CNRS Nantes University UFIP UFIP
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***  KINASE 24-MAY-02 1GZN  ***

elNémo ID: 210805032357144549

Job options:

ID        	=	 210805032357144549
JOBID     	=	 KINASE 24-MAY-02 1GZN
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    KINASE                                  24-MAY-02   1GZN              
TITLE     STRUCTURE OF PKB KINASE DOMAIN                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAC-BETA SERINE/THREONINE PROTEIN KINASE;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN AND HYDROPHOBIC MOTIF, RESIDUES              
COMPND   5  146-480;                                                            
COMPND   6 SYNONYM: PROTEIN KINASE AKT-2, PROTEIN KINASE B BETA,                
COMPND   7  RAC-PK-BETA, PKB BETA;                                              
COMPND   8 EC: 2.7.1.-;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: INSECT CELLS;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE,                 
KEYWDS   2 ATP-BINDING                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BARFORD,J.YANG,B.A.HEMMINGS                                         
REVDAT   2   24-FEB-09 1GZN    1       VERSN                                    
REVDAT   1   22-MAY-03 1GZN    0                                                
JRNL        AUTH   J.YANG,P.CRON,V.THOMPSON,V.GOOD,D.HESS,                      
JRNL        AUTH 2 B.A.HEMMINGS,D.BARFORD                                       
JRNL        TITL   MOLECULAR MECHANISM FOR THE REGULATION OF PROTEIN            
JRNL        TITL 2 KINASE B/AKT BY HYDROPHOBIC MOTIF PHOSPHORYLATION            
JRNL        REF    MOL.CELL                      V.   9  1227 2002              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12086620                                                     
JRNL        DOI    10.1016/S1097-2765(02)00550-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1673968.91                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 15915                          
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 SET) : 0.268                           
REMARK   3   FREE R VALUE                     : 0.319                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1598                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.5                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2337                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.389                        
REMARK   3   BIN FREE R VALUE                    : 0.473                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.4                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 242                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2198                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 247                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.5                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.46                                                 
REMARK   3    B22 (A**2) : 7.46                                                 
REMARK   3    B33 (A**2) : -14.92                                               
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.44                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.52                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.57                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.68                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.5                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.9                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.90                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINE                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.60  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.72  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.97  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.14  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.380217                                             
REMARK   3   BSOL        : 96.4037                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GZN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAY-02.                  
REMARK 100 THE PDBE ID CODE IS EBI-9892.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.92                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16090                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1CDK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 49                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8K, 0.2 M LITHIUM SULPHATE       
REMARK 280  0.1 M TRIS, 10 MG/ML PROTEIN                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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       19.52750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       74.76150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       74.76150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        9.76375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       74.76150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       74.76150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.29125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       74.76150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       74.76150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        9.76375            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       74.76150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       74.76150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       29.29125            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       19.52750            
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 GENERATING THE BIOMOLECULE                                           
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  FUNCTION: PROTEIN KINASE PHOSPHORYLATING SEVERAL                    
REMARK 400   KNOWN PROTEINS.                                                    
REMARK 400  TISSUE SPECIFICITY: ALL HUMAN CELL TYPES.                           
REMARK 400  DISEASE: ALTERATIONS MAY CONTRIBUTE TO THE PATHOGENESIS OF          
REMARK 400   OVARIAN CARCINOMAS.                                                
REMARK 400  SIMILARITY: MEMBER OF THE SER/THR FAMILY OF PROTEIN KINASES.        
REMARK 400   RAC SUBFAMILY.                                                     
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     ILE A   189                                                      
REMARK 465     ALA A   190                                                      
REMARK 465     LYS A   191                                                      
REMARK 465     ASP A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     VAL A   194                                                      
REMARK 465     ALA A   195                                                      
REMARK 465     HIS A   196                                                      
REMARK 465     THR A   197                                                      
REMARK 465     CYS A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     GLU A   299                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     ILE A   301                                                      
REMARK 465     SER A   302                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     MET A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     THR A   309                                                      
REMARK 465     PHE A   310                                                      
REMARK 465     CYS A   311                                                      
REMARK 465     GLY A   312                                                      
REMARK 465     PHE A   443                                                      
REMARK 465     THR A   444                                                      
REMARK 465     ALA A   445                                                      
REMARK 465     GLN A   446                                                      
REMARK 465     SER A   447                                                      
REMARK 465     ILE A   448                                                      
REMARK 465     THR A   449                                                      
REMARK 465     ILE A   450                                                      
REMARK 465     THR A   451                                                      
REMARK 465     PRO A   452                                                      
REMARK 465     PRO A   453                                                      
REMARK 465     ASP A   454                                                      
REMARK 465     ARG A   455                                                      
REMARK 465     TYR A   456                                                      
REMARK 465     ASP A   457                                                      
REMARK 465     SER A   458                                                      
REMARK 465     LEU A   459                                                      
REMARK 465     GLY A   460                                                      
REMARK 465     LEU A   461                                                      
REMARK 465     LEU A   462                                                      
REMARK 465     GLU A   463                                                      
REMARK 465     LEU A   464                                                      
REMARK 465     ASP A   465                                                      
REMARK 465     GLN A   466                                                      
REMARK 465     ARG A   467                                                      
REMARK 465     THR A   468                                                      
REMARK 465     HIS A   469                                                      
REMARK 465     PHE A   470                                                      
REMARK 465     PRO A   471                                                      
REMARK 465     GLN A   472                                                      
REMARK 465     PHE A   473                                                      
REMARK 465     SER A   474                                                      
REMARK 465     TYR A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     ALA A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 465     ILE A   479                                                      
REMARK 465     ARG A   480                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     VAL A 147    CG1  CG2                                            
REMARK 470     VAL A 198    CG1  CG2                                            
REMARK 470     THR A 199    OG1  CG2                                            
REMARK 470     GLU A 200    CG   CD   OE1  OE2                                  
REMARK 470     SER A 201    OG                                                  
REMARK 470     ARG A 202    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 203    CG1  CG2                                            
REMARK 470     LEU A 204    CG   CD1  CD2                                       
REMARK 470     GLN A 205    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 206    CG   OD1  ND2                                       
REMARK 470     ARG A 253    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 296    CG   CD1  CD2                                       
REMARK 470     GLU A 442    CA   C    O    CB   CG   CD   OE1  OE2              
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     ASP A 435     N                                                  
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   OH   TYR A   273  -  O    HOH A  2110              2.09            
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 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    ALA A 173      -75.05    -68.57                                   
REMARK 500    ARG A 202      -59.45     60.68                                   
REMARK 500    HIS A 209      132.59    175.30                                   
REMARK 500    ASP A 223       27.86   -148.39                                   
REMARK 500    ARG A 245      -42.96     62.98                                   
REMARK 500    GLU A 249      -17.20    -49.02                                   
REMARK 500    ARG A 274      -32.45     69.44                                   
REMARK 500    LEU A 278      -38.75    -39.07                                   
REMARK 500    LYS A 285       -8.67    -51.93                                   
REMARK 500    ASP A 293       45.88    -87.68                                   
REMARK 500    ASN A 325       29.19     45.81                                   
REMARK 500    ASN A 352      -76.30    -93.37                                   
REMARK 500    GLN A 353      119.53    -21.85                                   
REMARK 500    ASP A 354     -109.54      3.78                                   
REMARK 500    HIS A 355      -38.30    176.27                                   
REMARK 500    PRO A 370      160.22    -49.17                                   
REMARK 500    THR A 372       34.14    -68.88                                   
REMARK 500    PRO A 397      -15.74    -49.00                                   
REMARK 500    ASP A 399     -129.09     51.47                                   
REMARK 500    PHE A 409       55.82   -106.82                                   
REMARK 500    SER A 411       21.91    -59.32                                   
REMARK 500    TRP A 414      -16.50    -49.24                                   
REMARK 500    LEU A 422      158.38    -46.42                                   
REMARK 500    PRO A 428      151.37    -48.70                                   
REMARK 500    THR A 431      -70.17    -68.67                                   
REMARK 500    GLU A 433       -4.62    -59.03                                   
REMARK 500    ASP A 435       99.39    -66.58                                   
REMARK 500    THR A 436       49.27    -89.12                                   
REMARK 500    TYR A 438       20.11    -72.85                                   
REMARK 500    ASP A 440     -111.82   -123.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GZK   RELATED DB: PDB                                   
REMARK 900  MOLECULAR MECHANISM FOR THE REGULATION OF                           
REMARK 900  PROTEIN KINASE B/AKT BY HYDROPHOBIC MOTIF                           
REMARK 900  PHOSPHORYLATION                                                     
REMARK 900 RELATED ID: 1GZO   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PROTEIN KINASE B                                       
REMARK 900  UNPHOSPHORYLATED                                                    
REMARK 900 RELATED ID: 1O6K   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ACTIVATED FORM OF PKB KINASE                           
REMARK 900  DOMAIN S474D WITH GSK3 PEPTIDE AND AMP-PNP                          
REMARK 900 RELATED ID: 1O6L   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN ACTIVATED AKT/                              
REMARK 900  PROTEIN KINASE B (PKB-PIF CHIMERA) TERNARY                          
REMARK 900  COMPLEX WITH AMP-PNP AND GSK3 PEPTIDE                               
DBREF  1GZN A  146   480  UNP    P31751   AKT2_HUMAN     146    480             
SEQRES   1 A  335  LYS VAL THR MET ASN ASP PHE ASP TYR LEU LYS LEU LEU          
SEQRES   2 A  335  GLY LYS GLY THR PHE GLY LYS VAL ILE LEU VAL ARG GLU          
SEQRES   3 A  335  LYS ALA THR GLY ARG TYR TYR ALA MET LYS ILE LEU ARG          
SEQRES   4 A  335  LYS GLU VAL ILE ILE ALA LYS ASP GLU VAL ALA HIS THR          
SEQRES   5 A  335  VAL THR GLU SER ARG VAL LEU GLN ASN THR ARG HIS PRO          
SEQRES   6 A  335  PHE LEU THR ALA LEU LYS TYR ALA PHE GLN THR HIS ASP          
SEQRES   7 A  335  ARG LEU CYS PHE VAL MET GLU TYR ALA ASN GLY GLY GLU          
SEQRES   8 A  335  LEU PHE PHE HIS LEU SER ARG GLU ARG VAL PHE THR GLU          
SEQRES   9 A  335  GLU ARG ALA ARG PHE TYR GLY ALA GLU ILE VAL SER ALA          
SEQRES  10 A  335  LEU GLU TYR LEU HIS SER ARG ASP VAL VAL TYR ARG ASP          
SEQRES  11 A  335  ILE LYS LEU GLU ASN LEU MET LEU ASP LYS ASP GLY HIS          
SEQRES  12 A  335  ILE LYS ILE THR ASP PHE GLY LEU CYS LYS GLU GLY ILE          
SEQRES  13 A  335  SER ASP GLY ALA THR MET LYS THR PHE CYS GLY THR PRO          
SEQRES  14 A  335  GLU TYR LEU ALA PRO GLU VAL LEU GLU ASP ASN ASP TYR          
SEQRES  15 A  335  GLY ARG ALA VAL ASP TRP TRP GLY LEU GLY VAL VAL MET          
SEQRES  16 A  335  TYR GLU MET MET CYS GLY ARG LEU PRO PHE TYR ASN GLN          
SEQRES  17 A  335  ASP HIS GLU ARG LEU PHE GLU LEU ILE LEU MET GLU GLU          
SEQRES  18 A  335  ILE ARG PHE PRO ARG THR LEU SER PRO GLU ALA LYS SER          
SEQRES  19 A  335  LEU LEU ALA GLY LEU LEU LYS LYS ASP PRO LYS GLN ARG          
SEQRES  20 A  335  LEU GLY GLY GLY PRO SER ASP ALA LYS GLU VAL MET GLU          
SEQRES  21 A  335  HIS ARG PHE PHE LEU SER ILE ASN TRP GLN ASP VAL VAL          
SEQRES  22 A  335  GLN LYS LYS LEU LEU PRO PRO PHE LYS PRO GLN VAL THR          
SEQRES  23 A  335  SER GLU VAL ASP THR ARG TYR PHE ASP ASP GLU PHE THR          
SEQRES  24 A  335  ALA GLN SER ILE THR ILE THR PRO PRO ASP ARG TYR ASP          
SEQRES  25 A  335  SER LEU GLY LEU LEU GLU LEU ASP GLN ARG THR HIS PHE          
SEQRES  26 A  335  PRO GLN PHE SER TYR SER ALA SER ILE ARG                      
FORMUL   2  HOH   *247(H2 O1)                                                   
HELIX    1   1 THR A  148  ASN A  150  5                                   3    
HELIX    2   2 ARG A  202  THR A  207  1                                   6    
HELIX    3   3 GLU A  236  ARG A  245  1                                  10    
HELIX    4   4 THR A  248  ARG A  269  1                                  22    
HELIX    5   5 LYS A  277  GLU A  279  5                                   3    
HELIX    6   6 ALA A  318  ASN A  325  1                                   8    
HELIX    7   7 ARG A  329  GLY A  346  1                                  18    
HELIX    8   8 ARG A  357  GLU A  365  1                                   9    
HELIX    9   9 GLU A  376  LEU A  385  1                                  10    
HELIX   10  10 ASP A  388  ARG A  392  5                                   5    
HELIX   11  11 ASP A  399  GLU A  405  1                                   7    
HELIX   12  12 HIS A  406  LEU A  410  5                                   5    
HELIX   13  13 ASN A  413  GLN A  419  1                                   7    
SHEET    1  AA 5 PHE A 152  LYS A 160  0                                        
SHEET    2  AA 5 GLY A 164  GLU A 171 -1  O  VAL A 166   N  LEU A 158           
SHEET    3  AA 5 TYR A 177  ARG A 184 -1  O  TYR A 178   N  VAL A 169           
SHEET    4  AA 5 ARG A 224  GLU A 230 -1  O  LEU A 225   N  LEU A 183           
SHEET    5  AA 5 LEU A 215  GLN A 220 -1  N  LYS A 216   O  VAL A 228           
SHEET    1  AB 2 LEU A 281  LEU A 283  0                                        
SHEET    2  AB 2 ILE A 289  ILE A 291 -1  O  LYS A 290   N  MET A 282           
CRYST1  149.523  149.523   39.055  90.00  90.00  90.00 P 41 21 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      0.006688  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006688  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025605        0.00000                         
ATOM      1  N   LYS A 146     -39.973  82.494 -47.814  1.00 70.81           N  
ATOM      2  CA  LYS A 146     -38.532  82.146 -48.018  1.00 71.27           C  
ATOM      3  C   LYS A 146     -38.368  81.486 -49.380  1.00 70.62           C  
ATOM      4  O   LYS A 146     -38.974  80.443 -49.651  1.00 70.38           O  
ATOM      5  CB  LYS A 146     -38.038  81.194 -46.909  1.00 71.54           C  
ATOM      6  N   VAL A 147     -37.552  82.101 -50.235  1.00 69.32           N  
ATOM      7  CA  VAL A 147     -37.311  81.581 -51.575  1.00 66.53           C  
ATOM      8  C   VAL A 147     -36.379  80.400 -51.494  1.00 65.42           C  
ATOM      9  O   VAL A 147     -35.737  80.164 -50.473  1.00 65.05           O  
ATOM     10  CB  VAL A 147     -36.701  82.650 -52.443  1.00 66.78           C  
ATOM     11  N   THR A 148     -36.294  79.656 -52.581  1.00 64.79           N  
ATOM     12  CA  THR A 148     -35.418  78.506 -52.610  1.00 64.55           C  
ATOM     13  C   THR A 148     -35.204  78.058 -54.039  1.00 64.69           C  
ATOM     14  O   THR A 148     -35.996  78.380 -54.926  1.00 64.40           O  
ATOM     15  CB  THR A 148     -36.000  77.352 -51.749  1.00 65.50           C  
ATOM     16  OG1 THR A 148     -35.147  77.143 -50.621  1.00 65.88           O  
ATOM     17  CG2 THR A 148     -36.119  76.049 -52.542  1.00 64.71           C  
ATOM     18  N   MET A 149     -34.124  77.317 -54.251  1.00 64.05           N  
ATOM     19  CA  MET A 149     -33.780  76.809 -55.564  1.00 64.48           C  
ATOM     20  C   MET A 149     -34.965  76.251 -56.326  1.00 65.32           C  
ATOM     21  O   MET A 149     -35.168  76.573 -57.494  1.00 66.17           O  
ATOM     22  CB  MET A 149     -32.709  75.732 -55.436  1.00 63.31           C  
ATOM     23  CG  MET A 149     -31.299  76.285 -55.380  1.00 62.01           C  
ATOM     24  SD  MET A 149     -30.919  77.222 -56.876  1.00 61.30           S  
ATOM     25  CE  MET A 149     -29.920  78.511 -56.204  1.00 61.48           C  
ATOM     26  N   ASN A 150     -35.759  75.429 -55.651  1.00 66.95           N  
ATOM     27  CA  ASN A 150     -36.910  74.785 -56.265  1.00 66.75           C  
ATOM     28  C   ASN A 150     -38.085  75.701 -56.616  1.00 66.01           C  
ATOM     29  O   ASN A 150     -39.083  75.248 -57.183  1.00 65.59           O  
ATOM     30  CB  ASN A 150     -37.387  73.659 -55.361  1.00 68.91           C  
ATOM     31  CG  ASN A 150     -38.132  72.592 -56.118  1.00 72.34           C  
ATOM     32  OD1 ASN A 150     -38.586  71.614 -55.533  1.00 75.51           O  
ATOM     33  ND2 ASN A 150     -38.260  72.767 -57.433  1.00 74.67           N  
ATOM     34  N   ASP A 151     -37.982  76.981 -56.276  1.00 64.20           N  
ATOM     35  CA  ASP A 151     -39.049  77.919 -56.595  1.00 63.54           C  
ATOM     36  C   ASP A 151     -38.909  78.439 -58.023  1.00 62.89           C  
ATOM     37  O   ASP A 151     -39.786  79.147 -58.506  1.00 63.67           O  
ATOM     38  CB  ASP A 151     -39.020  79.128 -55.652  1.00 65.00           C  
ATOM     39  CG  ASP A 151     -39.490  78.802 -54.238  1.00 66.85           C  
ATOM     40  OD1 ASP A 151     -40.554  78.164 -54.090  1.00 67.48           O  
ATOM     41  OD2 ASP A 151     -38.807  79.206 -53.267  1.00 68.28           O  
ATOM     42  N   PHE A 152     -37.822  78.086 -58.706  1.00 61.89           N  
ATOM     43  CA  PHE A 152     -37.579  78.603 -60.052  1.00 60.49           C  
ATOM     44  C   PHE A 152     -37.284  77.556 -61.118  1.00 61.74           C  
ATOM     45  O   PHE A 152     -36.883  76.426 -60.816  1.00 62.43           O  
ATOM     46  CB  PHE A 152     -36.379  79.565 -60.044  1.00 58.74           C  
ATOM     47  CG  PHE A 152     -36.425  80.620 -58.974  1.00 56.12           C  
ATOM     48  CD1 PHE A 152     -37.115  81.801 -59.173  1.00 54.99           C  
ATOM     49  CD2 PHE A 152     -35.750  80.432 -57.768  1.00 55.57           C  
ATOM     50  CE1 PHE A 152     -37.136  82.786 -58.179  1.00 55.18           C  
ATOM     51  CE2 PHE A 152     -35.760  81.400 -56.774  1.00 54.70           C  
ATOM     52  CZ  PHE A 152     -36.452  82.579 -56.978  1.00 55.82           C  
ATOM     53  N   ASP A 153     -37.458  77.973 -62.375  1.00 61.57           N  
ATOM     54  CA  ASP A 153     -37.178  77.150 -63.545  1.00 60.28           C  
ATOM     55  C   ASP A 153     -35.992  77.774 -64.272  1.00 59.11           C  
ATOM     56  O   ASP A 153     -35.891  78.998 -64.387  1.00 58.69           O  
ATOM     57  CB  ASP A 153     -38.379  77.111 -64.493  1.00 62.95           C  
ATOM     58  CG  ASP A 153     -39.517  76.236 -63.973  1.00 65.98           C  
ATOM     59  OD1 ASP A 153     -39.297  75.021 -63.764  1.00 67.08           O  
ATOM     60  OD2 ASP A 153     -40.636  76.763 -63.779  1.00 67.23           O  
ATOM     61  N   TYR A 154     -35.099  76.925 -64.760  1.00 56.97           N  
ATOM     62  CA  TYR A 154     -33.918  77.366 -65.475  1.00 55.98           C  
ATOM     63  C   TYR A 154     -34.146  77.694 -66.949  1.00 56.09           C  
ATOM     64  O   TYR A 154     -34.715  76.898 -67.682  1.00 58.01           O  
ATOM     65  CB  TYR A 154     -32.856  76.282 -65.405  1.00 56.02           C  
ATOM     66  CG  TYR A 154     -31.632  76.579 -66.248  1.00 57.01           C  
ATOM     67  CD1 TYR A 154     -30.660  77.485 -65.813  1.00 57.73           C  
ATOM     68  CD2 TYR A 154     -31.423  75.918 -67.451  1.00 56.00           C  
ATOM     69  CE1 TYR A 154     -29.515  77.711 -66.553  1.00 59.20           C  
ATOM     70  CE2 TYR A 154     -30.278  76.133 -68.193  1.00 57.55           C  
ATOM     71  CZ  TYR A 154     -29.327  77.024 -67.739  1.00 59.46           C  
ATOM     72  OH  TYR A 154     -28.165  77.185 -68.452  1.00 60.78           O  
ATOM     73  N   LEU A 155     -33.678  78.849 -67.405  1.00 55.69           N  
ATOM     74  CA  LEU A 155     -33.836  79.179 -68.816  1.00 54.06           C  
ATOM     75  C   LEU A 155     -32.498  79.199 -69.527  1.00 53.50           C  
ATOM     76  O   LEU A 155     -32.247  78.384 -70.412  1.00 52.05           O  
ATOM     77  CB  LEU A 155     -34.554  80.519 -68.981  1.00 52.09           C  
ATOM     78  CG  LEU A 155     -35.982  80.397 -68.459  1.00 52.43           C  
ATOM     79  CD1 LEU A 155     -36.671  81.722 -68.473  1.00 51.71           C  
ATOM     80  CD2 LEU A 155     -36.738  79.377 -69.306  1.00 52.64           C  
ATOM     81  N   LYS A 156     -31.622  80.111 -69.125  1.00 55.10           N  
ATOM     82  CA  LYS A 156     -30.319  80.210 -69.774  1.00 56.23           C  
ATOM     83  C   LYS A 156     -29.213  80.796 -68.914  1.00 55.77           C  
ATOM     84  O   LYS A 156     -29.447  81.368 -67.843  1.00 54.81           O  
ATOM     85  CB  LYS A 156     -30.438  81.052 -71.056  1.00 56.69           C  
ATOM     86  CG  LYS A 156     -31.162  82.394 -70.854  1.00 58.21           C  
ATOM     87  CD  LYS A 156     -31.156  83.250 -72.125  1.00 58.44           C  
ATOM     88  CE  LYS A 156     -29.778  83.830 -72.408  1.00 57.73           C  
ATOM     89  NZ  LYS A 156     -29.771  84.739 -73.587  1.00 59.12           N  
ATOM     90  N   LEU A 157     -28.000  80.644 -69.418  1.00 56.19           N  
ATOM     91  CA  LEU A 157     -26.819  81.162 -68.764  1.00 58.36           C  
ATOM     92  C   LEU A 157     -26.644  82.592 -69.244  1.00 59.96           C  
