HEADER    TRANSFERASE                             04-JUL-03   1PXP              
TITLE     HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR N-[4-(2, 
TITLE    2 4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4- 
TITLE    3 DIAMINE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HI5;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, CELL DIVISION, MITOSIS,  
KEYWDS   2 INHIBITION, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-       
KEYWDS   3 BINDING, 3D-STRUCTURE.                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.WANG,C.MEADES,G.WOOD,A.OSNOWSKI,S.ANDERSON,R.YUILL,M.THOMAS,        
AUTHOR   2 M.MEZNA,W.JACKSON,C.MIDGLEY,G.GRIFFITHS,I.MCNAE,S.Y.WU,C.MCINNES,    
AUTHOR   3 D.ZHELEVA,M.D.WALKINSHAW,P.M.FISCHER                                 
REVDAT   3   16-AUG-23 1PXP    1       REMARK                                   
REVDAT   2   24-FEB-09 1PXP    1       VERSN                                    
REVDAT   1   13-APR-04 1PXP    0                                                
JRNL        AUTH   S.WANG,C.MEADES,G.WOOD,A.OSNOWSKI,S.ANDERSON,R.YUILL,        
JRNL        AUTH 2 M.THOMAS,M.MEZNA,W.JACKSON,C.MIDGLEY,G.GRIFFITHS,I.FLEMING,  
JRNL        AUTH 3 S.GREEN,I.MCNAE,S.Y.WU,C.MCINNES,D.ZHELEVA,M.D.WALKINSHAW,   
JRNL        AUTH 4 P.M.FISCHER                                                  
JRNL        TITL   2-ANILINO-4-(THIAZOL-5-YL)PYRIMIDINE CDK INHIBITORS:         
JRNL        TITL 2 SYNTHESIS, SAR ANALYSIS, X-RAY CRYSTALLOGRAPHY, AND          
JRNL        TITL 3 BIOLOGICAL ACTIVITY.                                         
JRNL        REF    J.MED.CHEM.                   V.  47  1662 2004              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15027857                                                     
JRNL        DOI    10.1021/JM0309957                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,            
REMARK   1  AUTH 2 K.J.STEWART,S.WANG,D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR, 
REMARK   1  AUTH 3 P.M.FISCHER,M.D.WALKINSHAW                                   
REMARK   1  TITL   DISCOVERY OF A NOVEL FAMILY OF CDK INHIBITORS WITH THE       
REMARK   1  TITL 2 PROGRAM LIDAEUS: STRUCTURAL BASIS FOR LIGAND-INDUCED         
REMARK   1  TITL 3 DISORDERING OF THE ACTIVATION LOOP.                          
REMARK   1  REF    STRUCTURE                     V.  11   399 2003              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  DOI    10.1016/S0969-2126(03)00060-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1197377.910                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 12512                          
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) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 642                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1877                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 111                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.029                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2366                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 87                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.44000                                             
REMARK   3    B22 (A**2) : 7.53000                                              
REMARK   3    B33 (A**2) : -7.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
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) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.880                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.790 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.130 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.120 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.220 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 63.23                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : FRA_PAR.TXT                                    
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : FRA_TOP.TXT                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019676.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12686                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.50000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.14800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HCL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NA-HEPES, PH 7.8, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.66850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.70700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.89700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.70700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.66850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.89700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  25      -70.96    -98.90                                   
REMARK 500    VAL A  44      128.29     61.31                                   
REMARK 500    ARG A 126      -16.90     79.85                                   
REMARK 500    ASP A 127       45.25   -142.37                                   
REMARK 500    ASP A 145       32.65     70.73                                   
REMARK 500    PHE A 152      -92.14   -139.30                                   
REMARK 500    PRO A 155     -146.04    -82.51                                   
REMARK 500    THR A 160        4.04    -66.80                                   
REMARK 500    GLU A 162     -140.42    -86.93                                   
REMARK 500    TYR A 179       60.62   -117.77                                   
REMARK 500    SER A 181     -168.68   -111.48                                   
REMARK 500    PRO A 254       35.68    -96.36                                   
REMARK 500    ASP A 288       40.97   -109.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN CK8 500 HAS ALTERNATE CONFORMATION WITH HOH 501,502,       
REMARK 600 503,504,505,506,507,508,AND 509.                                     
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CK8 A 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                          
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2058    
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 6027    
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5-SULPHONATE BOUND                               
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH    
REMARK 900 AN OXINDOLE INHIBITOR                                                
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR 
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) IN       
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR    
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR    
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR    
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL-2'-OXO)BUTOXYPURINE                               
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [(6-AMINO-4-PYRIMIDINYL) AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED) IN COMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-1,2-DIHYDRO-3H- INDOL-3-     
REMARK 900 YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE                              
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-   
REMARK 900 OXO-6,7-DIHYDRO-8H-[1,3]THIAZOLO[5,4-E]INDOL-8-YLIDENE)HYDRAZINO]    
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,  
REMARK 900 3-DIHYDRO-2-BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3-OXAZOL-5-YL)-1,  
REMARK 900 3-DIHYDRO-2H-INDOL-2-ONE                                             
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WIT4-{[(2-OXO-1,2-        
REMARK 900 DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2-YL)        
REMARK 900 BENZENESULFONAMIDEH                                                  
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WIT3-{[4-({[AMINO(IMINO)  
REMARK 900 METHYL]AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-DIHYDRO-1H-INDOLEH 
REMARK 900 RELATED ID: 1PXM   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 3-[4-   
REMARK 900 (2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL              
REMARK 900 RELATED ID: 1PXN   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 4-[4-   
REMARK 900 (4-METHYL-2-METHYLAMINO-THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL    
REMARK 900 RELATED ID: 1PXO   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR [4-(2-  
