   HOH A2012      52.338  16.682  27.440  1.00 35.65           O  
HETATM 1670  O   HOH A2013      46.311  14.274  26.797  1.00 20.18           O  
HETATM 1671  O   HOH A2014      48.328   7.239  27.853  1.00 36.78           O  
HETATM 1672  O   HOH A2015      47.117  11.298  29.380  1.00 50.27           O  
HETATM 1673  O   HOH A2016      44.101  30.289  34.410  1.00 47.06           O  
HETATM 1674  O   HOH A2017      43.521  28.073  27.700  1.00 33.18           O  
HETATM 1675  O   HOH A2018      53.310  14.193  26.791  1.00 36.34           O  
HETATM 1676  O   HOH A2019      54.539  17.682  25.162  1.00 38.05           O  
HETATM 1677  O   HOH A2020      52.903  10.516  26.077  1.00 30.79           O  
HETATM 1678  O   HOH A2021      56.716  15.858  25.269  1.00 42.28           O  
HETATM 1679  O   HOH A2022      50.299  18.050   9.497  1.00 60.83           O  
HETATM 1680  O   HOH A2023      48.181  20.061  18.846  1.00 21.96           O  
HETATM 1681  O   HOH A2024      55.476  15.826  18.634  1.00 52.19           O  
HETATM 1682  O   HOH A2025      51.220  15.966  13.690  1.00 39.84           O  
HETATM 1683  O   HOH A2026      43.451  22.244   4.352  1.00 45.33           O  
HETATM 1684  O   HOH A2027      50.958  17.485   6.223  1.00 59.14           O  
HETATM 1685  O   HOH A2028      39.491  21.249   2.653  1.00 26.45           O  
HETATM 1686  O   HOH A2029      40.289  23.099  -2.031  1.00 27.29           O  
HETATM 1687  O   HOH A2030      41.251  20.341   9.365  1.00 22.99           O  
HETATM 1688  O   HOH A2031      42.559  17.161   7.883  1.00 21.65           O  
HETATM 1689  O   HOH A2032      43.158  21.157   7.012  1.00 37.90           O  
HETATM 1690  O   HOH A2033      42.937  23.717   9.309  1.00 38.71           O  
HETATM 1691  O   HOH A2034      32.646   1.231  15.955  1.00 55.60           O  
HETATM 1692  O   HOH A2035      34.211   7.922  23.105  1.00 33.85           O  
HETATM 1693  O   HOH A2036      42.595  12.908  37.073  1.00 50.33           O  
HETATM 1694  O   HOH A2037      49.423  14.446   7.285  1.00 35.62           O  
HETATM 1695  O   HOH A2038      49.283   3.050  26.461  1.00 42.19           O  
HETATM 1696  O   HOH A2039      46.855  15.228   2.043  1.00 36.43           O  
HETATM 1697  O   HOH A2040      48.572  18.275   3.512  1.00 37.27           O  
HETATM 1698  O   HOH A2041      41.672  20.161   4.220  1.00 25.96           O  
HETATM 1699  O   HOH A2042      40.453  18.620   6.465  1.00 20.06           O  
HETATM 1700  O   HOH A2043      38.241   9.815   2.637  1.00 52.41           O  
HETATM 1701  O   HOH A2044      35.698  20.280   2.739  1.00 34.19           O  
HETATM 1702  O   HOH A2045      34.621  17.839   0.046  1.00 33.95           O  
HETATM 1703  O   HOH A2046      38.876  20.916   0.127  1.00 22.79           O  
HETATM 1704  O   HOH A2047      34.013   8.523   4.021  1.00 21.09           O  
HETATM 1705  O   HOH A2048      33.312  14.504   1.483  1.00 32.41           O  
HETATM 1706  O   HOH A2049      40.818  23.013   7.084  1.00 27.54           O  
HETATM 1707  O   HOH A2050      31.847  11.274   3.232  1.00 40.48           O  
HETATM 1708  O   HOH A2051      30.091  15.512   0.202  1.00 35.11           O  
HETATM 1709  O   HOH A2052      32.858  16.565   3.357  1.00 19.31           O  
HETATM 1710  O   HOH A2053      20.228  16.295  27.936  1.00 33.56           O  
HETATM 1711  O   HOH A2054      29.573  11.936   9.137  1.00 34.30           O  
HETATM 1712  O   HOH A2055      31.602   5.768  12.228  1.00 49.71           O  
HETATM 1713  O   HOH A2056      22.668  26.044  20.522  1.00 28.70           O  
HETATM 1714  O   HOH A2057      17.775  29.088  17.101  1.00 50.86           O  