ATOM     93  O   LEU A 157     -26.534  82.826 -70.441  1.00 60.37           O  
ATOM     94  CB  LEU A 157     -25.604  80.336 -69.161  1.00 57.51           C  
ATOM     95  CG  LEU A 157     -24.256  80.791 -68.607  1.00 56.59           C  
ATOM     96  CD1 LEU A 157     -24.330  80.986 -67.101  1.00 55.60           C  
ATOM     97  CD2 LEU A 157     -23.211  79.742 -68.966  1.00 56.33           C  
ATOM     98  N   LEU A 158     -26.632  83.541 -68.311  1.00 62.08           N  
ATOM     99  CA  LEU A 158     -26.480  84.954 -68.647  1.00 64.15           C  
ATOM    100  C   LEU A 158     -25.024  85.359 -68.582  1.00 65.74           C  
ATOM    101  O   LEU A 158     -24.566  86.154 -69.385  1.00 66.65           O  
ATOM    102  CB  LEU A 158     -27.291  85.832 -67.689  1.00 62.69           C  
ATOM    103  CG  LEU A 158     -28.814  85.750 -67.821  1.00 62.25           C  
ATOM    104  CD1 LEU A 158     -29.457  86.404 -66.607  1.00 62.24           C  
ATOM    105  CD2 LEU A 158     -29.270  86.421 -69.109  1.00 60.21           C  
ATOM    106  N   GLY A 159     -24.298  84.804 -67.625  1.00 68.39           N  
ATOM    107  CA  GLY A 159     -22.895  85.139 -67.494  1.00 72.27           C  
ATOM    108  C   GLY A 159     -22.215  84.276 -66.456  1.00 74.59           C  
ATOM    109  O   GLY A 159     -22.840  83.849 -65.490  1.00 74.62           O  
ATOM    110  N   LYS A 160     -20.934  84.006 -66.657  1.00 77.46           N  
ATOM    111  CA  LYS A 160     -20.186  83.188 -65.710  1.00 80.68           C  
ATOM    112  C   LYS A 160     -19.072  84.052 -65.100  1.00 82.48           C  
ATOM    113  O   LYS A 160     -19.025  85.263 -65.340  1.00 82.98           O  
ATOM    114  CB  LYS A 160     -19.600  81.968 -66.428  1.00 81.50           C  
ATOM    115  CG  LYS A 160     -19.286  80.795 -65.512  1.00 83.42           C  
ATOM    116  CD  LYS A 160     -18.705  79.613 -66.283  1.00 84.59           C  
ATOM    117  CE  LYS A 160     -18.593  78.367 -65.396  1.00 85.93           C  
ATOM    118  NZ  LYS A 160     -17.868  77.240 -66.058  1.00 85.96           N  
ATOM    119  N   GLY A 161     -18.189  83.452 -64.304  1.00 83.71           N  
ATOM    120  CA  GLY A 161     -17.116  84.235 -63.715  1.00 85.03           C  
ATOM    121  C   GLY A 161     -16.253  83.558 -62.666  1.00 85.89           C  
ATOM    122  O   GLY A 161     -16.388  82.366 -62.394  1.00 85.90           O  
ATOM    123  N   THR A 162     -15.352  84.341 -62.079  1.00 87.10           N  
ATOM    124  CA  THR A 162     -14.442  83.859 -61.042  1.00 87.47           C  
ATOM    125  C   THR A 162     -15.119  84.083 -59.688  1.00 86.80           C  
ATOM    126  O   THR A 162     -14.593  83.718 -58.635  1.00 87.25           O  
ATOM    127  CB  THR A 162     -13.109  84.639 -61.078  1.00 88.69           C  
ATOM    128  OG1 THR A 162     -12.755  84.919 -62.442  1.00 89.63           O  
ATOM    129  CG2 THR A 162     -12.000  83.821 -60.438  1.00 88.94           C  
ATOM    130  N   PHE A 163     -16.298  84.694 -59.743  1.00 85.42           N  
ATOM    131  CA  PHE A 163     -17.098  84.983 -58.562  1.00 83.84           C  
ATOM    132  C   PHE A 163     -18.269  83.990 -58.512  1.00 82.17           C  
ATOM    133  O   PHE A 163     -18.797  83.678 -57.441  1.00 81.18           O  
ATOM    134  CB  PHE A 163     -17.620  86.409 -58.663  1.00 84.78           C  
ATOM    135  CG  PHE A 163     -18.367  86.686 -59.943  1.00 86.36           C  
ATOM    136  CD1 PHE A 163     -19.706  86.313 -60.083  1.00 86.35           C  
ATOM    137  CD2 PHE A 163     -17.729  87.308 -61.013  1.00 87.23           C  
ATOM    138  CE1 PHE A 163     -20.403  86.560 -61.262  1.00 86.87           C  
ATOM    139  CE2 PHE A 163     -18.416  87.561 -62.201  1.00 88.15           C  
ATOM    140  CZ  PHE A 163     -19.761  87.183 -62.325  1.00 87.83           C  
ATOM    141  N   GLY A 164     -18.654  83.499 -59.691  1.00 79.86           N  
ATOM    142  CA  GLY A 164     -19.751  82.552 -59.807  1.00 76.70           C  
ATOM    143  C   GLY A 164     -20.414  82.557 -61.181  1.00 73.84           C  
ATOM    144  O   GLY A 164     -19.757  82.319 -62.203  1.00 73.57           O  
ATOM    145  N   LYS A 165     -21.721  82.808 -61.212  1.00 70.69           N  
ATOM    146  CA  LYS A 165     -22.457  82.844 -62.471  1.00 67.52           C  
ATOM    147  C   LYS A 165     -23.818  83.521 -62.316  1.00 65.27           C  
ATOM    148  O   LYS A 165     -24.328  83.676 -61.205  1.00 64.06           O  
ATOM    149  CB  LYS A 165     -22.642  81.420 -63.023  1.00 67.89           C  
ATOM    150  CG  LYS A 165     -23.791  80.627 -62.431  1.00 69.04           C  
ATOM    151  CD  LYS A 165     -23.723  79.153 -62.824  1.00 71.89           C  
ATOM    152  CE  LYS A 165     -22.523  78.462 -62.159  1.00 74.23           C  
ATOM    153  NZ  LYS A 165     -22.550  76.965 -62.206  1.00 73.73           N  
ATOM    154  N   VAL A 166     -24.386  83.940 -63.442  1.00 62.94           N  
ATOM    155  CA  VAL A 166     -25.697  84.579 -63.460  1.00 60.27           C  
ATOM    156  C   VAL A 166     -26.553  83.780 -64.430  1.00 59.66           C  
ATOM    157  O   VAL A 166     -26.161  83.530 -65.570  1.00 57.59           O  
ATOM    158  CB  VAL A 166     -25.633  86.040 -63.936  1.00 59.05           C  
ATOM    159  CG1 VAL A 166     -26.987  86.689 -63.762  1.00 58.36           C  
ATOM    160  CG2 VAL A 166     -24.573  86.800 -63.163  1.00 57.73           C  
ATOM    161  N   ILE A 167     -27.728  83.389 -63.957  1.00 59.97           N  
ATOM    162  CA  ILE A 167     -28.656  82.581 -64.730  1.00 59.43           C  
ATOM    163  C   ILE A 167     -29.975  83.297 -64.945  1.00 60.07           C  
ATOM    164  O   ILE A 167     -30.381  84.128 -64.134  1.00 61.60           O  
ATOM    165  CB  ILE A 167     -28.970  81.289 -63.979  1.00 58.43           C  
ATOM    166  CG1 ILE A 167     -27.685  80.518 -63.696  1.00 59.05           C  
ATOM    167  CG2 ILE A 167     -29.944  80.464 -64.768  1.00 59.87           C  
ATOM    168  CD1 ILE A 167     -26.997  79.990 -64.930  1.00 59.86           C  
ATOM    169  N   LEU A 168     -30.651  82.969 -66.036  1.00 59.40           N  
ATOM    170  CA  LEU A 168     -31.957  83.553 -66.313  1.00 57.95           C  
ATOM    171  C   LEU A 168     -32.934  82.506 -65.807  1.00 57.63           C  
ATOM    172  O   LEU A 168     -32.858  81.344 -66.210  1.00 58.33           O  
ATOM    173  CB  LEU A 168     -32.152  83.764 -67.820  1.00 57.83           C  
ATOM    174  CG  LEU A 168     -33.463  84.396 -68.300  1.00 57.62           C  
ATOM    175  CD1 LEU A 168     -33.747  85.672 -67.521  1.00 56.75           C  
ATOM    176  CD2 LEU A 168     -33.366  84.690 -69.790  1.00 58.76           C  
ATOM    177  N   VAL A 169     -33.830  82.900 -64.908  1.00 56.98           N  
ATOM    178  CA  VAL A 169     -34.819  81.967 -64.367  1.00 55.78           C  
ATOM    179  C   VAL A 169     -36.215  82.566 -64.319  1.00 56.93           C  
ATOM    180  O   VAL A 169     -36.400  83.778 -64.458  1.00 54.27           O  
ATOM    181  CB  VAL A 169     -34.457  81.502 -62.931  1.00 54.37           C  
ATOM    182  CG1 VAL A 169     -33.076  80.892 -62.916  1.00 51.74           C  
ATOM    183  CG2 VAL A 169     -34.544  82.668 -61.965  1.00 50.45           C  
ATOM    184  N   ARG A 170     -37.194  81.691 -64.120  1.00 58.84           N  
ATOM    185  CA  ARG A 170     -38.582  82.090 -64.026  1.00 61.41           C  
ATOM    186  C   ARG A 170     -39.131  81.629 -62.686  1.00 62.99           C  
ATOM    187  O   ARG A 170     -39.107  80.439 -62.385  1.00 64.01           O  
ATOM    188  CB  ARG A 170     -39.410  81.449 -65.148  1.00 62.47           C  
ATOM    189  CG  ARG A 170     -40.825  82.053 -65.318  1.00 63.83           C  
ATOM    190  CD  ARG A 170     -41.746  81.157 -66.154  1.00 64.35           C  
ATOM    191  NE  ARG A 170     -41.068  80.639 -67.342  1.00 65.77           N  
ATOM    192  CZ  ARG A 170     -40.827  79.347 -67.572  1.00 65.38           C  
ATOM    193  NH1 ARG A 170     -41.213  78.427 -66.693  1.00 64.52           N  
ATOM    194  NH2 ARG A 170     -40.194  78.976 -68.682  1.00 65.16           N  
ATOM    195  N   GLU A 171     -39.609  82.563 -61.875  1.00 64.89           N  
ATOM    196  CA  GLU A 171     -40.200  82.198 -60.599  1.00 67.11           C  
ATOM    197  C   GLU A 171     -41.451  81.415 -60.981  1.00 69.59           C  
ATOM    198  O   GLU A 171     -42.307  81.922 -61.701  1.00 70.29           O  
ATOM    199  CB  GLU A 171     -40.559  83.454 -59.808  1.00 66.48           C  
ATOM    200  CG  GLU A 171     -41.489  83.212 -58.645  1.00 67.91           C  
ATOM    201  CD  GLU A 171     -41.577  84.399 -57.692  1.00 69.32           C  
ATOM    202  OE1 GLU A 171     -41.646  85.567 -58.160  1.00 68.57           O  
ATOM    203  OE2 GLU A 171     -41.586  84.151 -56.466  1.00 68.84           O  
ATOM    204  N   LYS A 172     -41.552  80.171 -60.529  1.00 71.37           N  
ATOM    205  CA  LYS A 172     -42.703  79.355 -60.875  1.00 72.47           C  
ATOM    206  C   LYS A 172     -44.037  79.891 -60.379  1.00 73.84           C  
ATOM    207  O   LYS A 172     -45.072  79.663 -61.004  1.00 74.45           O  
ATOM    208  CB  LYS A 172     -42.483  77.922 -60.399  1.00 72.53           C  
ATOM    209  CG  LYS A 172     -41.471  77.214 -61.274  1.00 74.23           C  
ATOM    210  CD  LYS A 172     -41.241  75.757 -60.912  1.00 75.00           C  
ATOM    211  CE  LYS A 172     -40.397  75.598 -59.660  1.00 74.57           C  
ATOM    212  NZ  LYS A 172     -39.910  74.195 -59.515  1.00 73.65           N  
ATOM    213  N   ALA A 173     -44.023  80.612 -59.265  1.00 75.31           N  
ATOM    214  CA  ALA A 173     -45.258  81.174 -58.729  1.00 77.02           C  
ATOM    215  C   ALA A 173     -45.770  82.272 -59.661  1.00 77.74           C  
ATOM    216  O   ALA A 173     -46.722  82.068 -60.419  1.00 77.87           O  
ATOM    217  CB  ALA A 173     -45.016  81.745 -57.330  1.00 76.87           C  
ATOM    218  N   THR A 174     -45.106  83.427 -59.610  1.00 77.75           N  
ATOM    219  CA  THR A 174     -45.474  84.588 -60.414  1.00 77.10           C  
ATOM    220  C   THR A 174     -45.237  84.476 -61.918  1.00 76.57           C  
ATOM    221  O   THR A 174     -45.724  85.306 -62.675  1.00 77.25           O  
ATOM    222  CB  THR A 174     -44.739  85.874 -59.929  1.00 77.68           C  
ATOM    223  OG1 THR A 174     -43.332  85.759 -60.187  1.00 77.94           O  
ATOM    224  CG2 THR A 174     -44.965  86.097 -58.437  1.00 78.07           C  
ATOM    225  N   GLY A 175     -44.496  83.470 -62.361  1.00 75.98           N  
ATOM    226  CA  GLY A 175     -44.233  83.350 -63.784  1.00 74.80           C  
ATOM    227  C   GLY A 175     -43.262  84.417 -64.268  1.00 74.59           C  
ATOM    228  O   GLY A 175     -42.861  84.413 -65.431  1.00 74.82           O  
ATOM    229  N   ARG A 176     -42.881  85.323 -63.370  1.00 73.78           N  
ATOM    230  CA  ARG A 176     -41.957  86.411 -63.680  1.00 74.12           C  
ATOM    231  C   ARG A 176     -40.524  85.936 -63.997  1.00 72.88           C  
ATOM    232  O   ARG A 176     -40.163  84.791 -63.725  1.00 72.72           O  
ATOM    233  CB  ARG A 176     -41.906  87.392 -62.505  1.00 77.80           C  
ATOM    234  CG  ARG A 176     -43.242  88.006 -62.109  1.00 82.32           C  
ATOM    235  CD  ARG A 176     -43.796  88.927 -63.190  1.00 86.50           C  
ATOM    236  NE  ARG A 176     -45.072  89.523 -62.788  1.00 90.76           N  
ATOM    237  CZ  ARG A 176     -45.910  90.140 -63.621  1.00 92.99           C  
ATOM    238  NH1 ARG A 176     -45.610  90.243 -64.912  1.00 93.63           N  
ATOM    239  NH2 ARG A 176     -47.048  90.659 -63.165  1.00 93.52           N  
ATOM    240  N   TYR A 177     -39.712  86.836 -64.556  1.00 69.90           N  
ATOM    241  CA  TYR A 177     -38.330  86.529 -64.915  1.00 66.77           C  
ATOM    242  C   TYR A 177     -37.304  87.288 -64.082  1.00 64.20           C  
ATOM    243  O   TYR A 177     -37.422  88.490 -63.863  1.00 64.35           O  
ATOM    244  CB  TYR A 177     -38.078  86.842 -66.390  1.00 67.54           C  
ATOM    245  CG  TYR A 177     -38.757  85.900 -67.346  1.00 69.67           C  
ATOM    246  CD1 TYR A 177     -40.141  85.889 -67.483  1.00 71.38           C  
ATOM    247  CD2 TYR A 177     -38.018  85.007 -68.110  1.00 70.50           C  
ATOM    248  CE1 TYR A 177     -40.770  85.008 -68.358  1.00 71.46           C  
ATOM    249  CE2 TYR A 177     -38.640  84.126 -68.986  1.00 71.41           C  
ATOM    250  CZ  TYR A 177     -40.012  84.131 -69.102  1.00 71.90           C  
ATOM    251  OH  TYR A 177     -40.625  83.249 -69.958  1.00 73.26           O  
ATOM    252  N   TYR A 178     -36.284  86.575 -63.626  1.00 61.17           N  
ATOM    253  CA  TYR A 178     -35.226  87.176 -62.833  1.00 58.52           C  
ATOM    254  C   TYR A 178     -33.900  86.642 -63.311  1.00 56.92           C  
ATOM    255  O   TYR A 178     -33.844  85.715 -64.107  1.00 54.52           O  
ATOM    256  CB  TYR A 178     -35.401  86.848 -61.346  1.00 58.38           C  
ATOM    257  CG  TYR A 178     -36.695  87.370 -60.759  1.00 58.60           C  
ATOM    258  CD1 TYR A 178     -37.903  86.683 -60.948  1.00 57.61           C  
ATOM    259  CD2 TYR A 178     -36.726  88.591 -60.078  1.00 57.64           C  
ATOM    260  CE1 TYR A 178     -39.101  87.203 -60.482  1.00 57.67           C  
ATOM    261  CE2 TYR A 178     -37.917  89.119 -59.609  1.00 58.38           C  
ATOM    262  CZ  TYR A 178     -39.100  88.422 -59.816  1.00 59.03           C  
ATOM    263  OH  TYR A 178     -40.279  88.963 -59.366  1.00 62.26           O  
ATOM    264  N   ALA A 179     -32.835  87.261 -62.834  1.00 57.43           N  
ATOM    265  CA  ALA A 179     -31.483  86.849 -63.167  1.00 59.64           C  
ATOM    266  C   ALA A 179     -30.897  86.427 -61.835  1.00 61.26           C  
ATOM    267  O   ALA A 179     -30.706  87.252 -60.938  1.00 63.31           O  
ATOM    268  CB  ALA A 179     -30.692  88.012 -63.758  1.00 58.88           C  
ATOM    269  N   MET A 180     -30.632  85.137 -61.695  1.00 61.33           N  
ATOM    270  CA  MET A 180     -30.103  84.617 -60.444  1.00 61.26           C  
ATOM    271  C   MET A 180     -28.575  84.624 -60.398  1.00 61.61           C  
ATOM    272  O   MET A 180     -27.924  83.813 -61.053  1.00 62.88           O  
ATOM    273  CB  MET A 180     -30.634  83.202 -60.223  1.00 59.66           C  
ATOM    274  CG  MET A 180     -30.405  82.667 -58.837  1.00 59.80           C  
ATOM    275  SD  MET A 180     -30.840  80.947 -58.736  1.00 58.31           S  
ATOM    276  CE  MET A 180     -32.520  81.084 -58.339  1.00 60.17           C  
ATOM    277  N   LYS A 181     -28.011  85.554 -59.634  1.00 61.61           N  
ATOM    278  CA  LYS A 181     -26.565  85.655 -59.485  1.00 62.18           C  
ATOM    279  C   LYS A 181     -26.174  84.633 -58.420  1.00 62.85           C  
ATOM    280  O   LYS A 181     -26.638  84.709 -57.279  1.00 62.55           O  
ATOM    281  CB  LYS A 181     -26.171  87.067 -59.034  1.00 63.00           C  
ATOM    282  CG  LYS A 181     -24.668  87.288 -58.867  1.00 65.89           C  
ATOM    283  CD  LYS A 181     -24.298  88.765 -58.618  1.00 66.68           C  
ATOM    284  CE  LYS A 181     -22.782  88.973 -58.688  1.00 67.78           C  
ATOM    285  NZ  LYS A 181     -22.348  90.393 -58.617  1.00 67.64           N  
ATOM    286  N   ILE A 182     -25.334  83.672 -58.794  1.00 62.65           N  
ATOM    287  CA  ILE A 182     -24.908  82.627 -57.866  1.00 63.30           C  
ATOM    288  C   ILE A 182     -23.412  82.712 -57.532  1.00 65.14           C  
ATOM    289  O   ILE A 182     -22.560  82.616 -58.413  1.00 64.86           O  
ATOM    290  CB  ILE A 182     -25.222  81.227 -58.447  1.00 61.40           C  
ATOM    291  CG1 ILE A 182     -26.653  81.202 -58.994  1.00 59.82           C  
ATOM    292  CG2 ILE A 182     -25.096  80.166 -57.359  1.00 61.73           C  
ATOM    293  CD1 ILE A 182     -27.053  79.869 -59.563  1.00 57.04           C  
ATOM    294  N   LEU A 183     -23.098  82.873 -56.252  1.00 66.86           N  
ATOM    295  CA  LEU A 183     -21.707  82.985 -55.820  1.00 69.49           C  
ATOM    296  C   LEU A 183     -21.210  81.848 -54.920  1.00 71.50           C  
ATOM    297  O   LEU A 183     -21.897  81.450 -53.980  1.00 70.84           O  
ATOM    298  CB  LEU A 183     -21.515  84.307 -55.079  1.00 68.32           C  
ATOM    299  CG  LEU A 183     -21.909  85.553 -55.859  1.00 68.44           C  
ATOM    300  CD1 LEU A 183     -21.690  86.766 -54.988  1.00 67.49           C  
ATOM    301  CD2 LEU A 183     -21.089  85.643 -57.136  1.00 67.44           C  
ATOM    302  N   ARG A 184     -20.011  81.341 -55.206  1.00 74.46           N  
ATOM    303  CA  ARG A 184     -19.419  80.281 -54.388  1.00 78.84           C  
ATOM    304  C   ARG A 184     -19.011  80.912 -53.044  1.00 80.56           C  
ATOM    305  O   ARG A 184     -18.384  81.969 -53.029  1.00 80.71           O  
ATOM    306  CB  ARG A 184     -18.155  79.713 -55.050  1.00 79.03           C  
ATOM    307  CG  ARG A 184     -18.268  79.293 -56.510  1.00 81.36           C  
ATOM    308  CD  ARG A 184     -18.797  77.878 -56.657  1.00 83.04           C  
ATOM    309  NE  ARG A 184     -18.527  77.272 -57.971  1.00 85.45           N  
ATOM    310  CZ  ARG A 184     -18.831  77.815 -59.152  1.00 86.85           C  
ATOM    311  NH1 ARG A 184     -19.418  79.005 -59.231  1.00 87.81           N  
ATOM    312  NH2 ARG A 184     -18.572  77.148 -60.268  1.00 87.21           N  
ATOM    313  N   LYS A 185     -19.375  80.285 -51.925  1.00 83.17           N  
ATOM    314  CA  LYS A 185     -18.993  80.798 -50.606  1.00 85.71           C  
ATOM    315  C   LYS A 185     -17.489  80.550 -50.457  1.00 88.06           C  
ATOM    316  O   LYS A 185     -16.768  81.280 -49.760  1.00 87.73           O  
ATOM    317  CB  LYS A 185     -19.742  80.056 -49.497  1.00 84.98           C  
ATOM    318  CG  LYS A 185     -21.219  80.385 -49.403  1.00 86.38           C  
ATOM    319  CD  LYS A 185     -21.881  79.652 -48.230  1.00 86.53           C  
ATOM    320  CE  LYS A 185     -23.367  79.996 -48.113  1.00 86.29           C  
ATOM    321  NZ  LYS A 185     -24.098  79.175 -47.103  1.00 84.89           N  
ATOM    322  N   GLU A 186     -17.050  79.498 -51.144  1.00 90.22           N  
ATOM    323  CA  GLU A 186     -15.667  79.043 -51.184  1.00 92.23           C  
ATOM    324  C   GLU A 186     -14.751  80.101 -51.808  1.00 92.48           C  
ATOM    325  O   GLU A 186     -13.632  80.311 -51.346  1.00 93.21           O  
ATOM    326  CB  GLU A 186     -15.618  77.738 -51.989  1.00 93.98           C  
ATOM    327  CG  GLU A 186     -14.247  77.095 -52.150  1.00 95.52           C  
ATOM    328  CD  GLU A 186     -14.316  75.782 -52.925  1.00 95.76           C  
ATOM    329  OE1 GLU A 186     -14.841  75.784 -54.064  1.00 95.28           O  
ATOM    330  OE2 GLU A 186     -13.845  74.752 -52.391  1.00 96.14           O  
ATOM    331  N   VAL A 187     -15.227  80.760 -52.859  1.00 92.98           N  
ATOM    332  CA  VAL A 187     -14.451  81.806 -53.525  1.00 93.74           C  
ATOM    333  C   VAL A 187     -14.249  82.999 -52.592  1.00 93.83           C  
ATOM    334  O   VAL A 187     -13.149  83.538 -52.495  1.00 94.09           O  
ATOM    335  CB  VAL A 187     -15.155  82.287 -54.813  1.00 94.00           C  
ATOM    336  CG1 VAL A 187     -14.562  83.618 -55.277  1.00 93.72           C  
ATOM    337  CG2 VAL A 187     -15.014  81.225 -55.902  1.00 94.15           C  
ATOM    338  N   ILE A 188     -15.317  83.405 -51.912  1.00 94.10           N  
ATOM    339  CA  ILE A 188     -15.251  84.520 -50.974  1.00 94.51           C  
ATOM    340  C   ILE A 188     -15.082  84.000 -49.543  1.00 94.67           C  
ATOM    341  O   ILE A 188     -14.092  83.338 -49.216  1.00 94.65           O  
ATOM    342  CB  ILE A 188     -16.533  85.390 -51.038  1.00 94.93           C  
ATOM    343  CG1 ILE A 188     -16.456  86.511 -49.991  1.00 95.63           C  
ATOM    344  CG2 ILE A 188     -17.765  84.521 -50.815  1.00 94.63           C  
ATOM    345  CD1 ILE A 188     -17.633  87.478 -49.997  1.00 95.84           C  
ATOM    346  N   VAL A 198     -18.432  91.977 -49.977  1.00115.94           N  
ATOM    347  CA  VAL A 198     -19.657  92.421 -49.318  1.00116.15           C  
ATOM    348  C   VAL A 198     -20.108  93.785 -49.838  1.00116.11           C  
ATOM    349  O   VAL A 198     -21.090  94.347 -49.353  1.00115.03           O  
ATOM    350  CB  VAL A 198     -19.440  92.483 -47.809  1.00116.08           C  
ATOM    351  N   THR A 199     -19.383  94.304 -50.830  1.00116.73           N  
ATOM    352  CA  THR A 199     -19.679  95.608 -51.432  1.00116.64           C  
ATOM    353  C   THR A 199     -20.810  95.530 -52.452  1.00116.34           C  
ATOM    354  O   THR A 199     -21.239  96.552 -52.996  1.00117.01           O  
ATOM    355  CB  THR A 199     -18.422  96.179 -52.095  1.00116.31           C  
ATOM    356  N   GLU A 200     -21.279  94.314 -52.717  1.00115.54           N  
ATOM    357  CA  GLU A 200     -22.372  94.091 -53.660  1.00114.81           C  
ATOM    358  C   GLU A 200     -23.613  93.684 -52.862  1.00114.26           C  
ATOM    359  O   GLU A 200     -24.727  94.145 -53.124  1.00113.75           O  
ATOM    360  CB  GLU A 200     -21.991  92.987 -54.656  1.00114.31           C  
ATOM    361  N   SER A 201     -23.391  92.819 -51.877  1.00114.02           N  
ATOM    362  CA  SER A 201     -24.449  92.316 -51.007  1.00113.43           C  
ATOM    363  C   SER A 201     -24.886  93.387 -50.008  1.00112.60           C  
ATOM    364  O   SER A 201     -24.098  94.260 -49.644  1.00112.97           O  
ATOM    365  CB  SER A 201     -23.954  91.075 -50.261  1.00113.70           C  
ATOM    366  N   ARG A 202     -26.139  93.305 -49.564  1.00111.11           N  
ATOM    367  CA  ARG A 202     -26.701  94.261 -48.610  1.00109.15           C  
ATOM    368  C   ARG A 202     -26.695  95.691 -49.159  1.00107.67           C  
ATOM    369  O   ARG A 202     -27.748  96.316 -49.280  1.00107.03           O  
ATOM    370  CB  ARG A 202     -25.936  94.196 -47.292  1.00109.06           C  
ATOM    371  N   VAL A 203     -25.509  96.200 -49.487  1.00106.07           N  
ATOM    372  CA  VAL A 203     -25.353  97.551 -50.026  1.00104.11           C  
ATOM    373  C   VAL A 203     -26.216  97.731 -51.272  1.00102.86           C  
ATOM    374  O   VAL A 203     -27.076  98.615 -51.315  1.00102.69           O  
ATOM    375  CB  VAL A 203     -23.883  97.817 -50.363  1.00103.29           C  
ATOM    376  N   LEU A 204     -25.980  96.888 -52.278  1.00100.98           N  
ATOM    377  CA  LEU A 204     -26.733  96.939 -53.527  1.00 98.39           C  
ATOM    378  C   LEU A 204     -28.120  96.312 -53.379  1.00 96.96           C  
ATOM    379  O   LEU A 204     -28.937  96.392 -54.290  1.00 96.52           O  
ATOM    380  CB  LEU A 204     -25.961  96.229 -54.628  1.00 98.22           C  
ATOM    381  N   GLN A 205     -28.381  95.690 -52.232  1.00 95.37           N  
ATOM    382  CA  GLN A 205     -29.671  95.049 -51.975  1.00 93.06           C  
ATOM    383  C   GLN A 205     -30.721  96.040 -51.480  1.00 91.48           C  
ATOM    384  O   GLN A 205     -31.908  95.894 -51.775  1.00 91.50           O  
ATOM    385  CB  GLN A 205     -29.505  93.932 -50.955  1.00 93.27           C  
ATOM    386  N   ASN A 206     -30.279  97.045 -50.726  1.00 89.04           N  
ATOM    387  CA  ASN A 206     -31.183  98.053 -50.178  1.00 85.85           C  
ATOM    388  C   ASN A 206     -31.217  99.346 -51.006  1.00 83.68           C  
ATOM    389  O   ASN A 206     -32.114 100.179 -50.834  1.00 83.74           O  
ATOM    390  CB  ASN A 206     -30.801  98.360 -48.721  1.00 85.37           C  
ATOM    391  N   THR A 207     -30.248  99.520 -51.899  1.00 80.80           N  
ATOM    392  CA  THR A 207     -30.231 100.712 -52.735  1.00 77.34           C  
ATOM    393  C   THR A 207     -31.184 100.490 -53.900  1.00 74.28           C  
ATOM    394  O   THR A 207     -30.847  99.845 -54.897  1.00 74.43           O  
ATOM    395  CB  THR A 207     -28.823 101.026 -53.286  1.00 78.15           C  
ATOM    396  OG1 THR A 207     -28.258  99.834 -53.848  1.00 79.55           O  
ATOM    397  CG2 THR A 207     -27.918 101.576 -52.185  1.00 76.08           C  
ATOM    398  N   ARG A 208     -32.392 101.015 -53.733  1.00 70.80           N  
ATOM    399  CA  ARG A 208     -33.450 100.934 -54.725  1.00 66.36           C  
ATOM    400  C   ARG A 208     -33.257 102.162 -55.614  1.00 61.14           C  
ATOM    401  O   ARG A 208     -32.694 103.146 -55.163  1.00 60.38           O  
ATOM    402  CB  ARG A 208     -34.805 101.004 -54.014  1.00 68.85           C  
ATOM    403  CG  ARG A 208     -36.005 100.761 -54.912  1.00 74.38           C  
ATOM    404  CD  ARG A 208     -36.284  99.268 -55.079  1.00 77.62           C  
ATOM    405  NE  ARG A 208     -37.338  99.008 -56.060  1.00 80.33           N  
ATOM    406  CZ  ARG A 208     -37.984  97.849 -56.187  1.00 81.16           C  
ATOM    407  NH1 ARG A 208     -37.696  96.822 -55.392  1.00 79.98           N  
ATOM    408  NH2 ARG A 208     -38.922  97.716 -57.116  1.00 82.27           N  
ATOM    409  N   HIS A 209     -33.693 102.091 -56.871  1.00 56.25           N  
ATOM    410  CA  HIS A 209     -33.596 103.216 -57.808  1.00 49.80           C  
ATOM    411  C   HIS A 209     -34.051 102.883 -59.224  1.00 47.90           C  
ATOM    412  O   HIS A 209     -33.667 101.874 -59.792  1.00 48.20           O  
ATOM    413  CB  HIS A 209     -32.180 103.743 -57.869  1.00 46.99           C  
ATOM    414  CG  HIS A 209     -32.029 104.974 -58.700  1.00 43.60           C  
ATOM    415  ND1 HIS A 209     -32.323 105.004 -60.047  1.00 42.65           N  
ATOM    416  CD2 HIS A 209     -31.525 106.195 -58.398  1.00 44.28           C  
ATOM    417  CE1 HIS A 209     -31.996 106.186 -60.540  1.00 42.73           C  
ATOM    418  NE2 HIS A 209     -31.507 106.927 -59.561  1.00 43.21           N  
ATOM    419  N   PRO A 210     -34.884 103.746 -59.813  1.00 47.06           N  
ATOM    420  CA  PRO A 210     -35.419 103.594 -61.163  1.00 46.11           C  
ATOM    421  C   PRO A 210     -34.502 102.943 -62.188  1.00 44.46           C  
ATOM    422  O   PRO A 210     -34.944 102.085 -62.941  1.00 44.71           O  
ATOM    423  CB  PRO A 210     -35.758 105.026 -61.544  1.00 45.19           C  
ATOM    424  CG  PRO A 210     -36.306 105.535 -60.293  1.00 45.79           C  
ATOM    425  CD  PRO A 210     -35.383 104.998 -59.215  1.00 46.87           C  
ATOM    426  N   PHE A 211     -33.236 103.338 -62.239  1.00 42.42           N  
ATOM    427  CA  PHE A 211     -32.382 102.749 -63.255  1.00 44.68           C  
ATOM    428  C   PHE A 211     -31.352 101.730 -62.782  1.00 44.59           C  