REMARK 900 AMINO-4-METHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-NITRO-PHENYL)-AMINE  
DBREF  1PXP A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    CK8  A 500      23                                                       
HETNAM     CK8 N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-          
HETNAM   2 CK8  DIMETHYL-BENZENE-1,4-DIAMINE                                    
FORMUL   2  CK8    C17 H19 N5 S                                                 
FORMUL   3  HOH   *87(H2 O)                                                     
HELIX    1   1 PRO A   45  LEU A   55  1                                  11    
HELIX    2   2 LEU A   87  ALA A   95  1                                   9    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  247  VAL A  252  1                                   6    
HELIX   10  10 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  ALA A  282  1                                   7    
HELIX   12  12 HIS A  283  GLN A  287  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 GLY A  16  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  THR A  72 -1  N  ILE A  70   O  TYR A  77           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0         0.21                     
SITE     1 AC1 21 ILE A  10  ALA A  31  LYS A  33  PHE A  80                    
SITE     2 AC1 21 GLU A  81  PHE A  82  LEU A  83  HIS A  84                    
SITE     3 AC1 21 LYS A  89  LEU A 134  ASP A 145  HOH A 501                    
SITE     4 AC1 21 HOH A 502  HOH A 503  HOH A 504  HOH A 505                    
SITE     5 AC1 21 HOH A 506  HOH A 507  HOH A 508  HOH A 509                    
SITE     6 AC1 21 HOH A 510                                                     
CRYST1   53.337   71.794   71.414  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018749  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014003        0.00000                         
ATOM      1  N   MET A   1      39.523  42.075  -1.634  1.00 80.65           N  
ATOM      2  CA  MET A   1      40.057  41.064  -2.588  1.00 80.62           C  
ATOM      3  C   MET A   1      39.419  41.191  -3.966  1.00 79.36           C  
ATOM      4  O   MET A   1      38.325  41.734  -4.110  1.00 79.09           O  
ATOM      5  CB  MET A   1      39.830  39.651  -2.046  1.00 82.66           C  
ATOM      6  CG  MET A   1      40.219  38.553  -3.022  1.00 85.53           C  
ATOM      7  SD  MET A   1      40.250  36.919  -2.284  1.00 90.46           S  
ATOM      8  CE  MET A   1      41.995  36.771  -1.896  1.00 90.02           C  
ATOM      9  N   GLU A   2      40.115  40.676  -4.974  1.00 77.90           N  
ATOM     10  CA  GLU A   2      39.649  40.729  -6.351  1.00 75.97           C  
ATOM     11  C   GLU A   2      38.497  39.767  -6.607  1.00 73.54           C  
ATOM     12  O   GLU A   2      37.837  39.846  -7.641  1.00 73.79           O  
ATOM     13  CB  GLU A   2      40.799  40.396  -7.308  1.00 77.10           C  
ATOM     14  CG  GLU A   2      42.162  40.916  -6.870  1.00 79.33           C  
ATOM     15  CD  GLU A   2      42.887  39.958  -5.938  1.00 80.81           C  
ATOM     16  OE1 GLU A   2      42.335  39.619  -4.872  1.00 81.53           O  
ATOM     17  OE2 GLU A   2      44.015  39.541  -6.274  1.00 81.20           O  
ATOM     18  N   ASN A   3      38.258  38.856  -5.670  1.00 70.67           N  
ATOM     19  CA  ASN A   3      37.186  37.878  -5.824  1.00 67.29           C  
ATOM     20  C   ASN A   3      35.869  38.350  -5.225  1.00 64.77           C  
ATOM     21  O   ASN A   3      34.983  37.541  -4.958  1.00 65.39           O  
ATOM     22  CB  ASN A   3      37.581  36.549  -5.175  1.00 68.30           C  
ATOM     23  CG  ASN A   3      38.855  35.968  -5.758  1.00 68.50           C  
ATOM     24  OD1 ASN A   3      38.950  35.730  -6.961  1.00 69.32           O  
ATOM     25  ND2 ASN A   3      39.840  35.730  -4.902  1.00 68.54           N  
ATOM     26  N   PHE A   4      35.738  39.653  -5.004  1.00 61.67           N  
ATOM     27  CA  PHE A   4      34.513  40.194  -4.429  1.00 59.42           C  
ATOM     28  C   PHE A   4      34.207  41.579  -4.961  1.00 59.60           C  
ATOM     29  O   PHE A   4      35.106  42.398  -5.132  1.00 60.54           O  
ATOM     30  CB  PHE A   4      34.609  40.283  -2.902  1.00 56.69           C  
ATOM     31  CG  PHE A   4      34.943  38.985  -2.230  1.00 54.96           C  
ATOM     32  CD1 PHE A   4      36.261  38.649  -1.957  1.00 53.25           C  
ATOM     33  CD2 PHE A   4      33.938  38.097  -1.867  1.00 54.89           C  
ATOM     34  CE1 PHE A   4      36.579  37.448  -1.329  1.00 53.19           C  
ATOM     35  CE2 PHE A   4      34.244  36.890  -1.239  1.00 53.66           C  
ATOM     36  CZ  PHE A   4      35.568  36.565  -0.970  1.00 53.66           C  
ATOM     37  N   GLN A   5      32.930  41.835  -5.215  1.00 60.23           N  
ATOM     38  CA  GLN A   5      32.495  43.135  -5.703  1.00 60.91           C  
ATOM     39  C   GLN A   5      31.533  43.727  -4.684  1.00 59.93           C  
ATOM     40  O   GLN A   5      30.433  43.216  -4.477  1.00 60.13           O  
ATOM     41  CB  GLN A   5      31.816  42.997  -7.070  1.00 63.08           C  
ATOM     42  CG  GLN A   5      30.788  41.883  -7.142  1.00 68.22           C  
ATOM     43  CD  GLN A   5      30.262  41.661  -8.549  1.00 72.04           C  
ATOM     44  OE1 GLN A   5      29.671  42.557  -9.152  1.00 73.98           O  
ATOM     45  NE2 GLN A   5      30.483  40.462  -9.083  1.00 73.26           N  
ATOM     46  N   LYS A   6      31.965  44.802  -4.037  1.00 59.43           N  
ATOM     47  CA  LYS A   6      31.158  45.467  -3.027  1.00 60.70           C  
ATOM     48  C   LYS A   6      29.902  46.072  -3.645  1.00 60.57           C  
ATOM     49  O   LYS A   6      29.985  46.860  -4.585  1.00 61.39           O  
ATOM     50  CB  LYS A   6      31.988  46.558  -2.342  1.00 61.27           C  
ATOM     51  CG  LYS A   6      33.262  46.034  -1.688  1.00 62.81           C  
ATOM     52  CD  LYS A   6      34.104  47.154  -1.093  1.00 65.19           C  
ATOM     53  CE  LYS A   6      34.636  48.086  -2.169  1.00 66.72           C  
ATOM     54  NZ  LYS A   6      35.490  47.363  -3.148  1.00 68.50           N  
ATOM     55  N   VAL A   7      28.739  45.696  -3.119  1.00 60.10           N  
ATOM     56  CA  VAL A   7      27.474  46.215  -3.629  1.00 59.30           C  
ATOM     57  C   VAL A   7      26.968  47.364  -2.771  1.00 59.02           C  
ATOM     58  O   VAL A   7      26.433  48.341  -3.289  1.00 59.53           O  
ATOM     59  CB  VAL A   7      26.383  45.121  -3.684  1.00 59.12           C  
ATOM     60  CG1 VAL A   7      26.226  44.484  -2.331  1.00 59.97           C  
ATOM     61  CG2 VAL A   7      25.053  45.722  -4.128  1.00 58.94           C  
ATOM     62  N   GLU A   8      27.140  47.254  -1.459  1.00 58.91           N  
ATOM     63  CA  GLU A   8      26.690  48.312  -0.569  1.00 59.39           C  
ATOM     64  C   GLU A   8      27.292  48.243   0.828  1.00 59.49           C  
ATOM     65  O   GLU A   8      27.627  47.169   1.325  1.00 59.18           O  
ATOM     66  CB  GLU A   8      25.160  48.306  -0.476  1.00 60.33           C  
ATOM     67  CG  GLU A   8      24.539  46.943  -0.195  1.00 61.50           C  
ATOM     68  CD  GLU A   8      23.026  47.010  -0.049  1.00 62.78           C  
ATOM     69  OE1 GLU A   8      22.546  47.569   0.961  1.00 61.96           O  
ATOM     70  OE2 GLU A   8      22.314  46.509  -0.948  1.00 65.28           O  
ATOM     71  N   LYS A   9      27.441  49.407   1.451  1.00 59.80           N  
ATOM     72  CA  LYS A   9      27.976  49.477   2.801  1.00 61.34           C  
ATOM     73  C   LYS A   9      26.848  49.013   3.706  1.00 61.66           C  
ATOM     74  O   LYS A   9      25.861  49.721   3.903  1.00 61.81           O  
ATOM     75  CB  LYS A   9      28.390  50.911   3.151  1.00 62.43           C  
ATOM     76  CG  LYS A   9      29.016  51.054   4.532  1.00 64.77           C  
ATOM     77  CD  LYS A   9      29.537  52.468   4.788  1.00 67.23           C  
ATOM     78  CE  LYS A   9      30.777  52.785   3.958  1.00 69.74           C  
ATOM     79  NZ  LYS A   9      30.512  52.832   2.492  1.00 70.28           N  
ATOM     80  N   ILE A  10      26.997  47.810   4.244  1.00 61.66           N  
ATOM     81  CA  ILE A  10      25.981  47.225   5.099  1.00 61.52           C  
ATOM     82  C   ILE A  10      26.119  47.696   6.544  1.00 62.29           C  