HETATM 1715  O   HOH A2058      25.869  30.711   9.041  1.00 32.47           O  
HETATM 1716  O   HOH A2059      33.427   5.318  14.110  1.00 37.92           O  
HETATM 1717  O   HOH A2060      34.257   7.785  16.671  1.00 20.12           O  
HETATM 1718  O   HOH A2061      26.174  26.716  23.242  1.00 48.62           O  
HETATM 1719  O   HOH A2062      29.054  13.280  20.368  1.00 17.86           O  
HETATM 1720  O   HOH A2063      33.601   4.600  16.145  1.00 40.70           O  
HETATM 1721  O   HOH A2064      28.182   3.465  15.770  1.00 35.94           O  
HETATM 1722  O   HOH A2065      31.511   7.202  23.821  1.00 24.57           O  
HETATM 1723  O   HOH A2066      35.884   6.646  20.521  1.00 42.66           O  
HETATM 1724  O   HOH A2067      38.917   7.023  36.056  1.00 50.28           O  
HETATM 1725  O   HOH A2068      36.339   9.265  39.102  1.00 43.12           O  
HETATM 1726  O   HOH A2069      40.359  14.215  38.175  1.00 35.12           O  
HETATM 1727  O   HOH A2070      23.565   2.301  17.655  1.00 18.44           O  
HETATM 1728  O   HOH A2071      27.002   2.051  19.550  1.00 16.18           O  
HETATM 1729  O   HOH A2072      30.464   0.015  19.592  1.00 32.94           O  
HETATM 1730  O   HOH A2073      29.702   1.187  24.438  1.00 24.02           O  
HETATM 1731  O   HOH A2074      29.870   3.090  17.554  1.00 35.99           O  
HETATM 1732  O   HOH A2075      32.525   5.402  18.511  1.00 26.29           O  
HETATM 1733  O   HOH A2076      52.917   5.878  21.311  1.00 36.13           O  
HETATM 1734  O   HOH A2077      51.682   8.314  18.014  1.00 37.91           O  
HETATM 1735  O   HOH A2078      51.181   3.486  23.534  1.00 38.16           O  
HETATM 1736  O   HOH A2079      23.234   0.491  19.784  1.00 30.04           O  
HETATM 1737  O   HOH A2080      28.475  -0.329  22.448  1.00 37.69           O  
HETATM 1738  O   HOH A2081      27.501  -2.351  26.315  1.00 42.36           O  
HETATM 1739  O   HOH A2082      31.272   6.349  26.233  1.00 26.97           O  
HETATM 1740  O   HOH A2083      27.930  -0.468  30.641  1.00 32.43           O  
HETATM 1741  O   HOH A2084      33.329   4.649  30.206  1.00 44.82           O  
HETATM 1742  O   HOH A2085      33.787   0.674  28.225  0.50 29.36           O  
HETATM 1743  O   HOH A2086      17.237   1.249  26.800  1.00 54.68           O  
HETATM 1744  O   HOH A2087      19.470   0.716  20.627  1.00 33.22           O  
HETATM 1745  O   HOH A2088      16.677   2.970  21.247  1.00 26.78           O  
HETATM 1746  O   HOH A2089      43.535  11.603   2.196  1.00 38.94           O  
HETATM 1747  O   HOH A2090      46.723  11.460   5.305  1.00 35.48           O  
HETATM 1748  O   HOH A2091      25.350  -7.571  33.527  1.00 29.17           O  
HETATM 1749  O   HOH A2092      24.283  -4.702  33.641  1.00 24.53           O  
HETATM 1750  O   HOH A2093      26.242   5.048  35.699  1.00  9.45           O  
HETATM 1751  O   HOH A2094      24.480  -1.530  36.603  1.00 31.13           O  
HETATM 1752  O   HOH A2095      30.026   2.994  35.335  1.00 38.77           O  
HETATM 1753  O   HOH A2096      33.420   3.405   9.295  1.00 63.60           O  
HETATM 1754  O   HOH A2097      36.489   0.076  16.564  1.00 49.11           O  
HETATM 1755  O   HOH A2098      17.087  -0.167  30.474  1.00 38.92           O  
HETATM 1756  O   HOH A2099      19.268  -8.370  34.232  1.00 67.37           O  
HETATM 1757  O   HOH A2100      16.674  -5.380  37.056  1.00 47.69           O  
HETATM 1758  O   HOH A2101      26.222  -3.573  34.699  1.00 40.16           O  
HETATM 1759  O   HOH A2102      42.255  25.219  14.584  1.00 43.82           O  
HETATM 1760  O   HOH A2103      39.063  29.826  25.063  1.00 39.34           O  