ATOM    429  O   PHE A 211     -30.536 101.294 -63.570  1.00 44.06           O  
ATOM    430  CB  PHE A 211     -31.700 103.856 -64.063  1.00 46.00           C  
ATOM    431  CG  PHE A 211     -32.607 105.030 -64.370  1.00 46.43           C  
ATOM    432  CD1 PHE A 211     -33.765 104.861 -65.118  1.00 45.31           C  
ATOM    433  CD2 PHE A 211     -32.311 106.298 -63.880  1.00 46.16           C  
ATOM    434  CE1 PHE A 211     -34.612 105.933 -65.370  1.00 43.91           C  
ATOM    435  CE2 PHE A 211     -33.158 107.378 -64.129  1.00 44.87           C  
ATOM    436  CZ  PHE A 211     -34.305 107.189 -64.874  1.00 43.47           C  
ATOM    437  N   LEU A 212     -31.376 101.366 -61.502  1.00 45.38           N  
ATOM    438  CA  LEU A 212     -30.456 100.355 -60.986  1.00 45.00           C  
ATOM    439  C   LEU A 212     -31.300  99.098 -60.887  1.00 46.07           C  
ATOM    440  O   LEU A 212     -32.479  99.175 -60.560  1.00 46.70           O  
ATOM    441  CB  LEU A 212     -29.932 100.715 -59.600  1.00 44.56           C  
ATOM    442  CG  LEU A 212     -28.978 101.901 -59.401  1.00 46.26           C  
ATOM    443  CD1 LEU A 212     -28.542 101.926 -57.944  1.00 45.21           C  
ATOM    444  CD2 LEU A 212     -27.753 101.797 -60.292  1.00 43.12           C  
ATOM    445  N   THR A 213     -30.721  97.952 -61.214  1.00 46.50           N  
ATOM    446  CA  THR A 213     -31.443  96.682 -61.135  1.00 48.23           C  
ATOM    447  C   THR A 213     -31.830  96.335 -59.683  1.00 47.83           C  
ATOM    448  O   THR A 213     -30.996  96.357 -58.769  1.00 45.80           O  
ATOM    449  CB  THR A 213     -30.578  95.530 -61.691  1.00 49.60           C  
ATOM    450  OG1 THR A 213     -30.281  95.780 -63.072  1.00 52.57           O  
ATOM    451  CG2 THR A 213     -31.299  94.201 -61.560  1.00 48.95           C  
ATOM    452  N   ALA A 214     -33.096  96.001 -59.473  1.00 48.63           N  
ATOM    453  CA  ALA A 214     -33.577  95.660 -58.131  1.00 50.62           C  
ATOM    454  C   ALA A 214     -33.289  94.222 -57.723  1.00 50.23           C  
ATOM    455  O   ALA A 214     -33.410  93.300 -58.523  1.00 50.03           O  
ATOM    456  CB  ALA A 214     -35.075  95.911 -58.030  1.00 48.96           C  
ATOM    457  N   LEU A 215     -32.915  94.043 -56.467  1.00 51.90           N  
ATOM    458  CA  LEU A 215     -32.654  92.717 -55.934  1.00 54.19           C  
ATOM    459  C   LEU A 215     -33.936  92.232 -55.304  1.00 55.43           C  
ATOM    460  O   LEU A 215     -34.271  92.662 -54.218  1.00 56.30           O  
ATOM    461  CB  LEU A 215     -31.605  92.789 -54.854  1.00 55.78           C  
ATOM    462  CG  LEU A 215     -31.542  91.471 -54.114  1.00 58.10           C  
ATOM    463  CD1 LEU A 215     -31.035  90.396 -55.080  1.00 59.93           C  
ATOM    464  CD2 LEU A 215     -30.637  91.617 -52.903  1.00 59.21           C  
ATOM    465  N   LYS A 216     -34.650  91.341 -55.974  1.00 58.27           N  
ATOM    466  CA  LYS A 216     -35.920  90.832 -55.456  1.00 61.26           C  
ATOM    467  C   LYS A 216     -35.789  89.932 -54.209  1.00 63.11           C  
ATOM    468  O   LYS A 216     -36.374  90.244 -53.175  1.00 64.09           O  
ATOM    469  CB  LYS A 216     -36.669  90.102 -56.577  1.00 61.84           C  
ATOM    470  CG  LYS A 216     -38.104  89.755 -56.260  1.00 65.46           C  
ATOM    471  CD  LYS A 216     -38.818  90.910 -55.545  1.00 68.59           C  
ATOM    472  CE  LYS A 216     -40.336  90.820 -55.730  1.00 70.77           C  
ATOM    473  NZ  LYS A 216     -40.855  89.419 -55.593  1.00 73.30           N  
ATOM    474  N   TYR A 217     -35.041  88.827 -54.303  1.00 64.47           N  
ATOM    475  CA  TYR A 217     -34.836  87.915 -53.162  1.00 65.21           C  
ATOM    476  C   TYR A 217     -33.356  87.635 -52.974  1.00 65.73           C  
ATOM    477  O   TYR A 217     -32.584  87.654 -53.928  1.00 66.59           O  
ATOM    478  CB  TYR A 217     -35.464  86.540 -53.382  1.00 65.54           C  
ATOM    479  CG  TYR A 217     -36.864  86.505 -53.916  1.00 68.87           C  
ATOM    480  CD1 TYR A 217     -37.221  85.555 -54.871  1.00 69.34           C  
ATOM    481  CD2 TYR A 217     -37.839  87.400 -53.469  1.00 70.20           C  
ATOM    482  CE1 TYR A 217     -38.507  85.493 -55.377  1.00 71.79           C  
ATOM    483  CE2 TYR A 217     -39.142  87.349 -53.972  1.00 71.44           C  
ATOM    484  CZ  TYR A 217     -39.464  86.392 -54.931  1.00 72.55           C  
ATOM    485  OH  TYR A 217     -40.725  86.350 -55.479  1.00 73.22           O  
ATOM    486  N   ALA A 218     -32.970  87.332 -51.743  1.00 66.06           N  
ATOM    487  CA  ALA A 218     -31.586  86.982 -51.450  1.00 66.97           C  
ATOM    488  C   ALA A 218     -31.573  85.783 -50.494  1.00 66.49           C  
ATOM    489  O   ALA A 218     -32.059  85.874 -49.366  1.00 67.05           O  
ATOM    490  CB  ALA A 218     -30.854  88.166 -50.830  1.00 66.80           C  
ATOM    491  N   PHE A 219     -31.043  84.654 -50.954  1.00 65.75           N  
ATOM    492  CA  PHE A 219     -30.969  83.470 -50.116  1.00 65.15           C  
ATOM    493  C   PHE A 219     -29.630  82.766 -50.242  1.00 66.36           C  
ATOM    494  O   PHE A 219     -28.763  83.176 -51.008  1.00 66.09           O  
ATOM    495  CB  PHE A 219     -32.091  82.485 -50.454  1.00 64.93           C  
ATOM    496  CG  PHE A 219     -31.932  81.783 -51.783  1.00 64.81           C  
ATOM    497  CD1 PHE A 219     -32.509  82.302 -52.936  1.00 65.12           C  
ATOM    498  CD2 PHE A 219     -31.254  80.568 -51.870  1.00 65.32           C  
ATOM    499  CE1 PHE A 219     -32.422  81.617 -54.161  1.00 65.45           C  
ATOM    500  CE2 PHE A 219     -31.162  79.881 -53.084  1.00 65.11           C  
ATOM    501  CZ  PHE A 219     -31.752  80.409 -54.233  1.00 65.12           C  
ATOM    502  N   GLN A 220     -29.462  81.697 -49.480  1.00 67.70           N  
ATOM    503  CA  GLN A 220     -28.224  80.944 -49.542  1.00 69.01           C  
ATOM    504  C   GLN A 220     -28.425  79.441 -49.419  1.00 67.86           C  
ATOM    505  O   GLN A 220     -29.275  78.970 -48.666  1.00 67.47           O  
ATOM    506  CB  GLN A 220     -27.263  81.403 -48.448  1.00 71.12           C  
ATOM    507  CG  GLN A 220     -27.842  81.326 -47.058  1.00 74.46           C  
ATOM    508  CD  GLN A 220     -26.798  80.964 -46.013  1.00 77.22           C  
ATOM    509  OE1 GLN A 220     -25.706  81.555 -45.958  1.00 77.53           O  
ATOM    510  NE2 GLN A 220     -27.131  79.989 -45.167  1.00 78.19           N  
ATOM    511  N   THR A 221     -27.630  78.703 -50.182  1.00 66.05           N  
ATOM    512  CA  THR A 221     -27.661  77.263 -50.141  1.00 65.06           C  
ATOM    513  C   THR A 221     -26.565  76.895 -49.153  1.00 65.69           C  
ATOM    514  O   THR A 221     -26.013  77.751 -48.466  1.00 65.66           O  
ATOM    515  CB  THR A 221     -27.335  76.637 -51.513  1.00 64.83           C  
ATOM    516  OG1 THR A 221     -26.037  77.065 -51.946  1.00 63.95           O  
ATOM    517  CG2 THR A 221     -28.374  77.037 -52.541  1.00 64.06           C  
ATOM    518  N   HIS A 222     -26.237  75.618 -49.084  1.00 66.51           N  
ATOM    519  CA  HIS A 222     -25.211  75.173 -48.159  1.00 66.87           C  
ATOM    520  C   HIS A 222     -23.792  75.633 -48.536  1.00 66.79           C  
ATOM    521  O   HIS A 222     -22.905  75.669 -47.686  1.00 66.87           O  
ATOM    522  CB  HIS A 222     -25.294  73.646 -48.033  1.00 65.51           C  
ATOM    523  CG  HIS A 222     -24.006  72.994 -47.649  1.00 64.08           C  
ATOM    524  ND1 HIS A 222     -23.053  72.637 -48.579  1.00 62.66           N  
ATOM    525  CD2 HIS A 222     -23.502  72.654 -46.439  1.00 61.64           C  
ATOM    526  CE1 HIS A 222     -22.016  72.103 -47.959  1.00 62.38           C  
ATOM    527  NE2 HIS A 222     -22.263  72.102 -46.659  1.00 62.63           N  
ATOM    528  N   ASP A 223     -23.572  76.008 -49.792  1.00 66.61           N  
ATOM    529  CA  ASP A 223     -22.235  76.440 -50.186  1.00 67.01           C  
ATOM    530  C   ASP A 223     -22.213  77.503 -51.289  1.00 66.02           C  
ATOM    531  O   ASP A 223     -21.252  77.591 -52.054  1.00 65.51           O  
ATOM    532  CB  ASP A 223     -21.414  75.226 -50.629  1.00 68.82           C  
ATOM    533  CG  ASP A 223     -21.555  74.931 -52.114  1.00 71.28           C  
ATOM    534  OD1 ASP A 223     -22.658  75.130 -52.673  1.00 73.50           O  
ATOM    535  OD2 ASP A 223     -20.561  74.490 -52.726  1.00 72.73           O  
ATOM    536  N   ARG A 224     -23.265  78.308 -51.371  1.00 64.36           N  
ATOM    537  CA  ARG A 224     -23.338  79.344 -52.390  1.00 62.86           C  
ATOM    538  C   ARG A 224     -24.286  80.450 -51.969  1.00 62.48           C  
ATOM    539  O   ARG A 224     -25.214  80.227 -51.189  1.00 63.26           O  
ATOM    540  CB  ARG A 224     -23.817  78.756 -53.727  1.00 62.25           C  
ATOM    541  CG  ARG A 224     -22.984  77.588 -54.244  1.00 61.61           C  
ATOM    542  CD  ARG A 224     -23.124  77.399 -55.734  1.00 62.40           C  
ATOM    543  NE  ARG A 224     -22.335  76.268 -56.207  1.00 63.51           N  
ATOM    544  CZ  ARG A 224     -22.020  76.057 -57.482  1.00 66.56           C  
ATOM    545  NH1 ARG A 224     -22.421  76.903 -58.425  1.00 66.60           N  
ATOM    546  NH2 ARG A 224     -21.301  74.995 -57.823  1.00 67.95           N  
ATOM    547  N   LEU A 225     -24.043  81.655 -52.472  1.00 61.44           N  
ATOM    548  CA  LEU A 225     -24.921  82.779 -52.172  1.00 60.47           C  
ATOM    549  C   LEU A 225     -25.755  83.075 -53.424  1.00 59.67           C  
ATOM    550  O   LEU A 225     -25.226  83.122 -54.532  1.00 59.50           O  
ATOM    551  CB  LEU A 225     -24.102  84.001 -51.753  1.00 59.82           C  
ATOM    552  CG  LEU A 225     -23.503  83.911 -50.345  1.00 60.74           C  
ATOM    553  CD1 LEU A 225     -22.685  85.158 -50.037  1.00 57.84           C  
ATOM    554  CD2 LEU A 225     -24.630  83.739 -49.329  1.00 58.46           C  
ATOM    555  N   CYS A 226     -27.060  83.252 -53.246  1.00 58.27           N  
ATOM    556  CA  CYS A 226     -27.944  83.522 -54.371  1.00 57.20           C  
ATOM    557  C   CYS A 226     -28.686  84.839 -54.277  1.00 56.92           C  
ATOM    558  O   CYS A 226     -29.344  85.120 -53.276  1.00 57.20           O  
ATOM    559  CB  CYS A 226     -28.967  82.405 -54.509  1.00 55.32           C  
ATOM    560  SG  CYS A 226     -28.212  80.855 -54.887  1.00 57.09           S  
ATOM    561  N   PHE A 227     -28.586  85.641 -55.332  1.00 56.57           N  
ATOM    562  CA  PHE A 227     -29.286  86.920 -55.387  1.00 55.93           C  
ATOM    563  C   PHE A 227     -30.169  86.933 -56.623  1.00 55.49           C  
ATOM    564  O   PHE A 227     -29.690  87.051 -57.747  1.00 55.43           O  
ATOM    565  CB  PHE A 227     -28.287  88.079 -55.422  1.00 56.67           C  
ATOM    566  CG  PHE A 227     -27.312  88.061 -54.284  1.00 56.69           C  
ATOM    567  CD1 PHE A 227     -26.098  87.394 -54.406  1.00 56.88           C  
ATOM    568  CD2 PHE A 227     -27.633  88.661 -53.071  1.00 55.81           C  
ATOM    569  CE1 PHE A 227     -25.218  87.323 -53.335  1.00 57.66           C  
ATOM    570  CE2 PHE A 227     -26.765  88.595 -51.992  1.00 56.93           C  
ATOM    571  CZ  PHE A 227     -25.554  87.926 -52.120  1.00 58.12           C  
ATOM    572  N   VAL A 228     -31.467  86.769 -56.413  1.00 56.23           N  
ATOM    573  CA  VAL A 228     -32.412  86.756 -57.520  1.00 56.34           C  
ATOM    574  C   VAL A 228     -32.715  88.198 -57.855  1.00 58.34           C  
ATOM    575  O   VAL A 228     -33.132  88.966 -56.990  1.00 58.31           O  
ATOM    576  CB  VAL A 228     -33.701  86.055 -57.114  1.00 55.51           C  
ATOM    577  CG1 VAL A 228     -34.648  85.996 -58.278  1.00 53.98           C  
ATOM    578  CG2 VAL A 228     -33.380  84.675 -56.586  1.00 54.42           C  
ATOM    579  N   MET A 229     -32.503  88.586 -59.105  1.00 59.69           N  
ATOM    580  CA  MET A 229     -32.771  89.968 -59.452  1.00 60.78           C  
ATOM    581  C   MET A 229     -33.614  90.215 -60.689  1.00 60.63           C  
ATOM    582  O   MET A 229     -33.666  89.405 -61.608  1.00 58.00           O  
ATOM    583  CB  MET A 229     -31.461  90.721 -59.549  1.00 63.27           C  
ATOM    584  CG  MET A 229     -30.643  90.590 -58.306  1.00 65.71           C  
ATOM    585  SD  MET A 229     -29.164  91.540 -58.504  1.00 74.37           S  
ATOM    586  CE  MET A 229     -28.364  90.629 -59.918  1.00 70.06           C  
ATOM    587  N   GLU A 230     -34.295  91.356 -60.672  1.00 62.36           N  
ATOM    588  CA  GLU A 230     -35.166  91.784 -61.757  1.00 63.28           C  
ATOM    589  C   GLU A 230     -34.408  91.886 -63.083  1.00 62.25           C  
ATOM    590  O   GLU A 230     -33.374  92.564 -63.180  1.00 60.10           O  
ATOM    591  CB  GLU A 230     -35.790  93.141 -61.414  1.00 66.11           C  
ATOM    592  CG  GLU A 230     -34.762  94.247 -61.183  1.00 68.51           C  
ATOM    593  CD  GLU A 230     -35.252  95.636 -61.612  1.00 70.30           C  
ATOM    594  OE1 GLU A 230     -35.747  95.779 -62.757  1.00 70.13           O  
ATOM    595  OE2 GLU A 230     -35.121  96.590 -60.813  1.00 70.04           O  
ATOM    596  N   TYR A 231     -34.946  91.214 -64.099  1.00 61.20           N  
ATOM    597  CA  TYR A 231     -34.344  91.192 -65.423  1.00 61.12           C  
ATOM    598  C   TYR A 231     -35.099  92.070 -66.428  1.00 60.17           C  
ATOM    599  O   TYR A 231     -36.259  91.807 -66.768  1.00 59.31           O  
ATOM    600  CB  TYR A 231     -34.292  89.748 -65.939  1.00 62.56           C  
ATOM    601  CG  TYR A 231     -33.449  89.561 -67.178  1.00 63.90           C  
ATOM    602  CD1 TYR A 231     -32.097  89.907 -67.186  1.00 64.47           C  
ATOM    603  CD2 TYR A 231     -33.998  89.033 -68.340  1.00 64.89           C  
ATOM    604  CE1 TYR A 231     -31.309  89.729 -68.331  1.00 65.06           C  
ATOM    605  CE2 TYR A 231     -33.224  88.850 -69.485  1.00 66.04           C  
ATOM    606  CZ  TYR A 231     -31.882  89.201 -69.480  1.00 66.26           C  
ATOM    607  OH  TYR A 231     -31.133  89.040 -70.634  1.00 67.36           O  
ATOM    608  N   ALA A 232     -34.424  93.119 -66.886  1.00 58.91           N  
ATOM    609  CA  ALA A 232     -34.978  94.040 -67.868  1.00 57.36           C  
ATOM    610  C   ALA A 232     -35.137  93.239 -69.142  1.00 58.02           C  
ATOM    611  O   ALA A 232     -34.228  92.518 -69.539  1.00 58.79           O  
ATOM    612  CB  ALA A 232     -34.019  95.188 -68.095  1.00 53.93           C  
ATOM    613  N   ASN A 233     -36.282  93.351 -69.795  1.00 59.21           N  
ATOM    614  CA  ASN A 233     -36.480  92.577 -71.011  1.00 60.40           C  
ATOM    615  C   ASN A 233     -36.516  93.423 -72.276  1.00 59.68           C  
ATOM    616  O   ASN A 233     -37.156  93.057 -73.256  1.00 60.47           O  
ATOM    617  CB  ASN A 233     -37.747  91.738 -70.891  1.00 61.00           C  
ATOM    618  CG  ASN A 233     -38.967  92.585 -70.651  1.00 63.21           C  
ATOM    619  OD1 ASN A 233     -39.462  93.241 -71.560  1.00 64.18           O  
ATOM    620  ND2 ASN A 233     -39.449  92.595 -69.416  1.00 64.87           N  
ATOM    621  N   GLY A 234     -35.833  94.559 -72.252  1.00 58.93           N  
ATOM    622  CA  GLY A 234     -35.772  95.391 -73.437  1.00 58.67           C  
ATOM    623  C   GLY A 234     -34.464  95.150 -74.188  1.00 58.13           C  
ATOM    624  O   GLY A 234     -34.115  95.916 -75.087  1.00 59.16           O  
ATOM    625  N   GLY A 235     -33.739  94.086 -73.836  1.00 57.13           N  
ATOM    626  CA  GLY A 235     -32.479  93.791 -74.499  1.00 56.14           C  
ATOM    627  C   GLY A 235     -31.341  94.707 -74.058  1.00 56.73           C  
ATOM    628  O   GLY A 235     -31.579  95.820 -73.565  1.00 55.37           O  
ATOM    629  N   GLU A 236     -30.097  94.263 -74.246  1.00 55.91           N  
ATOM    630  CA  GLU A 236     -28.964  95.069 -73.818  1.00 55.93           C  
ATOM    631  C   GLU A 236     -28.561  96.142 -74.803  1.00 54.07           C  
ATOM    632  O   GLU A 236     -28.650  95.964 -76.006  1.00 52.50           O  
ATOM    633  CB  GLU A 236     -27.746  94.193 -73.452  1.00 57.90           C  
ATOM    634  CG  GLU A 236     -27.375  93.077 -74.411  1.00 62.12           C  
ATOM    635  CD  GLU A 236     -28.072  91.754 -74.100  1.00 64.54           C  
ATOM    636  OE1 GLU A 236     -29.250  91.600 -74.489  1.00 67.19           O  
ATOM    637  OE2 GLU A 236     -27.444  90.872 -73.464  1.00 64.74           O  
ATOM    638  N   LEU A 237     -28.137  97.276 -74.265  1.00 54.53           N  
ATOM    639  CA  LEU A 237     -27.723  98.394 -75.087  1.00 56.61           C  
ATOM    640  C   LEU A 237     -26.744  97.979 -76.157  1.00 56.67           C  
ATOM    641  O   LEU A 237     -26.962  98.271 -77.331  1.00 56.07           O  
ATOM    642  CB  LEU A 237     -27.106  99.494 -74.235  1.00 56.58           C  
ATOM    643  CG  LEU A 237     -28.152 100.550 -73.958  1.00 57.61           C  
ATOM    644  CD1 LEU A 237     -27.529 101.709 -73.212  1.00 59.12           C  
ATOM    645  CD2 LEU A 237     -28.739 101.003 -75.284  1.00 58.30           C  
ATOM    646  N   PHE A 238     -25.666  97.309 -75.752  1.00 58.25           N  
ATOM    647  CA  PHE A 238     -24.662  96.843 -76.700  1.00 59.77           C  
ATOM    648  C   PHE A 238     -25.337  96.271 -77.957  1.00 59.22           C  
ATOM    649  O   PHE A 238     -24.963  96.604 -79.088  1.00 58.82           O  
ATOM    650  CB  PHE A 238     -23.785  95.771 -76.066  1.00 63.32           C  
ATOM    651  CG  PHE A 238     -23.085  94.932 -77.064  1.00 67.74           C  
ATOM    652  CD1 PHE A 238     -22.148  95.501 -77.926  1.00 70.42           C  
ATOM    653  CD2 PHE A 238     -23.418  93.592 -77.212  1.00 70.06           C  
ATOM    654  CE1 PHE A 238     -21.548  94.754 -78.933  1.00 72.13           C  
ATOM    655  CE2 PHE A 238     -22.828  92.821 -78.215  1.00 73.38           C  
ATOM    656  CZ  PHE A 238     -21.887  93.406 -79.083  1.00 74.70           C  
ATOM    657  N   PHE A 239     -26.328  95.408 -77.754  1.00 57.06           N  
ATOM    658  CA  PHE A 239     -27.048  94.832 -78.873  1.00 57.30           C  
ATOM    659  C   PHE A 239     -27.613  95.961 -79.749  1.00 57.90           C  
ATOM    660  O   PHE A 239     -27.362  95.989 -80.959  1.00 57.96           O  
ATOM    661  CB  PHE A 239     -28.184  93.935 -78.357  1.00 59.35           C  
ATOM    662  CG  PHE A 239     -29.231  93.605 -79.394  1.00 58.27           C  
ATOM    663  CD1 PHE A 239     -29.021  92.591 -80.318  1.00 58.58           C  
ATOM    664  CD2 PHE A 239     -30.408  94.349 -79.469  1.00 57.95           C  
ATOM    665  CE1 PHE A 239     -29.963  92.324 -81.315  1.00 58.81           C  
ATOM    666  CE2 PHE A 239     -31.357  94.095 -80.456  1.00 57.58           C  
ATOM    667  CZ  PHE A 239     -31.135  93.079 -81.385  1.00 58.93           C  
ATOM    668  N   HIS A 240     -28.365  96.882 -79.125  1.00 56.19           N  
ATOM    669  CA  HIS A 240     -28.981  98.023 -79.816  1.00 54.93           C  
ATOM    670  C   HIS A 240     -27.977  98.951 -80.489  1.00 54.76           C  
ATOM    671  O   HIS A 240     -28.146  99.314 -81.657  1.00 54.19           O  
ATOM    672  CB  HIS A 240     -29.832  98.858 -78.851  1.00 54.54           C  
ATOM    673  CG  HIS A 240     -31.104  98.192 -78.439  1.00 50.82           C  
ATOM    674  ND1 HIS A 240     -32.061  97.801 -79.349  1.00 50.99           N  
ATOM    675  CD2 HIS A 240     -31.538  97.772 -77.229  1.00 50.75           C  
ATOM    676  CE1 HIS A 240     -33.027  97.155 -78.719  1.00 50.26           C  
ATOM    677  NE2 HIS A 240     -32.734  97.123 -77.432  1.00 52.61           N  
ATOM    678  N   LEU A 241     -26.942  99.346 -79.759  1.00 54.30           N  
ATOM    679  CA  LEU A 241     -25.937 100.226 -80.333  1.00 55.48           C  
ATOM    680  C   LEU A 241     -25.276  99.631 -81.587  1.00 58.25           C  
ATOM    681  O   LEU A 241     -25.051 100.340 -82.579  1.00 58.07           O  
ATOM    682  CB  LEU A 241     -24.851 100.540 -79.315  1.00 53.09           C  
ATOM    683  CG  LEU A 241     -23.814 101.485 -79.922  1.00 51.84           C  
ATOM    684  CD1 LEU A 241     -24.461 102.838 -80.219  1.00 52.24           C  
ATOM    685  CD2 LEU A 241     -22.644 101.641 -78.980  1.00 51.92           C  
ATOM    686  N   SER A 242     -24.950  98.340 -81.544  1.00 59.60           N  
ATOM    687  CA  SER A 242     -24.313  97.705 -82.685  1.00 60.90           C  
ATOM    688  C   SER A 242     -25.246  97.725 -83.895  1.00 62.02           C  
ATOM    689  O   SER A 242     -24.793  97.840 -85.030  1.00 62.01           O  
ATOM    690  CB  SER A 242     -23.945  96.264 -82.350  1.00 61.47           C  
ATOM    691  OG  SER A 242     -25.104  95.454 -82.301  1.00 62.26           O  
ATOM    692  N   ARG A 243     -26.549  97.613 -83.651  1.00 63.39           N  
ATOM    693  CA  ARG A 243     -27.524  97.624 -84.740  1.00 65.66           C  
ATOM    694  C   ARG A 243     -27.602  98.989 -85.434  1.00 65.65           C  
ATOM    695  O   ARG A 243     -27.903  99.091 -86.625  1.00 67.32           O  
ATOM    696  CB  ARG A 243     -28.920  97.246 -84.225  1.00 66.91           C  
ATOM    697  CG  ARG A 243     -29.062  95.800 -83.756  1.00 71.64           C  
ATOM    698  CD  ARG A 243     -30.487  95.301 -83.978  1.00 73.97           C  
ATOM    699  NE  ARG A 243     -30.846  95.409 -85.392  1.00 78.53           N  
ATOM    700  CZ  ARG A 243     -31.959  94.928 -85.944  1.00 79.75           C  
ATOM    701  NH1 ARG A 243     -32.857  94.289 -85.201  1.00 81.92           N  
ATOM    702  NH2 ARG A 243     -32.169  95.081 -87.249  1.00 78.18           N  
ATOM    703  N   GLU A 244     -27.321 100.040 -84.683  1.00 64.96           N  
ATOM    704  CA  GLU A 244     -27.387 101.379 -85.225  1.00 64.35           C  
ATOM    705  C   GLU A 244     -26.036 102.020 -85.428  1.00 62.48           C  
ATOM    706  O   GLU A 244     -25.969 103.169 -85.861  1.00 63.14           O  
ATOM    707  CB  GLU A 244     -28.246 102.255 -84.315  1.00 65.81           C  
ATOM    708  CG  GLU A 244     -29.719 101.911 -84.408  1.00 68.68           C  
ATOM    709  CD  GLU A 244     -30.519 102.489 -83.268  1.00 71.31           C  
ATOM    710  OE1 GLU A 244     -30.407 101.962 -82.136  1.00 72.41           O  
ATOM    711  OE2 GLU A 244     -31.257 103.472 -83.505  1.00 73.57           O  
ATOM    712  N   ARG A 245     -24.971 101.280 -85.133  1.00 59.62           N  
ATOM    713  CA  ARG A 245     -23.615 101.792 -85.283  1.00 58.50           C  
ATOM    714  C   ARG A 245     -23.358 102.986 -84.358  1.00 57.00           C  
ATOM    715  O   ARG A 245     -22.300 103.074 -83.736  1.00 57.51           O  
ATOM    716  CB  ARG A 245     -23.356 102.182 -86.744  1.00 58.81           C  
ATOM    717  CG  ARG A 245     -22.008 102.841 -86.994  1.00 60.78           C  
ATOM    718  CD  ARG A 245     -20.823 101.908 -86.739  1.00 64.40           C  
ATOM    719  NE  ARG A 245     -20.294 101.255 -87.946  1.00 67.35           N  
ATOM    720  CZ  ARG A 245     -20.907 100.293 -88.643  1.00 68.72           C  
ATOM    721  NH1 ARG A 245     -22.106  99.837 -88.276  1.00 70.45           N  
ATOM    722  NH2 ARG A 245     -20.310  99.770 -89.711  1.00 68.30           N  
ATOM    723  N   VAL A 246     -24.327 103.898 -84.273  1.00 55.12           N  
ATOM    724  CA  VAL A 246     -24.231 105.079 -83.425  1.00 54.54           C  
ATOM    725  C   VAL A 246     -25.614 105.591 -83.015  1.00 54.92           C  
ATOM    726  O   VAL A 246     -26.624 105.216 -83.599  1.00 55.11           O  
ATOM    727  CB  VAL A 246     -23.514 106.234 -84.128  1.00 54.99           C  
ATOM    728  CG1 VAL A 246     -23.012 107.211 -83.110  1.00 54.11           C  
ATOM    729  CG2 VAL A 246     -22.368 105.728 -84.938  1.00 56.33           C  
ATOM    730  N   PHE A 247     -25.633 106.454 -82.002  1.00 53.81           N  
ATOM    731  CA  PHE A 247     -26.849 107.048 -81.462  1.00 53.03           C  
ATOM    732  C   PHE A 247     -26.821 108.565 -81.648  1.00 54.68           C  
ATOM    733  O   PHE A 247     -25.744 109.163 -81.763  1.00 53.54           O  
ATOM    734  CB  PHE A 247     -26.962 106.771 -79.960  1.00 51.39           C  
ATOM    735  CG  PHE A 247     -27.359 105.363 -79.613  1.00 50.26           C  
ATOM    736  CD1 PHE A 247     -28.332 104.697 -80.344  1.00 48.01           C  
ATOM    737  CD2 PHE A 247     -26.812 104.730 -78.492  1.00 51.86           C  
ATOM    738  CE1 PHE A 247     -28.761 103.434 -79.967  1.00 46.34           C  
ATOM    739  CE2 PHE A 247     -27.242 103.452 -78.107  1.00 50.23           C  
ATOM    740  CZ  PHE A 247     -28.219 102.809 -78.849  1.00 48.43           C  
ATOM    741  N   THR A 248     -28.000 109.186 -81.645  1.00 54.91           N  
ATOM    742  CA  THR A 248     -28.104 110.633 -81.792  1.00 56.66           C  
ATOM    743  C   THR A 248     -27.595 111.270 -80.535  1.00 55.44           C  
ATOM    744  O   THR A 248     -27.885 110.783 -79.457  1.00 56.71           O  
ATOM    745  CB  THR A 248     -29.547 111.063 -81.957  1.00 60.27           C  
ATOM    746  OG1 THR A 248     -29.983 110.739 -83.280  1.00 63.88           O  
ATOM    747  CG2 THR A 248     -29.701 112.564 -81.699  1.00 63.05           C  
ATOM    748  N   GLU A 249     -26.852 112.362 -80.662  1.00 55.38           N  
ATOM    749  CA  GLU A 249     -26.322 113.044 -79.489  1.00 56.31           C  
ATOM    750  C   GLU A 249     -27.405 113.283 -78.435  1.00 57.00           C  
ATOM    751  O   GLU A 249     -27.112 113.574 -77.275  1.00 57.41           O  
ATOM    752  CB  GLU A 249     -25.697 114.371 -79.879  1.00 55.73           C  
ATOM    753  CG  GLU A 249     -24.435 114.251 -80.671  1.00 58.95           C  
ATOM    754  CD  GLU A 249     -23.588 115.496 -80.526  1.00 61.20           C  
ATOM    755  OE1 GLU A 249     -23.859 116.250 -79.575  1.00 63.10           O  
ATOM    756  OE2 GLU A 249     -22.656 115.722 -81.333  1.00 63.13           O  
ATOM    757  N   GLU A 250     -28.659 113.184 -78.848  1.00 56.51           N  
ATOM    758  CA  GLU A 250     -29.751 113.358 -77.921  1.00 57.01           C  
ATOM    759  C   GLU A 250     -29.924 112.019 -77.238  1.00 56.38           C  
ATOM    760  O   GLU A 250     -30.025 111.947 -76.002  1.00 56.66           O  
ATOM    761  CB  GLU A 250     -31.032 113.731 -78.660  1.00 60.80           C  
ATOM    762  CG  GLU A 250     -31.430 115.197 -78.537  1.00 61.13           C  
ATOM    763  CD  GLU A 250     -31.662 115.600 -77.106  1.00 61.03           C  
ATOM    764  OE1 GLU A 250     -30.666 115.956 -76.439  1.00 60.90           O  
ATOM    765  OE2 GLU A 250     -32.830 115.534 -76.657  1.00 60.72           O  