ATOM     83  O   ILE A  10      25.207  47.531   7.355  1.00 61.32           O  
ATOM     84  CB  ILE A  10      26.048  45.675   5.012  1.00 60.81           C  
ATOM     85  CG1 ILE A  10      24.648  45.115   4.778  1.00 62.26           C  
ATOM     86  CG2 ILE A  10      26.679  45.084   6.264  1.00 60.38           C  
ATOM     87  CD1 ILE A  10      24.059  45.482   3.432  1.00 62.09           C  
ATOM     88  N   GLY A  11      27.265  48.290   6.859  1.00 63.76           N  
ATOM     89  CA  GLY A  11      27.488  48.773   8.209  1.00 66.57           C  
ATOM     90  C   GLY A  11      28.940  49.082   8.513  1.00 68.39           C  
ATOM     91  O   GLY A  11      29.821  48.867   7.679  1.00 68.47           O  
ATOM     92  N   GLU A  12      29.183  49.598   9.715  1.00 70.09           N  
ATOM     93  CA  GLU A  12      30.529  49.940  10.164  1.00 72.09           C  
ATOM     94  C   GLU A  12      30.714  49.459  11.601  1.00 72.86           C  
ATOM     95  O   GLU A  12      30.340  50.148  12.548  1.00 72.50           O  
ATOM     96  CB  GLU A  12      30.756  51.458  10.082  1.00 73.12           C  
ATOM     97  CG  GLU A  12      30.693  52.032   8.664  1.00 75.82           C  
ATOM     98  CD  GLU A  12      30.880  53.546   8.618  1.00 77.81           C  
ATOM     99  OE1 GLU A  12      30.057  54.271   9.219  1.00 78.02           O  
ATOM    100  OE2 GLU A  12      31.850  54.010   7.979  1.00 78.42           O  
ATOM    101  N   GLY A  13      31.289  48.268  11.750  1.00 74.57           N  
ATOM    102  CA  GLY A  13      31.511  47.699  13.068  1.00 76.03           C  
ATOM    103  C   GLY A  13      32.595  48.383  13.883  1.00 77.41           C  
ATOM    104  O   GLY A  13      32.932  49.545  13.645  1.00 76.43           O  
ATOM    105  N   THR A  14      33.144  47.652  14.849  1.00 78.86           N  
ATOM    106  CA  THR A  14      34.188  48.179  15.723  1.00 79.45           C  
ATOM    107  C   THR A  14      35.575  48.011  15.116  1.00 79.44           C  
ATOM    108  O   THR A  14      36.392  48.933  15.141  1.00 79.09           O  
ATOM    109  CB  THR A  14      34.178  47.468  17.094  1.00 79.71           C  
ATOM    110  OG1 THR A  14      32.870  47.553  17.672  1.00 79.96           O  
ATOM    111  CG2 THR A  14      35.183  48.116  18.036  1.00 80.22           C  
ATOM    112  N   TYR A  15      35.830  46.829  14.568  1.00 78.94           N  
ATOM    113  CA  TYR A  15      37.122  46.520  13.970  1.00 78.55           C  
ATOM    114  C   TYR A  15      37.242  46.991  12.528  1.00 76.22           C  
ATOM    115  O   TYR A  15      38.348  47.145  12.009  1.00 76.77           O  
ATOM    116  CB  TYR A  15      37.368  45.017  14.050  1.00 81.43           C  
ATOM    117  CG  TYR A  15      37.234  44.486  15.453  1.00 84.63           C  
ATOM    118  CD1 TYR A  15      38.103  44.905  16.458  1.00 86.41           C  
ATOM    119  CD2 TYR A  15      36.215  43.597  15.789  1.00 85.82           C  
ATOM    120  CE1 TYR A  15      37.961  44.454  17.764  1.00 88.09           C  
ATOM    121  CE2 TYR A  15      36.063  43.140  17.091  1.00 87.17           C  
ATOM    122  CZ  TYR A  15      36.939  43.573  18.073  1.00 88.33           C  
ATOM    123  OH  TYR A  15      36.796  43.129  19.366  1.00 90.02           O  
ATOM    124  N   GLY A  16      36.105  47.221  11.881  1.00 72.89           N  
ATOM    125  CA  GLY A  16      36.139  47.676  10.505  1.00 68.69           C  
ATOM    126  C   GLY A  16      34.770  47.830   9.877  1.00 65.45           C  
ATOM    127  O   GLY A  16      33.748  47.600  10.519  1.00 65.25           O  
ATOM    128  N   VAL A  17      34.757  48.228   8.610  1.00 62.96           N  
ATOM    129  CA  VAL A  17      33.518  48.414   7.873  1.00 60.02           C  
ATOM    130  C   VAL A  17      33.028  47.074   7.337  1.00 57.36           C  
ATOM    131  O   VAL A  17      33.826  46.180   7.047  1.00 55.05           O  
ATOM    132  CB  VAL A  17      33.717  49.386   6.688  1.00 60.04           C  
ATOM    133  CG1 VAL A  17      32.419  49.559   5.925  1.00 60.23           C  
ATOM    134  CG2 VAL A  17      34.198  50.730   7.201  1.00 62.40           C  
ATOM    135  N   VAL A  18      31.710  46.937   7.216  1.00 54.72           N  
ATOM    136  CA  VAL A  18      31.119  45.706   6.705  1.00 51.64           C  
ATOM    137  C   VAL A  18      30.404  46.006   5.393  1.00 49.18           C  
ATOM    138  O   VAL A  18      29.650  46.970   5.295  1.00 48.58           O  
ATOM    139  CB  VAL A  18      30.106  45.108   7.703  1.00 51.10           C  
ATOM    140  CG1 VAL A  18      29.662  43.735   7.223  1.00 52.39           C  
ATOM    141  CG2 VAL A  18      30.726  45.019   9.085  1.00 50.82           C  
ATOM    142  N   TYR A  19      30.645  45.178   4.386  1.00 48.38           N  
ATOM    143  CA  TYR A  19      30.024  45.369   3.080  1.00 49.00           C  
ATOM    144  C   TYR A  19      29.293  44.126   2.595  1.00 46.63           C  
ATOM    145  O   TYR A  19      29.665  43.004   2.928  1.00 45.32           O  
ATOM    146  CB  TYR A  19      31.085  45.734   2.030  1.00 52.81           C  
ATOM    147  CG  TYR A  19      31.642  47.138   2.138  1.00 57.62           C  
ATOM    148  CD1 TYR A  19      30.899  48.238   1.717  1.00 59.29           C  
ATOM    149  CD2 TYR A  19      32.912  47.366   2.669  1.00 59.20           C  
ATOM    150  CE1 TYR A  19      31.407  49.534   1.820  1.00 62.06           C  
ATOM    151  CE2 TYR A  19      33.428  48.654   2.778  1.00 61.71           C  
ATOM    152  CZ  TYR A  19      32.671  49.733   2.353  1.00 62.83           C  
ATOM    153  OH  TYR A  19      33.176  51.010   2.464  1.00 65.16           O  
ATOM    154  N   LYS A  20      28.239  44.340   1.816  1.00 44.68           N  
ATOM    155  CA  LYS A  20      27.501  43.237   1.216  1.00 42.56           C  
ATOM    156  C   LYS A  20      28.307  43.050  -0.058  1.00 41.72           C  
ATOM    157  O   LYS A  20      28.462  43.994  -0.827  1.00 40.06           O  
ATOM    158  CB  LYS A  20      26.065  43.652   0.874  1.00 40.48           C  
ATOM    159  CG  LYS A  20      25.246  42.562   0.180  1.00 39.56           C  
ATOM    160  CD  LYS A  20      23.823  43.047  -0.141  1.00 39.50           C  
ATOM    161  CE  LYS A  20      23.036  41.996  -0.919  1.00 37.06           C  
ATOM    162  NZ  LYS A  20      21.603  42.344  -1.077  1.00 39.48           N  
ATOM    163  N   ALA A  21      28.850  41.860  -0.278  1.00 43.21           N  
ATOM    164  CA  ALA A  21      29.657  41.648  -1.474  1.00 45.19           C  
ATOM    165  C   ALA A  21      29.254  40.433  -2.298  1.00 46.08           C  
ATOM    166  O   ALA A  21      28.571  39.536  -1.814  1.00 44.47           O  
ATOM    167  CB  ALA A  21      31.135  41.566  -1.090  1.00 43.42           C  
ATOM    168  N   ARG A  22      29.694  40.414  -3.550  1.00 48.61           N  
ATOM    169  CA  ARG A  22      29.366  39.326  -4.461  1.00 53.42           C  
ATOM    170  C   ARG A  22      30.617  38.602  -4.949  1.00 54.83           C  
ATOM    171  O   ARG A  22      31.431  39.167  -5.678  1.00 55.04           O  
ATOM    172  CB  ARG A  22      28.586  39.885  -5.654  1.00 54.39           C  
ATOM    173  CG  ARG A  22      27.957  38.840  -6.560  1.00 57.27           C  
ATOM    174  CD  ARG A  22      27.369  39.491  -7.807  1.00 59.00           C  
ATOM    175  NE  ARG A  22      26.535  40.653  -7.494  1.00 59.88           N  
ATOM    176  CZ  ARG A  22      25.339  40.588  -6.917  1.00 59.76           C  
ATOM    177  NH1 ARG A  22      24.827  39.412  -6.585  1.00 59.36           N  
ATOM    178  NH2 ARG A  22      24.652  41.698  -6.678  1.00 59.16           N  
ATOM    179  N   ASN A  23      30.774  37.350  -4.535  1.00 56.58           N  
ATOM    180  CA  ASN A  23      31.924  36.563  -4.953  1.00 59.00           C  
ATOM    181  C   ASN A  23      31.870  36.429  -6.471  1.00 61.73           C  
ATOM    182  O   ASN A  23      31.063  35.668  -7.007  1.00 61.45           O  
ATOM    183  CB  ASN A  23      31.881  35.180  -4.307  1.00 57.88           C  
ATOM    184  CG  ASN A  23      33.067  34.314  -4.698  1.00 57.77           C  
ATOM    185  OD1 ASN A  23      33.425  34.228  -5.871  1.00 55.69           O  
ATOM    186  ND2 ASN A  23      33.674  33.662  -3.715  1.00 54.39           N  
ATOM    187  N   LYS A  24      32.728  37.180  -7.154  1.00 64.30           N  