HETATM 1761  O   HOH A2104      14.648   3.065  35.471  1.00 41.87           O  
HETATM 1762  O   HOH A2105      20.681   7.706  38.168  1.00 34.37           O  
HETATM 1763  O   HOH A2106      38.675  12.998  39.869  1.00 29.34           O  
HETATM 1764  O   HOH A2107      37.095  15.023  41.498  1.00 46.51           O  
HETATM 1765  O   HOH A2108      44.773  27.881  23.627  1.00 50.52           O  
HETATM 1766  O   HOH A2109      51.923  20.481  22.186  1.00 31.34           O  
HETATM 1767  O   HOH A2110      53.581  21.278  25.920  1.00 52.61           O  
HETATM 1768  O   HOH A2111      17.554  11.107  29.636  1.00 27.56           O  
HETATM 1769  O   HOH A2112      14.987   5.372  25.540  1.00 32.38           O  
HETATM 1770  O   HOH A2113      15.673   5.414  22.796  1.00 24.95           O  
HETATM 1771  O   HOH A2114      19.001  16.184  26.079  1.00 31.69           O  
HETATM 1772  O   HOH A2115      14.083  10.933  23.884  1.00 34.81           O  
HETATM 1773  O   HOH A2116      14.246  11.446  21.085  1.00 41.27           O  
HETATM 1774  O   HOH A2117      20.978  26.496  27.606  1.00 34.93           O  
HETATM 1775  O   HOH A2118      19.132  18.712  24.328  1.00 16.71           O  
HETATM 1776  O   HOH A2119      14.510  15.053  22.723  1.00 39.07           O  
HETATM 1777  O   HOH A2120      24.507  24.664  18.814  1.00 18.52           O  
HETATM 1778  O   HOH A2121      28.535  28.091  23.141  1.00 39.64           O  
HETATM 1779  O   HOH A2122      29.993  26.343  27.044  1.00 47.19           O  
HETATM 1780  O   HOH A2123      19.343  26.301  17.808  1.00 23.98           O  
HETATM 1781  O   HOH A2124      20.489  31.828  18.941  1.00 59.66           O  
HETATM 1782  O   HOH A2125      20.362  26.797  19.910  1.00 24.82           O  
HETATM 1783  O   HOH A2126      26.998  31.024  11.206  1.00 27.09           O  
HETATM 1784  O   HOH A2127      18.228  29.148   9.664  1.00 45.93           O  
HETATM 1785  O   HOH A2128      27.667  25.152   1.371  1.00 56.71           O  
HETATM 1786  O   HOH A2129      16.145  15.422   9.984  1.00 46.38           O  
HETATM 1787  O   HOH A2130      26.799  34.961  19.654  1.00 62.03           O  
HETATM 1788  O   HOH A2131      25.355  28.005  20.752  1.00 34.32           O  
HETATM 1789  O   HOH A2132      16.664  12.408   6.323  1.00 39.05           O  
HETATM 1790  O   HOH A2133      18.419  14.048  10.202  1.00 28.05           O  
HETATM 1791  O   HOH A2134      20.466  13.005   0.909  1.00 28.43           O  
HETATM 1792  O   HOH A2135      22.018   8.648   1.570  1.00 49.48           O  
HETATM 1793  O   HOH A2136      24.305  10.664  -0.111  1.00 43.52           O  
HETATM 1794  O   HOH A2137      28.774  32.778  10.918  1.00 43.18           O  
HETATM 1795  O   HOH A2138      20.601   9.382  -1.795  1.00 49.10           O  
HETATM 1796  O   HOH A2139      17.811   9.056  11.206  1.00 47.25           O  
HETATM 1797  O   HOH A2140      25.095  24.386  22.784  1.00 26.63           O  
HETATM 1798  O   HOH A2141      27.513  14.442  22.571  1.00 16.69           O  
HETATM 1799  O   HOH A2142      14.701  33.075  10.674  1.00 67.79           O  
HETATM 1800  O   HOH A2143      27.465  10.345  27.327  1.00 15.12           O  
HETATM 1801  O   HOH A2144      22.391  14.960  28.146  1.00 27.22           O  
HETATM 1802  O   HOH A2145      32.373   7.275  31.071  1.00 27.72           O  
HETATM 1803  O   HOH A2146      30.950   8.607  28.007  1.00 32.51           O  
HETATM 1804  O   HOH A2147      36.331   7.805  36.725  1.00 36.13           O  
HETATM 1805  O   HOH A2148      41.262  16.176  39.397  1.00 29.27           O  
HETATM 1806  O   HOH A2149      37.410  19.354  40.240  1.00 41.53           O  