ATOM    766  N   ARG A 251     -29.959 110.963 -78.053  1.00 54.63           N  
ATOM    767  CA  ARG A 251     -30.073 109.586 -77.554  1.00 51.21           C  
ATOM    768  C   ARG A 251     -29.005 109.367 -76.478  1.00 48.63           C  
ATOM    769  O   ARG A 251     -29.300 109.000 -75.341  1.00 45.94           O  
ATOM    770  CB  ARG A 251     -29.866 108.588 -78.692  1.00 51.13           C  
ATOM    771  CG  ARG A 251     -31.075 107.734 -79.023  1.00 52.38           C  
ATOM    772  CD  ARG A 251     -30.792 106.241 -78.788  1.00 54.26           C  
ATOM    773  NE  ARG A 251     -31.509 105.381 -79.727  1.00 54.06           N  
ATOM    774  CZ  ARG A 251     -31.772 104.094 -79.528  1.00 54.26           C  
ATOM    775  NH1 ARG A 251     -31.386 103.496 -78.418  1.00 55.11           N  
ATOM    776  NH2 ARG A 251     -32.420 103.398 -80.445  1.00 57.29           N  
ATOM    777  N   ALA A 252     -27.755 109.610 -76.828  1.00 47.49           N  
ATOM    778  CA  ALA A 252     -26.708 109.436 -75.838  1.00 48.67           C  
ATOM    779  C   ALA A 252     -27.215 110.236 -74.651  1.00 48.66           C  
ATOM    780  O   ALA A 252     -27.503 109.671 -73.603  1.00 50.01           O  
ATOM    781  CB  ALA A 252     -25.374 109.994 -76.337  1.00 47.04           C  
ATOM    782  N   ARG A 253     -27.351 111.550 -74.834  1.00 48.58           N  
ATOM    783  CA  ARG A 253     -27.850 112.436 -73.783  1.00 46.08           C  
ATOM    784  C   ARG A 253     -28.946 111.748 -72.958  1.00 43.51           C  
ATOM    785  O   ARG A 253     -28.860 111.687 -71.739  1.00 42.92           O  
ATOM    786  CB  ARG A 253     -28.379 113.721 -74.395  1.00 47.35           C  
ATOM    787  N   PHE A 254     -29.964 111.211 -73.605  1.00 39.97           N  
ATOM    788  CA  PHE A 254     -31.004 110.548 -72.841  1.00 40.40           C  
ATOM    789  C   PHE A 254     -30.448 109.517 -71.830  1.00 39.81           C  
ATOM    790  O   PHE A 254     -30.562 109.717 -70.618  1.00 39.93           O  
ATOM    791  CB  PHE A 254     -31.966 109.856 -73.777  1.00 43.80           C  
ATOM    792  CG  PHE A 254     -33.084 109.171 -73.075  1.00 48.65           C  
ATOM    793  CD1 PHE A 254     -34.144 109.908 -72.559  1.00 49.02           C  
ATOM    794  CD2 PHE A 254     -33.098 107.783 -72.953  1.00 50.22           C  
ATOM    795  CE1 PHE A 254     -35.212 109.281 -71.932  1.00 51.78           C  
ATOM    796  CE2 PHE A 254     -34.167 107.137 -72.325  1.00 50.70           C  
ATOM    797  CZ  PHE A 254     -35.228 107.890 -71.816  1.00 51.89           C  
ATOM    798  N   TYR A 255     -29.860 108.420 -72.336  1.00 38.72           N  
ATOM    799  CA  TYR A 255     -29.263 107.327 -71.525  1.00 31.16           C  
ATOM    800  C   TYR A 255     -28.287 107.870 -70.525  1.00 29.48           C  
ATOM    801  O   TYR A 255     -28.308 107.513 -69.350  1.00 29.76           O  
ATOM    802  CB  TYR A 255     -28.545 106.320 -72.423  1.00 30.08           C  
ATOM    803  CG  TYR A 255     -29.498 105.630 -73.390  1.00 30.38           C  
ATOM    804  CD1 TYR A 255     -30.676 105.070 -72.938  1.00 30.21           C  
ATOM    805  CD2 TYR A 255     -29.238 105.592 -74.758  1.00 28.56           C  
ATOM    806  CE1 TYR A 255     -31.586 104.494 -73.828  1.00 32.49           C  
ATOM    807  CE2 TYR A 255     -30.130 105.029 -75.647  1.00 28.91           C  
ATOM    808  CZ  TYR A 255     -31.309 104.484 -75.180  1.00 31.48           C  
ATOM    809  OH  TYR A 255     -32.236 103.968 -76.058  1.00 30.19           O  
ATOM    810  N   GLY A 256     -27.443 108.770 -70.984  1.00 25.98           N  
ATOM    811  CA  GLY A 256     -26.474 109.351 -70.098  1.00 27.64           C  
ATOM    812  C   GLY A 256     -27.112 109.949 -68.868  1.00 32.37           C  
ATOM    813  O   GLY A 256     -26.577 109.746 -67.753  1.00 34.33           O  
ATOM    814  N   ALA A 257     -28.241 110.670 -69.048  1.00 31.72           N  
ATOM    815  CA  ALA A 257     -28.923 111.323 -67.933  1.00 30.84           C  
ATOM    816  C   ALA A 257     -29.514 110.319 -66.936  1.00 32.91           C  
ATOM    817  O   ALA A 257     -29.375 110.514 -65.726  1.00 30.95           O  
ATOM    818  CB  ALA A 257     -30.041 112.328 -68.450  1.00 32.90           C  
ATOM    819  N   GLU A 258     -30.174 109.264 -67.418  1.00 31.33           N  
ATOM    820  CA  GLU A 258     -30.703 108.280 -66.487  1.00 36.06           C  
ATOM    821  C   GLU A 258     -29.516 107.661 -65.717  1.00 39.01           C  
ATOM    822  O   GLU A 258     -29.586 107.446 -64.480  1.00 40.22           O  
ATOM    823  CB  GLU A 258     -31.513 107.204 -67.227  1.00 36.77           C  
ATOM    824  CG  GLU A 258     -32.633 107.806 -68.066  1.00 39.34           C  
ATOM    825  CD  GLU A 258     -33.728 106.821 -68.411  1.00 42.53           C  
ATOM    826  OE1 GLU A 258     -33.406 105.642 -68.711  1.00 42.23           O  
ATOM    827  OE2 GLU A 258     -34.916 107.225 -68.391  1.00 39.67           O  
ATOM    828  N   ILE A 259     -28.410 107.427 -66.427  1.00 37.61           N  
ATOM    829  CA  ILE A 259     -27.246 106.862 -65.769  1.00 39.68           C  
ATOM    830  C   ILE A 259     -26.754 107.871 -64.753  1.00 39.33           C  
ATOM    831  O   ILE A 259     -26.461 107.494 -63.614  1.00 40.77           O  
ATOM    832  CB  ILE A 259     -26.061 106.538 -66.743  1.00 38.81           C  
ATOM    833  CG1 ILE A 259     -26.493 105.531 -67.800  1.00 38.93           C  
ATOM    834  CG2 ILE A 259     -24.909 105.968 -65.969  1.00 36.03           C  
ATOM    835  CD1 ILE A 259     -25.437 105.291 -68.852  1.00 43.96           C  
ATOM    836  N   VAL A 260     -26.656 109.144 -65.164  1.00 38.38           N  
ATOM    837  CA  VAL A 260     -26.176 110.200 -64.254  1.00 36.67           C  
ATOM    838  C   VAL A 260     -27.100 110.305 -63.039  1.00 36.87           C  
ATOM    839  O   VAL A 260     -26.676 110.673 -61.949  1.00 34.89           O  
ATOM    840  CB  VAL A 260     -26.066 111.595 -64.954  1.00 36.15           C  
ATOM    841  CG1 VAL A 260     -25.551 112.633 -63.980  1.00 32.98           C  
ATOM    842  CG2 VAL A 260     -25.111 111.532 -66.149  1.00 33.09           C  
ATOM    843  N   SER A 261     -28.366 109.948 -63.226  1.00 39.02           N  
ATOM    844  CA  SER A 261     -29.316 109.992 -62.128  1.00 41.18           C  
ATOM    845  C   SER A 261     -29.023 108.826 -61.183  1.00 41.35           C  
ATOM    846  O   SER A 261     -29.071 108.965 -59.963  1.00 41.83           O  
ATOM    847  CB  SER A 261     -30.750 109.902 -62.652  1.00 39.70           C  
ATOM    848  OG  SER A 261     -31.672 109.806 -61.591  1.00 36.35           O  
ATOM    849  N   ALA A 262     -28.705 107.676 -61.764  1.00 43.35           N  
ATOM    850  CA  ALA A 262     -28.395 106.486 -60.971  1.00 41.13           C  
ATOM    851  C   ALA A 262     -27.152 106.697 -60.117  1.00 40.90           C  
ATOM    852  O   ALA A 262     -27.131 106.329 -58.940  1.00 43.46           O  
ATOM    853  CB  ALA A 262     -28.224 105.289 -61.880  1.00 40.46           C  
ATOM    854  N   LEU A 263     -26.129 107.317 -60.680  1.00 39.94           N  
ATOM    855  CA  LEU A 263     -24.910 107.534 -59.919  1.00 40.37           C  
ATOM    856  C   LEU A 263     -24.969 108.689 -58.943  1.00 41.43           C  
ATOM    857  O   LEU A 263     -24.247 108.669 -57.954  1.00 43.52           O  
ATOM    858  CB  LEU A 263     -23.708 107.744 -60.833  1.00 38.29           C  
ATOM    859  CG  LEU A 263     -23.493 106.752 -61.964  1.00 39.66           C  
ATOM    860  CD1 LEU A 263     -22.215 107.141 -62.723  1.00 37.46           C  
ATOM    861  CD2 LEU A 263     -23.411 105.349 -61.393  1.00 39.03           C  
ATOM    862  N   GLU A 264     -25.768 109.721 -59.212  1.00 42.36           N  
ATOM    863  CA  GLU A 264     -25.852 110.821 -58.239  1.00 42.24           C  
ATOM    864  C   GLU A 264     -26.382 110.190 -56.953  1.00 41.18           C  
ATOM    865  O   GLU A 264     -25.895 110.474 -55.848  1.00 37.64           O  
ATOM    866  CB  GLU A 264     -26.829 111.903 -58.680  1.00 43.30           C  
ATOM    867  CG  GLU A 264     -26.912 113.061 -57.671  1.00 50.18           C  
ATOM    868  CD  GLU A 264     -28.131 113.968 -57.861  1.00 51.33           C  
ATOM    869  OE1 GLU A 264     -29.238 113.454 -58.170  1.00 50.33           O  
ATOM    870  OE2 GLU A 264     -27.982 115.195 -57.672  1.00 51.97           O  
ATOM    871  N   TYR A 265     -27.372 109.307 -57.136  1.00 41.55           N  
ATOM    872  CA  TYR A 265     -28.005 108.608 -56.041  1.00 41.35           C  
ATOM    873  C   TYR A 265     -27.009 107.763 -55.254  1.00 39.77           C  
ATOM    874  O   TYR A 265     -26.976 107.846 -54.015  1.00 35.31           O  
ATOM    875  CB  TYR A 265     -29.120 107.687 -56.543  1.00 46.23           C  
ATOM    876  CG  TYR A 265     -30.016 107.222 -55.405  1.00 53.65           C  
ATOM    877  CD1 TYR A 265     -30.944 108.110 -54.826  1.00 57.17           C  
ATOM    878  CD2 TYR A 265     -29.925 105.928 -54.878  1.00 54.30           C  
ATOM    879  CE1 TYR A 265     -31.756 107.729 -53.757  1.00 58.02           C  
ATOM    880  CE2 TYR A 265     -30.736 105.527 -53.803  1.00 57.53           C  
ATOM    881  CZ  TYR A 265     -31.655 106.441 -53.246  1.00 59.76           C  
ATOM    882  OH  TYR A 265     -32.488 106.103 -52.187  1.00 59.20           O  
ATOM    883  N   LEU A 266     -26.224 106.951 -55.986  1.00 39.13           N  
ATOM    884  CA  LEU A 266     -25.225 106.047 -55.395  1.00 37.17           C  
ATOM    885  C   LEU A 266     -24.129 106.786 -54.685  1.00 35.39           C  
ATOM    886  O   LEU A 266     -23.849 106.508 -53.550  1.00 33.68           O  
ATOM    887  CB  LEU A 266     -24.625 105.101 -56.444  1.00 35.64           C  
ATOM    888  CG  LEU A 266     -25.576 103.988 -56.927  1.00 34.24           C  
ATOM    889  CD1 LEU A 266     -25.211 103.561 -58.332  1.00 34.29           C  
ATOM    890  CD2 LEU A 266     -25.551 102.810 -55.979  1.00 32.35           C  
ATOM    891  N   HIS A 267     -23.523 107.751 -55.344  1.00 36.83           N  
ATOM    892  CA  HIS A 267     -22.468 108.502 -54.713  1.00 38.39           C  
ATOM    893  C   HIS A 267     -22.974 109.212 -53.478  1.00 41.53           C  
ATOM    894  O   HIS A 267     -22.187 109.612 -52.628  1.00 40.61           O  
ATOM    895  CB  HIS A 267     -21.913 109.539 -55.671  1.00 39.68           C  
ATOM    896  CG  HIS A 267     -21.177 108.961 -56.835  1.00 41.12           C  
ATOM    897  ND1 HIS A 267     -20.524 109.745 -57.759  1.00 40.21           N  
ATOM    898  CD2 HIS A 267     -21.001 107.683 -57.234  1.00 40.79           C  
ATOM    899  CE1 HIS A 267     -19.978 108.973 -58.680  1.00 41.33           C  
ATOM    900  NE2 HIS A 267     -20.253 107.717 -58.384  1.00 42.04           N  
ATOM    901  N   SER A 268     -24.287 109.406 -53.384  1.00 45.78           N  
ATOM    902  CA  SER A 268     -24.829 110.110 -52.232  1.00 49.77           C  
ATOM    903  C   SER A 268     -24.871 109.149 -51.062  1.00 49.62           C  
ATOM    904  O   SER A 268     -24.747 109.553 -49.916  1.00 51.12           O  
ATOM    905  CB  SER A 268     -26.224 110.671 -52.527  1.00 50.34           C  
ATOM    906  OG  SER A 268     -27.199 109.637 -52.556  1.00 57.46           O  
ATOM    907  N   ARG A 269     -25.056 107.875 -51.355  1.00 50.06           N  
ATOM    908  CA  ARG A 269     -25.060 106.869 -50.312  1.00 51.97           C  
ATOM    909  C   ARG A 269     -23.613 106.382 -50.143  1.00 51.28           C  
ATOM    910  O   ARG A 269     -23.389 105.247 -49.745  1.00 49.78           O  
ATOM    911  CB  ARG A 269     -25.949 105.693 -50.712  1.00 55.91           C  
ATOM    912  CG  ARG A 269     -27.399 106.037 -50.921  1.00 61.69           C  
ATOM    913  CD  ARG A 269     -28.018 106.576 -49.645  1.00 66.53           C  
ATOM    914  NE  ARG A 269     -29.466 106.764 -49.759  1.00 71.92           N  
ATOM    915  CZ  ARG A 269     -30.064 107.657 -50.552  1.00 73.60           C  
ATOM    916  NH1 ARG A 269     -29.349 108.472 -51.326  1.00 75.38           N  
ATOM    917  NH2 ARG A 269     -31.389 107.741 -50.569  1.00 73.49           N  
ATOM    918  N   ASP A 270     -22.646 107.236 -50.487  1.00 51.19           N  
ATOM    919  CA  ASP A 270     -21.218 106.921 -50.381  1.00 51.43           C  
ATOM    920  C   ASP A 270     -20.845 105.572 -51.051  1.00 50.47           C  
ATOM    921  O   ASP A 270     -19.967 104.857 -50.579  1.00 51.61           O  
ATOM    922  CB  ASP A 270     -20.827 106.915 -48.894  1.00 54.84           C  
ATOM    923  CG  ASP A 270     -19.328 107.150 -48.655  1.00 60.06           C  
ATOM    924  OD1 ASP A 270     -18.507 106.243 -48.926  1.00 63.84           O  
ATOM    925  OD2 ASP A 270     -18.965 108.250 -48.185  1.00 60.79           O  
ATOM    926  N   VAL A 271     -21.500 105.246 -52.164  1.00 47.21           N  
ATOM    927  CA  VAL A 271     -21.282 103.999 -52.896  1.00 44.41           C  
ATOM    928  C   VAL A 271     -20.655 104.189 -54.268  1.00 44.62           C  
ATOM    929  O   VAL A 271     -21.259 104.830 -55.118  1.00 45.24           O  
ATOM    930  CB  VAL A 271     -22.597 103.308 -53.150  1.00 43.46           C  
ATOM    931  CG1 VAL A 271     -22.411 102.187 -54.152  1.00 44.78           C  
ATOM    932  CG2 VAL A 271     -23.158 102.816 -51.868  1.00 44.89           C  
ATOM    933  N   VAL A 272     -19.475 103.613 -54.504  1.00 44.34           N  
ATOM    934  CA  VAL A 272     -18.802 103.732 -55.812  1.00 42.07           C  
ATOM    935  C   VAL A 272     -19.195 102.568 -56.701  1.00 40.64           C  
ATOM    936  O   VAL A 272     -18.938 101.421 -56.376  1.00 41.65           O  
ATOM    937  CB  VAL A 272     -17.265 103.711 -55.695  1.00 41.28           C  
ATOM    938  CG1 VAL A 272     -16.650 103.699 -57.095  1.00 40.86           C  
ATOM    939  CG2 VAL A 272     -16.779 104.907 -54.920  1.00 38.38           C  
ATOM    940  N   TYR A 273     -19.790 102.842 -57.844  1.00 38.75           N  
ATOM    941  CA  TYR A 273     -20.202 101.732 -58.678  1.00 35.81           C  
ATOM    942  C   TYR A 273     -19.148 100.794 -59.311  1.00 34.83           C  
ATOM    943  O   TYR A 273     -19.391  99.593 -59.426  1.00 32.25           O  
ATOM    944  CB  TYR A 273     -21.125 102.229 -59.766  1.00 30.60           C  
ATOM    945  CG  TYR A 273     -22.007 101.116 -60.224  1.00 26.96           C  
ATOM    946  CD1 TYR A 273     -22.905 100.536 -59.354  1.00 26.90           C  
ATOM    947  CD2 TYR A 273     -21.917 100.613 -61.511  1.00 26.07           C  
ATOM    948  CE1 TYR A 273     -23.703  99.472 -59.756  1.00 27.85           C  
ATOM    949  CE2 TYR A 273     -22.714  99.550 -61.923  1.00 27.30           C  
ATOM    950  CZ  TYR A 273     -23.608  98.988 -61.035  1.00 25.99           C  
ATOM    951  OH  TYR A 273     -24.438  97.962 -61.443  1.00 30.23           O  
ATOM    952  N   ARG A 274     -18.032 101.347 -59.771  1.00 35.60           N  
ATOM    953  CA  ARG A 274     -16.952 100.573 -60.400  1.00 40.10           C  
ATOM    954  C   ARG A 274     -17.244  99.968 -61.769  1.00 41.43           C  
ATOM    955  O   ARG A 274     -16.346  99.832 -62.604  1.00 42.42           O  
ATOM    956  CB  ARG A 274     -16.509  99.420 -59.490  1.00 40.35           C  
ATOM    957  CG  ARG A 274     -15.915  99.829 -58.157  1.00 42.88           C  
ATOM    958  CD  ARG A 274     -15.293  98.607 -57.485  1.00 45.33           C  
ATOM    959  NE  ARG A 274     -14.693  98.910 -56.188  1.00 46.99           N  
ATOM    960  CZ  ARG A 274     -13.499  98.474 -55.796  1.00 45.53           C  
ATOM    961  NH1 ARG A 274     -12.765  97.716 -56.608  1.00 47.01           N  
ATOM    962  NH2 ARG A 274     -13.048  98.780 -54.588  1.00 43.26           N  
ATOM    963  N   ASP A 275     -18.498  99.594 -61.993  1.00 43.34           N  
ATOM    964  CA  ASP A 275     -18.877  98.934 -63.231  1.00 42.09           C  
ATOM    965  C   ASP A 275     -19.752  99.681 -64.219  1.00 39.25           C  
ATOM    966  O   ASP A 275     -20.620  99.074 -64.844  1.00 38.71           O  
ATOM    967  CB  ASP A 275     -19.548  97.603 -62.910  1.00 46.72           C  
ATOM    968  CG  ASP A 275     -18.578  96.578 -62.322  1.00 52.78           C  
ATOM    969  OD1 ASP A 275     -17.969  96.835 -61.252  1.00 51.61           O  
ATOM    970  OD2 ASP A 275     -18.433  95.493 -62.939  1.00 58.27           O  
ATOM    971  N   ILE A 276     -19.563 100.982 -64.381  1.00 35.78           N  
ATOM    972  CA  ILE A 276     -20.376 101.616 -65.392  1.00 33.43           C  
ATOM    973  C   ILE A 276     -19.757 101.302 -66.764  1.00 33.13           C  
ATOM    974  O   ILE A 276     -18.703 101.837 -67.122  1.00 32.09           O  
ATOM    975  CB  ILE A 276     -20.452 103.147 -65.234  1.00 34.47           C  
ATOM    976  CG1 ILE A 276     -21.172 103.516 -63.920  1.00 30.88           C  
ATOM    977  CG2 ILE A 276     -21.139 103.741 -66.479  1.00 30.02           C  
ATOM    978  CD1 ILE A 276     -22.513 102.917 -63.772  1.00 26.51           C  
ATOM    979  N   LYS A 277     -20.405 100.442 -67.538  1.00 31.46           N  
ATOM    980  CA  LYS A 277     -19.865 100.132 -68.833  1.00 35.91           C  
ATOM    981  C   LYS A 277     -20.945  99.493 -69.652  1.00 36.20           C  
ATOM    982  O   LYS A 277     -21.787  98.779 -69.120  1.00 36.94           O  
ATOM    983  CB  LYS A 277     -18.602  99.230 -68.694  1.00 38.36           C  
ATOM    984  CG  LYS A 277     -18.758  97.959 -67.894  1.00 38.67           C  
ATOM    985  CD  LYS A 277     -17.397  97.537 -67.358  1.00 48.05           C  
ATOM    986  CE  LYS A 277     -17.280  96.033 -67.084  1.00 47.89           C  
ATOM    987  NZ  LYS A 277     -17.231  95.212 -68.335  1.00 48.97           N  
ATOM    988  N   LEU A 278     -20.892  99.745 -70.956  1.00 39.25           N  
ATOM    989  CA  LEU A 278     -21.901  99.300 -71.921  1.00 41.51           C  
ATOM    990  C   LEU A 278     -22.514  97.915 -71.765  1.00 43.17           C  
ATOM    991  O   LEU A 278     -23.717  97.712 -72.009  1.00 41.64           O  
ATOM    992  CB  LEU A 278     -21.344  99.464 -73.341  1.00 44.08           C  
ATOM    993  CG  LEU A 278     -22.252  99.148 -74.535  1.00 45.28           C  
ATOM    994  CD1 LEU A 278     -23.423 100.103 -74.582  1.00 45.97           C  
ATOM    995  CD2 LEU A 278     -21.430  99.245 -75.820  1.00 47.91           C  
ATOM    996  N   GLU A 279     -21.684  96.953 -71.382  1.00 44.99           N  
ATOM    997  CA  GLU A 279     -22.139  95.576 -71.210  1.00 45.04           C  
ATOM    998  C   GLU A 279     -23.131  95.509 -70.056  1.00 42.66           C  
ATOM    999  O   GLU A 279     -24.081  94.751 -70.100  1.00 42.65           O  
ATOM   1000  CB  GLU A 279     -20.931  94.662 -70.943  1.00 49.50           C  
ATOM   1001  CG  GLU A 279     -19.682  94.964 -71.808  1.00 53.21           C  
ATOM   1002  CD  GLU A 279     -19.043  96.309 -71.458  1.00 58.29           C  
ATOM   1003  OE1 GLU A 279     -19.369  96.848 -70.374  1.00 59.53           O  
ATOM   1004  OE2 GLU A 279     -18.214  96.826 -72.250  1.00 61.56           O  
ATOM   1005  N   ASN A 280     -22.906  96.318 -69.027  1.00 40.78           N  
ATOM   1006  CA  ASN A 280     -23.795  96.357 -67.878  1.00 41.87           C  
ATOM   1007  C   ASN A 280     -25.007  97.272 -68.142  1.00 41.66           C  
ATOM   1008  O   ASN A 280     -25.556  97.807 -67.194  1.00 42.64           O  
ATOM   1009  CB  ASN A 280     -23.067  96.910 -66.635  1.00 43.23           C  
ATOM   1010  CG  ASN A 280     -21.964  96.003 -66.130  1.00 45.80           C  
ATOM   1011  OD1 ASN A 280     -21.175  95.489 -66.896  1.00 50.79           O  
ATOM   1012  ND2 ASN A 280     -21.889  95.833 -64.829  1.00 47.06           N  
ATOM   1013  N   LEU A 281     -25.414  97.487 -69.390  1.00 40.75           N  
ATOM   1014  CA  LEU A 281     -26.565  98.375 -69.637  1.00 40.76           C  
ATOM   1015  C   LEU A 281     -27.634  97.710 -70.465  1.00 41.66           C  
ATOM   1016  O   LEU A 281     -27.381  97.229 -71.563  1.00 41.78           O  
ATOM   1017  CB  LEU A 281     -26.170  99.688 -70.343  1.00 37.18           C  
ATOM   1018  CG  LEU A 281     -25.149 100.642 -69.685  1.00 39.20           C  
ATOM   1019  CD1 LEU A 281     -24.893 101.863 -70.562  1.00 34.40           C  
ATOM   1020  CD2 LEU A 281     -25.652 101.071 -68.330  1.00 37.74           C  
ATOM   1021  N   MET A 282     -28.837  97.666 -69.924  1.00 42.47           N  
ATOM   1022  CA  MET A 282     -29.945  97.091 -70.655  1.00 46.89           C  
ATOM   1023  C   MET A 282     -31.086  98.112 -70.770  1.00 48.18           C  
ATOM   1024  O   MET A 282     -30.938  99.274 -70.362  1.00 48.98           O  
ATOM   1025  CB  MET A 282     -30.410  95.828 -69.966  1.00 46.68           C  
ATOM   1026  CG  MET A 282     -29.524  94.663 -70.284  1.00 47.81           C  
ATOM   1027  SD  MET A 282     -30.209  93.186 -69.538  1.00 47.77           S  
ATOM   1028  CE  MET A 282     -29.278  93.263 -68.055  1.00 48.29           C  
ATOM   1029  N   LEU A 283     -32.202  97.686 -71.344  1.00 46.85           N  
ATOM   1030  CA  LEU A 283     -33.344  98.564 -71.500  1.00 46.85           C  
ATOM   1031  C   LEU A 283     -34.554  97.828 -70.964  1.00 48.68           C  
ATOM   1032  O   LEU A 283     -34.693  96.632 -71.194  1.00 47.69           O  
ATOM   1033  CB  LEU A 283     -33.541  98.923 -72.979  1.00 43.77           C  
ATOM   1034  CG  LEU A 283     -32.426  99.762 -73.629  1.00 44.31           C  
ATOM   1035  CD1 LEU A 283     -32.831 100.189 -75.043  1.00 44.50           C  
ATOM   1036  CD2 LEU A 283     -32.158 101.005 -72.796  1.00 44.45           C  
ATOM   1037  N   ASP A 284     -35.417  98.511 -70.216  1.00 51.28           N  
ATOM   1038  CA  ASP A 284     -36.606  97.829 -69.716  1.00 54.69           C  
ATOM   1039  C   ASP A 284     -37.677  97.878 -70.809  1.00 56.01           C  
ATOM   1040  O   ASP A 284     -37.495  98.527 -71.832  1.00 54.38           O  
ATOM   1041  CB  ASP A 284     -37.127  98.448 -68.398  1.00 54.71           C  
ATOM   1042  CG  ASP A 284     -37.609  99.892 -68.548  1.00 54.44           C  
ATOM   1043  OD1 ASP A 284     -38.024 100.291 -69.657  1.00 53.61           O  
ATOM   1044  OD2 ASP A 284     -37.593 100.623 -67.530  1.00 54.79           O  
ATOM   1045  N   LYS A 285     -38.785  97.185 -70.589  1.00 58.77           N  
ATOM   1046  CA  LYS A 285     -39.870  97.136 -71.562  1.00 60.58           C  
ATOM   1047  C   LYS A 285     -40.399  98.477 -72.085  1.00 59.61           C  
ATOM   1048  O   LYS A 285     -41.191  98.489 -73.018  1.00 60.34           O  
ATOM   1049  CB  LYS A 285     -41.027  96.323 -70.983  1.00 62.63           C  
ATOM   1050  CG  LYS A 285     -41.474  96.804 -69.621  1.00 65.98           C  
ATOM   1051  CD  LYS A 285     -42.522  95.868 -69.033  1.00 67.82           C  
ATOM   1052  CE  LYS A 285     -42.837  96.237 -67.587  1.00 69.38           C  
ATOM   1053  NZ  LYS A 285     -41.661  96.089 -66.665  1.00 69.25           N  
ATOM   1054  N   ASP A 286     -39.972  99.594 -71.504  1.00 57.95           N  
ATOM   1055  CA  ASP A 286     -40.450 100.902 -71.955  1.00 56.87           C  
ATOM   1056  C   ASP A 286     -39.318 101.725 -72.550  1.00 57.22           C  
ATOM   1057  O   ASP A 286     -39.468 102.922 -72.818  1.00 57.57           O  
ATOM   1058  CB  ASP A 286     -41.104 101.685 -70.796  1.00 53.79           C  
ATOM   1059  CG  ASP A 286     -42.263 100.924 -70.147  1.00 52.93           C  
ATOM   1060  OD1 ASP A 286     -43.056 100.323 -70.906  1.00 52.11           O  
ATOM   1061  OD2 ASP A 286     -42.386 100.927 -68.892  1.00 50.37           O  
ATOM   1062  N   GLY A 287     -38.177 101.082 -72.749  1.00 56.66           N  
ATOM   1063  CA  GLY A 287     -37.045 101.776 -73.321  1.00 53.57           C  
ATOM   1064  C   GLY A 287     -36.218 102.535 -72.313  1.00 53.36           C  
ATOM   1065  O   GLY A 287     -35.337 103.302 -72.706  1.00 54.13           O  
ATOM   1066  N   HIS A 288     -36.503 102.364 -71.021  1.00 52.23           N  
ATOM   1067  CA  HIS A 288     -35.700 103.031 -69.985  1.00 51.11           C  
ATOM   1068  C   HIS A 288     -34.468 102.199 -69.620  1.00 49.05           C  
ATOM   1069  O   HIS A 288     -34.501 100.967 -69.649  1.00 48.04           O  
ATOM   1070  CB  HIS A 288     -36.535 103.298 -68.735  1.00 52.36           C  
ATOM   1071  CG  HIS A 288     -37.412 104.500 -68.849  1.00 52.60           C  
ATOM   1072  ND1 HIS A 288     -36.906 105.783 -68.882  1.00 52.73           N  
ATOM   1073  CD2 HIS A 288     -38.754 104.620 -68.949  1.00 52.36           C  
ATOM   1074  CE1 HIS A 288     -37.904 106.642 -68.993  1.00 53.29           C  
ATOM   1075  NE2 HIS A 288     -39.037 105.962 -69.035  1.00 52.28           N  
ATOM   1076  N   ILE A 289     -33.388 102.882 -69.270  1.00 46.90           N  
ATOM   1077  CA  ILE A 289     -32.133 102.231 -68.928  1.00 43.65           C  
ATOM   1078  C   ILE A 289     -32.132 101.434 -67.604  1.00 43.36           C  
ATOM   1079  O   ILE A 289     -32.836 101.778 -66.648  1.00 42.85           O  
ATOM   1080  CB  ILE A 289     -31.022 103.293 -68.889  1.00 44.24           C  
ATOM   1081  CG1 ILE A 289     -29.994 103.011 -69.984  1.00 45.62           C  
ATOM   1082  CG2 ILE A 289     -30.430 103.389 -67.495  1.00 44.61           C  
ATOM   1083  CD1 ILE A 289     -28.768 103.925 -69.940  1.00 47.16           C  
ATOM   1084  N   LYS A 290     -31.341 100.359 -67.564  1.00 40.98           N  
ATOM   1085  CA  LYS A 290     -31.213  99.537 -66.361  1.00 38.87           C  
ATOM   1086  C   LYS A 290     -29.780  99.076 -66.203  1.00 38.82           C  
ATOM   1087  O   LYS A 290     -29.315  98.213 -66.959  1.00 36.63           O  
ATOM   1088  CB  LYS A 290     -32.108  98.286 -66.403  1.00 37.03           C  
ATOM   1089  CG  LYS A 290     -33.506  98.445 -65.867  1.00 38.64           C  
ATOM   1090  CD  LYS A 290     -33.569  98.783 -64.376  1.00 39.12           C  
ATOM   1091  CE  LYS A 290     -35.040  98.949 -63.917  1.00 39.58           C  
ATOM   1092  NZ  LYS A 290     -35.202  99.399 -62.491  1.00 40.12           N  
ATOM   1093  N   ILE A 291     -29.095  99.659 -65.221  1.00 39.18           N  
ATOM   1094  CA  ILE A 291     -27.726  99.314 -64.899  1.00 40.96           C  
ATOM   1095  C   ILE A 291     -27.760  97.937 -64.242  1.00 41.19           C  
ATOM   1096  O   ILE A 291     -28.153  97.791 -63.099  1.00 40.36           O  
ATOM   1097  CB  ILE A 291     -27.135 100.321 -63.935  1.00 39.86           C  
ATOM   1098  CG1 ILE A 291     -27.179 101.715 -64.579  1.00 42.74           C  
ATOM   1099  CG2 ILE A 291     -25.725  99.908 -63.581  1.00 41.24           C  
ATOM   1100  CD1 ILE A 291     -26.529 102.835 -63.793  1.00 38.10           C  
ATOM   1101  N   THR A 292     -27.355  96.933 -65.001  1.00 44.54           N  
ATOM   1102  CA  THR A 292     -27.341  95.543 -64.579  1.00 48.99           C  