ATOM    188  CA  LYS A  24      32.787  37.172  -8.613  1.00 66.57           C  
ATOM    189  C   LYS A  24      32.953  35.768  -9.187  1.00 67.42           C  
ATOM    190  O   LYS A  24      32.688  35.539 -10.366  1.00 67.77           O  
ATOM    191  CB  LYS A  24      33.946  38.046  -9.094  1.00 67.40           C  
ATOM    192  CG  LYS A  24      33.965  39.449  -8.513  1.00 69.98           C  
ATOM    193  CD  LYS A  24      35.207  40.203  -8.976  1.00 72.58           C  
ATOM    194  CE  LYS A  24      35.337  41.559  -8.295  1.00 74.02           C  
ATOM    195  NZ  LYS A  24      36.599  42.257  -8.674  1.00 74.66           N  
ATOM    196  N   LEU A  25      33.391  34.831  -8.353  1.00 68.46           N  
ATOM    197  CA  LEU A  25      33.602  33.459  -8.798  1.00 70.04           C  
ATOM    198  C   LEU A  25      32.440  32.528  -8.441  1.00 70.89           C  
ATOM    199  O   LEU A  25      31.690  32.095  -9.318  1.00 70.88           O  
ATOM    200  CB  LEU A  25      34.905  32.921  -8.200  1.00 70.81           C  
ATOM    201  CG  LEU A  25      36.147  33.798  -8.394  1.00 71.92           C  
ATOM    202  CD1 LEU A  25      37.326  33.188  -7.652  1.00 71.70           C  
ATOM    203  CD2 LEU A  25      36.460  33.940  -9.876  1.00 72.44           C  
ATOM    204  N   THR A  26      32.297  32.221  -7.156  1.00 71.23           N  
ATOM    205  CA  THR A  26      31.234  31.335  -6.685  1.00 71.79           C  
ATOM    206  C   THR A  26      29.836  31.859  -7.006  1.00 71.08           C  
ATOM    207  O   THR A  26      28.901  31.083  -7.196  1.00 71.57           O  
ATOM    208  CB  THR A  26      31.329  31.113  -5.158  1.00 73.14           C  
ATOM    209  OG1 THR A  26      32.608  30.555  -4.830  1.00 75.88           O  
ATOM    210  CG2 THR A  26      30.247  30.165  -4.690  1.00 74.90           C  
ATOM    211  N   GLY A  27      29.692  33.177  -7.065  1.00 69.95           N  
ATOM    212  CA  GLY A  27      28.392  33.750  -7.356  1.00 67.70           C  
ATOM    213  C   GLY A  27      27.508  33.805  -6.123  1.00 65.99           C  
ATOM    214  O   GLY A  27      26.329  34.149  -6.206  1.00 66.51           O  
ATOM    215  N   GLU A  28      28.077  33.456  -4.975  1.00 62.34           N  
ATOM    216  CA  GLU A  28      27.351  33.483  -3.710  1.00 60.20           C  
ATOM    217  C   GLU A  28      27.496  34.898  -3.145  1.00 56.45           C  
ATOM    218  O   GLU A  28      28.496  35.565  -3.400  1.00 55.51           O  
ATOM    219  CB  GLU A  28      27.955  32.443  -2.751  1.00 62.87           C  
ATOM    220  CG  GLU A  28      27.422  32.424  -1.320  1.00 66.66           C  
ATOM    221  CD  GLU A  28      25.939  32.114  -1.237  1.00 70.19           C  
ATOM    222  OE1 GLU A  28      25.512  31.475  -0.249  1.00 70.12           O  
ATOM    223  OE2 GLU A  28      25.195  32.519  -2.153  1.00 71.87           O  
ATOM    224  N   VAL A  29      26.489  35.378  -2.421  1.00 51.75           N  
ATOM    225  CA  VAL A  29      26.578  36.713  -1.842  1.00 47.99           C  
ATOM    226  C   VAL A  29      26.890  36.569  -0.358  1.00 45.02           C  
ATOM    227  O   VAL A  29      26.310  35.737   0.333  1.00 44.50           O  
ATOM    228  CB  VAL A  29      25.272  37.522  -2.025  1.00 49.71           C  
ATOM    229  CG1 VAL A  29      24.868  37.559  -3.500  1.00 49.42           C  
ATOM    230  CG2 VAL A  29      24.177  36.934  -1.183  1.00 49.05           C  
ATOM    231  N   VAL A  30      27.816  37.383   0.123  1.00 42.68           N  
ATOM    232  CA  VAL A  30      28.235  37.320   1.510  1.00 41.10           C  
ATOM    233  C   VAL A  30      28.420  38.720   2.088  1.00 41.00           C  
ATOM    234  O   VAL A  30      28.297  39.720   1.382  1.00 38.46           O  
ATOM    235  CB  VAL A  30      29.588  36.568   1.621  1.00 42.38           C  
ATOM    236  CG1 VAL A  30      29.457  35.141   1.076  1.00 40.89           C  
ATOM    237  CG2 VAL A  30      30.660  37.316   0.826  1.00 40.01           C  
ATOM    238  N   ALA A  31      28.688  38.784   3.386  1.00 41.26           N  
ATOM    239  CA  ALA A  31      28.955  40.060   4.027  1.00 41.28           C  
ATOM    240  C   ALA A  31      30.459  40.013   4.211  1.00 40.75           C  
ATOM    241  O   ALA A  31      30.975  39.113   4.865  1.00 42.49           O  
ATOM    242  CB  ALA A  31      28.256  40.158   5.379  1.00 39.72           C  
ATOM    243  N   LEU A  32      31.164  40.954   3.603  1.00 40.73           N  
ATOM    244  CA  LEU A  32      32.616  40.977   3.702  1.00 42.19           C  
ATOM    245  C   LEU A  32      33.051  42.007   4.729  1.00 42.27           C  
ATOM    246  O   LEU A  32      32.678  43.177   4.632  1.00 39.07           O  
ATOM    247  CB  LEU A  32      33.229  41.336   2.348  1.00 42.73           C  
ATOM    248  CG  LEU A  32      34.633  40.832   1.994  1.00 44.65           C  
ATOM    249  CD1 LEU A  32      35.312  41.897   1.151  1.00 43.39           C  
ATOM    250  CD2 LEU A  32      35.451  40.551   3.238  1.00 45.95           C  
ATOM    251  N  ALYS A  33      33.775  41.683   5.840  0.80 59.44           N  
ATOM    252  N  BLYS A  33      33.982  41.509   5.497  0.20 65.02           N  
ATOM    253  CA ALYS A  33      34.258  42.575   6.882  0.80 58.02           C  
ATOM    254  CA BLYS A  33      34.388  42.483   6.496  0.20 64.90           C  
ATOM    255  C  ALYS A  33      35.748  42.790   6.656  0.80 58.83           C  
ATOM    256  C  BLYS A  33      35.895  42.696   6.489  0.20 65.49           C  
ATOM    257  O  ALYS A  33      36.543  41.858   6.764  0.80 57.71           O  
ATOM    258  O  BLYS A  33      36.664  41.759   6.679  0.20 65.46           O  
ATOM    259  CB ALYS A  33      34.026  41.966   8.268  0.80 56.54           C  
ATOM    260  CB BLYS A  33      33.938  42.030   7.887  0.20 63.59           C  
ATOM    261  CG ALYS A  33      34.289  42.931   9.416  0.80 54.76           C  
ATOM    262  CG BLYS A  33      32.444  41.746   7.996  0.20 62.63           C  
ATOM    263  CD ALYS A  33      33.991  42.285  10.761  0.80 55.07           C  
ATOM    264  CD BLYS A  33      31.995  41.665   9.450  0.20 61.47           C  
ATOM    265  CE ALYS A  33      33.865  43.319  11.873  0.80 54.42           C  
ATOM    266  CE BLYS A  33      30.480  41.661   9.556  0.20 60.63           C  
ATOM    267  NZ ALYS A  33      35.114  44.098  12.089  0.80 55.43           N  
ATOM    268  NZ BLYS A  33      30.009  41.848  10.964  0.20 60.32           N  
ATOM    269  N   LYS A  34      36.205  43.988   6.328  1.00 81.32           N  
ATOM    270  CA  LYS A  34      37.605  44.345   6.197  1.00 79.82           C  
ATOM    271  C   LYS A  34      38.092  45.066   7.451  1.00 78.54           C  
ATOM    272  O   LYS A  34      37.509  46.061   7.883  1.00 77.58           O  
ATOM    273  CB  LYS A  34      37.798  45.215   4.953  1.00 79.87           C  
ATOM    274  CG  LYS A  34      36.788  46.335   4.814  1.00 81.66           C  
ATOM    275  CD  LYS A  34      36.530  46.668   3.346  1.00 82.92           C  
ATOM    276  CE  LYS A  34      37.796  47.103   2.621  1.00 82.84           C  
ATOM    277  NZ  LYS A  34      37.523  47.410   1.188  1.00 83.81           N  
ATOM    278  N   ILE A  35      39.165  44.542   8.032  1.00 78.22           N  
ATOM    279  CA  ILE A  35      39.743  45.111   9.240  1.00 78.09           C  
ATOM    280  C   ILE A  35      41.110  45.705   8.925  1.00 78.58           C  
ATOM    281  O   ILE A  35      41.986  45.009   8.415  1.00 78.32           O  
ATOM    282  CB  ILE A  35      39.916  44.024  10.309  1.00 77.22           C  
ATOM    283  CG1 ILE A  35      38.613  43.234  10.449  1.00 77.24           C  
ATOM    284  CG2 ILE A  35      40.319  44.654  11.633  1.00 77.01           C  
ATOM    285  CD1 ILE A  35      38.755  41.936  11.223  1.00 77.23           C  
ATOM    286  N   ARG A  36      41.287  46.990   9.218  1.00 79.82           N  
ATOM    287  CA  ARG A  36      42.561  47.655   8.963  1.00 81.20           C  
ATOM    288  C   ARG A  36      43.705  46.927   9.663  1.00 81.20           C  
ATOM    289  O   ARG A  36      44.713  47.536  10.027  1.00 81.21           O  
ATOM    290  CB  ARG A  36      42.518  49.109   9.445  1.00 83.02           C  
ATOM    291  CG  ARG A  36      42.079  50.125   8.396  1.00 85.42           C  
ATOM    292  CD  ARG A  36      40.638  49.923   7.948  1.00 87.27           C  
ATOM    293  NE  ARG A  36      40.181  51.029   7.108  1.00 88.89           N  