HETATM 1807  O   HOH A2150      41.422  15.502  27.912  1.00 18.96           O  
HETATM 1808  O   HOH A2151      45.560  14.141  29.852  1.00 28.95           O  
HETATM 1809  O   HOH A2152      47.197   8.224  30.349  1.00 61.87           O  
HETATM 1810  O   HOH A2153      43.885   8.039  27.619  1.00 23.29           O  
HETATM 1811  O   HOH A2154      33.765   8.793  26.816  1.00 33.71           O  
HETATM 1812  O   HOH A2155      34.870   5.939  26.227  1.00 31.34           O  
HETATM 1813  O   HOH A2156      35.885   5.174  29.349  1.00 45.61           O  
HETATM 1814  O   HOH A2157      39.466   4.890  22.838  1.00 43.62           O  
HETATM 1815  O   HOH A2158      50.966   7.279  20.529  1.00 33.30           O  
HETATM 1816  O   HOH A2159      45.977   6.761  26.195  1.00 29.23           O  
HETATM 1817  O   HOH A2160      53.330   3.541  26.203  1.00 62.88           O  
HETATM 1818  O   HOH A2161      48.622   0.988  19.617  1.00 34.11           O  
HETATM 1819  O   HOH A2162      44.288   1.545  20.347  1.00 37.55           O  
HETATM 1820  O   HOH A2163      50.043  -0.274  17.684  1.00 41.28           O  
HETATM 1821  O   HOH A2164      52.781   4.960  14.685  1.00 48.09           O  
HETATM 1822  O   HOH A2165      54.191   2.993  14.929  1.00 54.04           O  
HETATM 1823  O   HOH A2166      48.740  -1.284  15.223  1.00 41.32           O  
HETATM 1824  O   HOH A2167      43.855  11.302   4.718  1.00 39.58           O  
HETATM 1825  O   HOH A2168      36.224   6.175  11.139  1.00 22.45           O  
HETATM 1826  O   HOH A2169      35.760   5.591   6.163  1.00 53.06           O  
HETATM 1827  O   HOH A2170      35.105   3.904  17.453  1.00 39.37           O  
HETATM 1828  O   HOH A2171      40.457  -1.218  15.135  1.00 35.81           O  
HETATM 1829  O   HOH A2172      35.846   3.961   8.689  1.00 41.13           O  
HETATM 1830  O   HOH A2173      34.897   2.980  13.005  1.00 48.17           O  
HETATM 1831  O   HOH A2174      42.235   3.266  20.519  1.00 35.97           O  
HETATM 1832  O   HOH A2175      37.425   1.886  18.727  1.00 39.53           O  
HETATM 1833  O   HOH A2176      36.374   6.802  17.873  1.00 20.79           O  
HETATM 1834  O   HOH A2177      36.828   9.132  20.473  1.00 20.47           O  
HETATM 1835  O   HOH A2178      42.445  14.689  25.234  1.00 18.14           O  
HETATM 1836  O   HOH A2179      40.454  23.178  14.218  1.00 23.28           O  
HETATM 1837  O   HOH A2180      35.193  29.797  18.876  1.00 38.48           O  
HETATM 1838  O   HOH A2181      41.740  26.435  16.957  1.00 28.45           O  
HETATM 1839  O   HOH A2182      33.440  29.494  15.944  1.00 30.46           O  
HETATM 1840  O   HOH A2183      36.529  29.595  25.343  1.00 33.33           O  
HETATM 1841  O   HOH A2184      23.910  11.900  36.431  1.00 23.91           O  
HETATM 1842  O   HOH A2185      24.546  13.930  40.611  1.00 59.89           O  
HETATM 1843  O   HOH A2186      31.150   4.589  33.843  1.00 31.85           O  
HETATM 1844  O   HOH A2187      30.353  13.715  35.645  1.00 21.57           O  
HETATM 1845  O   HOH A2188      26.130   7.750  34.367  1.00 20.16           O  
HETATM 1846  O   HOH A2189      23.736  10.588  40.341  1.00 49.75           O  
HETATM 1847  O   HOH A2190      26.122   5.115  39.100  1.00 43.20           O  
HETATM 1848  O   HOH A2191      36.405  11.881  38.580  1.00 26.36           O  
HETATM 1849  O   HOH A2192      23.717  17.942  36.213  1.00 39.47           O  
HETATM 1850  O   HOH A2193      26.840  19.013  38.969  1.00 39.52           O  
HETATM 1851  O   HOH A2194      34.648  15.397  40.961  1.00 45.29           O  