ATOM   1103  C   THR A 292     -26.045  95.219 -63.844  1.00 51.32           C  
ATOM   1104  O   THR A 292     -25.023  95.744 -64.205  1.00 52.44           O  
ATOM   1105  CB  THR A 292     -27.473  94.688 -65.814  1.00 47.88           C  
ATOM   1106  OG1 THR A 292     -28.211  93.514 -65.489  1.00 48.38           O  
ATOM   1107  CG2 THR A 292     -26.108  94.330 -66.360  1.00 49.14           C  
ATOM   1108  N   ASP A 293     -26.065  94.357 -62.832  1.00 57.14           N  
ATOM   1109  CA  ASP A 293     -24.821  94.066 -62.078  1.00 63.64           C  
ATOM   1110  C   ASP A 293     -23.898  92.954 -62.585  1.00 64.58           C  
ATOM   1111  O   ASP A 293     -23.428  92.142 -61.795  1.00 65.31           O  
ATOM   1112  CB  ASP A 293     -25.132  93.760 -60.602  1.00 66.55           C  
ATOM   1113  CG  ASP A 293     -23.910  93.957 -59.688  1.00 69.99           C  
ATOM   1114  OD1 ASP A 293     -22.797  93.515 -60.066  1.00 70.67           O  
ATOM   1115  OD2 ASP A 293     -24.066  94.558 -58.588  1.00 71.18           O  
ATOM   1116  N   PHE A 294     -23.619  92.922 -63.881  1.00 66.53           N  
ATOM   1117  CA  PHE A 294     -22.743  91.888 -64.429  1.00 69.39           C  
ATOM   1118  C   PHE A 294     -22.446  92.054 -65.921  1.00 72.30           C  
ATOM   1119  O   PHE A 294     -23.146  92.787 -66.637  1.00 73.05           O  
ATOM   1120  CB  PHE A 294     -23.363  90.512 -64.170  1.00 68.53           C  
ATOM   1121  CG  PHE A 294     -24.852  90.465 -64.391  1.00 66.63           C  
ATOM   1122  CD1 PHE A 294     -25.374  90.204 -65.653  1.00 65.88           C  
ATOM   1123  CD2 PHE A 294     -25.733  90.702 -63.334  1.00 65.41           C  
ATOM   1124  CE1 PHE A 294     -26.752  90.171 -65.864  1.00 65.64           C  
ATOM   1125  CE2 PHE A 294     -27.112  90.672 -63.527  1.00 65.80           C  
ATOM   1126  CZ  PHE A 294     -27.624  90.405 -64.801  1.00 65.41           C  
ATOM   1127  N   GLY A 295     -21.405  91.370 -66.387  1.00 73.27           N  
ATOM   1128  CA  GLY A 295     -21.057  91.448 -67.794  1.00 75.61           C  
ATOM   1129  C   GLY A 295     -21.847  90.436 -68.605  1.00 77.23           C  
ATOM   1130  O   GLY A 295     -21.644  89.232 -68.449  1.00 75.85           O  
ATOM   1131  N   LEU A 296     -22.744  90.923 -69.468  1.00 80.08           N  
ATOM   1132  CA  LEU A 296     -23.589  90.056 -70.301  1.00 81.54           C  
ATOM   1133  C   LEU A 296     -22.814  88.866 -70.859  1.00 82.98           C  
ATOM   1134  O   LEU A 296     -22.495  87.925 -70.129  1.00 83.79           O  
ATOM   1135  CB  LEU A 296     -24.207  90.857 -71.446  1.00 80.52           C  
ATOM   1136  N   THR A 313     -14.714  92.203 -75.369  1.00 59.15           N  
ATOM   1137  CA  THR A 313     -14.670  93.623 -75.035  1.00 58.88           C  
ATOM   1138  C   THR A 313     -13.420  94.061 -74.252  1.00 56.73           C  
ATOM   1139  O   THR A 313     -13.128  93.540 -73.176  1.00 55.94           O  
ATOM   1140  CB  THR A 313     -15.922  94.044 -74.210  1.00 61.34           C  
ATOM   1141  OG1 THR A 313     -16.167  93.077 -73.179  1.00 62.68           O  
ATOM   1142  CG2 THR A 313     -17.153  94.165 -75.111  1.00 64.02           C  
ATOM   1143  N   PRO A 314     -12.661  95.022 -74.803  1.00 53.89           N  
ATOM   1144  CA  PRO A 314     -11.447  95.537 -74.149  1.00 53.39           C  
ATOM   1145  C   PRO A 314     -11.816  96.331 -72.891  1.00 53.68           C  
ATOM   1146  O   PRO A 314     -12.652  97.240 -72.954  1.00 56.86           O  
ATOM   1147  CB  PRO A 314     -10.831  96.445 -75.212  1.00 51.38           C  
ATOM   1148  CG  PRO A 314     -11.326  95.856 -76.510  1.00 53.31           C  
ATOM   1149  CD  PRO A 314     -12.751  95.465 -76.206  1.00 52.85           C  
ATOM   1150  N   GLU A 315     -11.217  95.992 -71.752  1.00 52.89           N  
ATOM   1151  CA  GLU A 315     -11.486  96.709 -70.498  1.00 50.87           C  
ATOM   1152  C   GLU A 315     -10.973  98.141 -70.578  1.00 50.00           C  
ATOM   1153  O   GLU A 315      -9.901  98.381 -71.126  1.00 48.77           O  
ATOM   1154  CB  GLU A 315     -10.772  96.041 -69.326  1.00 53.27           C  
ATOM   1155  CG  GLU A 315     -11.462  94.835 -68.718  1.00 57.90           C  
ATOM   1156  CD  GLU A 315     -11.720  95.019 -67.225  1.00 60.11           C  
ATOM   1157  OE1 GLU A 315     -12.813  95.521 -66.858  1.00 62.25           O  
ATOM   1158  OE2 GLU A 315     -10.821  94.681 -66.422  1.00 61.09           O  
ATOM   1159  N   TYR A 316     -11.723  99.099 -70.037  1.00 47.44           N  
ATOM   1160  CA  TYR A 316     -11.262 100.487 -70.037  1.00 44.07           C  
ATOM   1161  C   TYR A 316     -11.312 101.038 -68.614  1.00 44.48           C  
ATOM   1162  O   TYR A 316     -12.122 101.930 -68.287  1.00 44.77           O  
ATOM   1163  CB  TYR A 316     -12.120 101.355 -70.954  1.00 43.32           C  
ATOM   1164  CG  TYR A 316     -11.603 101.488 -72.365  1.00 41.87           C  
ATOM   1165  CD1 TYR A 316     -11.992 100.596 -73.353  1.00 40.57           C  
ATOM   1166  CD2 TYR A 316     -10.773 102.563 -72.731  1.00 42.15           C  
ATOM   1167  CE1 TYR A 316     -11.590 100.765 -74.671  1.00 40.46           C  
ATOM   1168  CE2 TYR A 316     -10.363 102.743 -74.056  1.00 39.01           C  
ATOM   1169  CZ  TYR A 316     -10.782 101.837 -75.014  1.00 39.92           C  
ATOM   1170  OH  TYR A 316     -10.400 101.988 -76.327  1.00 43.13           O  
ATOM   1171  N   LEU A 317     -10.472 100.468 -67.759  1.00 41.46           N  
ATOM   1172  CA  LEU A 317     -10.397 100.902 -66.377  1.00 40.06           C  
ATOM   1173  C   LEU A 317      -9.955 102.349 -66.354  1.00 39.32           C  
ATOM   1174  O   LEU A 317      -9.159 102.777 -67.188  1.00 38.89           O  
ATOM   1175  CB  LEU A 317      -9.395 100.053 -65.582  1.00 37.12           C  
ATOM   1176  CG  LEU A 317      -9.778  98.578 -65.467  1.00 38.03           C  
ATOM   1177  CD1 LEU A 317      -8.704  97.838 -64.631  1.00 34.16           C  
ATOM   1178  CD2 LEU A 317     -11.196  98.444 -64.855  1.00 32.06           C  
ATOM   1179  N   ALA A 318     -10.470 103.098 -65.393  1.00 38.52           N  
ATOM   1180  CA  ALA A 318     -10.109 104.494 -65.280  1.00 38.97           C  
ATOM   1181  C   ALA A 318      -8.604 104.570 -65.061  1.00 37.84           C  
ATOM   1182  O   ALA A 318      -8.029 103.712 -64.432  1.00 39.02           O  
ATOM   1183  CB  ALA A 318     -10.853 105.129 -64.092  1.00 36.74           C  
ATOM   1184  N   PRO A 319      -7.950 105.604 -65.582  1.00 37.61           N  
ATOM   1185  CA  PRO A 319      -6.511 105.711 -65.377  1.00 37.27           C  
ATOM   1186  C   PRO A 319      -6.068 105.611 -63.928  1.00 38.12           C  
ATOM   1187  O   PRO A 319      -5.090 104.906 -63.616  1.00 39.31           O  
ATOM   1188  CB  PRO A 319      -6.155 107.065 -66.012  1.00 38.19           C  
ATOM   1189  CG  PRO A 319      -7.466 107.750 -66.171  1.00 40.33           C  
ATOM   1190  CD  PRO A 319      -8.415 106.643 -66.505  1.00 37.28           C  
ATOM   1191  N   GLU A 320      -6.766 106.288 -63.020  1.00 39.66           N  
ATOM   1192  CA  GLU A 320      -6.338 106.211 -61.616  1.00 40.61           C  
ATOM   1193  C   GLU A 320      -6.555 104.785 -61.068  1.00 41.50           C  
ATOM   1194  O   GLU A 320      -6.004 104.416 -60.026  1.00 41.30           O  
ATOM   1195  CB  GLU A 320      -7.040 107.272 -60.729  1.00 42.01           C  
ATOM   1196  CG  GLU A 320      -8.528 107.061 -60.511  1.00 42.28           C  
ATOM   1197  CD  GLU A 320      -9.384 107.677 -61.606  1.00 44.84           C  
ATOM   1198  OE1 GLU A 320      -8.905 107.784 -62.759  1.00 44.48           O  
ATOM   1199  OE2 GLU A 320     -10.547 108.029 -61.314  1.00 43.82           O  
ATOM   1200  N   VAL A 321      -7.368 103.983 -61.752  1.00 41.48           N  
ATOM   1201  CA  VAL A 321      -7.527 102.616 -61.303  1.00 43.46           C  
ATOM   1202  C   VAL A 321      -6.272 101.877 -61.807  1.00 45.96           C  
ATOM   1203  O   VAL A 321      -5.638 101.142 -61.052  1.00 46.04           O  
ATOM   1204  CB  VAL A 321      -8.793 101.942 -61.886  1.00 42.90           C  
ATOM   1205  CG1 VAL A 321      -8.723 100.458 -61.658  1.00 40.77           C  
ATOM   1206  CG2 VAL A 321     -10.056 102.509 -61.224  1.00 41.50           C  
ATOM   1207  N   LEU A 322      -5.896 102.093 -63.070  1.00 46.19           N  
ATOM   1208  CA  LEU A 322      -4.715 101.428 -63.624  1.00 48.00           C  
ATOM   1209  C   LEU A 322      -3.419 101.770 -62.898  1.00 48.98           C  
ATOM   1210  O   LEU A 322      -2.587 100.890 -62.624  1.00 48.72           O  
ATOM   1211  CB  LEU A 322      -4.532 101.776 -65.098  1.00 45.28           C  
ATOM   1212  CG  LEU A 322      -5.572 101.131 -65.995  1.00 44.88           C  
ATOM   1213  CD1 LEU A 322      -5.338 101.564 -67.424  1.00 43.60           C  
ATOM   1214  CD2 LEU A 322      -5.482  99.601 -65.844  1.00 46.21           C  
ATOM   1215  N   GLU A 323      -3.246 103.046 -62.584  1.00 48.43           N  
ATOM   1216  CA  GLU A 323      -2.024 103.473 -61.931  1.00 48.74           C  
ATOM   1217  C   GLU A 323      -1.976 103.279 -60.423  1.00 49.31           C  
ATOM   1218  O   GLU A 323      -1.038 102.670 -59.924  1.00 51.48           O  
ATOM   1219  CB  GLU A 323      -1.723 104.930 -62.303  1.00 47.78           C  
ATOM   1220  CG  GLU A 323      -0.531 105.544 -61.605  1.00 49.29           C  
ATOM   1221  CD  GLU A 323      -0.121 106.897 -62.196  1.00 51.10           C  
ATOM   1222  OE1 GLU A 323      -0.996 107.667 -62.659  1.00 49.60           O  
ATOM   1223  OE2 GLU A 323       1.088 107.199 -62.173  1.00 51.60           O  
ATOM   1224  N   ASP A 324      -2.976 103.758 -59.689  1.00 49.30           N  
ATOM   1225  CA  ASP A 324      -2.935 103.625 -58.242  1.00 50.09           C  
ATOM   1226  C   ASP A 324      -3.988 102.746 -57.624  1.00 49.94           C  
ATOM   1227  O   ASP A 324      -4.235 102.840 -56.425  1.00 50.33           O  
ATOM   1228  CB  ASP A 324      -2.998 105.000 -57.569  1.00 52.06           C  
ATOM   1229  CG  ASP A 324      -1.834 105.890 -57.953  1.00 54.90           C  
ATOM   1230  OD1 ASP A 324      -0.719 105.351 -58.197  1.00 56.43           O  
ATOM   1231  OD2 ASP A 324      -2.030 107.132 -57.999  1.00 54.85           O  
ATOM   1232  N   ASN A 325      -4.599 101.886 -58.424  1.00 50.22           N  
ATOM   1233  CA  ASN A 325      -5.650 100.995 -57.930  1.00 50.82           C  
ATOM   1234  C   ASN A 325      -6.677 101.719 -57.046  1.00 51.62           C  
ATOM   1235  O   ASN A 325      -7.292 101.126 -56.156  1.00 51.31           O  
ATOM   1236  CB  ASN A 325      -5.045  99.844 -57.145  1.00 49.40           C  
ATOM   1237  CG  ASN A 325      -6.033  98.728 -56.940  1.00 51.09           C  
ATOM   1238  OD1 ASN A 325      -6.692  98.301 -57.891  1.00 50.12           O  
ATOM   1239  ND2 ASN A 325      -6.143  98.239 -55.709  1.00 51.32           N  
ATOM   1240  N   ASP A 326      -6.860 103.003 -57.320  1.00 52.10           N  
ATOM   1241  CA  ASP A 326      -7.778 103.855 -56.578  1.00 52.40           C  
ATOM   1242  C   ASP A 326      -9.175 103.941 -57.228  1.00 50.99           C  
ATOM   1243  O   ASP A 326      -9.360 104.610 -58.246  1.00 51.40           O  
ATOM   1244  CB  ASP A 326      -7.126 105.233 -56.459  1.00 55.91           C  
ATOM   1245  CG  ASP A 326      -8.052 106.279 -55.921  1.00 57.93           C  
ATOM   1246  OD1 ASP A 326      -7.591 107.424 -55.741  1.00 60.62           O  
ATOM   1247  OD2 ASP A 326      -9.231 105.974 -55.686  1.00 61.37           O  
ATOM   1248  N   TYR A 327     -10.145 103.255 -56.621  1.00 47.51           N  
ATOM   1249  CA  TYR A 327     -11.521 103.229 -57.104  1.00 46.05           C  
ATOM   1250  C   TYR A 327     -12.406 104.263 -56.388  1.00 46.29           C  
ATOM   1251  O   TYR A 327     -13.294 103.873 -55.617  1.00 45.81           O  
ATOM   1252  CB  TYR A 327     -12.174 101.844 -56.887  1.00 44.52           C  
ATOM   1253  CG  TYR A 327     -11.801 100.745 -57.861  1.00 44.13           C  
ATOM   1254  CD1 TYR A 327     -10.607 100.030 -57.726  1.00 44.42           C  
ATOM   1255  CD2 TYR A 327     -12.642 100.421 -58.924  1.00 43.88           C  
ATOM   1256  CE1 TYR A 327     -10.265  99.026 -58.620  1.00 44.03           C  
ATOM   1257  CE2 TYR A 327     -12.305  99.420 -59.828  1.00 45.11           C  
ATOM   1258  CZ  TYR A 327     -11.113  98.722 -59.672  1.00 46.51           C  
ATOM   1259  OH  TYR A 327     -10.775  97.734 -60.583  1.00 47.73           O  
ATOM   1260  N   GLY A 328     -12.182 105.555 -56.642  1.00 45.42           N  
ATOM   1261  CA  GLY A 328     -13.003 106.592 -56.028  1.00 44.56           C  
ATOM   1262  C   GLY A 328     -14.168 107.043 -56.905  1.00 44.89           C  
ATOM   1263  O   GLY A 328     -14.212 106.706 -58.091  1.00 45.84           O  
ATOM   1264  N   ARG A 329     -15.100 107.806 -56.332  1.00 43.79           N  
ATOM   1265  CA  ARG A 329     -16.280 108.314 -57.057  1.00 45.00           C  
ATOM   1266  C   ARG A 329     -16.017 108.549 -58.548  1.00 44.34           C  
ATOM   1267  O   ARG A 329     -16.807 108.160 -59.418  1.00 44.67           O  
ATOM   1268  CB  ARG A 329     -16.745 109.667 -56.494  1.00 46.72           C  
ATOM   1269  CG  ARG A 329     -16.740 109.839 -54.996  1.00 50.80           C  
ATOM   1270  CD  ARG A 329     -16.236 111.251 -54.601  1.00 52.39           C  
ATOM   1271  NE  ARG A 329     -16.644 112.263 -55.563  1.00 53.61           N  
ATOM   1272  CZ  ARG A 329     -16.066 113.450 -55.706  1.00 54.19           C  
ATOM   1273  NH1 ARG A 329     -15.038 113.807 -54.948  1.00 53.30           N  
ATOM   1274  NH2 ARG A 329     -16.520 114.280 -56.630  1.00 57.73           N  
ATOM   1275  N   ALA A 330     -14.904 109.231 -58.806  1.00 44.40           N  
ATOM   1276  CA  ALA A 330     -14.463 109.614 -60.134  1.00 43.64           C  
ATOM   1277  C   ALA A 330     -14.551 108.554 -61.218  1.00 42.49           C  
ATOM   1278  O   ALA A 330     -14.952 108.843 -62.339  1.00 43.59           O  
ATOM   1279  CB  ALA A 330     -13.052 110.143 -60.053  1.00 43.03           C  
ATOM   1280  N   VAL A 331     -14.193 107.323 -60.903  1.00 41.64           N  
ATOM   1281  CA  VAL A 331     -14.235 106.295 -61.938  1.00 41.10           C  
ATOM   1282  C   VAL A 331     -15.621 106.018 -62.527  1.00 40.28           C  
ATOM   1283  O   VAL A 331     -15.728 105.397 -63.596  1.00 40.48           O  
ATOM   1284  CB  VAL A 331     -13.607 104.964 -61.440  1.00 40.63           C  
ATOM   1285  CG1 VAL A 331     -12.330 105.257 -60.703  1.00 39.18           C  
ATOM   1286  CG2 VAL A 331     -14.576 104.212 -60.563  1.00 39.26           C  
ATOM   1287  N   ASP A 332     -16.687 106.458 -61.865  1.00 36.73           N  
ATOM   1288  CA  ASP A 332     -17.983 106.192 -62.457  1.00 37.81           C  
ATOM   1289  C   ASP A 332     -18.231 107.187 -63.588  1.00 36.06           C  
ATOM   1290  O   ASP A 332     -18.927 106.888 -64.568  1.00 35.40           O  
ATOM   1291  CB  ASP A 332     -19.117 106.275 -61.430  1.00 39.48           C  
ATOM   1292  CG  ASP A 332     -19.090 105.143 -60.432  1.00 41.28           C  
ATOM   1293  OD1 ASP A 332     -18.807 104.002 -60.846  1.00 42.57           O  
ATOM   1294  OD2 ASP A 332     -19.371 105.388 -59.236  1.00 40.86           O  
ATOM   1295  N   TRP A 333     -17.652 108.371 -63.446  1.00 35.64           N  
ATOM   1296  CA  TRP A 333     -17.817 109.414 -64.434  1.00 36.78           C  
ATOM   1297  C   TRP A 333     -17.060 108.981 -65.681  1.00 36.91           C  
ATOM   1298  O   TRP A 333     -17.605 109.055 -66.801  1.00 34.53           O  
ATOM   1299  CB  TRP A 333     -17.321 110.745 -63.853  1.00 38.47           C  
ATOM   1300  CG  TRP A 333     -18.209 111.198 -62.715  1.00 40.22           C  
ATOM   1301  CD1 TRP A 333     -17.811 111.630 -61.473  1.00 42.01           C  
ATOM   1302  CD2 TRP A 333     -19.644 111.173 -62.688  1.00 37.46           C  
ATOM   1303  NE1 TRP A 333     -18.912 111.859 -60.680  1.00 40.96           N  
ATOM   1304  CE2 TRP A 333     -20.050 111.582 -61.402  1.00 38.54           C  
ATOM   1305  CE3 TRP A 333     -20.629 110.829 -63.625  1.00 36.64           C  
ATOM   1306  CZ2 TRP A 333     -21.397 111.670 -61.026  1.00 37.30           C  
ATOM   1307  CZ3 TRP A 333     -21.967 110.915 -63.254  1.00 36.57           C  
ATOM   1308  CH2 TRP A 333     -22.337 111.330 -61.960  1.00 34.77           C  
ATOM   1309  N   TRP A 334     -15.824 108.508 -65.470  1.00 36.47           N  
ATOM   1310  CA  TRP A 334     -14.979 107.985 -66.546  1.00 33.94           C  
ATOM   1311  C   TRP A 334     -15.814 106.882 -67.206  1.00 31.22           C  
ATOM   1312  O   TRP A 334     -15.976 106.805 -68.446  1.00 27.52           O  
ATOM   1313  CB  TRP A 334     -13.684 107.430 -65.945  1.00 38.39           C  
ATOM   1314  CG  TRP A 334     -12.897 106.601 -66.905  1.00 43.61           C  
ATOM   1315  CD1 TRP A 334     -13.054 105.266 -67.154  1.00 44.90           C  
ATOM   1316  CD2 TRP A 334     -11.885 107.059 -67.802  1.00 44.64           C  
ATOM   1317  NE1 TRP A 334     -12.203 104.871 -68.154  1.00 47.69           N  
ATOM   1318  CE2 TRP A 334     -11.478 105.951 -68.572  1.00 46.04           C  
ATOM   1319  CE3 TRP A 334     -11.287 108.303 -68.039  1.00 45.41           C  
ATOM   1320  CZ2 TRP A 334     -10.496 106.045 -69.556  1.00 46.52           C  
ATOM   1321  CZ3 TRP A 334     -10.312 108.398 -69.017  1.00 45.68           C  
ATOM   1322  CH2 TRP A 334      -9.927 107.276 -69.767  1.00 45.59           C  
ATOM   1323  N   GLY A 335     -16.388 106.040 -66.359  1.00 30.86           N  
ATOM   1324  CA  GLY A 335     -17.246 104.975 -66.847  1.00 29.48           C  
ATOM   1325  C   GLY A 335     -18.265 105.585 -67.767  1.00 30.33           C  
ATOM   1326  O   GLY A 335     -18.422 105.124 -68.883  1.00 33.27           O  
ATOM   1327  N   LEU A 336     -18.950 106.630 -67.302  1.00 30.55           N  
ATOM   1328  CA  LEU A 336     -19.966 107.316 -68.103  1.00 29.98           C  
ATOM   1329  C   LEU A 336     -19.299 107.801 -69.376  1.00 30.34           C  
ATOM   1330  O   LEU A 336     -19.747 107.488 -70.486  1.00 28.56           O  
ATOM   1331  CB  LEU A 336     -20.548 108.517 -67.346  1.00 32.97           C  
ATOM   1332  CG  LEU A 336     -21.643 109.289 -68.099  1.00 33.86           C  
ATOM   1333  CD1 LEU A 336     -22.851 108.369 -68.323  1.00 37.77           C  
ATOM   1334  CD2 LEU A 336     -22.039 110.545 -67.321  1.00 36.76           C  
ATOM   1335  N   GLY A 337     -18.231 108.578 -69.198  1.00 28.71           N  
ATOM   1336  CA  GLY A 337     -17.477 109.061 -70.329  1.00 31.35           C  
ATOM   1337  C   GLY A 337     -17.185 107.988 -71.375  1.00 34.54           C  
ATOM   1338  O   GLY A 337     -17.617 108.136 -72.527  1.00 37.69           O  
ATOM   1339  N   VAL A 338     -16.479 106.914 -71.011  1.00 33.92           N  
ATOM   1340  CA  VAL A 338     -16.186 105.844 -71.987  1.00 33.12           C  
ATOM   1341  C   VAL A 338     -17.481 105.308 -72.639  1.00 34.33           C  
ATOM   1342  O   VAL A 338     -17.538 105.071 -73.863  1.00 30.31           O  
ATOM   1343  CB  VAL A 338     -15.401 104.640 -71.340  1.00 30.17           C  
ATOM   1344  CG1 VAL A 338     -15.010 103.655 -72.393  1.00 27.91           C  
ATOM   1345  CG2 VAL A 338     -14.177 105.137 -70.605  1.00 24.89           C  
ATOM   1346  N   VAL A 339     -18.525 105.132 -71.830  1.00 35.92           N  
ATOM   1347  CA  VAL A 339     -19.805 104.657 -72.378  1.00 38.12           C  
ATOM   1348  C   VAL A 339     -20.395 105.698 -73.324  1.00 38.39           C  
ATOM   1349  O   VAL A 339     -21.040 105.359 -74.302  1.00 40.37           O  
ATOM   1350  CB  VAL A 339     -20.863 104.396 -71.283  1.00 37.33           C  
ATOM   1351  CG1 VAL A 339     -22.073 103.703 -71.881  1.00 38.07           C  
ATOM   1352  CG2 VAL A 339     -20.275 103.573 -70.166  1.00 39.52           C  
ATOM   1353  N   MET A 340     -20.184 106.973 -73.042  1.00 40.82           N  
ATOM   1354  CA  MET A 340     -20.744 107.986 -73.923  1.00 44.76           C  
ATOM   1355  C   MET A 340     -19.815 108.409 -75.045  1.00 44.84           C  
ATOM   1356  O   MET A 340     -20.173 109.222 -75.910  1.00 45.50           O  
ATOM   1357  CB  MET A 340     -21.231 109.194 -73.131  1.00 43.73           C  
ATOM   1358  CG  MET A 340     -22.389 108.841 -72.275  1.00 47.96           C  
ATOM   1359  SD  MET A 340     -23.278 110.256 -71.668  1.00 52.18           S  
ATOM   1360  CE  MET A 340     -21.879 111.190 -70.904  1.00 52.67           C  
ATOM   1361  N   TYR A 341     -18.606 107.887 -75.035  1.00 43.49           N  
ATOM   1362  CA  TYR A 341     -17.761 108.207 -76.150  1.00 43.69           C  
ATOM   1363  C   TYR A 341     -18.177 107.170 -77.188  1.00 43.45           C  
ATOM   1364  O   TYR A 341     -18.176 107.451 -78.382  1.00 43.14           O  
ATOM   1365  CB  TYR A 341     -16.292 108.076 -75.787  1.00 42.81           C  
ATOM   1366  CG  TYR A 341     -15.357 108.298 -76.945  1.00 42.62           C  
ATOM   1367  CD1 TYR A 341     -15.388 107.468 -78.071  1.00 43.07           C  
ATOM   1368  CD2 TYR A 341     -14.403 109.298 -76.895  1.00 44.62           C  
ATOM   1369  CE1 TYR A 341     -14.490 107.628 -79.118  1.00 41.27           C  
ATOM   1370  CE2 TYR A 341     -13.486 109.475 -77.939  1.00 42.80           C  
ATOM   1371  CZ  TYR A 341     -13.538 108.641 -79.041  1.00 42.49           C  
ATOM   1372  OH  TYR A 341     -12.652 108.844 -80.063  1.00 40.17           O  
ATOM   1373  N   GLU A 342     -18.608 105.993 -76.729  1.00 44.13           N  
ATOM   1374  CA  GLU A 342     -18.999 104.938 -77.664  1.00 44.80           C  
ATOM   1375  C   GLU A 342     -20.311 105.165 -78.353  1.00 43.75           C  
ATOM   1376  O   GLU A 342     -20.346 105.169 -79.566  1.00 45.55           O  
ATOM   1377  CB  GLU A 342     -19.023 103.555 -77.006  1.00 45.71           C  
ATOM   1378  CG  GLU A 342     -18.486 102.458 -77.930  1.00 49.43           C  
ATOM   1379  CD  GLU A 342     -18.742 101.013 -77.446  1.00 51.76           C  
ATOM   1380  OE1 GLU A 342     -18.360 100.648 -76.303  1.00 53.29           O  
ATOM   1381  OE2 GLU A 342     -19.316 100.232 -78.233  1.00 49.29           O  
ATOM   1382  N   MET A 343     -21.387 105.360 -77.596  1.00 44.37           N  
ATOM   1383  CA  MET A 343     -22.736 105.558 -78.163  1.00 44.21           C  
ATOM   1384  C   MET A 343     -22.830 106.589 -79.277  1.00 45.84           C  
ATOM   1385  O   MET A 343     -23.570 106.379 -80.243  1.00 43.66           O  
ATOM   1386  CB  MET A 343     -23.738 105.975 -77.076  1.00 44.20           C  
ATOM   1387  CG  MET A 343     -24.381 104.877 -76.274  1.00 43.28           C  
ATOM   1388  SD  MET A 343     -25.048 105.637 -74.779  1.00 43.11           S  
ATOM   1389  CE  MET A 343     -26.173 104.315 -74.111  1.00 42.78           C  
ATOM   1390  N   MET A 344     -22.113 107.707 -79.114  1.00 46.96           N  
ATOM   1391  CA  MET A 344     -22.120 108.800 -80.083  1.00 49.57           C  
ATOM   1392  C   MET A 344     -21.060 108.598 -81.186  1.00 53.05           C  
ATOM   1393  O   MET A 344     -21.308 108.906 -82.357  1.00 54.17           O  
ATOM   1394  CB  MET A 344     -21.906 110.152 -79.363  1.00 48.27           C  
ATOM   1395  CG  MET A 344     -23.080 110.600 -78.422  1.00 49.83           C  
ATOM   1396  SD  MET A 344     -22.914 112.225 -77.512  1.00 49.62           S  
ATOM   1397  CE  MET A 344     -21.418 111.976 -76.565  1.00 48.61           C  
ATOM   1398  N   CYS A 345     -19.881 108.085 -80.806  1.00 54.51           N  
ATOM   1399  CA  CYS A 345     -18.792 107.826 -81.745  1.00 51.84           C  
ATOM   1400  C   CYS A 345     -18.930 106.460 -82.434  1.00 52.58           C  
ATOM   1401  O   CYS A 345     -18.421 106.275 -83.532  1.00 52.34           O  
ATOM   1402  CB  CYS A 345     -17.446 107.898 -81.033  1.00 51.59           C  
ATOM   1403  SG  CYS A 345     -16.911 109.518 -80.366  1.00 50.17           S  
ATOM   1404  N   GLY A 346     -19.630 105.519 -81.797  1.00 53.70           N  
ATOM   1405  CA  GLY A 346     -19.823 104.182 -82.359  1.00 54.77           C  
ATOM   1406  C   GLY A 346     -18.639 103.222 -82.176  1.00 56.78           C  
ATOM   1407  O   GLY A 346     -18.619 102.110 -82.711  1.00 56.75           O  
ATOM   1408  N   ARG A 347     -17.648 103.643 -81.400  1.00 57.65           N  
ATOM   1409  CA  ARG A 347     -16.457 102.832 -81.187  1.00 58.72           C  
ATOM   1410  C   ARG A 347     -15.717 103.403 -79.982  1.00 57.80           C  
ATOM   1411  O   ARG A 347     -15.957 104.554 -79.596  1.00 57.03           O  
ATOM   1412  CB  ARG A 347     -15.565 102.910 -82.426  1.00 60.82           C  
ATOM   1413  CG  ARG A 347     -15.306 104.335 -82.851  1.00 63.91           C  
ATOM   1414  CD  ARG A 347     -14.072 104.457 -83.713  1.00 68.47           C  
ATOM   1415  NE  ARG A 347     -13.477 105.793 -83.627  1.00 72.78           N  
ATOM   1416  CZ  ARG A 347     -14.030 106.899 -84.124  1.00 75.44           C  
ATOM   1417  NH1 ARG A 347     -15.201 106.834 -84.751  1.00 73.81           N  
ATOM   1418  NH2 ARG A 347     -13.408 108.075 -84.001  1.00 76.84           N  
ATOM   1419  N   LEU A 348     -14.813 102.616 -79.402  1.00 55.69           N  
ATOM   1420  CA  LEU A 348     -14.080 103.053 -78.224  1.00 54.00           C  
ATOM   1421  C   LEU A 348     -12.971 104.037 -78.586  1.00 56.33           C  
ATOM   1422  O   LEU A 348     -12.520 104.098 -79.719  1.00 57.31           O  
ATOM   1423  CB  LEU A 348     -13.539 101.834 -77.486  1.00 51.86           C  
ATOM   1424  CG  LEU A 348     -14.603 100.859 -76.953  1.00 50.86           C  
ATOM   1425  CD1 LEU A 348     -13.980  99.518 -76.642  1.00 52.57           C  
ATOM   1426  CD2 LEU A 348     -15.253 101.425 -75.707  1.00 52.43           C  
ATOM   1427  N   PRO A 349     -12.517 104.835 -77.625  1.00 57.25           N  
ATOM   1428  CA  PRO A 349     -11.464 105.777 -77.993  1.00 59.36           C  
ATOM   1429  C   PRO A 349     -10.225 105.212 -78.671  1.00 61.01           C  
ATOM   1430  O   PRO A 349      -9.471 105.945 -79.300  1.00 61.78           O  
ATOM   1431  CB  PRO A 349     -11.156 106.502 -76.671  1.00 58.84           C  
ATOM   1432  CG  PRO A 349     -11.694 105.606 -75.620  1.00 59.16           C  
ATOM   1433  CD  PRO A 349     -12.930 105.013 -76.230  1.00 57.94           C  
ATOM   1434  N   PHE A 350     -10.008 103.914 -78.576  1.00 62.84           N  
ATOM   1435  CA  PHE A 350      -8.819 103.351 -79.205  1.00 64.79           C  
ATOM   1436  C   PHE A 350      -9.173 102.076 -79.974  1.00 67.36           C  
ATOM   1437  O   PHE A 350      -8.336 101.197 -80.134  1.00 67.66           O  
ATOM   1438  CB  PHE A 350      -7.768 103.028 -78.130  1.00 61.96           C  