ATOM    294  CZ  ARG A  36      38.968  51.112   6.570  1.00 90.19           C  
ATOM    295  NH1 ARG A  36      38.077  50.152   6.779  1.00 90.25           N  
ATOM    296  NH2 ARG A  36      38.641  52.161   5.826  1.00 90.20           N  
ATOM    297  N   THR A  41      48.361  49.389  10.033  1.00139.03           N  
ATOM    298  CA  THR A  41      48.695  48.300   9.122  1.00138.77           C  
ATOM    299  C   THR A  41      50.148  47.869   9.308  1.00138.20           C  
ATOM    300  O   THR A  41      50.967  47.999   8.398  1.00138.38           O  
ATOM    301  CB  THR A  41      48.483  48.719   7.653  1.00139.12           C  
ATOM    302  OG1 THR A  41      49.360  49.805   7.330  1.00139.13           O  
ATOM    303  CG2 THR A  41      47.043  49.159   7.431  1.00139.27           C  
ATOM    304  N   GLU A  42      50.459  47.356  10.495  1.00137.15           N  
ATOM    305  CA  GLU A  42      51.813  46.910  10.807  1.00135.80           C  
ATOM    306  C   GLU A  42      52.054  45.488  10.306  1.00134.25           C  
ATOM    307  O   GLU A  42      53.197  45.045  10.196  1.00134.22           O  
ATOM    308  CB  GLU A  42      52.051  46.976  12.318  1.00136.40           C  
ATOM    309  CG  GLU A  42      51.808  48.353  12.921  1.00137.01           C  
ATOM    310  CD  GLU A  42      52.068  48.394  14.414  1.00137.30           C  
ATOM    311  OE1 GLU A  42      51.459  47.588  15.149  1.00137.12           O  
ATOM    312  OE2 GLU A  42      52.877  49.238  14.854  1.00137.66           O  
ATOM    313  N   GLY A  43      50.970  44.779  10.004  1.00132.22           N  
ATOM    314  CA  GLY A  43      51.088  43.415   9.518  1.00129.11           C  
ATOM    315  C   GLY A  43      50.145  42.446  10.206  1.00126.83           C  
ATOM    316  O   GLY A  43      50.228  41.237   9.991  1.00126.99           O  
ATOM    317  N   VAL A  44      49.249  42.979  11.033  1.00124.22           N  
ATOM    318  CA  VAL A  44      48.277  42.171  11.768  1.00121.19           C  
ATOM    319  C   VAL A  44      48.952  41.181  12.714  1.00118.46           C  
ATOM    320  O   VAL A  44      49.829  40.419  12.307  1.00118.52           O  
ATOM    321  CB  VAL A  44      47.351  41.386  10.808  1.00121.58           C  
ATOM    322  CG1 VAL A  44      46.392  40.512  11.605  1.00121.47           C  
ATOM    323  CG2 VAL A  44      46.573  42.354   9.929  1.00121.48           C  
ATOM    324  N   PRO A  45      48.543  41.178  13.993  1.00115.69           N  
ATOM    325  CA  PRO A  45      49.122  40.270  14.987  1.00112.94           C  
ATOM    326  C   PRO A  45      48.855  38.806  14.652  1.00109.98           C  
ATOM    327  O   PRO A  45      47.750  38.445  14.244  1.00109.94           O  
ATOM    328  CB  PRO A  45      48.446  40.707  16.283  1.00113.43           C  
ATOM    329  CG  PRO A  45      47.101  41.160  15.814  1.00114.63           C  
ATOM    330  CD  PRO A  45      47.446  41.966  14.582  1.00115.37           C  
ATOM    331  N   SER A  46      49.874  37.969  14.824  1.00106.25           N  
ATOM    332  CA  SER A  46      49.754  36.545  14.538  1.00102.11           C  
ATOM    333  C   SER A  46      48.717  35.881  15.438  1.00 98.99           C  
ATOM    334  O   SER A  46      47.942  35.036  14.988  1.00 98.58           O  
ATOM    335  CB  SER A  46      51.112  35.854  14.714  1.00102.65           C  
ATOM    336  OG  SER A  46      51.583  35.967  16.047  1.00103.24           O  
ATOM    337  N   THR A  47      48.706  36.272  16.710  1.00 94.97           N  
ATOM    338  CA  THR A  47      47.768  35.715  17.678  1.00 90.83           C  
ATOM    339  C   THR A  47      46.325  35.865  17.204  1.00 87.75           C  
ATOM    340  O   THR A  47      45.524  34.937  17.323  1.00 87.17           O  
ATOM    341  CB  THR A  47      47.911  36.404  19.054  1.00 91.09           C  
ATOM    342  OG1 THR A  47      47.587  37.796  18.932  1.00 90.87           O  
ATOM    343  CG2 THR A  47      49.337  36.264  19.570  1.00 90.77           C  
ATOM    344  N   ALA A  48      46.004  37.038  16.666  1.00 83.58           N  
ATOM    345  CA  ALA A  48      44.662  37.320  16.173  1.00 79.42           C  
ATOM    346  C   ALA A  48      44.276  36.337  15.074  1.00 76.83           C  
ATOM    347  O   ALA A  48      43.222  35.701  15.136  1.00 76.35           O  
ATOM    348  CB  ALA A  48      44.590  38.748  15.648  1.00 79.48           C  
ATOM    349  N   ILE A  49      45.137  36.218  14.069  1.00 73.69           N  
ATOM    350  CA  ILE A  49      44.899  35.310  12.953  1.00 71.43           C  
ATOM    351  C   ILE A  49      44.534  33.906  13.437  1.00 69.61           C  
ATOM    352  O   ILE A  49      43.507  33.346  13.047  1.00 66.68           O  
ATOM    353  CB  ILE A  49      46.151  35.212  12.050  1.00 71.52           C  
ATOM    354  CG1 ILE A  49      46.434  36.571  11.403  1.00 71.15           C  
ATOM    355  CG2 ILE A  49      45.954  34.134  10.990  1.00 72.21           C  
ATOM    356  CD1 ILE A  49      45.301  37.095  10.529  1.00 71.03           C  
ATOM    357  N   ARG A  50      45.389  33.348  14.287  1.00 68.91           N  
ATOM    358  CA  ARG A  50      45.187  32.015  14.840  1.00 68.70           C  
ATOM    359  C   ARG A  50      43.881  31.925  15.631  1.00 68.05           C  
ATOM    360  O   ARG A  50      43.171  30.920  15.563  1.00 67.31           O  
ATOM    361  CB  ARG A  50      46.382  31.651  15.727  1.00 68.81           C  
ATOM    362  CG  ARG A  50      47.699  31.616  14.956  1.00 71.29           C  
ATOM    363  CD  ARG A  50      48.918  31.834  15.845  1.00 72.33           C  
ATOM    364  NE  ARG A  50      49.099  30.786  16.845  1.00 73.34           N  
ATOM    365  CZ  ARG A  50      50.104  30.756  17.714  1.00 74.11           C  
ATOM    366  NH1 ARG A  50      51.019  31.718  17.704  1.00 74.77           N  
ATOM    367  NH2 ARG A  50      50.198  29.766  18.591  1.00 74.50           N  
ATOM    368  N   GLU A  51      43.564  32.981  16.374  1.00 66.91           N  
ATOM    369  CA  GLU A  51      42.342  33.008  17.165  1.00 66.17           C  
ATOM    370  C   GLU A  51      41.126  33.093  16.257  1.00 64.52           C  
ATOM    371  O   GLU A  51      40.182  32.315  16.391  1.00 64.84           O  
ATOM    372  CB  GLU A  51      42.356  34.200  18.125  1.00 68.37           C  
ATOM    373  CG  GLU A  51      43.359  34.067  19.260  1.00 71.06           C  
ATOM    374  CD  GLU A  51      43.089  32.854  20.132  1.00 73.69           C  
ATOM    375  OE1 GLU A  51      42.003  32.790  20.749  1.00 74.65           O  
ATOM    376  OE2 GLU A  51      43.961  31.961  20.196  1.00 74.83           O  
ATOM    377  N   ILE A  52      41.159  34.041  15.329  1.00 62.38           N  
ATOM    378  CA  ILE A  52      40.061  34.232  14.393  1.00 61.48           C  
ATOM    379  C   ILE A  52      39.831  32.982  13.549  1.00 60.41           C  
ATOM    380  O   ILE A  52      38.691  32.632  13.243  1.00 60.47           O  
ATOM    381  CB  ILE A  52      40.335  35.440  13.462  1.00 62.26           C  
ATOM    382  CG1 ILE A  52      40.338  36.732  14.285  1.00 61.73           C  
ATOM    383  CG2 ILE A  52      39.282  35.511  12.364  1.00 63.45           C  
ATOM    384  CD1 ILE A  52      40.719  37.971  13.499  1.00 62.24           C  
ATOM    385  N   SER A  53      40.915  32.304  13.188  1.00 60.45           N  
ATOM    386  CA  SER A  53      40.824  31.093  12.378  1.00 60.20           C  
ATOM    387  C   SER A  53      40.057  29.976  13.074  1.00 59.97           C  
ATOM    388  O   SER A  53      39.310  29.239  12.430  1.00 60.64           O  
ATOM    389  CB  SER A  53      42.224  30.603  11.994  1.00 60.27           C  
ATOM    390  OG  SER A  53      42.832  31.481  11.061  1.00 59.98           O  
ATOM    391  N   LEU A  54      40.238  29.849  14.385  1.00 59.23           N  
ATOM    392  CA  LEU A  54      39.545  28.817  15.149  1.00 59.30           C  
ATOM    393  C   LEU A  54      38.035  28.994  15.007  1.00 59.88           C  
ATOM    394  O   LEU A  54      37.281  28.021  14.974  1.00 59.29           O  
ATOM    395  CB  LEU A  54      39.922  28.912  16.627  1.00 60.85           C  
ATOM    396  CG  LEU A  54      41.403  28.808  17.007  1.00 63.56           C  
ATOM    397  CD1 LEU A  54      41.572  29.177  18.471  1.00 63.80           C  
ATOM    398  CD2 LEU A  54      41.921  27.399  16.744  1.00 64.09           C  