HETATM 1852  O   HOH A2195      40.688  25.894  25.678  1.00 36.86           O  
HETATM 1853  O   HOH A2196      34.974  26.190  29.317  1.00 39.13           O  
HETATM 1854  O   HOH A2197      43.217  25.308  23.621  1.00 20.27           O  
HETATM 1855  O   HOH A2198      39.336  29.514  20.217  1.00 29.38           O  
HETATM 1856  O   HOH A2199      40.384  27.796  23.796  1.00 26.07           O  
HETATM 1857  O   HOH A2200      49.397  24.894  25.314  1.00 46.88           O  
HETATM 1858  O   HOH A2201      47.171  22.427  17.159  1.00 31.67           O  
HETATM 1859  O   HOH A2202      50.633  19.410  24.708  1.00 25.11           O  
HETATM 1860  O   HOH A2203      50.593  21.600  19.947  1.00 30.87           O  
HETATM 1861  O   HOH A2204      46.411  20.416  20.663  1.00 18.30           O  
HETATM 1862  O   HOH A2205      43.370  25.589  26.738  1.00 25.70           O  
HETATM 1863  O   HOH A2206      39.291  26.613  27.621  1.00 25.04           O  
HETATM 1864  O   HOH A2207      36.786  24.225  30.701  1.00 16.82           O  
HETATM 1865  O   HOH A2208      38.627  22.111  37.198  1.00 25.86           O  
HETATM 1866  O   HOH A2209      39.511  29.593  29.572  1.00 43.93           O  
HETATM 1867  O   HOH A2210      31.511  25.878  32.261  1.00 41.80           O  
HETATM 1868  O   HOH A2211      25.215  22.886  36.278  1.00 47.09           O  
HETATM 1869  O   HOH A2212      20.476  27.846  29.807  1.00 31.05           O  
HETATM 1870  O   HOH A2213      20.263  27.042  34.530  1.00 40.80           O  
HETATM 1871  O   HOH A2214      20.439  19.975  29.332  1.00 57.17           O  
HETATM 1872  O   HOH A2215      18.573  15.190  30.529  1.00 41.98           O  
HETATM 1873  O   HOH A2216      21.640  14.278  37.520  1.00 33.45           O  
HETATM 1874  O   HOH A2217      19.677  12.142  30.865  1.00 23.30           O  
HETATM 1875  O   HOH A2218      24.710  22.690  30.027  1.00 34.34           O  
HETATM 1876  O   HOH A2219      25.114  24.232  26.005  1.00 44.36           O  
HETATM 1877  O   HOH A2220      31.348  29.562  17.979  1.00 36.41           O  
HETATM 1878  O   HOH A2221      30.702  26.690  24.587  1.00 34.52           O  
HETATM 1879  O   HOH A2222      40.304  22.633  10.715  1.00 34.51           O  
HETATM 1880  O   HOH A2223      37.357  30.553  11.495  1.00 28.64           O  
HETATM 1881  O   HOH A2224      31.173  32.545   7.434  1.00 54.33           O  
HETATM 1882  O   HOH A2225      34.572  25.723   2.723  1.00 36.94           O  
HETATM 1883  O   HOH A2226      36.879  22.519   3.408  1.00 42.77           O  
HETATM 1884  O   HOH A2227      31.343  28.848   6.030  1.00 34.69           O  
HETATM 1885  O   HOH A2228      27.526  31.550   6.953  1.00 40.86           O  
HETATM 1886  O   HOH A2229      29.497  21.016   0.417  1.00 33.28           O  
HETATM 1887  O   HOH A2230      29.432  26.721   3.108  1.00 41.35           O  
HETATM 1888  O   HOH A2231      33.144  22.029   1.913  1.00 39.86           O  
HETATM 1889  O   HOH A2232      30.940  25.468   4.717  1.00 19.45           O  
HETATM 1890  O   HOH A2233      30.512  24.386   1.012  1.00 44.91           O  
HETATM 1891  O   HOH A2234      33.695  20.743   4.638  1.00 22.12           O  
HETATM 1892  O   HOH A2235      25.006  28.024   7.727  1.00 25.45           O  
HETATM 1893  O   HOH A2236      19.263  25.440   7.754  1.00 26.84           O  
HETATM 1894  O   HOH A2237      15.136  18.665  11.014  1.00 34.43           O  
HETATM 1895  O   HOH A2238      19.211  16.765   2.499  1.00 21.64           O  
HETATM 1896  O   HOH A2239      18.667  23.684   4.702  1.00 29.94           O  
HETATM 1897  O   HOH A2240      32.656  18.955   1.859  1.00 45.13           O  