ATOM   1439  CG  PHE A 350      -7.373 104.204 -77.264  1.00 59.60           C  
ATOM   1440  CD1 PHE A 350      -7.537 104.151 -75.880  1.00 59.31           C  
ATOM   1441  CD2 PHE A 350      -6.765 105.331 -77.815  1.00 59.30           C  
ATOM   1442  CE1 PHE A 350      -7.097 105.200 -75.057  1.00 57.97           C  
ATOM   1443  CE2 PHE A 350      -6.319 106.385 -76.998  1.00 56.58           C  
ATOM   1444  CZ  PHE A 350      -6.483 106.316 -75.620  1.00 56.94           C  
ATOM   1445  N   TYR A 351     -10.414 101.990 -80.447  1.00 71.11           N  
ATOM   1446  CA  TYR A 351     -10.928 100.814 -81.162  1.00 74.44           C  
ATOM   1447  C   TYR A 351      -9.991 100.174 -82.187  1.00 76.11           C  
ATOM   1448  O   TYR A 351     -10.102  98.975 -82.470  1.00 76.82           O  
ATOM   1449  CB  TYR A 351     -12.249 101.146 -81.860  1.00 75.96           C  
ATOM   1450  CG  TYR A 351     -12.068 101.741 -83.240  1.00 78.85           C  
ATOM   1451  CD1 TYR A 351     -12.807 101.265 -84.323  1.00 78.88           C  
ATOM   1452  CD2 TYR A 351     -11.154 102.777 -83.467  1.00 78.95           C  
ATOM   1453  CE1 TYR A 351     -12.640 101.804 -85.595  1.00 79.90           C  
ATOM   1454  CE2 TYR A 351     -10.982 103.321 -84.734  1.00 79.28           C  
ATOM   1455  CZ  TYR A 351     -11.727 102.831 -85.787  1.00 79.67           C  
ATOM   1456  OH  TYR A 351     -11.578 103.376 -87.033  1.00 81.04           O  
ATOM   1457  N   ASN A 352      -9.093 100.960 -82.768  1.00 76.78           N  
ATOM   1458  CA  ASN A 352      -8.168 100.394 -83.734  1.00 78.75           C  
ATOM   1459  C   ASN A 352      -6.853  99.971 -83.070  1.00 79.37           C  
ATOM   1460  O   ASN A 352      -6.638  98.783 -82.830  1.00 80.08           O  
ATOM   1461  CB  ASN A 352      -7.914 101.381 -84.874  1.00 79.35           C  
ATOM   1462  CG  ASN A 352      -7.613 102.771 -84.382  1.00 80.14           C  
ATOM   1463  OD1 ASN A 352      -7.431 103.688 -85.173  1.00 79.88           O  
ATOM   1464  ND2 ASN A 352      -7.561 102.939 -83.067  1.00 80.63           N  
ATOM   1465  N   GLN A 353      -5.991 100.932 -82.753  1.00 79.44           N  
ATOM   1466  CA  GLN A 353      -4.704 100.640 -82.124  1.00 79.90           C  
ATOM   1467  C   GLN A 353      -4.640  99.298 -81.401  1.00 80.47           C  
ATOM   1468  O   GLN A 353      -5.395  99.046 -80.468  1.00 80.84           O  
ATOM   1469  CB  GLN A 353      -4.330 101.762 -81.165  1.00 79.35           C  
ATOM   1470  CG  GLN A 353      -4.343 103.105 -81.834  1.00 79.37           C  
ATOM   1471  CD  GLN A 353      -3.603 104.136 -81.040  1.00 81.25           C  
ATOM   1472  OE1 GLN A 353      -2.406 103.992 -80.786  1.00 80.84           O  
ATOM   1473  NE2 GLN A 353      -4.305 105.191 -80.638  1.00 81.42           N  
ATOM   1474  N   ASP A 354      -3.724  98.450 -81.866  1.00 81.80           N  
ATOM   1475  CA  ASP A 354      -3.486  97.104 -81.342  1.00 82.37           C  
ATOM   1476  C   ASP A 354      -4.459  96.681 -80.233  1.00 82.18           C  
ATOM   1477  O   ASP A 354      -5.641  96.437 -80.498  1.00 82.54           O  
ATOM   1478  CB  ASP A 354      -2.036  96.999 -80.852  1.00 83.92           C  
ATOM   1479  CG  ASP A 354      -1.518  95.567 -80.842  1.00 86.18           C  
ATOM   1480  OD1 ASP A 354      -2.119  94.708 -80.151  1.00 88.52           O  
ATOM   1481  OD2 ASP A 354      -0.504  95.302 -81.528  1.00 86.08           O  
ATOM   1482  N   HIS A 355      -3.964  96.586 -79.000  1.00 81.04           N  
ATOM   1483  CA  HIS A 355      -4.799  96.195 -77.879  1.00 79.88           C  
ATOM   1484  C   HIS A 355      -4.057  96.050 -76.560  1.00 78.86           C  
ATOM   1485  O   HIS A 355      -4.595  96.378 -75.504  1.00 78.11           O  
ATOM   1486  CB  HIS A 355      -5.490  94.878 -78.157  1.00 81.82           C  
ATOM   1487  CG  HIS A 355      -6.368  94.442 -77.037  1.00 84.40           C  
ATOM   1488  ND1 HIS A 355      -7.600  95.012 -76.801  1.00 85.89           N  
ATOM   1489  CD2 HIS A 355      -6.152  93.571 -76.023  1.00 85.99           C  
ATOM   1490  CE1 HIS A 355      -8.105  94.512 -75.687  1.00 87.34           C  
ATOM   1491  NE2 HIS A 355      -7.246  93.637 -75.194  1.00 87.56           N  
ATOM   1492  N   GLU A 356      -2.841  95.520 -76.618  1.00 77.90           N  
ATOM   1493  CA  GLU A 356      -2.026  95.338 -75.419  1.00 76.85           C  
ATOM   1494  C   GLU A 356      -1.505  96.714 -75.015  1.00 75.16           C  
ATOM   1495  O   GLU A 356      -0.868  96.877 -73.969  1.00 74.10           O  
ATOM   1496  CB  GLU A 356      -0.847  94.420 -75.722  1.00 79.04           C  
ATOM   1497  CG  GLU A 356      -1.193  93.207 -76.563  1.00 82.14           C  
ATOM   1498  CD  GLU A 356       0.001  92.724 -77.378  1.00 84.91           C  
ATOM   1499  OE1 GLU A 356       0.459  93.483 -78.265  1.00 85.92           O  
ATOM   1500  OE2 GLU A 356       0.489  91.597 -77.132  1.00 86.09           O  
ATOM   1501  N   ARG A 357      -1.793  97.694 -75.873  1.00 72.51           N  
ATOM   1502  CA  ARG A 357      -1.397  99.078 -75.675  1.00 70.56           C  
ATOM   1503  C   ARG A 357      -2.360  99.925 -74.836  1.00 67.74           C  
ATOM   1504  O   ARG A 357      -2.093 101.108 -74.603  1.00 68.30           O  
ATOM   1505  CB  ARG A 357      -1.191  99.739 -77.037  1.00 72.58           C  
ATOM   1506  CG  ARG A 357       0.195  99.502 -77.581  1.00 78.15           C  
ATOM   1507  CD  ARG A 357       0.263  99.418 -79.105  1.00 80.60           C  
ATOM   1508  NE  ARG A 357       1.516  98.766 -79.495  1.00 83.56           N  
ATOM   1509  CZ  ARG A 357       1.806  98.354 -80.724  1.00 84.87           C  
ATOM   1510  NH1 ARG A 357       0.932  98.530 -81.707  1.00 85.98           N  
ATOM   1511  NH2 ARG A 357       2.963  97.747 -80.966  1.00 84.98           N  
ATOM   1512  N   LEU A 358      -3.462  99.338 -74.369  1.00 62.46           N  
ATOM   1513  CA  LEU A 358      -4.426 100.101 -73.573  1.00 58.36           C  
ATOM   1514  C   LEU A 358      -3.847 100.675 -72.302  1.00 56.32           C  
ATOM   1515  O   LEU A 358      -4.130 101.821 -71.971  1.00 56.03           O  
ATOM   1516  CB  LEU A 358      -5.656  99.260 -73.228  1.00 56.41           C  
ATOM   1517  CG  LEU A 358      -6.603  99.058 -74.406  1.00 54.17           C  
ATOM   1518  CD1 LEU A 358      -7.651  98.053 -74.043  1.00 53.18           C  
ATOM   1519  CD2 LEU A 358      -7.227 100.391 -74.799  1.00 54.46           C  
ATOM   1520  N   PHE A 359      -3.034  99.898 -71.588  1.00 53.96           N  
ATOM   1521  CA  PHE A 359      -2.448 100.396 -70.347  1.00 50.86           C  
ATOM   1522  C   PHE A 359      -1.749 101.729 -70.619  1.00 52.65           C  
ATOM   1523  O   PHE A 359      -2.036 102.741 -69.961  1.00 53.12           O  
ATOM   1524  CB  PHE A 359      -1.434  99.407 -69.769  1.00 45.51           C  
ATOM   1525  CG  PHE A 359      -0.904  99.808 -68.422  1.00 40.62           C  
ATOM   1526  CD1 PHE A 359      -1.547  99.405 -67.257  1.00 36.54           C  
ATOM   1527  CD2 PHE A 359       0.207 100.633 -68.319  1.00 38.17           C  
ATOM   1528  CE1 PHE A 359      -1.099  99.815 -66.011  1.00 37.24           C  
ATOM   1529  CE2 PHE A 359       0.670 101.055 -67.069  1.00 38.27           C  
ATOM   1530  CZ  PHE A 359       0.018 100.650 -65.912  1.00 37.22           C  
ATOM   1531  N   GLU A 360      -0.836 101.731 -71.587  1.00 52.33           N  
ATOM   1532  CA  GLU A 360      -0.116 102.952 -71.931  1.00 53.13           C  
ATOM   1533  C   GLU A 360      -1.079 103.993 -72.541  1.00 51.54           C  
ATOM   1534  O   GLU A 360      -0.979 105.186 -72.265  1.00 51.60           O  
ATOM   1535  CB  GLU A 360       1.008 102.670 -72.943  1.00 54.50           C  
ATOM   1536  CG  GLU A 360       1.838 101.412 -72.700  1.00 58.19           C  
ATOM   1537  CD  GLU A 360       1.293 100.190 -73.435  1.00 59.74           C  
ATOM   1538  OE1 GLU A 360       0.748  99.292 -72.760  1.00 62.50           O  
ATOM   1539  OE2 GLU A 360       1.401 100.125 -74.683  1.00 58.87           O  
ATOM   1540  N   LEU A 361      -2.004 103.533 -73.371  1.00 48.70           N  
ATOM   1541  CA  LEU A 361      -2.941 104.430 -74.024  1.00 47.56           C  
ATOM   1542  C   LEU A 361      -3.874 105.190 -73.079  1.00 46.72           C  
ATOM   1543  O   LEU A 361      -3.886 106.423 -73.059  1.00 44.89           O  
ATOM   1544  CB  LEU A 361      -3.773 103.655 -75.044  1.00 47.53           C  
ATOM   1545  CG  LEU A 361      -3.043 103.239 -76.317  1.00 47.61           C  
ATOM   1546  CD1 LEU A 361      -4.047 102.750 -77.322  1.00 47.35           C  
ATOM   1547  CD2 LEU A 361      -2.290 104.440 -76.891  1.00 49.78           C  
ATOM   1548  N   ILE A 362      -4.657 104.443 -72.310  1.00 44.55           N  
ATOM   1549  CA  ILE A 362      -5.590 105.027 -71.368  1.00 43.47           C  
ATOM   1550  C   ILE A 362      -4.899 105.970 -70.406  1.00 43.85           C  
ATOM   1551  O   ILE A 362      -5.489 106.937 -69.945  1.00 44.43           O  
ATOM   1552  CB  ILE A 362      -6.303 103.938 -70.556  1.00 41.24           C  
ATOM   1553  CG1 ILE A 362      -7.096 103.049 -71.500  1.00 40.65           C  
ATOM   1554  CG2 ILE A 362      -7.225 104.568 -69.518  1.00 39.93           C  
ATOM   1555  CD1 ILE A 362      -7.636 101.818 -70.838  1.00 41.11           C  
ATOM   1556  N   LEU A 363      -3.644 105.701 -70.108  1.00 45.52           N  
ATOM   1557  CA  LEU A 363      -2.926 106.538 -69.174  1.00 48.90           C  
ATOM   1558  C   LEU A 363      -2.241 107.743 -69.757  1.00 50.67           C  
ATOM   1559  O   LEU A 363      -2.322 108.813 -69.177  1.00 52.09           O  
ATOM   1560  CB  LEU A 363      -1.884 105.721 -68.432  1.00 48.29           C  
ATOM   1561  CG  LEU A 363      -2.428 104.872 -67.298  1.00 50.05           C  
ATOM   1562  CD1 LEU A 363      -1.435 103.757 -66.994  1.00 47.90           C  
ATOM   1563  CD2 LEU A 363      -2.671 105.750 -66.077  1.00 48.39           C  
ATOM   1564  N   MET A 364      -1.581 107.580 -70.899  1.00 52.13           N  
ATOM   1565  CA  MET A 364      -0.815 108.671 -71.494  1.00 54.39           C  
ATOM   1566  C   MET A 364      -1.159 109.093 -72.910  1.00 54.96           C  
ATOM   1567  O   MET A 364      -0.388 109.797 -73.542  1.00 56.73           O  
ATOM   1568  CB  MET A 364       0.668 108.311 -71.453  1.00 54.41           C  
ATOM   1569  CG  MET A 364       1.154 107.902 -70.088  1.00 56.96           C  
ATOM   1570  SD  MET A 364       2.845 107.242 -70.080  1.00 59.49           S  
ATOM   1571  CE  MET A 364       2.525 105.577 -70.470  1.00 58.17           C  
ATOM   1572  N   GLU A 365      -2.299 108.682 -73.421  1.00 55.69           N  
ATOM   1573  CA  GLU A 365      -2.654 109.048 -74.783  1.00 57.06           C  
ATOM   1574  C   GLU A 365      -3.877 109.980 -74.866  1.00 57.56           C  
ATOM   1575  O   GLU A 365      -4.943 109.652 -74.336  1.00 56.40           O  
ATOM   1576  CB  GLU A 365      -2.927 107.767 -75.574  1.00 58.83           C  
ATOM   1577  CG  GLU A 365      -3.351 107.998 -76.995  1.00 60.72           C  
ATOM   1578  CD  GLU A 365      -2.242 108.579 -77.814  1.00 63.15           C  
ATOM   1579  OE1 GLU A 365      -1.669 109.608 -77.386  1.00 63.66           O  
ATOM   1580  OE2 GLU A 365      -1.940 108.003 -78.882  1.00 65.19           O  
ATOM   1581  N   GLU A 366      -3.740 111.128 -75.531  1.00 58.32           N  
ATOM   1582  CA  GLU A 366      -4.885 112.034 -75.655  1.00 60.19           C  
ATOM   1583  C   GLU A 366      -5.965 111.308 -76.444  1.00 59.03           C  
ATOM   1584  O   GLU A 366      -5.682 110.679 -77.466  1.00 59.44           O  
ATOM   1585  CB  GLU A 366      -4.514 113.327 -76.389  1.00 63.51           C  
ATOM   1586  CG  GLU A 366      -4.218 113.143 -77.890  1.00 68.75           C  
ATOM   1587  CD  GLU A 366      -4.067 114.469 -78.658  1.00 70.31           C  
ATOM   1588  OE1 GLU A 366      -5.100 115.096 -78.995  1.00 71.19           O  
ATOM   1589  OE2 GLU A 366      -2.912 114.880 -78.918  1.00 71.20           O  
ATOM   1590  N   ILE A 367      -7.193 111.382 -75.949  1.00 57.05           N  
ATOM   1591  CA  ILE A 367      -8.326 110.740 -76.594  1.00 57.53           C  
ATOM   1592  C   ILE A 367      -8.866 111.695 -77.656  1.00 59.09           C  
ATOM   1593  O   ILE A 367      -9.357 112.786 -77.346  1.00 60.06           O  
ATOM   1594  CB  ILE A 367      -9.436 110.401 -75.557  1.00 56.79           C  
ATOM   1595  CG1 ILE A 367      -8.989 109.216 -74.691  1.00 56.66           C  
ATOM   1596  CG2 ILE A 367     -10.740 110.094 -76.259  1.00 55.59           C  
ATOM   1597  CD1 ILE A 367     -10.002 108.764 -73.650  1.00 54.59           C  
ATOM   1598  N   ARG A 368      -8.768 111.268 -78.910  1.00 59.38           N  
ATOM   1599  CA  ARG A 368      -9.204 112.053 -80.060  1.00 58.86           C  
ATOM   1600  C   ARG A 368     -10.716 111.927 -80.280  1.00 57.74           C  
ATOM   1601  O   ARG A 368     -11.290 110.876 -80.011  1.00 55.80           O  
ATOM   1602  CB  ARG A 368      -8.402 111.582 -81.290  1.00 60.76           C  
ATOM   1603  CG  ARG A 368      -8.695 112.294 -82.587  1.00 66.47           C  
ATOM   1604  CD  ARG A 368      -7.459 112.359 -83.502  1.00 70.76           C  
ATOM   1605  NE  ARG A 368      -6.505 113.424 -83.147  1.00 73.37           N  
ATOM   1606  CZ  ARG A 368      -6.734 114.740 -83.254  1.00 75.22           C  
ATOM   1607  NH1 ARG A 368      -7.901 115.210 -83.709  1.00 73.92           N  
ATOM   1608  NH2 ARG A 368      -5.779 115.598 -82.912  1.00 76.07           N  
ATOM   1609  N   PHE A 369     -11.349 113.006 -80.761  1.00 57.41           N  
ATOM   1610  CA  PHE A 369     -12.804 113.052 -81.010  1.00 55.72           C  
ATOM   1611  C   PHE A 369     -13.191 113.310 -82.466  1.00 56.10           C  
ATOM   1612  O   PHE A 369     -12.643 114.207 -83.109  1.00 56.30           O  
ATOM   1613  CB  PHE A 369     -13.452 114.164 -80.175  1.00 53.27           C  
ATOM   1614  CG  PHE A 369     -13.170 114.067 -78.723  1.00 48.89           C  
ATOM   1615  CD1 PHE A 369     -13.747 113.070 -77.958  1.00 48.09           C  
ATOM   1616  CD2 PHE A 369     -12.291 114.950 -78.125  1.00 49.39           C  
ATOM   1617  CE1 PHE A 369     -13.444 112.951 -76.620  1.00 48.27           C  
ATOM   1618  CE2 PHE A 369     -11.980 114.839 -76.782  1.00 49.44           C  
ATOM   1619  CZ  PHE A 369     -12.558 113.840 -76.028  1.00 48.72           C  
ATOM   1620  N   PRO A 370     -14.161 112.549 -82.997  1.00 55.70           N  
ATOM   1621  CA  PRO A 370     -14.578 112.758 -84.381  1.00 56.98           C  
ATOM   1622  C   PRO A 370     -14.837 114.252 -84.600  1.00 59.66           C  
ATOM   1623  O   PRO A 370     -15.027 114.996 -83.633  1.00 58.83           O  
ATOM   1624  CB  PRO A 370     -15.851 111.930 -84.479  1.00 55.11           C  
ATOM   1625  CG  PRO A 370     -15.597 110.815 -83.562  1.00 54.54           C  
ATOM   1626  CD  PRO A 370     -14.923 111.456 -82.380  1.00 55.32           C  
ATOM   1627  N   ARG A 371     -14.829 114.694 -85.860  1.00 62.08           N  
ATOM   1628  CA  ARG A 371     -15.067 116.103 -86.166  1.00 63.91           C  
ATOM   1629  C   ARG A 371     -16.585 116.329 -86.113  1.00 63.37           C  
ATOM   1630  O   ARG A 371     -17.051 117.381 -85.713  1.00 63.20           O  
ATOM   1631  CB  ARG A 371     -14.529 116.464 -87.567  1.00 66.97           C  
ATOM   1632  CG  ARG A 371     -13.042 116.127 -87.862  1.00 69.09           C  
ATOM   1633  CD  ARG A 371     -12.645 116.430 -89.354  1.00 71.36           C  
ATOM   1634  NE  ARG A 371     -13.489 115.727 -90.341  1.00 73.99           N  
ATOM   1635  CZ  ARG A 371     -13.244 114.522 -90.870  1.00 74.50           C  
ATOM   1636  NH1 ARG A 371     -12.153 113.835 -90.543  1.00 75.61           N  
ATOM   1637  NH2 ARG A 371     -14.120 113.978 -91.708  1.00 73.83           N  
ATOM   1638  N   THR A 372     -17.340 115.314 -86.505  1.00 63.07           N  
ATOM   1639  CA  THR A 372     -18.796 115.362 -86.517  1.00 64.92           C  
ATOM   1640  C   THR A 372     -19.458 115.402 -85.115  1.00 66.98           C  
ATOM   1641  O   THR A 372     -20.558 114.862 -84.912  1.00 67.46           O  
ATOM   1642  CB  THR A 372     -19.317 114.141 -87.307  1.00 64.89           C  
ATOM   1643  OG1 THR A 372     -20.589 113.722 -86.800  1.00 64.87           O  
ATOM   1644  CG2 THR A 372     -18.316 112.984 -87.205  1.00 66.25           C  
ATOM   1645  N   LEU A 373     -18.812 116.058 -84.151  1.00 67.04           N  
ATOM   1646  CA  LEU A 373     -19.349 116.103 -82.786  1.00 65.44           C  
ATOM   1647  C   LEU A 373     -19.754 117.491 -82.339  1.00 64.29           C  
ATOM   1648  O   LEU A 373     -18.989 118.434 -82.505  1.00 62.57           O  
ATOM   1649  CB  LEU A 373     -18.308 115.549 -81.805  1.00 65.99           C  
ATOM   1650  CG  LEU A 373     -18.834 114.570 -80.754  1.00 65.29           C  
ATOM   1651  CD1 LEU A 373     -19.565 113.431 -81.463  1.00 64.54           C  
ATOM   1652  CD2 LEU A 373     -17.700 114.043 -79.905  1.00 64.31           C  
ATOM   1653  N   SER A 374     -20.948 117.609 -81.760  1.00 64.18           N  
ATOM   1654  CA  SER A 374     -21.437 118.903 -81.281  1.00 64.87           C  
ATOM   1655  C   SER A 374     -20.435 119.443 -80.259  1.00 64.70           C  
ATOM   1656  O   SER A 374     -20.113 118.771 -79.291  1.00 65.79           O  
ATOM   1657  CB  SER A 374     -22.794 118.740 -80.612  1.00 65.06           C  
ATOM   1658  OG  SER A 374     -22.640 118.150 -79.329  1.00 66.28           O  
ATOM   1659  N   PRO A 375     -19.964 120.681 -80.439  1.00 64.59           N  
ATOM   1660  CA  PRO A 375     -18.985 121.271 -79.509  1.00 64.00           C  
ATOM   1661  C   PRO A 375     -19.214 120.995 -78.020  1.00 63.75           C  
ATOM   1662  O   PRO A 375     -18.270 121.022 -77.221  1.00 62.42           O  
ATOM   1663  CB  PRO A 375     -19.020 122.761 -79.863  1.00 64.05           C  
ATOM   1664  CG  PRO A 375     -20.407 122.944 -80.470  1.00 64.81           C  
ATOM   1665  CD  PRO A 375     -20.566 121.710 -81.304  1.00 64.12           C  
ATOM   1666  N   GLU A 376     -20.465 120.730 -77.655  1.00 63.84           N  
ATOM   1667  CA  GLU A 376     -20.807 120.427 -76.268  1.00 63.82           C  
ATOM   1668  C   GLU A 376     -20.451 118.964 -75.950  1.00 62.78           C  
ATOM   1669  O   GLU A 376     -19.781 118.695 -74.932  1.00 62.38           O  
ATOM   1670  CB  GLU A 376     -22.299 120.682 -75.995  1.00 63.11           C  
ATOM   1671  CG  GLU A 376     -23.240 120.197 -77.079  1.00 65.78           C  
ATOM   1672  CD  GLU A 376     -23.425 121.213 -78.208  1.00 67.46           C  
ATOM   1673  OE1 GLU A 376     -22.465 121.962 -78.522  1.00 68.11           O  
ATOM   1674  OE2 GLU A 376     -24.530 121.249 -78.794  1.00 66.07           O  
ATOM   1675  N   ALA A 377     -20.880 118.035 -76.817  1.00 59.79           N  
ATOM   1676  CA  ALA A 377     -20.578 116.611 -76.629  1.00 57.39           C  
ATOM   1677  C   ALA A 377     -19.067 116.435 -76.512  1.00 55.19           C  
ATOM   1678  O   ALA A 377     -18.576 115.721 -75.646  1.00 54.72           O  
ATOM   1679  CB  ALA A 377     -21.120 115.793 -77.786  1.00 56.79           C  
ATOM   1680  N   LYS A 378     -18.332 117.119 -77.374  1.00 54.34           N  
ATOM   1681  CA  LYS A 378     -16.882 117.063 -77.347  1.00 55.31           C  
ATOM   1682  C   LYS A 378     -16.347 117.663 -76.051  1.00 53.62           C  
ATOM   1683  O   LYS A 378     -15.250 117.308 -75.592  1.00 53.98           O  
ATOM   1684  CB  LYS A 378     -16.307 117.800 -78.567  1.00 57.61           C  
ATOM   1685  CG  LYS A 378     -14.766 117.884 -78.630  1.00 61.09           C  
ATOM   1686  CD  LYS A 378     -14.298 118.366 -80.020  1.00 62.65           C  
ATOM   1687  CE  LYS A 378     -12.782 118.471 -80.126  1.00 64.73           C  
ATOM   1688  NZ  LYS A 378     -12.305 118.762 -81.519  1.00 64.97           N  
ATOM   1689  N   SER A 379     -17.125 118.566 -75.457  1.00 52.28           N  
ATOM   1690  CA  SER A 379     -16.728 119.212 -74.198  1.00 49.65           C  
ATOM   1691  C   SER A 379     -16.964 118.221 -73.067  1.00 47.29           C  
ATOM   1692  O   SER A 379     -16.132 118.073 -72.169  1.00 45.72           O  
ATOM   1693  CB  SER A 379     -17.551 120.496 -73.934  1.00 50.37           C  
ATOM   1694  OG  SER A 379     -16.845 121.401 -73.069  1.00 48.80           O  
ATOM   1695  N   LEU A 380     -18.111 117.551 -73.143  1.00 43.52           N  
ATOM   1696  CA  LEU A 380     -18.497 116.564 -72.167  1.00 41.35           C  
ATOM   1697  C   LEU A 380     -17.436 115.429 -72.144  1.00 42.31           C  
ATOM   1698  O   LEU A 380     -16.745 115.192 -71.128  1.00 38.28           O  
ATOM   1699  CB  LEU A 380     -19.878 116.017 -72.526  1.00 37.00           C  
ATOM   1700  CG  LEU A 380     -20.533 115.044 -71.528  1.00 37.81           C  
ATOM   1701  CD1 LEU A 380     -20.838 115.719 -70.185  1.00 35.50           C  
ATOM   1702  CD2 LEU A 380     -21.806 114.513 -72.114  1.00 33.10           C  
ATOM   1703  N   LEU A 381     -17.309 114.736 -73.266  1.00 43.23           N  
ATOM   1704  CA  LEU A 381     -16.356 113.647 -73.349  1.00 44.65           C  
ATOM   1705  C   LEU A 381     -15.011 114.079 -72.834  1.00 44.13           C  
ATOM   1706  O   LEU A 381     -14.420 113.404 -72.008  1.00 45.53           O  
ATOM   1707  CB  LEU A 381     -16.247 113.161 -74.779  1.00 46.30           C  
ATOM   1708  CG  LEU A 381     -17.641 112.708 -75.191  1.00 47.66           C  
ATOM   1709  CD1 LEU A 381     -17.711 112.436 -76.691  1.00 47.23           C  
ATOM   1710  CD2 LEU A 381     -17.980 111.495 -74.381  1.00 46.44           C  
ATOM   1711  N   ALA A 382     -14.519 115.217 -73.285  1.00 44.00           N  
ATOM   1712  CA  ALA A 382     -13.220 115.632 -72.793  1.00 44.46           C  
ATOM   1713  C   ALA A 382     -13.241 115.731 -71.263  1.00 44.54           C  
ATOM   1714  O   ALA A 382     -12.266 115.396 -70.594  1.00 44.94           O  
ATOM   1715  CB  ALA A 382     -12.815 116.967 -73.425  1.00 43.81           C  
ATOM   1716  N   GLY A 383     -14.363 116.183 -70.710  1.00 45.49           N  
ATOM   1717  CA  GLY A 383     -14.465 116.312 -69.263  1.00 44.70           C  
ATOM   1718  C   GLY A 383     -14.568 114.980 -68.527  1.00 43.38           C  
ATOM   1719  O   GLY A 383     -13.926 114.776 -67.501  1.00 41.80           O  
ATOM   1720  N   LEU A 384     -15.384 114.075 -69.050  1.00 41.38           N  
ATOM   1721  CA  LEU A 384     -15.541 112.788 -68.432  1.00 42.70           C  
ATOM   1722  C   LEU A 384     -14.294 111.928 -68.593  1.00 45.30           C  
ATOM   1723  O   LEU A 384     -14.144 110.902 -67.924  1.00 48.49           O  
ATOM   1724  CB  LEU A 384     -16.736 112.078 -69.038  1.00 39.50           C  
ATOM   1725  CG  LEU A 384     -18.061 112.778 -68.723  1.00 39.15           C  
ATOM   1726  CD1 LEU A 384     -19.241 111.945 -69.258  1.00 35.01           C  
ATOM   1727  CD2 LEU A 384     -18.168 112.974 -67.188  1.00 37.62           C  
ATOM   1728  N   LEU A 385     -13.381 112.351 -69.459  1.00 44.32           N  
ATOM   1729  CA  LEU A 385     -12.193 111.565 -69.708  1.00 42.02           C  
ATOM   1730  C   LEU A 385     -10.885 112.173 -69.281  1.00 43.43           C  
ATOM   1731  O   LEU A 385      -9.840 111.689 -69.699  1.00 42.58           O  
ATOM   1732  CB  LEU A 385     -12.124 111.220 -71.171  1.00 39.03           C  
ATOM   1733  CG  LEU A 385     -13.379 110.487 -71.586  1.00 39.73           C  
ATOM   1734  CD1 LEU A 385     -13.433 110.335 -73.108  1.00 40.51           C  
ATOM   1735  CD2 LEU A 385     -13.395 109.163 -70.886  1.00 40.39           C  
ATOM   1736  N   LYS A 386     -10.914 113.224 -68.468  1.00 43.17           N  
ATOM   1737  CA  LYS A 386      -9.661 113.789 -68.005  1.00 46.92           C  
ATOM   1738  C   LYS A 386      -8.954 112.644 -67.258  1.00 48.46           C  
ATOM   1739  O   LYS A 386      -9.555 111.985 -66.418  1.00 47.32           O  
ATOM   1740  CB  LYS A 386      -9.910 114.978 -67.070  1.00 48.50           C  
ATOM   1741  CG  LYS A 386     -10.478 116.202 -67.757  1.00 52.64           C  
ATOM   1742  CD  LYS A 386      -9.449 116.873 -68.663  1.00 54.04           C  
ATOM   1743  CE  LYS A 386      -8.889 118.178 -68.061  1.00 57.54           C  
ATOM   1744  NZ  LYS A 386      -8.176 118.012 -66.747  1.00 57.48           N  
ATOM   1745  N   LYS A 387      -7.686 112.405 -67.575  1.00 49.94           N  
ATOM   1746  CA  LYS A 387      -6.939 111.329 -66.940  1.00 52.56           C  
ATOM   1747  C   LYS A 387      -6.670 111.596 -65.461  1.00 53.98           C  
ATOM   1748  O   LYS A 387      -6.152 110.748 -64.742  1.00 54.18           O  
ATOM   1749  CB  LYS A 387      -5.638 111.096 -67.715  1.00 51.76           C  
ATOM   1750  CG  LYS A 387      -5.908 110.577 -69.121  1.00 51.32           C  
ATOM   1751  CD  LYS A 387      -4.667 110.602 -69.989  1.00 50.36           C  
ATOM   1752  CE  LYS A 387      -4.637 109.426 -70.975  1.00 49.95           C  
ATOM   1753  NZ  LYS A 387      -5.836 109.281 -71.860  1.00 45.83           N  
ATOM   1754  N   ASP A 388      -7.041 112.783 -65.006  1.00 55.48           N  
ATOM   1755  CA  ASP A 388      -6.857 113.155 -63.608  1.00 57.89           C  
ATOM   1756  C   ASP A 388      -8.238 113.098 -62.946  1.00 59.42           C  
ATOM   1757  O   ASP A 388      -9.153 113.822 -63.353  1.00 59.94           O  
ATOM   1758  CB  ASP A 388      -6.310 114.576 -63.523  1.00 57.60           C  
ATOM   1759  CG  ASP A 388      -5.664 114.873 -62.198  1.00 59.14           C  
ATOM   1760  OD1 ASP A 388      -6.186 114.405 -61.164  1.00 60.33           O  
ATOM   1761  OD2 ASP A 388      -4.634 115.588 -62.189  1.00 60.00           O  
ATOM   1762  N   PRO A 389      -8.426 112.229 -61.932  1.00 59.98           N  
ATOM   1763  CA  PRO A 389      -9.776 112.235 -61.348  1.00 59.84           C  
ATOM   1764  C   PRO A 389     -10.104 113.602 -60.746  1.00 59.69           C  
ATOM   1765  O   PRO A 389     -11.205 114.116 -60.914  1.00 59.54           O  
ATOM   1766  CB  PRO A 389      -9.720 111.105 -60.314  1.00 59.39           C  
ATOM   1767  CG  PRO A 389      -8.258 111.024 -59.954  1.00 58.95           C  
ATOM   1768  CD  PRO A 389      -7.562 111.229 -61.278  1.00 59.60           C  
ATOM   1769  N   LYS A 390      -9.122 114.201 -60.083  1.00 60.10           N  
ATOM   1770  CA  LYS A 390      -9.290 115.501 -59.462  1.00 60.09           C  
ATOM   1771  C   LYS A 390      -9.783 116.547 -60.453  1.00 59.61           C  
ATOM   1772  O   LYS A 390     -10.512 117.472 -60.082  1.00 59.81           O  
ATOM   1773  CB  LYS A 390      -7.967 115.944 -58.824  1.00 61.02           C  
ATOM   1774  CG  LYS A 390      -7.835 115.572 -57.343  1.00 63.57           C  
ATOM   1775  CD  LYS A 390      -6.398 115.721 -56.844  1.00 67.32           C  