ATOM    399  N   LEU A  55      37.609  30.251  14.919  1.00 58.82           N  
ATOM    400  CA  LEU A  55      36.201  30.595  14.793  1.00 57.35           C  
ATOM    401  C   LEU A  55      35.559  29.988  13.555  1.00 56.48           C  
ATOM    402  O   LEU A  55      34.339  29.848  13.490  1.00 56.53           O  
ATOM    403  CB  LEU A  55      36.040  32.116  14.763  1.00 57.50           C  
ATOM    404  CG  LEU A  55      36.520  32.854  16.011  1.00 57.91           C  
ATOM    405  CD1 LEU A  55      36.521  34.346  15.747  1.00 60.01           C  
ATOM    406  CD2 LEU A  55      35.626  32.519  17.195  1.00 56.30           C  
ATOM    407  N   LYS A  56      36.375  29.632  12.569  1.00 55.99           N  
ATOM    408  CA  LYS A  56      35.847  29.035  11.345  1.00 55.92           C  
ATOM    409  C   LYS A  56      35.217  27.678  11.631  1.00 55.71           C  
ATOM    410  O   LYS A  56      34.427  27.168  10.834  1.00 53.07           O  
ATOM    411  CB  LYS A  56      36.949  28.858  10.300  1.00 55.06           C  
ATOM    412  CG  LYS A  56      37.418  30.149   9.663  1.00 57.06           C  
ATOM    413  CD  LYS A  56      38.208  29.894   8.378  1.00 57.12           C  
ATOM    414  CE  LYS A  56      39.449  29.046   8.625  1.00 57.41           C  
ATOM    415  NZ  LYS A  56      40.280  28.898   7.391  1.00 56.07           N  
ATOM    416  N   GLU A  57      35.573  27.101  12.775  1.00 55.58           N  
ATOM    417  CA  GLU A  57      35.059  25.797  13.155  1.00 57.31           C  
ATOM    418  C   GLU A  57      33.779  25.840  13.972  1.00 56.06           C  
ATOM    419  O   GLU A  57      32.958  24.928  13.873  1.00 54.78           O  
ATOM    420  CB  GLU A  57      36.134  25.014  13.909  1.00 60.97           C  
ATOM    421  CG  GLU A  57      37.017  24.185  13.002  1.00 67.10           C  
ATOM    422  CD  GLU A  57      37.492  24.960  11.791  1.00 70.95           C  
ATOM    423  OE1 GLU A  57      38.281  25.915  11.962  1.00 74.63           O  
ATOM    424  OE2 GLU A  57      37.068  24.616  10.666  1.00 72.39           O  
ATOM    425  N   LEU A  58      33.597  26.891  14.768  1.00 54.78           N  
ATOM    426  CA  LEU A  58      32.393  26.988  15.577  1.00 54.19           C  
ATOM    427  C   LEU A  58      31.189  27.341  14.720  1.00 52.36           C  
ATOM    428  O   LEU A  58      30.884  28.507  14.488  1.00 53.71           O  
ATOM    429  CB  LEU A  58      32.573  28.000  16.722  1.00 56.73           C  
ATOM    430  CG  LEU A  58      32.821  29.502  16.543  1.00 58.97           C  
ATOM    431  CD1 LEU A  58      31.516  30.258  16.347  1.00 59.01           C  
ATOM    432  CD2 LEU A  58      33.502  30.021  17.800  1.00 59.69           C  
ATOM    433  N   ASN A  59      30.512  26.312  14.233  1.00 49.46           N  
ATOM    434  CA  ASN A  59      29.336  26.512  13.409  1.00 47.64           C  
ATOM    435  C   ASN A  59      28.093  26.091  14.182  1.00 44.62           C  
ATOM    436  O   ASN A  59      28.079  25.056  14.852  1.00 43.95           O  
ATOM    437  CB  ASN A  59      29.453  25.717  12.105  1.00 50.45           C  
ATOM    438  CG  ASN A  59      30.620  26.182  11.238  1.00 52.20           C  
ATOM    439  OD1 ASN A  59      31.781  25.884  11.524  1.00 54.23           O  
ATOM    440  ND2 ASN A  59      30.313  26.923  10.179  1.00 53.03           N  
ATOM    441  N   HIS A  60      27.053  26.911  14.099  1.00 40.84           N  
ATOM    442  CA  HIS A  60      25.803  26.639  14.794  1.00 36.53           C  
ATOM    443  C   HIS A  60      24.690  27.341  14.029  1.00 34.73           C  
ATOM    444  O   HIS A  60      24.914  28.387  13.433  1.00 34.07           O  
ATOM    445  CB  HIS A  60      25.881  27.182  16.224  1.00 35.86           C  
ATOM    446  CG  HIS A  60      24.657  26.914  17.042  1.00 32.92           C  
ATOM    447  ND1 HIS A  60      24.466  25.740  17.735  1.00 33.88           N  
ATOM    448  CD2 HIS A  60      23.553  27.665  17.262  1.00 34.33           C  
ATOM    449  CE1 HIS A  60      23.297  25.778  18.351  1.00 33.43           C  
ATOM    450  NE2 HIS A  60      22.723  26.937  18.079  1.00 34.18           N  
ATOM    451  N   PRO A  61      23.480  26.769  14.033  1.00 35.31           N  
ATOM    452  CA  PRO A  61      22.317  27.336  13.338  1.00 35.63           C  
ATOM    453  C   PRO A  61      22.020  28.782  13.730  1.00 36.57           C  
ATOM    454  O   PRO A  61      21.442  29.536  12.945  1.00 37.31           O  
ATOM    455  CB  PRO A  61      21.180  26.409  13.756  1.00 36.95           C  
ATOM    456  CG  PRO A  61      21.869  25.099  13.960  1.00 38.47           C  
ATOM    457  CD  PRO A  61      23.127  25.496  14.687  1.00 35.96           C  
ATOM    458  N   ASN A  62      22.412  29.163  14.944  1.00 35.16           N  
ATOM    459  CA  ASN A  62      22.154  30.513  15.426  1.00 33.74           C  
ATOM    460  C   ASN A  62      23.397  31.373  15.545  1.00 32.34           C  
ATOM    461  O   ASN A  62      23.431  32.358  16.288  1.00 29.76           O  
ATOM    462  CB  ASN A  62      21.409  30.463  16.759  1.00 32.27           C  
ATOM    463  CG  ASN A  62      20.083  29.750  16.643  1.00 30.41           C  
ATOM    464  OD1 ASN A  62      19.926  28.629  17.117  1.00 30.46           O  
ATOM    465  ND2 ASN A  62      19.121  30.394  15.992  1.00 32.20           N  
ATOM    466  N   ILE A  63      24.420  30.990  14.797  1.00 31.12           N  
ATOM    467  CA  ILE A  63      25.654  31.748  14.764  1.00 32.60           C  
ATOM    468  C   ILE A  63      25.944  32.032  13.300  1.00 32.71           C  
ATOM    469  O   ILE A  63      25.903  31.125  12.468  1.00 32.25           O  
ATOM    470  CB  ILE A  63      26.817  30.959  15.395  1.00 34.04           C  
ATOM    471  CG1 ILE A  63      26.587  30.835  16.904  1.00 36.10           C  
ATOM    472  CG2 ILE A  63      28.131  31.667  15.134  1.00 32.88           C  
ATOM    473  CD1 ILE A  63      27.667  30.068  17.625  1.00 41.25           C  
ATOM    474  N   VAL A  64      26.191  33.298  12.984  1.00 33.23           N  
ATOM    475  CA  VAL A  64      26.497  33.695  11.612  1.00 34.66           C  
ATOM    476  C   VAL A  64      27.790  33.006  11.192  1.00 36.88           C  
ATOM    477  O   VAL A  64      28.867  33.298  11.723  1.00 35.95           O  
ATOM    478  CB  VAL A  64      26.683  35.223  11.495  1.00 34.89           C  
ATOM    479  CG1 VAL A  64      27.201  35.593  10.100  1.00 32.95           C  
ATOM    480  CG2 VAL A  64      25.360  35.916  11.754  1.00 36.94           C  
ATOM    481  N   LYS A  65      27.673  32.092  10.235  1.00 38.06           N  
ATOM    482  CA  LYS A  65      28.821  31.342   9.753  1.00 41.47           C  
ATOM    483  C   LYS A  65      29.931  32.180   9.125  1.00 41.01           C  
ATOM    484  O   LYS A  65      29.688  33.031   8.269  1.00 39.22           O  
ATOM    485  CB  LYS A  65      28.374  30.281   8.746  1.00 44.30           C  
ATOM    486  CG  LYS A  65      29.508  29.384   8.261  1.00 47.86           C  
ATOM    487  CD  LYS A  65      29.039  28.425   7.179  1.00 52.83           C  
ATOM    488  CE  LYS A  65      30.187  27.570   6.665  1.00 53.54           C  
ATOM    489  NZ  LYS A  65      29.761  26.693   5.538  1.00 55.13           N  
ATOM    490  N   LEU A  66      31.153  31.925   9.576  1.00 41.41           N  
ATOM    491  CA  LEU A  66      32.336  32.594   9.056  1.00 43.18           C  
ATOM    492  C   LEU A  66      32.881  31.634   8.006  1.00 45.54           C  
ATOM    493  O   LEU A  66      33.456  30.603   8.342  1.00 45.21           O  
ATOM    494  CB  LEU A  66      33.361  32.787  10.172  1.00 41.73           C  
ATOM    495  CG  LEU A  66      34.759  33.291   9.814  1.00 42.36           C  
ATOM    496  CD1 LEU A  66      34.687  34.621   9.065  1.00 41.15           C  
ATOM    497  CD2 LEU A  66      35.552  33.439  11.107  1.00 41.73           C  
ATOM    498  N   LEU A  67      32.677  31.966   6.736  1.00 47.89           N  
ATOM    499  CA  LEU A  67      33.130  31.116   5.646  1.00 50.24           C  
ATOM    500  C   LEU A  67      34.645  31.074   5.514  1.00 52.02           C  
ATOM    501  O   LEU A  67      35.250  30.004   5.581  1.00 52.69           O  
ATOM    502  CB  LEU A  67      32.509  31.571   4.319  1.00 49.63           C  
ATOM    503  CG  LEU A  67      30.998  31.388   4.117  1.00 49.68           C  
ATOM    504  CD1 LEU A  67      30.632  29.930   4.315  1.00 51.02           C  