HETATM 1898  O   HOH A2241      18.705  12.411   7.655  1.00 23.27           O  
HETATM 1899  O   HOH A2242      16.118  19.725   4.426  1.00 61.56           O  
HETATM 1900  O   HOH A2243      26.655  13.846  -0.857  1.00 21.20           O  
HETATM 1901  O   HOH A2244      22.415  11.426   2.203  1.00 24.21           O  
HETATM 1902  O   HOH A2245      22.212  14.563  -0.959  1.00 23.94           O  
HETATM 1903  O   HOH A2246      18.948  14.271   2.832  1.00 40.00           O  
HETATM 1904  O   HOH A2247      18.714   9.480   8.267  1.00 39.98           O  
HETATM 1905  O   HOH A2248      18.786  11.500  -0.324  1.00 40.60           O  
HETATM 1906  O   HOH A2249      30.012   6.183   6.500  1.00 40.42           O  
HETATM 1907  O   HOH A2250      28.030   4.891  12.389  1.00 37.69           O  
HETATM 1908  O   HOH A2251      27.421   7.479  13.161  1.00 15.38           O  
HETATM 1909  O   HOH A2252      26.703  11.415   9.931  1.00 22.90           O  
HETATM 1910  O   HOH A2253      19.820   7.110  12.080  1.00 29.27           O  
HETATM 1911  O   HOH A2254      18.336   4.049  12.637  1.00 33.39           O  
HETATM 1912  O   HOH A2255      24.704   3.818  10.643  1.00 29.04           O  
HETATM 1913  O   HOH A2256      18.814   0.756  13.911  1.00 37.29           O  
HETATM 1914  O   HOH A2257      18.359   6.559  14.540  1.00 22.34           O  
HETATM 1915  O   HOH A2258      15.836   4.521  17.483  1.00 30.79           O  
HETATM 1916  O   HOH A2259      16.652   8.642  14.144  1.00 35.05           O  
HETATM 1917  O   HOH A2260      17.651  11.931  11.991  1.00 37.27           O  
HETATM 1918  O   HOH A2261      16.532  12.529  19.694  1.00 18.46           O  
HETATM 1919  O   HOH A2262      13.303  12.463  16.244  1.00 55.59           O  
HETATM 1920  O   HOH A2263      12.992  19.368  14.108  1.00 18.25           O  
HETATM 1921  O   HOH A2264      15.043  15.000  13.111  1.00 26.60           O  
HETATM 1922  O   HOH A2265      18.042  22.420  11.241  1.00 23.65           O  
HETATM 1923  O   HOH A2266      16.545  25.420  17.706  1.00 25.31           O  
HETATM 1924  O   HOH A2267      19.841  24.877  10.642  1.00 34.18           O  
HETATM 1925  O   HOH A2268      15.307  28.466  16.583  1.00 47.72           O  
HETATM 1926  O   HOH A2269      14.613  31.142  12.659  1.00 57.00           O  
HETATM 1927  O   HOH A2270      11.592  27.404  11.806  1.00 65.26           O  
HETATM 1928  O   HOH A2271      16.377  25.352  10.730  1.00 43.51           O  
CONECT 1647 1695 1816                                                           
CONECT 1648 1649                                                                
CONECT 1649 1648 1650 1651                                                      
CONECT 1650 1649 1655                                                           
CONECT 1651 1649 1652                                                           
CONECT 1652 1651 1653 1654                                                      
CONECT 1653 1652                                                                
CONECT 1654 1652 1655                                                           
CONECT 1655 1650 1654 1656                                                      
CONECT 1656 1655 1657                                                           
CONECT 1657 1656                                                                
CONECT 1695 1647                                                                
CONECT 1816 1647                                                                
MASTER      514    0    2   10    8    0    4    6 1910    1   13   19          
END                                                                             