ATOM   1776  CE  LYS A 390      -6.316 116.072 -55.348  1.00 71.28           C  
ATOM   1777  NZ  LYS A 390      -6.920 115.057 -54.412  1.00 73.28           N  
ATOM   1778  N   GLN A 391      -9.404 116.400 -61.715  1.00 58.79           N  
ATOM   1779  CA  GLN A 391      -9.830 117.358 -62.729  1.00 57.41           C  
ATOM   1780  C   GLN A 391     -10.961 116.851 -63.600  1.00 55.45           C  
ATOM   1781  O   GLN A 391     -11.419 117.562 -64.484  1.00 57.42           O  
ATOM   1782  CB  GLN A 391      -8.670 117.734 -63.641  1.00 59.67           C  
ATOM   1783  CG  GLN A 391      -7.491 118.394 -62.966  1.00 64.85           C  
ATOM   1784  CD  GLN A 391      -6.344 118.587 -63.946  1.00 69.25           C  
ATOM   1785  OE1 GLN A 391      -6.492 119.260 -64.980  1.00 70.69           O  
ATOM   1786  NE2 GLN A 391      -5.193 117.982 -63.639  1.00 71.65           N  
ATOM   1787  N   ARG A 392     -11.426 115.633 -63.367  1.00 52.65           N  
ATOM   1788  CA  ARG A 392     -12.491 115.096 -64.203  1.00 50.36           C  
ATOM   1789  C   ARG A 392     -13.823 115.798 -64.008  1.00 49.33           C  
ATOM   1790  O   ARG A 392     -14.121 116.328 -62.947  1.00 49.23           O  
ATOM   1791  CB  ARG A 392     -12.660 113.599 -63.937  1.00 50.15           C  
ATOM   1792  CG  ARG A 392     -13.469 112.810 -64.973  1.00 48.47           C  
ATOM   1793  CD  ARG A 392     -13.170 111.289 -64.814  1.00 50.39           C  
ATOM   1794  NE  ARG A 392     -11.727 111.045 -64.788  1.00 49.84           N  
ATOM   1795  CZ  ARG A 392     -11.127 110.060 -64.127  1.00 49.59           C  
ATOM   1796  NH1 ARG A 392     -11.850 109.194 -63.431  1.00 50.02           N  
ATOM   1797  NH2 ARG A 392      -9.794 109.980 -64.121  1.00 47.70           N  
ATOM   1798  N   LEU A 393     -14.614 115.811 -65.060  1.00 48.14           N  
ATOM   1799  CA  LEU A 393     -15.924 116.386 -64.989  1.00 48.44           C  
ATOM   1800  C   LEU A 393     -16.630 115.436 -64.012  1.00 51.00           C  
ATOM   1801  O   LEU A 393     -16.912 114.285 -64.354  1.00 52.21           O  
ATOM   1802  CB  LEU A 393     -16.583 116.304 -66.362  1.00 45.45           C  
ATOM   1803  CG  LEU A 393     -17.757 117.184 -66.789  1.00 44.26           C  
ATOM   1804  CD1 LEU A 393     -18.598 116.420 -67.792  1.00 43.83           C  
ATOM   1805  CD2 LEU A 393     -18.593 117.562 -65.617  1.00 46.91           C  
ATOM   1806  N   GLY A 394     -16.903 115.902 -62.796  1.00 51.70           N  
ATOM   1807  CA  GLY A 394     -17.576 115.055 -61.826  1.00 51.15           C  
ATOM   1808  C   GLY A 394     -16.643 114.595 -60.728  1.00 50.56           C  
ATOM   1809  O   GLY A 394     -17.047 113.925 -59.780  1.00 48.85           O  
ATOM   1810  N   GLY A 395     -15.381 114.969 -60.872  1.00 52.02           N  
ATOM   1811  CA  GLY A 395     -14.374 114.592 -59.906  1.00 53.41           C  
ATOM   1812  C   GLY A 395     -14.268 115.729 -58.935  1.00 55.02           C  
ATOM   1813  O   GLY A 395     -13.474 115.705 -57.987  1.00 55.52           O  
ATOM   1814  N   GLY A 396     -15.085 116.741 -59.188  1.00 54.59           N  
ATOM   1815  CA  GLY A 396     -15.101 117.898 -58.320  1.00 54.97           C  
ATOM   1816  C   GLY A 396     -15.861 117.602 -57.042  1.00 55.08           C  
ATOM   1817  O   GLY A 396     -16.788 116.787 -57.038  1.00 52.21           O  
ATOM   1818  N   PRO A 397     -15.495 118.272 -55.940  1.00 55.82           N  
ATOM   1819  CA  PRO A 397     -16.123 118.103 -54.628  1.00 56.36           C  
ATOM   1820  C   PRO A 397     -17.641 118.166 -54.655  1.00 56.21           C  
ATOM   1821  O   PRO A 397     -18.292 117.753 -53.703  1.00 56.71           O  
ATOM   1822  CB  PRO A 397     -15.501 119.228 -53.801  1.00 57.42           C  
ATOM   1823  CG  PRO A 397     -15.187 120.261 -54.817  1.00 57.90           C  
ATOM   1824  CD  PRO A 397     -14.603 119.442 -55.934  1.00 56.21           C  
ATOM   1825  N   SER A 398     -18.188 118.677 -55.755  1.00 56.36           N  
ATOM   1826  CA  SER A 398     -19.627 118.805 -55.955  1.00 55.73           C  
ATOM   1827  C   SER A 398     -20.202 117.557 -56.613  1.00 55.36           C  
ATOM   1828  O   SER A 398     -21.421 117.424 -56.756  1.00 55.62           O  
ATOM   1829  CB  SER A 398     -19.910 120.019 -56.841  1.00 57.36           C  
ATOM   1830  OG  SER A 398     -21.222 119.962 -57.381  1.00 58.59           O  
ATOM   1831  N   ASP A 399     -19.304 116.666 -57.031  1.00 54.03           N  
ATOM   1832  CA  ASP A 399     -19.642 115.409 -57.688  1.00 51.88           C  
ATOM   1833  C   ASP A 399     -20.590 115.605 -58.868  1.00 50.57           C  
ATOM   1834  O   ASP A 399     -20.341 116.429 -59.720  1.00 50.76           O  
ATOM   1835  CB  ASP A 399     -20.239 114.408 -56.681  1.00 51.58           C  
ATOM   1836  CG  ASP A 399     -20.167 112.961 -57.175  1.00 52.42           C  
ATOM   1837  OD1 ASP A 399     -21.224 112.359 -57.451  1.00 51.52           O  
ATOM   1838  OD2 ASP A 399     -19.041 112.421 -57.295  1.00 52.96           O  
ATOM   1839  N   ALA A 400     -21.681 114.852 -58.906  1.00 49.01           N  
ATOM   1840  CA  ALA A 400     -22.631 114.931 -60.001  1.00 49.00           C  
ATOM   1841  C   ALA A 400     -23.067 116.335 -60.443  1.00 50.80           C  
ATOM   1842  O   ALA A 400     -23.289 116.553 -61.625  1.00 51.40           O  
ATOM   1843  CB  ALA A 400     -23.868 114.070 -59.687  1.00 44.05           C  
ATOM   1844  N   LYS A 401     -23.206 117.290 -59.532  1.00 53.20           N  
ATOM   1845  CA  LYS A 401     -23.634 118.619 -59.974  1.00 55.57           C  
ATOM   1846  C   LYS A 401     -22.851 119.057 -61.211  1.00 55.42           C  
ATOM   1847  O   LYS A 401     -23.438 119.391 -62.233  1.00 56.26           O  
ATOM   1848  CB  LYS A 401     -23.497 119.636 -58.838  1.00 56.69           C  
ATOM   1849  CG  LYS A 401     -24.688 119.577 -57.889  1.00 58.53           C  
ATOM   1850  CD  LYS A 401     -24.318 119.955 -56.464  1.00 61.10           C  
ATOM   1851  CE  LYS A 401     -25.286 119.355 -55.445  1.00 59.17           C  
ATOM   1852  NZ  LYS A 401     -24.950 119.774 -54.058  1.00 59.95           N  
ATOM   1853  N   GLU A 402     -21.531 119.018 -61.125  1.00 54.81           N  
ATOM   1854  CA  GLU A 402     -20.693 119.375 -62.250  1.00 55.86           C  
ATOM   1855  C   GLU A 402     -21.155 118.733 -63.556  1.00 55.64           C  
ATOM   1856  O   GLU A 402     -21.109 119.363 -64.603  1.00 58.06           O  
ATOM   1857  CB  GLU A 402     -19.246 118.959 -61.968  1.00 57.92           C  
ATOM   1858  CG  GLU A 402     -18.392 120.067 -61.410  1.00 60.23           C  
ATOM   1859  CD  GLU A 402     -17.300 119.560 -60.502  1.00 63.39           C  
ATOM   1860  OE1 GLU A 402     -16.447 118.777 -60.971  1.00 64.89           O  
ATOM   1861  OE2 GLU A 402     -17.297 119.951 -59.312  1.00 67.47           O  
ATOM   1862  N   VAL A 403     -21.594 117.482 -63.499  1.00 54.73           N  
ATOM   1863  CA  VAL A 403     -22.032 116.770 -64.700  1.00 55.06           C  
ATOM   1864  C   VAL A 403     -23.455 117.115 -65.063  1.00 55.82           C  
ATOM   1865  O   VAL A 403     -23.810 117.172 -66.232  1.00 57.57           O  
ATOM   1866  CB  VAL A 403     -21.892 115.217 -64.530  1.00 53.20           C  
ATOM   1867  CG1 VAL A 403     -22.520 114.482 -65.703  1.00 49.15           C  
ATOM   1868  CG2 VAL A 403     -20.420 114.858 -64.398  1.00 51.05           C  
ATOM   1869  N   MET A 404     -24.283 117.336 -64.061  1.00 56.74           N  
ATOM   1870  CA  MET A 404     -25.662 117.710 -64.322  1.00 57.74           C  
ATOM   1871  C   MET A 404     -25.696 119.117 -64.921  1.00 58.33           C  
ATOM   1872  O   MET A 404     -26.549 119.436 -65.745  1.00 56.57           O  
ATOM   1873  CB  MET A 404     -26.456 117.677 -63.028  1.00 57.30           C  
ATOM   1874  CG  MET A 404     -27.071 116.338 -62.746  1.00 58.76           C  
ATOM   1875  SD  MET A 404     -27.833 116.352 -61.173  1.00 61.03           S  
ATOM   1876  CE  MET A 404     -26.339 116.511 -60.161  1.00 58.78           C  
ATOM   1877  N   GLU A 405     -24.730 119.935 -64.518  1.00 59.37           N  
ATOM   1878  CA  GLU A 405     -24.634 121.308 -64.977  1.00 61.49           C  
ATOM   1879  C   GLU A 405     -23.659 121.578 -66.126  1.00 61.78           C  
ATOM   1880  O   GLU A 405     -23.259 122.734 -66.339  1.00 62.53           O  
ATOM   1881  CB  GLU A 405     -24.262 122.205 -63.807  1.00 63.22           C  
ATOM   1882  CG  GLU A 405     -25.212 122.114 -62.663  1.00 66.91           C  
ATOM   1883  CD  GLU A 405     -24.829 123.062 -61.576  1.00 69.51           C  
ATOM   1884  OE1 GLU A 405     -23.642 123.033 -61.169  1.00 70.57           O  
ATOM   1885  OE2 GLU A 405     -25.708 123.836 -61.134  1.00 72.02           O  
ATOM   1886  N   HIS A 406     -23.262 120.537 -66.858  1.00 59.98           N  
ATOM   1887  CA  HIS A 406     -22.364 120.746 -67.988  1.00 56.43           C  
ATOM   1888  C   HIS A 406     -23.187 121.185 -69.181  1.00 57.21           C  
ATOM   1889  O   HIS A 406     -24.339 120.764 -69.355  1.00 56.09           O  
ATOM   1890  CB  HIS A 406     -21.586 119.475 -68.369  1.00 51.28           C  
ATOM   1891  CG  HIS A 406     -20.810 119.609 -69.645  1.00 46.01           C  
ATOM   1892  ND1 HIS A 406     -21.345 119.294 -70.879  1.00 42.51           N  
ATOM   1893  CD2 HIS A 406     -19.573 120.110 -69.886  1.00 43.31           C  
ATOM   1894  CE1 HIS A 406     -20.472 119.601 -71.824  1.00 42.55           C  
ATOM   1895  NE2 HIS A 406     -19.390 120.099 -71.250  1.00 41.39           N  
ATOM   1896  N   ARG A 407     -22.564 122.028 -69.998  1.00 57.83           N  
ATOM   1897  CA  ARG A 407     -23.167 122.565 -71.205  1.00 58.64           C  
ATOM   1898  C   ARG A 407     -24.010 121.542 -71.976  1.00 56.65           C  
ATOM   1899  O   ARG A 407     -25.114 121.874 -72.432  1.00 56.85           O  
ATOM   1900  CB  ARG A 407     -22.063 123.126 -72.112  1.00 61.22           C  
ATOM   1901  CG  ARG A 407     -22.553 123.584 -73.474  1.00 65.51           C  
ATOM   1902  CD  ARG A 407     -21.392 124.001 -74.366  1.00 70.29           C  
ATOM   1903  NE  ARG A 407     -21.840 124.293 -75.730  1.00 75.25           N  
ATOM   1904  CZ  ARG A 407     -21.165 125.042 -76.602  1.00 78.09           C  
ATOM   1905  NH1 ARG A 407     -19.997 125.589 -76.257  1.00 78.98           N  
ATOM   1906  NH2 ARG A 407     -21.661 125.245 -77.822  1.00 78.61           N  
ATOM   1907  N   PHE A 408     -23.492 120.315 -72.116  1.00 52.96           N  
ATOM   1908  CA  PHE A 408     -24.175 119.246 -72.852  1.00 49.91           C  
ATOM   1909  C   PHE A 408     -25.531 118.877 -72.290  1.00 50.83           C  
ATOM   1910  O   PHE A 408     -26.377 118.361 -73.012  1.00 48.99           O  
ATOM   1911  CB  PHE A 408     -23.315 117.953 -72.912  1.00 49.20           C  
ATOM   1912  CG  PHE A 408     -24.011 116.792 -73.614  1.00 43.54           C  
ATOM   1913  CD1 PHE A 408     -24.103 116.753 -74.996  1.00 43.10           C  
ATOM   1914  CD2 PHE A 408     -24.700 115.834 -72.880  1.00 40.21           C  
ATOM   1915  CE1 PHE A 408     -24.881 115.780 -75.643  1.00 42.87           C  
ATOM   1916  CE2 PHE A 408     -25.483 114.860 -73.509  1.00 39.10           C  
ATOM   1917  CZ  PHE A 408     -25.574 114.834 -74.896  1.00 41.06           C  
ATOM   1918  N   PHE A 409     -25.736 119.142 -71.002  1.00 52.18           N  
ATOM   1919  CA  PHE A 409     -26.978 118.776 -70.338  1.00 54.68           C  
ATOM   1920  C   PHE A 409     -27.939 119.926 -70.009  1.00 57.15           C  
ATOM   1921  O   PHE A 409     -28.336 120.095 -68.846  1.00 56.56           O  
ATOM   1922  CB  PHE A 409     -26.654 118.021 -69.038  1.00 55.18           C  
ATOM   1923  CG  PHE A 409     -26.034 116.651 -69.239  1.00 53.39           C  
ATOM   1924  CD1 PHE A 409     -26.776 115.598 -69.778  1.00 51.92           C  
ATOM   1925  CD2 PHE A 409     -24.736 116.398 -68.810  1.00 52.39           C  
ATOM   1926  CE1 PHE A 409     -26.237 114.318 -69.873  1.00 49.73           C  
ATOM   1927  CE2 PHE A 409     -24.195 115.116 -68.905  1.00 51.29           C  
ATOM   1928  CZ  PHE A 409     -24.955 114.081 -69.437  1.00 48.05           C  
ATOM   1929  N   LEU A 410     -28.327 120.705 -71.018  1.00 58.41           N  
ATOM   1930  CA  LEU A 410     -29.252 121.819 -70.797  1.00 59.27           C  
ATOM   1931  C   LEU A 410     -30.710 121.381 -70.788  1.00 58.75           C  
ATOM   1932  O   LEU A 410     -31.413 121.574 -69.799  1.00 59.28           O  
ATOM   1933  CB  LEU A 410     -29.066 122.887 -71.868  1.00 60.42           C  
ATOM   1934  CG  LEU A 410     -30.276 123.781 -72.119  1.00 61.06           C  
ATOM   1935  CD1 LEU A 410     -29.781 125.191 -72.337  1.00 61.83           C  
ATOM   1936  CD2 LEU A 410     -31.095 123.263 -73.314  1.00 59.43           C  
ATOM   1937  N   SER A 411     -31.149 120.802 -71.898  1.00 57.38           N  
ATOM   1938  CA  SER A 411     -32.512 120.323 -72.058  1.00 57.41           C  
ATOM   1939  C   SER A 411     -32.864 119.277 -71.020  1.00 57.59           C  
ATOM   1940  O   SER A 411     -33.792 118.484 -71.213  1.00 57.88           O  
ATOM   1941  CB  SER A 411     -32.659 119.679 -73.426  1.00 59.49           C  
ATOM   1942  OG  SER A 411     -31.790 118.557 -73.550  1.00 61.22           O  
ATOM   1943  N   ILE A 412     -32.137 119.275 -69.914  1.00 56.76           N  
ATOM   1944  CA  ILE A 412     -32.347 118.256 -68.909  1.00 55.33           C  
ATOM   1945  C   ILE A 412     -33.180 118.611 -67.697  1.00 54.84           C  
ATOM   1946  O   ILE A 412     -32.866 119.527 -66.946  1.00 55.18           O  
ATOM   1947  CB  ILE A 412     -30.965 117.681 -68.469  1.00 54.04           C  
ATOM   1948  CG1 ILE A 412     -30.279 117.039 -69.687  1.00 51.60           C  
ATOM   1949  CG2 ILE A 412     -31.129 116.665 -67.341  1.00 52.51           C  
ATOM   1950  CD1 ILE A 412     -31.207 116.117 -70.531  1.00 45.43           C  
ATOM   1951  N   ASN A 413     -34.256 117.859 -67.516  1.00 55.07           N  
ATOM   1952  CA  ASN A 413     -35.139 118.054 -66.374  1.00 54.68           C  
ATOM   1953  C   ASN A 413     -34.870 116.926 -65.375  1.00 52.50           C  
ATOM   1954  O   ASN A 413     -35.589 115.909 -65.336  1.00 48.90           O  
ATOM   1955  CB  ASN A 413     -36.609 118.029 -66.807  1.00 54.76           C  
ATOM   1956  CG  ASN A 413     -37.497 118.734 -65.807  1.00 55.33           C  
ATOM   1957  OD1 ASN A 413     -38.330 118.116 -65.126  1.00 52.82           O  
ATOM   1958  ND2 ASN A 413     -37.297 120.044 -65.687  1.00 56.40           N  
ATOM   1959  N   TRP A 414     -33.838 117.132 -64.564  1.00 52.53           N  
ATOM   1960  CA  TRP A 414     -33.406 116.132 -63.596  1.00 55.12           C  
ATOM   1961  C   TRP A 414     -34.481 115.516 -62.699  1.00 55.06           C  
ATOM   1962  O   TRP A 414     -34.258 114.480 -62.116  1.00 56.26           O  
ATOM   1963  CB  TRP A 414     -32.261 116.699 -62.759  1.00 57.83           C  
ATOM   1964  CG  TRP A 414     -31.001 116.991 -63.578  1.00 63.28           C  
ATOM   1965  CD1 TRP A 414     -30.348 118.190 -63.671  1.00 65.51           C  
ATOM   1966  CD2 TRP A 414     -30.231 116.061 -64.370  1.00 64.82           C  
ATOM   1967  NE1 TRP A 414     -29.226 118.067 -64.465  1.00 66.83           N  
ATOM   1968  CE2 TRP A 414     -29.129 116.778 -64.904  1.00 65.44           C  
ATOM   1969  CE3 TRP A 414     -30.363 114.705 -64.677  1.00 65.27           C  
ATOM   1970  CZ2 TRP A 414     -28.161 116.172 -65.725  1.00 64.07           C  
ATOM   1971  CZ3 TRP A 414     -29.391 114.105 -65.502  1.00 65.42           C  
ATOM   1972  CH2 TRP A 414     -28.309 114.844 -66.011  1.00 63.57           C  
ATOM   1973  N   GLN A 415     -35.653 116.136 -62.605  1.00 55.66           N  
ATOM   1974  CA  GLN A 415     -36.733 115.608 -61.782  1.00 52.78           C  
ATOM   1975  C   GLN A 415     -37.532 114.650 -62.619  1.00 53.90           C  
ATOM   1976  O   GLN A 415     -38.101 113.698 -62.108  1.00 52.82           O  
ATOM   1977  CB  GLN A 415     -37.658 116.724 -61.304  1.00 52.75           C  
ATOM   1978  CG  GLN A 415     -37.491 117.064 -59.868  1.00 51.69           C  
ATOM   1979  CD  GLN A 415     -38.620 117.895 -59.319  1.00 51.19           C  
ATOM   1980  OE1 GLN A 415     -39.775 117.483 -59.319  1.00 53.33           O  
ATOM   1981  NE2 GLN A 415     -38.286 119.064 -58.821  1.00 50.64           N  
ATOM   1982  N   ASP A 416     -37.585 114.917 -63.916  1.00 55.20           N  
ATOM   1983  CA  ASP A 416     -38.328 114.061 -64.827  1.00 57.32           C  
ATOM   1984  C   ASP A 416     -37.632 112.747 -65.012  1.00 56.39           C  
ATOM   1985  O   ASP A 416     -38.271 111.713 -65.194  1.00 55.69           O  
ATOM   1986  CB  ASP A 416     -38.469 114.714 -66.189  1.00 61.41           C  
ATOM   1987  CG  ASP A 416     -39.587 115.700 -66.232  1.00 63.31           C  
ATOM   1988  OD1 ASP A 416     -40.718 115.322 -65.832  1.00 64.90           O  
ATOM   1989  OD2 ASP A 416     -39.326 116.841 -66.673  1.00 64.16           O  
ATOM   1990  N   VAL A 417     -36.308 112.807 -64.992  1.00 56.31           N  
ATOM   1991  CA  VAL A 417     -35.494 111.611 -65.141  1.00 55.69           C  
ATOM   1992  C   VAL A 417     -35.845 110.580 -64.084  1.00 55.61           C  
ATOM   1993  O   VAL A 417     -36.406 109.539 -64.411  1.00 55.29           O  
ATOM   1994  CB  VAL A 417     -34.027 111.919 -65.001  1.00 54.43           C  
ATOM   1995  CG1 VAL A 417     -33.252 110.664 -65.241  1.00 55.26           C  
ATOM   1996  CG2 VAL A 417     -33.627 113.023 -65.970  1.00 52.68           C  
ATOM   1997  N   VAL A 418     -35.535 110.876 -62.820  1.00 56.12           N  
ATOM   1998  CA  VAL A 418     -35.821 109.929 -61.739  1.00 58.35           C  
ATOM   1999  C   VAL A 418     -37.276 109.530 -61.780  1.00 60.05           C  
ATOM   2000  O   VAL A 418     -37.676 108.486 -61.247  1.00 61.76           O  
ATOM   2001  CB  VAL A 418     -35.553 110.522 -60.343  1.00 56.52           C  
ATOM   2002  CG1 VAL A 418     -34.146 110.989 -60.244  1.00 56.39           C  
ATOM   2003  CG2 VAL A 418     -36.505 111.658 -60.077  1.00 57.43           C  
ATOM   2004  N   GLN A 419     -38.068 110.368 -62.425  1.00 60.09           N  
ATOM   2005  CA  GLN A 419     -39.484 110.117 -62.501  1.00 63.44           C  
ATOM   2006  C   GLN A 419     -39.925 109.210 -63.651  1.00 64.78           C  
ATOM   2007  O   GLN A 419     -41.101 108.862 -63.743  1.00 65.42           O  
ATOM   2008  CB  GLN A 419     -40.211 111.459 -62.562  1.00 64.65           C  
ATOM   2009  CG  GLN A 419     -40.141 112.262 -61.265  1.00 65.43           C  
ATOM   2010  CD  GLN A 419     -40.918 111.616 -60.145  1.00 67.88           C  
ATOM   2011  OE1 GLN A 419     -42.108 111.329 -60.284  1.00 70.62           O  
ATOM   2012  NE2 GLN A 419     -40.254 111.386 -59.021  1.00 69.08           N  
ATOM   2013  N   LYS A 420     -38.986 108.798 -64.502  1.00 66.27           N  
ATOM   2014  CA  LYS A 420     -39.314 107.959 -65.651  1.00 66.15           C  
ATOM   2015  C   LYS A 420     -40.347 108.738 -66.454  1.00 66.54           C  
ATOM   2016  O   LYS A 420     -41.243 108.172 -67.099  1.00 66.17           O  
ATOM   2017  CB  LYS A 420     -39.885 106.610 -65.199  1.00 66.06           C  
ATOM   2018  CG  LYS A 420     -38.854 105.707 -64.557  1.00 66.00           C  
ATOM   2019  CD  LYS A 420     -39.145 104.232 -64.797  1.00 65.06           C  
ATOM   2020  CE  LYS A 420     -37.855 103.439 -64.661  1.00 66.09           C  
ATOM   2021  NZ  LYS A 420     -38.036 101.982 -64.890  1.00 65.07           N  
ATOM   2022  N   LYS A 421     -40.200 110.055 -66.382  1.00 66.97           N  
ATOM   2023  CA  LYS A 421     -41.084 110.993 -67.052  1.00 69.04           C  
ATOM   2024  C   LYS A 421     -40.679 111.199 -68.505  1.00 68.73           C  
ATOM   2025  O   LYS A 421     -41.530 111.117 -69.395  1.00 68.54           O  
ATOM   2026  CB  LYS A 421     -41.093 112.333 -66.302  1.00 70.42           C  
ATOM   2027  CG  LYS A 421     -42.469 112.725 -65.754  1.00 73.45           C  
ATOM   2028  CD  LYS A 421     -43.105 111.599 -64.918  1.00 75.67           C  
ATOM   2029  CE  LYS A 421     -44.591 111.858 -64.618  1.00 76.91           C  
ATOM   2030  NZ  LYS A 421     -44.864 113.113 -63.853  1.00 78.05           N  
ATOM   2031  N   LEU A 422     -39.394 111.465 -68.750  1.00 67.60           N  
ATOM   2032  CA  LEU A 422     -38.923 111.652 -70.122  1.00 65.89           C  
ATOM   2033  C   LEU A 422     -39.505 110.525 -70.959  1.00 64.91           C  
ATOM   2034  O   LEU A 422     -39.916 109.488 -70.428  1.00 63.89           O  
ATOM   2035  CB  LEU A 422     -37.397 111.583 -70.210  1.00 64.36           C  
ATOM   2036  CG  LEU A 422     -36.538 112.611 -69.467  1.00 64.37           C  
ATOM   2037  CD1 LEU A 422     -35.097 112.377 -69.864  1.00 64.00           C  
ATOM   2038  CD2 LEU A 422     -36.942 114.039 -69.801  1.00 63.36           C  
ATOM   2039  N   LEU A 423     -39.579 110.733 -72.263  1.00 64.51           N  
ATOM   2040  CA  LEU A 423     -40.096 109.688 -73.121  1.00 64.84           C  
ATOM   2041  C   LEU A 423     -38.883 108.956 -73.698  1.00 64.99           C  
ATOM   2042  O   LEU A 423     -37.938 109.577 -74.183  1.00 65.32           O  
ATOM   2043  CB  LEU A 423     -40.965 110.266 -74.254  1.00 63.35           C  
ATOM   2044  CG  LEU A 423     -41.521 109.187 -75.209  1.00 63.37           C  
ATOM   2045  CD1 LEU A 423     -42.684 108.433 -74.548  1.00 60.68           C  
ATOM   2046  CD2 LEU A 423     -41.961 109.815 -76.513  1.00 62.27           C  
ATOM   2047  N   PRO A 424     -38.879 107.626 -73.627  1.00 65.32           N  
ATOM   2048  CA  PRO A 424     -37.723 106.922 -74.181  1.00 66.07           C  
ATOM   2049  C   PRO A 424     -37.682 107.168 -75.694  1.00 66.52           C  
ATOM   2050  O   PRO A 424     -38.681 106.942 -76.391  1.00 66.91           O  
ATOM   2051  CB  PRO A 424     -38.013 105.464 -73.824  1.00 65.35           C  
ATOM   2052  CG  PRO A 424     -39.525 105.402 -73.908  1.00 65.69           C  
ATOM   2053  CD  PRO A 424     -39.933 106.682 -73.206  1.00 65.56           C  
ATOM   2054  N   PRO A 425     -36.543 107.668 -76.212  1.00 65.98           N  
ATOM   2055  CA  PRO A 425     -36.367 107.948 -77.643  1.00 65.29           C  
ATOM   2056  C   PRO A 425     -36.461 106.728 -78.556  1.00 65.07           C  
ATOM   2057  O   PRO A 425     -36.675 106.851 -79.760  1.00 65.62           O  
ATOM   2058  CB  PRO A 425     -34.996 108.641 -77.706  1.00 64.63           C  
ATOM   2059  CG  PRO A 425     -34.327 108.260 -76.431  1.00 64.81           C  
ATOM   2060  CD  PRO A 425     -35.442 108.255 -75.431  1.00 65.60           C  
ATOM   2061  N   PHE A 426     -36.294 105.549 -77.984  1.00 65.16           N  
ATOM   2062  CA  PHE A 426     -36.392 104.322 -78.752  1.00 65.68           C  
ATOM   2063  C   PHE A 426     -37.143 103.355 -77.864  1.00 66.49           C  
ATOM   2064  O   PHE A 426     -36.813 103.201 -76.692  1.00 67.68           O  
ATOM   2065  CB  PHE A 426     -35.000 103.789 -79.085  1.00 66.95           C  
ATOM   2066  CG  PHE A 426     -34.976 102.330 -79.402  1.00 66.85           C  
ATOM   2067  CD1 PHE A 426     -35.783 101.811 -80.402  1.00 66.99           C  
ATOM   2068  CD2 PHE A 426     -34.213 101.462 -78.641  1.00 67.00           C  
ATOM   2069  CE1 PHE A 426     -35.840 100.443 -80.632  1.00 67.51           C  
ATOM   2070  CE2 PHE A 426     -34.263 100.096 -78.862  1.00 67.71           C  
ATOM   2071  CZ  PHE A 426     -35.081  99.583 -79.860  1.00 68.22           C  
ATOM   2072  N   LYS A 427     -38.158 102.706 -78.403  1.00 66.64           N  
ATOM   2073  CA  LYS A 427     -38.933 101.802 -77.588  1.00 68.36           C  
ATOM   2074  C   LYS A 427     -38.824 100.355 -77.997  1.00 69.62           C  
ATOM   2075  O   LYS A 427     -39.300  99.971 -79.064  1.00 69.70           O  
ATOM   2076  CB  LYS A 427     -40.401 102.215 -77.609  1.00 69.67           C  
ATOM   2077  CG  LYS A 427     -41.350 101.193 -77.006  1.00 72.41           C  
ATOM   2078  CD  LYS A 427     -42.120 101.795 -75.838  1.00 74.87           C  
ATOM   2079  CE  LYS A 427     -43.040 100.776 -75.170  1.00 75.21           C  
ATOM   2080  NZ  LYS A 427     -43.801 101.410 -74.046  1.00 75.81           N  
ATOM   2081  N   PRO A 428     -38.187  99.526 -77.148  1.00 71.20           N  
ATOM   2082  CA  PRO A 428     -38.008  98.091 -77.395  1.00 71.87           C  
ATOM   2083  C   PRO A 428     -39.351  97.507 -77.798  1.00 73.38           C  
ATOM   2084  O   PRO A 428     -40.396  98.005 -77.383  1.00 73.45           O  
ATOM   2085  CB  PRO A 428     -37.523  97.583 -76.053  1.00 71.28           C  
ATOM   2086  CG  PRO A 428     -36.640  98.716 -75.610  1.00 70.49           C  
ATOM   2087  CD  PRO A 428     -37.468  99.936 -75.928  1.00 70.26           C  
ATOM   2088  N   GLN A 429     -39.322  96.449 -78.593  1.00 74.99           N  
ATOM   2089  CA  GLN A 429     -40.551  95.865 -79.100  1.00 77.95           C  
ATOM   2090  C   GLN A 429     -41.156  94.703 -78.317  1.00 79.45           C  
ATOM   2091  O   GLN A 429     -41.342  93.611 -78.850  1.00 79.84           O  
ATOM   2092  CB  GLN A 429     -40.317  95.497 -80.571  1.00 79.18           C  
ATOM   2093  CG  GLN A 429     -39.747  96.692 -81.355  1.00 80.47           C  
ATOM   2094  CD  GLN A 429     -38.917  96.322 -82.589  1.00 82.62           C  
ATOM   2095  OE1 GLN A 429     -38.118  95.374 -82.572  1.00 82.84           O  
ATOM   2096  NE2 GLN A 429     -39.084  97.098 -83.662  1.00 82.42           N  
ATOM   2097  N   VAL A 430     -41.498  94.955 -77.055  1.00 82.16           N  
ATOM   2098  CA  VAL A 430     -42.097  93.922 -76.206  1.00 85.37           C  
ATOM   2099  C   VAL A 430     -43.519  94.251 -75.722  1.00 87.32           C  
ATOM   2100  O   VAL A 430     -43.827  95.411 -75.408  1.00 87.63           O  
ATOM   2101  CB  VAL A 430     -41.211  93.626 -74.961  1.00 85.20           C  
ATOM   2102  CG1 VAL A 430     -39.913  92.962 -75.395  1.00 85.24           C  
ATOM   2103  CG2 VAL A 430     -40.923  94.908 -74.201  1.00 84.53           C  
ATOM   2104  N   THR A 431     -44.372  93.221 -75.671  1.00 88.78           N  
ATOM   2105  CA  THR A 431     -45.769  93.353 -75.223  1.00 90.01           C  
ATOM   2106  C   THR A 431     -45.789  93.658 -73.726  1.00 90.91           C  
ATOM   2107  O   THR A 431     -46.132  94.764 -73.295  1.00 90.18           O  
ATOM   2108  CB  THR A 431     -46.566  92.037 -75.446  1.00 89.82           C  
ATOM   2109  OG1 THR A 431     -46.459  91.626 -76.814  1.00 89.22           O  
ATOM   2110  CG2 THR A 431     -48.038  92.237 -75.094  1.00 90.31           C  
ATOM   2111  N   SER A 432     -45.419  92.645 -72.946  1.00 92.65           N  