ATOM    505  CD2 LEU A  67      30.225  32.249   5.093  1.00 51.27           C  
ATOM    506  N   ASP A  68      35.262  32.236   5.333  1.00 53.65           N  
ATOM    507  CA  ASP A  68      36.707  32.290   5.175  1.00 54.64           C  
ATOM    508  C   ASP A  68      37.350  33.550   5.746  1.00 55.42           C  
ATOM    509  O   ASP A  68      36.724  34.608   5.833  1.00 55.76           O  
ATOM    510  CB  ASP A  68      37.072  32.177   3.689  1.00 55.13           C  
ATOM    511  CG  ASP A  68      36.651  30.852   3.076  1.00 56.36           C  
ATOM    512  OD1 ASP A  68      37.218  29.811   3.467  1.00 56.98           O  
ATOM    513  OD2 ASP A  68      35.754  30.852   2.204  1.00 55.84           O  
ATOM    514  N   VAL A  69      38.610  33.411   6.139  1.00 56.02           N  
ATOM    515  CA  VAL A  69      39.393  34.518   6.666  1.00 57.94           C  
ATOM    516  C   VAL A  69      40.511  34.755   5.660  1.00 59.50           C  
ATOM    517  O   VAL A  69      41.374  33.901   5.460  1.00 59.18           O  
ATOM    518  CB  VAL A  69      40.022  34.188   8.037  1.00 57.21           C  
ATOM    519  CG1 VAL A  69      40.968  35.304   8.450  1.00 55.55           C  
ATOM    520  CG2 VAL A  69      38.934  34.013   9.084  1.00 57.42           C  
ATOM    521  N   ILE A  70      40.485  35.915   5.020  1.00 61.44           N  
ATOM    522  CA  ILE A  70      41.489  36.249   4.030  1.00 63.47           C  
ATOM    523  C   ILE A  70      42.473  37.277   4.569  1.00 65.88           C  
ATOM    524  O   ILE A  70      42.086  38.362   5.005  1.00 64.89           O  
ATOM    525  CB  ILE A  70      40.831  36.799   2.753  1.00 63.30           C  
ATOM    526  CG1 ILE A  70      39.808  35.790   2.223  1.00 63.16           C  
ATOM    527  CG2 ILE A  70      41.891  37.086   1.702  1.00 62.57           C  
ATOM    528  CD1 ILE A  70      39.070  36.250   0.978  1.00 63.63           C  
ATOM    529  N   HIS A  71      43.751  36.920   4.544  1.00 69.51           N  
ATOM    530  CA  HIS A  71      44.800  37.809   5.016  1.00 72.72           C  
ATOM    531  C   HIS A  71      45.789  38.037   3.882  1.00 75.50           C  
ATOM    532  O   HIS A  71      46.743  37.280   3.719  1.00 75.68           O  
ATOM    533  CB  HIS A  71      45.521  37.188   6.213  1.00 72.09           C  
ATOM    534  CG  HIS A  71      46.606  38.050   6.776  1.00 71.44           C  
ATOM    535  ND1 HIS A  71      47.580  37.562   7.620  1.00 72.18           N  
ATOM    536  CD2 HIS A  71      46.868  39.369   6.621  1.00 71.59           C  
ATOM    537  CE1 HIS A  71      48.397  38.544   7.959  1.00 72.22           C  
ATOM    538  NE2 HIS A  71      47.987  39.651   7.367  1.00 72.28           N  
ATOM    539  N   THR A  72      45.545  39.076   3.089  1.00 79.18           N  
ATOM    540  CA  THR A  72      46.419  39.402   1.968  1.00 82.64           C  
ATOM    541  C   THR A  72      46.979  40.806   2.146  1.00 83.92           C  
ATOM    542  O   THR A  72      46.314  41.680   2.702  1.00 83.75           O  
ATOM    543  CB  THR A  72      45.663  39.325   0.624  1.00 83.77           C  
ATOM    544  OG1 THR A  72      45.185  37.989   0.419  1.00 85.17           O  
ATOM    545  CG2 THR A  72      46.579  39.706  -0.529  1.00 84.73           C  
ATOM    546  N   GLU A  73      48.204  41.014   1.672  1.00 85.62           N  
ATOM    547  CA  GLU A  73      48.865  42.308   1.792  1.00 87.17           C  
ATOM    548  C   GLU A  73      48.857  42.725   3.260  1.00 87.04           C  
ATOM    549  O   GLU A  73      48.815  43.911   3.591  1.00 87.03           O  
ATOM    550  CB  GLU A  73      48.149  43.355   0.932  1.00 88.39           C  
ATOM    551  CG  GLU A  73      48.875  44.691   0.845  1.00 90.14           C  
ATOM    552  CD  GLU A  73      48.195  45.663  -0.097  1.00 91.68           C  
ATOM    553  OE1 GLU A  73      48.666  46.814  -0.209  1.00 92.14           O  
ATOM    554  OE2 GLU A  73      47.189  45.274  -0.728  1.00 93.17           O  
ATOM    555  N   ASN A  74      48.891  41.725   4.135  1.00 86.96           N  
ATOM    556  CA  ASN A  74      48.891  41.945   5.574  1.00 86.90           C  
ATOM    557  C   ASN A  74      47.640  42.659   6.078  1.00 85.48           C  
ATOM    558  O   ASN A  74      47.694  43.405   7.055  1.00 85.89           O  
ATOM    559  CB  ASN A  74      50.140  42.729   5.985  1.00 88.79           C  
ATOM    560  CG  ASN A  74      51.409  41.912   5.843  1.00 90.04           C  
ATOM    561  OD1 ASN A  74      51.728  41.420   4.760  1.00 90.67           O  
ATOM    562  ND2 ASN A  74      52.141  41.761   6.942  1.00 90.68           N  
ATOM    563  N   LYS A  75      46.515  42.427   5.407  1.00 83.16           N  
ATOM    564  CA  LYS A  75      45.249  43.038   5.803  1.00 79.68           C  
ATOM    565  C   LYS A  75      44.264  41.926   6.164  1.00 76.65           C  
ATOM    566  O   LYS A  75      44.438  40.779   5.748  1.00 76.57           O  
ATOM    567  CB  LYS A  75      44.684  43.891   4.661  1.00 80.22           C  
ATOM    568  CG  LYS A  75      45.716  44.745   3.926  1.00 80.55           C  
ATOM    569  CD  LYS A  75      46.602  45.573   4.863  1.00 80.83           C  
ATOM    570  CE  LYS A  75      45.815  46.586   5.683  1.00 81.48           C  
ATOM    571  NZ  LYS A  75      45.048  45.965   6.799  1.00 81.52           N  
ATOM    572  N   LEU A  76      43.234  42.256   6.937  1.00 72.59           N  
ATOM    573  CA  LEU A  76      42.255  41.252   7.339  1.00 67.85           C  
ATOM    574  C   LEU A  76      40.882  41.396   6.699  1.00 64.14           C  
ATOM    575  O   LEU A  76      40.303  42.481   6.661  1.00 64.12           O  
ATOM    576  CB  LEU A  76      42.100  41.238   8.860  1.00 68.20           C  
ATOM    577  CG  LEU A  76      42.954  40.211   9.606  1.00 68.63           C  
ATOM    578  CD1 LEU A  76      42.735  40.352  11.104  1.00 68.83           C  
ATOM    579  CD2 LEU A  76      42.585  38.811   9.141  1.00 69.01           C  
ATOM    580  N   TYR A  77      40.373  40.277   6.199  1.00 59.34           N  
ATOM    581  CA  TYR A  77      39.064  40.220   5.569  1.00 54.72           C  
ATOM    582  C   TYR A  77      38.326  39.012   6.118  1.00 51.23           C  
ATOM    583  O   TYR A  77      38.785  37.877   5.972  1.00 50.44           O  
ATOM    584  CB  TYR A  77      39.192  40.061   4.055  1.00 56.61           C  
ATOM    585  CG  TYR A  77      39.574  41.316   3.306  1.00 61.26           C  
ATOM    586  CD1 TYR A  77      38.628  42.303   3.030  1.00 61.58           C  
ATOM    587  CD2 TYR A  77      40.882  41.513   2.860  1.00 62.73           C  
ATOM    588  CE1 TYR A  77      38.975  43.454   2.325  1.00 64.05           C  
ATOM    589  CE2 TYR A  77      41.239  42.662   2.156  1.00 65.03           C  
ATOM    590  CZ  TYR A  77      40.281  43.627   1.892  1.00 65.11           C  
ATOM    591  OH  TYR A  77      40.631  44.763   1.198  1.00 66.61           O  
ATOM    592  N   LEU A  78      37.198  39.258   6.771  1.00 47.11           N  
ATOM    593  CA  LEU A  78      36.383  38.175   7.299  1.00 44.52           C  
ATOM    594  C   LEU A  78      35.226  38.050   6.329  1.00 42.14           C  
ATOM    595  O   LEU A  78      34.541  39.033   6.043  1.00 40.69           O  
ATOM    596  CB  LEU A  78      35.855  38.513   8.699  1.00 44.64           C  
ATOM    597  CG  LEU A  78      36.897  38.711   9.804  1.00 45.93           C  
ATOM    598  CD1 LEU A  78      36.200  39.085  11.103  1.00 47.25           C  
ATOM    599  CD2 LEU A  78      37.702  37.434   9.982  1.00 47.53           C  
ATOM    600  N   VAL A  79      35.027  36.855   5.792  1.00 41.75           N  
ATOM    601  CA  VAL A  79      33.933  36.647   4.858  1.00 41.87           C  
ATOM    602  C   VAL A  79      32.854  35.878   5.600  1.00 41.57           C  
ATOM    603  O   VAL A  79      33.062  34.740   6.028  1.00 41.75           O  
ATOM    604  CB  VAL A  79      34.390  35.858   3.614  1.00 44.06           C  
ATOM    605  CG1 VAL A  79      33.256  35.797   2.585  1.00 41.22           C  
ATOM    606  CG2 VAL A  79      35.628  36.515   3.011  1.00 43.32           C  
ATOM    607  N   PHE A  80      31.703  36.514   5.764  1.00 40.06           N  
ATOM    608  CA  PHE A  80      30.596  35.900   6.476  1.00 38.35           C  
ATOM    609  C   PHE A  80      29.404  35.586   5.581  1.00 38.06           C  