ATOM   2112  CA  SER A 432     -45.351  92.739 -71.491  1.00 94.18           C  
ATOM   2113  C   SER A 432     -43.965  92.270 -71.055  1.00 95.07           C  
ATOM   2114  O   SER A 432     -43.225  91.683 -71.851  1.00 95.53           O  
ATOM   2115  CB  SER A 432     -46.421  91.850 -70.844  1.00 94.16           C  
ATOM   2116  OG  SER A 432     -46.179  90.474 -71.095  1.00 94.36           O  
ATOM   2117  N   GLU A 433     -43.615  92.524 -69.797  1.00 95.64           N  
ATOM   2118  CA  GLU A 433     -42.314  92.119 -69.278  1.00 96.27           C  
ATOM   2119  C   GLU A 433     -42.084  90.610 -69.369  1.00 96.31           C  
ATOM   2120  O   GLU A 433     -40.996  90.119 -69.064  1.00 95.97           O  
ATOM   2121  CB  GLU A 433     -42.152  92.608 -67.836  1.00 96.64           C  
ATOM   2122  CG  GLU A 433     -43.433  92.581 -67.033  1.00 98.59           C  
ATOM   2123  CD  GLU A 433     -43.393  93.526 -65.847  1.00 99.80           C  
ATOM   2124  OE1 GLU A 433     -42.595  93.289 -64.910  1.00100.27           O  
ATOM   2125  OE2 GLU A 433     -44.164  94.513 -65.859  1.00100.38           O  
ATOM   2126  N   VAL A 434     -43.108  89.882 -69.805  1.00 96.24           N  
ATOM   2127  CA  VAL A 434     -43.014  88.436 -69.958  1.00 96.34           C  
ATOM   2128  C   VAL A 434     -42.673  88.111 -71.405  1.00 96.21           C  
ATOM   2129  O   VAL A 434     -42.399  86.960 -71.742  1.00 96.25           O  
ATOM   2130  CB  VAL A 434     -44.341  87.748 -69.603  1.00 96.92           C  
ATOM   2131  CG1 VAL A 434     -44.198  86.239 -69.712  1.00 96.83           C  
ATOM   2132  CG2 VAL A 434     -44.761  88.148 -68.203  1.00 97.24           C  
ATOM   2133  N   ASP A 435     -42.703  89.132 -72.258  0.00 96.61           N  
ATOM   2134  CA  ASP A 435     -42.385  88.963 -73.671  1.00 96.94           C  
ATOM   2135  C   ASP A 435     -40.901  88.600 -73.749  1.00 96.45           C  
ATOM   2136  O   ASP A 435     -40.027  89.463 -73.678  1.00 95.18           O  
ATOM   2137  CB  ASP A 435     -42.677  90.264 -74.434  1.00 97.77           C  
ATOM   2138  CG  ASP A 435     -42.591  90.090 -75.940  1.00 98.40           C  
ATOM   2139  OD1 ASP A 435     -43.270  89.187 -76.471  1.00 98.84           O  
ATOM   2140  OD2 ASP A 435     -41.849  90.858 -76.594  1.00 98.42           O  
ATOM   2141  N   THR A 436     -40.628  87.310 -73.898  1.00 96.53           N  
ATOM   2142  CA  THR A 436     -39.259  86.817 -73.935  1.00 97.07           C  
ATOM   2143  C   THR A 436     -38.584  86.764 -75.299  1.00 97.53           C  
ATOM   2144  O   THR A 436     -37.995  85.739 -75.650  1.00 98.13           O  
ATOM   2145  CB  THR A 436     -39.177  85.398 -73.327  1.00 96.65           C  
ATOM   2146  OG1 THR A 436     -39.806  84.458 -74.208  1.00 96.30           O  
ATOM   2147  CG2 THR A 436     -39.869  85.360 -71.979  1.00 95.96           C  
ATOM   2148  N   ARG A 437     -38.637  87.844 -76.072  1.00 97.87           N  
ATOM   2149  CA  ARG A 437     -37.990  87.788 -77.376  1.00 98.52           C  
ATOM   2150  C   ARG A 437     -36.546  88.239 -77.343  1.00 98.34           C  
ATOM   2151  O   ARG A 437     -35.704  87.652 -78.019  1.00 98.68           O  
ATOM   2152  CB  ARG A 437     -38.763  88.587 -78.429  1.00 99.37           C  
ATOM   2153  CG  ARG A 437     -38.677  90.098 -78.355  1.00 99.93           C  
ATOM   2154  CD  ARG A 437     -39.574  90.642 -79.444  1.00101.00           C  
ATOM   2155  NE  ARG A 437     -40.849  89.921 -79.422  1.00102.41           N  
ATOM   2156  CZ  ARG A 437     -41.742  89.912 -80.409  1.00102.52           C  
ATOM   2157  NH1 ARG A 437     -41.514  90.593 -81.525  1.00102.58           N  
ATOM   2158  NH2 ARG A 437     -42.861  89.207 -80.283  1.00101.95           N  
ATOM   2159  N   TYR A 438     -36.246  89.265 -76.557  1.00 98.15           N  
ATOM   2160  CA  TYR A 438     -34.871  89.738 -76.477  1.00 98.27           C  
ATOM   2161  C   TYR A 438     -33.987  88.776 -75.695  1.00 98.30           C  
ATOM   2162  O   TYR A 438     -32.919  89.164 -75.221  1.00 98.50           O  
ATOM   2163  CB  TYR A 438     -34.802  91.122 -75.831  1.00 98.13           C  
ATOM   2164  CG  TYR A 438     -35.278  92.236 -76.727  1.00 98.18           C  
ATOM   2165  CD1 TYR A 438     -36.610  92.645 -76.719  1.00 97.72           C  
ATOM   2166  CD2 TYR A 438     -34.398  92.865 -77.611  1.00 98.25           C  
ATOM   2167  CE1 TYR A 438     -37.055  93.650 -77.567  1.00 97.99           C  
ATOM   2168  CE2 TYR A 438     -34.831  93.869 -78.466  1.00 97.77           C  
ATOM   2169  CZ  TYR A 438     -36.160  94.255 -78.440  1.00 98.02           C  
ATOM   2170  OH  TYR A 438     -36.599  95.234 -79.300  1.00 99.32           O  
ATOM   2171  N   PHE A 439     -34.426  87.524 -75.569  1.00 98.21           N  
ATOM   2172  CA  PHE A 439     -33.662  86.522 -74.830  1.00 98.42           C  
ATOM   2173  C   PHE A 439     -32.857  85.571 -75.717  1.00 99.07           C  
ATOM   2174  O   PHE A 439     -32.461  84.495 -75.279  1.00 99.20           O  
ATOM   2175  CB  PHE A 439     -34.596  85.725 -73.910  1.00 97.33           C  
ATOM   2176  CG  PHE A 439     -35.216  86.547 -72.796  1.00 96.66           C  
ATOM   2177  CD1 PHE A 439     -36.189  85.994 -71.967  1.00 96.49           C  
ATOM   2178  CD2 PHE A 439     -34.833  87.868 -72.577  1.00 96.74           C  
ATOM   2179  CE1 PHE A 439     -36.773  86.739 -70.943  1.00 96.09           C  
ATOM   2180  CE2 PHE A 439     -35.411  88.620 -71.557  1.00 95.87           C  
ATOM   2181  CZ  PHE A 439     -36.382  88.052 -70.739  1.00 96.20           C  
ATOM   2182  N   ASP A 440     -32.615  85.975 -76.961  1.00100.26           N  
ATOM   2183  CA  ASP A 440     -31.832  85.177 -77.902  1.00101.51           C  
ATOM   2184  C   ASP A 440     -30.650  86.010 -78.415  1.00102.88           C  
ATOM   2185  O   ASP A 440     -29.738  86.315 -77.644  1.00103.71           O  
ATOM   2186  CB  ASP A 440     -32.709  84.713 -79.066  1.00101.66           C  
ATOM   2187  CG  ASP A 440     -33.772  83.719 -78.633  1.00101.78           C  
ATOM   2188  OD1 ASP A 440     -34.618  84.083 -77.791  1.00102.15           O  
ATOM   2189  OD2 ASP A 440     -33.761  82.574 -79.133  1.00101.98           O  
ATOM   2190  N   ASP A 441     -30.654  86.381 -79.698  1.00103.80           N  
ATOM   2191  CA  ASP A 441     -29.563  87.193 -80.259  1.00104.60           C  
ATOM   2192  C   ASP A 441     -30.034  88.355 -81.129  1.00104.56           C  
ATOM   2193  O   ASP A 441     -29.458  88.538 -82.226  1.00103.86           O  
ATOM   2194  CB  ASP A 441     -28.606  86.330 -81.085  1.00105.83           C  
ATOM   2195  CG  ASP A 441     -27.486  85.745 -80.257  1.00107.22           C  
ATOM   2196  OD1 ASP A 441     -27.749  84.815 -79.459  1.00107.63           O  
ATOM   2197  OD2 ASP A 441     -26.339  86.227 -80.405  1.00107.62           O  
ATOM   2198  N   GLU A 442     -30.956  89.080 -80.694  1.00104.68           N  
TER    2199      GLU A 442                                                      
HETATM 2200  O   HOH A2001     -32.998  79.952 -48.805  1.00 76.16           O  
HETATM 2201  O   HOH A2002     -39.546  70.684 -59.662  1.00 62.00           O  
HETATM 2202  O   HOH A2003     -27.673  75.363 -70.379  1.00 74.90           O  
HETATM 2203  O   HOH A2004     -35.923  76.665 -73.082  1.00 88.71           O  
HETATM 2204  O   HOH A2005     -14.153  87.119 -63.758  1.00 68.92           O  
HETATM 2205  O   HOH A2006     -22.630  77.355 -64.914  1.00 52.30           O  
HETATM 2206  O   HOH A2007     -29.683  79.225 -62.379  1.00 58.32           O  
HETATM 2207  O   HOH A2008     -35.655  83.715 -66.690  1.00 90.58           O  
HETATM 2208  O   HOH A2009     -44.272  80.569 -64.137  1.00 86.53           O  
HETATM 2209  O   HOH A2010     -42.018  80.510 -57.537  1.00 70.82           O  
HETATM 2210  O   HOH A2011     -42.986  86.709 -66.627  1.00 99.55           O  
HETATM 2211  O   HOH A2012     -40.479  91.734 -58.440  1.00 68.86           O  
HETATM 2212  O   HOH A2013     -25.520  91.421 -58.993  1.00 82.84           O  
HETATM 2213  O   HOH A2014     -24.005  90.870 -56.466  1.00 63.76           O  
HETATM 2214  O   HOH A2015     -21.137  80.560 -57.614  1.00 95.39           O  
HETATM 2215  O   HOH A2016     -22.720  80.213 -59.846  1.00128.56           O  
HETATM 2216  O   HOH A2017     -19.445  77.703 -62.696  1.00 92.42           O  
HETATM 2217  O   HOH A2018     -17.795  75.194 -56.614  1.00103.16           O  
HETATM 2218  O   HOH A2019     -21.152  78.015 -44.545  1.00 61.57           O  
HETATM 2219  O   HOH A2020     -10.718  83.937 -50.781  1.00 55.27           O  
HETATM 2220  O   HOH A2021     -15.987  93.183 -52.324  1.00 54.50           O  
HETATM 2221  O   HOH A2022     -16.620  90.320 -50.785  1.00 64.20           O  
HETATM 2222  O   HOH A2023     -20.303  89.918 -51.002  1.00 62.57           O  
HETATM 2223  O   HOH A2024     -22.650  98.270 -55.329  1.00 64.79           O  
HETATM 2224  O   HOH A2025     -27.445  92.326 -55.432  1.00104.04           O  
HETATM 2225  O   HOH A2026     -23.554  92.371 -47.328  1.00101.95           O  
HETATM 2226  O   HOH A2027     -25.348 100.591 -49.849  1.00 81.82           O  
HETATM 2227  O   HOH A2028     -24.964  98.917 -55.078  1.00 54.20           O  
HETATM 2228  O   HOH A2029     -36.169  94.852 -53.914  1.00 50.98           O  
HETATM 2229  O   HOH A2030     -39.901  97.291 -52.193  1.00 58.68           O  
HETATM 2230  O   HOH A2031     -33.579  99.455 -57.461  1.00121.46           O  
HETATM 2231  O   HOH A2032     -37.065 102.989 -56.757  1.00 52.46           O  
HETATM 2232  O   HOH A2033     -35.384 101.526 -65.535  1.00 72.78           O  
HETATM 2233  O   HOH A2034     -37.048  73.242 -74.272  1.00 49.20           O  
HETATM 2234  O   HOH A2035     -30.948  81.763 -46.481  1.00 62.63           O  
HETATM 2235  O   HOH A2036     -47.843  80.379 -64.135  1.00 58.61           O  
HETATM 2236  O   HOH A2037     -25.401  74.677 -52.567  1.00 97.51           O  
HETATM 2237  O   HOH A2038     -22.101  73.825 -55.182  1.00106.95           O  
HETATM 2238  O   HOH A2039     -20.905  75.083 -60.333  1.00 89.91           O  
HETATM 2239  O   HOH A2040     -19.609  72.745 -59.575  1.00 55.25           O  
HETATM 2240  O   HOH A2041     -14.469  88.506 -51.433  1.00 67.61           O  
HETATM 2241  O   HOH A2042     -15.575  95.883 -51.472  1.00 91.20           O  
HETATM 2242  O   HOH A2043     -31.040  90.727 -62.161  1.00125.41           O  
HETATM 2243  O   HOH A2044     -25.218  92.131 -45.479  1.00 63.63           O  
HETATM 2244  O   HOH A2045     -38.922 101.691 -58.270  1.00 98.47           O  
HETATM 2245  O   HOH A2046     -39.602  93.998 -67.457  1.00 72.71           O  
HETATM 2246  O   HOH A2047     -37.558  90.883 -73.852  1.00 54.88           O  
HETATM 2247  O   HOH A2048     -33.478  91.675 -72.540  1.00 43.41           O  
HETATM 2248  O   HOH A2049     -31.445  90.794 -73.675  1.00 74.46           O  
HETATM 2249  O   HOH A2050     -30.338  92.585 -76.714  1.00108.80           O  
HETATM 2250  O   HOH A2051     -33.763  81.288 -44.581  1.00 65.49           O  
HETATM 2251  O   HOH A2052     -33.181  83.277 -46.966  1.00 72.28           O  
HETATM 2252  O   HOH A2053     -48.990  77.329 -65.285  1.00 61.03           O  
HETATM 2253  O   HOH A2054     -25.751  91.368 -78.478  1.00 54.26           O  
HETATM 2254  O   HOH A2055     -32.001  99.414 -81.548  1.00 73.97           O  
HETATM 2255  O   HOH A2056     -22.575  92.336 -43.441  1.00 60.57           O  
HETATM 2256  O   HOH A2057     -29.294  92.995 -85.979  1.00 61.05           O  
HETATM 2257  O   HOH A2058     -31.320  98.646 -84.985  1.00101.64           O  
HETATM 2258  O   HOH A2059     -27.415  89.929 -85.543  1.00 53.22           O  
HETATM 2259  O   HOH A2060     -32.691 113.570 -83.528  1.00 92.08           O  
HETATM 2260  O   HOH A2061     -18.241 102.306 -89.316  1.00 97.53           O  
HETATM 2261  O   HOH A2062     -18.353  98.010 -88.985  1.00103.96           O  
HETATM 2262  O   HOH A2063     -31.966 115.257 -81.634  1.00 94.92           O  
HETATM 2263  O   HOH A2064     -20.353 112.035 -73.437  1.00109.06           O  
HETATM 2264  O   HOH A2065     -24.036 113.009 -71.653  1.00113.71           O  
HETATM 2265  O   HOH A2066     -22.769 112.806 -73.840  1.00 60.56           O  
HETATM 2266  O   HOH A2067     -23.711 110.440 -82.309  1.00 50.49           O  
HETATM 2267  O   HOH A2068     -31.683 109.565 -81.647  1.00 69.95           O  
HETATM 2268  O   HOH A2069     -27.144 117.541 -79.370  1.00 36.80           O  
HETATM 2269  O   HOH A2070     -41.024  98.946 -60.461  1.00 54.29           O  
HETATM 2270  O   HOH A2071     -31.483 113.973 -74.194  1.00 36.93           O  
HETATM 2271  O   HOH A2072     -28.598 115.945 -80.483  1.00 89.89           O  
HETATM 2272  O   HOH A2073     -29.677 116.091 -74.250  1.00110.71           O  
HETATM 2273  O   HOH A2074     -28.158 117.033 -76.907  1.00 48.96           O  
HETATM 2274  O   HOH A2075     -32.439 111.015 -77.093  1.00 93.38           O  
HETATM 2275  O   HOH A2076     -30.995 107.519 -76.234  1.00 47.87           O  
HETATM 2276  O   HOH A2077     -33.403 106.130 -77.985  1.00 76.96           O  
HETATM 2277  O   HOH A2078     -30.372 106.961 -82.277  1.00 68.26           O  
HETATM 2278  O   HOH A2079     -17.802 111.367 -50.596  1.00 64.41           O  
HETATM 2279  O   HOH A2080     -24.764 110.454 -73.650  1.00 59.25           O  
HETATM 2280  O   HOH A2081     -16.496  98.729 -51.917  1.00 66.35           O  
HETATM 2281  O   HOH A2082     -28.737 113.816 -70.544  1.00 88.84           O  
HETATM 2282  O   HOH A2083     -32.794 111.024 -68.824  1.00106.84           O  
HETATM 2283  O   HOH A2084     -31.159 112.205 -64.750  1.00 94.45           O  
HETATM 2284  O   HOH A2085     -36.523 109.555 -67.648  1.00 61.46           O  
HETATM 2285  O   HOH A2086     -31.424 106.525 -70.271  1.00144.97           O  
HETATM 2286  O   HOH A2087     -27.755 103.470 -66.606  1.00110.07           O  
HETATM 2287  O   HOH A2088     -24.452 109.908 -62.339  1.00 80.35           O  
HETATM 2288  O   HOH A2089     -39.218 100.823 -60.421  1.00 65.73           O  
HETATM 2289  O   HOH A2090     -18.711  90.537 -62.683  1.00 54.07           O  
HETATM 2290  O   HOH A2091     -20.407  90.237 -73.881  1.00 44.39           O  
HETATM 2291  O   HOH A2092     -17.729  89.087 -73.164  1.00 60.56           O  
HETATM 2292  O   HOH A2093     -19.809  86.420 -75.382  1.00 58.24           O  
HETATM 2293  O   HOH A2094     -24.229 112.256 -55.630  1.00 40.75           O  
HETATM 2294  O   HOH A2095     -25.598 115.479 -56.345  1.00 56.24           O  
HETATM 2295  O   HOH A2096     -26.852 118.188 -57.257  1.00 48.29           O  
HETATM 2296  O   HOH A2097     -29.253 116.342 -55.395  1.00 57.15           O  
HETATM 2297  O   HOH A2098     -31.140 114.548 -56.339  1.00 52.48           O  
HETATM 2298  O   HOH A2099     -31.274 103.379 -51.826  1.00125.90           O  
HETATM 2299  O   HOH A2100     -27.617 104.616 -54.961  1.00109.88           O  
HETATM 2300  O   HOH A2101     -19.973 111.319 -52.542  1.00 47.41           O  
HETATM 2301  O   HOH A2102     -26.743 109.839 -47.135  1.00 54.88           O  
HETATM 2302  O   HOH A2103     -20.513  90.392 -76.531  1.00 60.27           O  
HETATM 2303  O   HOH A2104     -12.883 122.829 -51.350  1.00 50.61           O  
HETATM 2304  O   HOH A2105     -13.865 127.291 -55.664  1.00 66.28           O  
HETATM 2305  O   HOH A2106     -17.189 106.753 -51.920  1.00 44.65           O  
HETATM 2306  O   HOH A2107      -4.045 107.148 -49.946  1.00 57.00           O  
HETATM 2307  O   HOH A2108     -17.619 102.102 -52.493  1.00 42.74           O  
HETATM 2308  O   HOH A2109     -13.742  93.007 -62.576  1.00 53.36           O  
HETATM 2309  O   HOH A2110     -23.554  97.041 -63.102  1.00 54.35           O  
HETATM 2310  O   HOH A2111     -14.287  99.143 -64.847  1.00 84.45           O  
HETATM 2311  O   HOH A2112     -15.616  96.600 -54.071  1.00 70.20           O  
HETATM 2312  O   HOH A2113     -22.668 100.024 -66.101  1.00158.74           O  
HETATM 2313  O   HOH A2114     -18.430  94.208 -65.102  1.00 92.53           O  
HETATM 2314  O   HOH A2115     -16.280 101.239 -66.115  1.00 50.22           O  
HETATM 2315  O   HOH A2116     -18.647  93.038 -70.008  1.00 60.38           O  
HETATM 2316  O   HOH A2117     -25.175  95.708 -73.068  1.00 50.82           O  
HETATM 2317  O   HOH A2118     -17.714 100.955 -71.187  1.00 60.60           O  
HETATM 2318  O   HOH A2119     -20.005 112.200 -78.821  1.00108.96           O  
HETATM 2319  O   HOH A2120     -25.697  92.664 -68.885  1.00 66.52           O  
HETATM 2320  O   HOH A2121     -17.643  98.286 -74.324  1.00 44.85           O  
HETATM 2321  O   HOH A2122     -23.296  93.673 -73.044  1.00 85.66           O  
HETATM 2322  O   HOH A2123     -16.148  98.312 -71.887  1.00 82.40           O  
HETATM 2323  O   HOH A2124      -8.330 108.845 -85.172  1.00 59.98           O  
HETATM 2324  O   HOH A2125     -37.843  98.707 -65.463  1.00 76.97           O  
HETATM 2325  O   HOH A2126     -40.075 101.931 -67.249  1.00 51.58           O  
HETATM 2326  O   HOH A2127     -39.901  98.826 -74.968  1.00105.36           O  
HETATM 2327  O   HOH A2128      -7.874 116.642 -87.594  1.00 63.41           O  
HETATM 2328  O   HOH A2129      -3.867 118.046 -85.348  1.00 76.18           O  
HETATM 2329  O   HOH A2130      -5.754 114.545 -88.180  1.00 44.59           O  
HETATM 2330  O   HOH A2131     -34.795 103.669 -75.122  1.00 70.42           O  
HETATM 2331  O   HOH A2132     -33.508 104.329 -71.475  1.00128.68           O  
HETATM 2332  O   HOH A2133     -36.075 105.384 -71.283  1.00109.44           O  
HETATM 2333  O   HOH A2134     -36.651 100.017 -59.561  1.00 78.58           O  
HETATM 2334  O   HOH A2135     -29.848  91.790 -64.074  1.00 51.72           O  
HETATM 2335  O   HOH A2136     -24.361  88.949 -61.408  1.00 94.27           O  
HETATM 2336  O   HOH A2137      -7.205 111.603 -56.621  1.00 51.71           O  
HETATM 2337  O   HOH A2138     -20.564  93.070 -63.487  1.00 54.49           O  
HETATM 2338  O   HOH A2139     -23.230  88.728 -66.431  1.00108.34           O  
HETATM 2339  O   HOH A2140     -19.609  88.765 -71.863  1.00 61.68           O  
HETATM 2340  O   HOH A2141     -20.768  90.813 -71.552  1.00 61.54           O  
HETATM 2341  O   HOH A2142     -18.744  92.097 -73.138  1.00 55.57           O  
HETATM 2342  O   HOH A2143     -13.081  90.301 -74.716  1.00 78.92           O  
HETATM 2343  O   HOH A2144     -17.722  92.098 -76.941  1.00 75.54           O  
HETATM 2344  O   HOH A2145     -12.611  91.681 -79.605  1.00 53.00           O  
HETATM 2345  O   HOH A2146     -16.221 123.986 -53.826  1.00 62.43           O  
HETATM 2346  O   HOH A2147     -14.629  98.513 -69.834  1.00 47.85           O  
HETATM 2347  O   HOH A2148     -26.931 126.107 -71.665  1.00 61.35           O  
HETATM 2348  O   HOH A2149     -12.751 101.404 -63.852  1.00 55.63           O  
HETATM 2349  O   HOH A2150     -10.847 108.163 -58.161  1.00 53.94           O  
HETATM 2350  O   HOH A2151     -39.670 103.275 -60.596  1.00 76.55           O  
HETATM 2351  O   HOH A2152       2.634 106.999 -59.689  1.00 44.06           O  
HETATM 2352  O   HOH A2153      -2.582 111.252 -61.347  1.00 63.04           O  
HETATM 2353  O   HOH A2154      -3.814 105.699 -53.606  1.00 57.67           O  
HETATM 2354  O   HOH A2155     -40.568  92.296 -86.674  1.00 64.00           O  
HETATM 2355  O   HOH A2156     -45.257 100.264 -64.437  1.00 65.97           O  
HETATM 2356  O   HOH A2157      -5.538 108.115 -57.303  1.00 60.15           O  
HETATM 2357  O   HOH A2158     -13.492  97.626 -62.513  1.00 73.20           O  
HETATM 2358  O   HOH A2159     -10.813  93.308 -60.006  1.00 71.94           O  
HETATM 2359  O   HOH A2160     -13.531 110.225 -57.101  1.00 45.59           O  
HETATM 2360  O   HOH A2161     -15.157 102.558 -64.601  1.00 27.34           O  
HETATM 2361  O   HOH A2162     -22.061 106.390 -65.510  1.00139.64           O  
HETATM 2362  O   HOH A2163     -17.616 103.074 -63.099  1.00 36.41           O  
HETATM 2363  O   HOH A2164     -17.903 106.223 -57.233  1.00111.09           O  
HETATM 2364  O   HOH A2165     -15.022 108.281 -72.715  1.00100.06           O  
HETATM 2365  O   HOH A2166     -17.343 102.484 -73.188  1.00 78.72           O  
HETATM 2366  O   HOH A2167     -23.310 107.488 -74.515  1.00107.83           O  
HETATM 2367  O   HOH A2168     -23.146 103.334 -74.388  1.00 84.60           O  
HETATM 2368  O   HOH A2169     -21.707 107.688 -76.681  1.00 78.48           O  
HETATM 2369  O   HOH A2170     -21.294  97.870 -79.101  1.00 57.10           O  
HETATM 2370  O   HOH A2171     -21.117 101.845 -76.666  1.00131.24           O  
HETATM 2371  O   HOH A2172     -19.294 101.248 -73.895  1.00114.15           O  
HETATM 2372  O   HOH A2173     -19.262 110.559 -81.294  1.00 93.16           O  
HETATM 2373  O   HOH A2174     -11.966 110.289 -86.531  1.00 56.62           O  
HETATM 2374  O   HOH A2175      -1.136 105.962 -80.208  1.00 93.87           O  
HETATM 2375  O   HOH A2176      -3.482  98.885 -78.668  1.00107.31           O  
HETATM 2376  O   HOH A2177      -9.140  95.619 -78.673  1.00 57.35           O  
HETATM 2377  O   HOH A2178      -4.263  95.763 -72.959  1.00 62.19           O  
HETATM 2378  O   HOH A2179      -0.557  94.041 -72.839  1.00 70.96           O  
HETATM 2379  O   HOH A2180       3.000 100.831 -76.613  1.00 70.98           O  
HETATM 2380  O   HOH A2181      -6.831 109.056 -79.337  1.00 55.03           O  
HETATM 2381  O   HOH A2182      -8.406 116.226 -81.494  1.00102.26           O  
HETATM 2382  O   HOH A2183      -7.502 112.874 -86.551  1.00 88.21           O  
HETATM 2383  O   HOH A2184      -6.750 117.327 -84.625  1.00 53.80           O  
HETATM 2384  O   HOH A2185      -6.064 113.190 -80.641  1.00 82.97           O  
HETATM 2385  O   HOH A2186     -10.475 113.309 -84.373  1.00 73.88           O  
HETATM 2386  O   HOH A2187     -10.815 115.537 -81.525  1.00 77.73           O  
HETATM 2387  O   HOH A2188     -15.950 117.562 -82.262  1.00 81.14           O  
HETATM 2388  O   HOH A2189     -15.464 112.410 -79.938  1.00101.36           O  
HETATM 2389  O   HOH A2190     -14.498 111.272 -91.417  1.00 99.65           O  
HETATM 2390  O   HOH A2191     -13.360 112.796 -87.736  1.00 50.05           O  
HETATM 2391  O   HOH A2192     -11.862 111.179 -90.005  1.00 60.50           O  
HETATM 2392  O   HOH A2193     -15.025 118.312 -89.771  1.00 56.42           O  
HETATM 2393  O   HOH A2194     -17.573 113.712 -84.502  1.00108.43           O  
HETATM 2394  O   HOH A2195     -17.385 119.055 -80.821  1.00116.05           O  
HETATM 2395  O   HOH A2196     -25.845 118.902 -77.997  1.00 99.61           O  
HETATM 2396  O   HOH A2197     -23.807 124.303 -80.685  1.00 55.54           O  
HETATM 2397  O   HOH A2198     -13.291 117.712 -84.014  1.00 85.14           O  
HETATM 2398  O   HOH A2199     -18.664 123.812 -72.193  1.00 47.43           O  
HETATM 2399  O   HOH A2200     -15.004 123.171 -72.873  1.00 62.48           O  
HETATM 2400  O   HOH A2201     -14.898 122.897 -70.515  1.00 70.52           O  
HETATM 2401  O   HOH A2202     -15.502 111.092 -65.948  1.00 91.94           O  
HETATM 2402  O   HOH A2203      -8.471 110.279 -71.660  1.00 73.29           O  
HETATM 2403  O   HOH A2204      -6.363 114.551 -69.692  1.00 50.68           O  
HETATM 2404  O   HOH A2205      -9.664 113.440 -56.086  1.00 58.12           O  
HETATM 2405  O   HOH A2206     -19.368 110.747 -54.934  1.00126.44           O  
HETATM 2406  O   HOH A2207     -25.133 114.645 -61.905  1.00117.01           O  
HETATM 2407  O   HOH A2208     -19.534 122.816 -60.513  1.00 55.34           O  
HETATM 2408  O   HOH A2209     -18.120 123.217 -57.412  1.00 68.74           O  
HETATM 2409  O   HOH A2210     -27.862 122.177 -61.186  1.00 51.99           O  
HETATM 2410  O   HOH A2211     -22.007 123.757 -63.602  1.00 79.33           O  
HETATM 2411  O   HOH A2212     -26.112 120.574 -60.165  1.00103.23           O  
HETATM 2412  O   HOH A2213     -25.892 121.805 -67.521  1.00 62.17           O  
HETATM 2413  O   HOH A2214     -16.810 120.032 -69.896  1.00 86.73           O  
HETATM 2414  O   HOH A2215     -20.355 123.203 -69.628  1.00 55.95           O  
HETATM 2415  O   HOH A2216     -26.172 121.826 -70.446  1.00 99.32           O  
HETATM 2416  O   HOH A2217     -28.743 117.565 -72.160  1.00134.52           O  
HETATM 2417  O   HOH A2218     -27.623 117.071 -74.436  1.00 48.32           O  
HETATM 2418  O   HOH A2219     -28.633 118.831 -66.826  1.00125.99           O  
HETATM 2419  O   HOH A2220     -29.000 120.084 -73.348  1.00 54.21           O  
HETATM 2420  O   HOH A2221     -27.341 123.774 -70.092  1.00 69.89           O  
HETATM 2421  O   HOH A2222     -33.007 116.295 -72.875  1.00130.40           O  
HETATM 2422  O   HOH A2223     -30.449 120.422 -66.954  1.00 49.67           O  
HETATM 2423  O   HOH A2224     -33.793 120.291 -64.846  1.00126.85           O  
HETATM 2424  O   HOH A2225     -34.891 116.991 -69.553  1.00 69.38           O  
HETATM 2425  O   HOH A2226     -32.915 115.097 -69.111  1.00 47.89           O  
HETATM 2426  O   HOH A2227     -35.589 120.474 -63.099  1.00 85.43           O  
HETATM 2427  O   HOH A2228     -32.286 112.812 -61.349  1.00 42.07           O  
HETATM 2428  O   HOH A2229     -30.065 119.754 -61.428  1.00 52.65           O  
HETATM 2429  O   HOH A2230     -40.593 115.921 -61.157  1.00 76.81           O  
HETATM 2430  O   HOH A2231     -39.412 105.973 -60.762  1.00 55.03           O  
HETATM 2431  O   HOH A2232     -44.239 110.368 -58.934  1.00 76.00           O  
HETATM 2432  O   HOH A2233     -41.186 101.886 -63.398  1.00 68.70           O  
HETATM 2433  O   HOH A2234     -37.978 101.579 -62.221  1.00112.48           O  
HETATM 2434  O   HOH A2235     -47.830 112.198 -64.687  1.00113.98           O  
HETATM 2435  O   HOH A2236     -42.857 114.573 -63.472  1.00 97.05           O  
HETATM 2436  O   HOH A2237     -42.005 107.878 -70.190  1.00 95.16           O  
HETATM 2437  O   HOH A2238     -36.606 111.229 -74.968  1.00 62.94           O  
HETATM 2438  O   HOH A2239     -41.914  95.291 -85.766  1.00 64.70           O  
HETATM 2439  O   HOH A2240     -40.326 100.805 -86.362  1.00 65.64           O  
HETATM 2440  O   HOH A2241     -39.670  95.363 -88.124  1.00 57.61           O  
HETATM 2441  O   HOH A2242     -45.686  89.248 -74.060  1.00 78.74           O  
HETATM 2442  O   HOH A2243     -47.202  94.576 -65.895  1.00 60.98           O  
HETATM 2443  O   HOH A2244     -45.064  97.484 -65.973  1.00 68.51           O  
HETATM 2444  O   HOH A2245     -40.267  90.357 -71.550  1.00100.81           O  
HETATM 2445  O   HOH A2246     -27.816  89.385 -78.676  1.00 85.10           O  
HETATM 2446  O   HOH A2247     -30.391  84.848 -82.737  1.00 67.92           O  
MASTER      421    0    0   13    7    0    0    6 2445    1    0   26          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.