ATOM    610  O   PHE A  80      29.240  36.152   4.501  1.00 37.64           O  
ATOM    611  CB  PHE A  80      30.115  36.825   7.601  1.00 36.38           C  
ATOM    612  CG  PHE A  80      31.057  36.936   8.769  1.00 36.32           C  
ATOM    613  CD1 PHE A  80      31.112  35.936   9.731  1.00 36.08           C  
ATOM    614  CD2 PHE A  80      31.852  38.064   8.933  1.00 36.96           C  
ATOM    615  CE1 PHE A  80      31.944  36.062  10.843  1.00 35.86           C  
ATOM    616  CE2 PHE A  80      32.685  38.200  10.040  1.00 38.43           C  
ATOM    617  CZ  PHE A  80      32.731  37.196  10.998  1.00 37.01           C  
ATOM    618  N   GLU A  81      28.582  34.667   6.064  1.00 36.66           N  
ATOM    619  CA  GLU A  81      27.340  34.267   5.416  1.00 37.65           C  
ATOM    620  C   GLU A  81      26.491  35.544   5.484  1.00 34.92           C  
ATOM    621  O   GLU A  81      26.473  36.209   6.514  1.00 35.91           O  
ATOM    622  CB  GLU A  81      26.701  33.155   6.255  1.00 38.49           C  
ATOM    623  CG  GLU A  81      25.242  32.885   6.017  1.00 43.84           C  
ATOM    624  CD  GLU A  81      24.611  32.097   7.166  1.00 46.89           C  
ATOM    625  OE1 GLU A  81      23.482  31.590   6.990  1.00 49.58           O  
ATOM    626  OE2 GLU A  81      25.238  31.997   8.249  1.00 44.32           O  
ATOM    627  N   PHE A  82      25.799  35.896   4.408  1.00 32.85           N  
ATOM    628  CA  PHE A  82      24.985  37.115   4.408  1.00 32.62           C  
ATOM    629  C   PHE A  82      23.535  36.893   4.834  1.00 32.63           C  
ATOM    630  O   PHE A  82      22.903  35.913   4.428  1.00 31.82           O  
ATOM    631  CB  PHE A  82      24.983  37.755   3.015  1.00 32.13           C  
ATOM    632  CG  PHE A  82      24.164  39.020   2.922  1.00 32.79           C  
ATOM    633  CD1 PHE A  82      24.652  40.219   3.433  1.00 34.44           C  
ATOM    634  CD2 PHE A  82      22.904  39.013   2.335  1.00 29.33           C  
ATOM    635  CE1 PHE A  82      23.894  41.388   3.357  1.00 33.07           C  
ATOM    636  CE2 PHE A  82      22.140  40.168   2.254  1.00 31.87           C  
ATOM    637  CZ  PHE A  82      22.636  41.363   2.767  1.00 32.76           C  
ATOM    638  N   LEU A  83      23.024  37.808   5.658  1.00 33.33           N  
ATOM    639  CA  LEU A  83      21.632  37.777   6.107  1.00 34.10           C  
ATOM    640  C   LEU A  83      21.000  39.098   5.675  1.00 35.11           C  
ATOM    641  O   LEU A  83      21.681  40.127   5.601  1.00 33.61           O  
ATOM    642  CB  LEU A  83      21.531  37.585   7.624  1.00 35.87           C  
ATOM    643  CG  LEU A  83      21.660  36.119   8.085  1.00 38.04           C  
ATOM    644  CD1 LEU A  83      23.125  35.754   8.232  1.00 37.40           C  
ATOM    645  CD2 LEU A  83      20.940  35.912   9.404  1.00 38.03           C  
ATOM    646  N   HIS A  84      19.702  39.084   5.390  1.00 36.66           N  
ATOM    647  CA  HIS A  84      19.047  40.293   4.905  1.00 39.13           C  
ATOM    648  C   HIS A  84      18.700  41.410   5.865  1.00 39.60           C  
ATOM    649  O   HIS A  84      18.425  42.531   5.428  1.00 39.74           O  
ATOM    650  CB  HIS A  84      17.800  39.924   4.107  1.00 43.84           C  
ATOM    651  CG  HIS A  84      18.099  39.516   2.700  1.00 47.02           C  
ATOM    652  ND1 HIS A  84      18.664  38.300   2.382  1.00 47.23           N  
ATOM    653  CD2 HIS A  84      17.969  40.189   1.532  1.00 46.79           C  
ATOM    654  CE1 HIS A  84      18.868  38.240   1.079  1.00 48.16           C  
ATOM    655  NE2 HIS A  84      18.455  39.373   0.540  1.00 48.05           N  
ATOM    656  N   GLN A  85      18.717  41.146   7.164  1.00 37.54           N  
ATOM    657  CA  GLN A  85      18.376  42.227   8.074  1.00 36.77           C  
ATOM    658  C   GLN A  85      18.915  42.078   9.489  1.00 35.36           C  
ATOM    659  O   GLN A  85      19.053  40.966  10.003  1.00 35.70           O  
ATOM    660  CB  GLN A  85      16.847  42.381   8.104  1.00 34.65           C  
ATOM    661  CG  GLN A  85      16.355  43.691   8.686  1.00 35.96           C  
ATOM    662  CD  GLN A  85      14.919  43.994   8.284  1.00 38.34           C  
ATOM    663  OE1 GLN A  85      14.621  44.219   7.103  1.00 37.38           O  
ATOM    664  NE2 GLN A  85      14.021  43.997   9.264  1.00 36.00           N  
ATOM    665  N   ASP A  86      19.230  43.209  10.113  1.00 34.12           N  
ATOM    666  CA  ASP A  86      19.708  43.186  11.486  1.00 34.11           C  
ATOM    667  C   ASP A  86      18.524  43.496  12.389  1.00 33.60           C  
ATOM    668  O   ASP A  86      17.488  43.969  11.925  1.00 33.59           O  
ATOM    669  CB  ASP A  86      20.837  44.196  11.701  1.00 35.72           C  
ATOM    670  CG  ASP A  86      20.373  45.632  11.627  1.00 36.70           C  
ATOM    671  OD1 ASP A  86      19.201  45.887  11.294  1.00 43.92           O  
ATOM    672  OD2 ASP A  86      21.199  46.514  11.907  1.00 36.23           O  
ATOM    673  N   LEU A  87      18.674  43.224  13.677  1.00 33.92           N  
ATOM    674  CA  LEU A  87      17.594  43.451  14.626  1.00 32.94           C  
ATOM    675  C   LEU A  87      17.220  44.921  14.782  1.00 34.89           C  
ATOM    676  O   LEU A  87      16.040  45.257  14.934  1.00 35.37           O  
ATOM    677  CB  LEU A  87      17.970  42.858  15.980  1.00 31.21           C  
ATOM    678  CG  LEU A  87      16.834  42.738  16.991  1.00 31.43           C  
ATOM    679  CD1 LEU A  87      15.702  41.879  16.413  1.00 26.84           C  
ATOM    680  CD2 LEU A  87      17.384  42.121  18.271  1.00 29.92           C  
ATOM    681  N   LYS A  88      18.222  45.794  14.750  1.00 36.50           N  
ATOM    682  CA  LYS A  88      17.994  47.229  14.882  1.00 37.90           C  
ATOM    683  C   LYS A  88      16.945  47.703  13.881  1.00 37.87           C  
ATOM    684  O   LYS A  88      15.892  48.213  14.269  1.00 38.45           O  
ATOM    685  CB  LYS A  88      19.308  47.989  14.664  1.00 40.43           C  
ATOM    686  CG  LYS A  88      19.175  49.513  14.633  1.00 42.03           C  
ATOM    687  CD  LYS A  88      18.769  50.088  15.978  1.00 43.39           C  
ATOM    688  CE  LYS A  88      18.969  51.603  15.996  1.00 45.64           C  
ATOM    689  NZ  LYS A  88      18.252  52.296  14.878  1.00 49.46           N  
ATOM    690  N   LYS A  89      17.236  47.525  12.594  1.00 39.63           N  
ATOM    691  CA  LYS A  89      16.320  47.931  11.531  1.00 40.53           C  
ATOM    692  C   LYS A  89      14.949  47.295  11.689  1.00 39.74           C  
ATOM    693  O   LYS A  89      13.931  47.979  11.603  1.00 41.03           O  
ATOM    694  CB  LYS A  89      16.890  47.558  10.157  1.00 44.35           C  
ATOM    695  CG  LYS A  89      17.993  48.477   9.646  1.00 50.63           C  
ATOM    696  CD  LYS A  89      17.471  49.887   9.399  1.00 53.97           C  
ATOM    697  CE  LYS A  89      18.453  50.716   8.580  1.00 55.89           C  
ATOM    698  NZ  LYS A  89      19.782  50.835   9.232  1.00 56.83           N  
ATOM    699  N   PHE A  90      14.921  45.982  11.905  1.00 38.28           N  
ATOM    700  CA  PHE A  90      13.655  45.290  12.079  1.00 37.77           C  
ATOM    701  C   PHE A  90      12.853  45.966  13.192  1.00 39.35           C  
ATOM    702  O   PHE A  90      11.648  46.178  13.057  1.00 37.43           O  
ATOM    703  CB  PHE A  90      13.887  43.815  12.415  1.00 35.56           C  
ATOM    704  CG  PHE A  90      12.615  43.035  12.617  1.00 35.28           C  
ATOM    705  CD1 PHE A  90      11.642  42.996  11.622  1.00 34.70           C  
ATOM    706  CD2 PHE A  90      12.384  42.346  13.806  1.00 33.20           C  
ATOM    707  CE1 PHE A  90      10.457  42.283  11.805  1.00 33.68           C  
ATOM    708  CE2 PHE A  90      11.208  41.631  14.001  1.00 33.93           C  
ATOM    709  CZ  PHE A  90      10.238  41.597  12.998  1.00 33.74           C  
ATOM    710  N   MET A  91      13.530  46.313  14.284  1.00 41.06           N  
ATOM    711  CA  MET A  91      12.874  46.979  15.410  1.00 44.92           C  
ATOM    712  C   MET A  91      12.327  48.344  15.005  1.00 44.69           C  
ATOM    713  O   MET A  91      11.166  48.647  15.266  1.00 44.06           O  
ATOM    714  CB  MET A  91      13.841  47.143  16.589  1.00 45.41           C  
ATOM    715  CG  MET A  91      14.224  45.832  17.264  1.00 49.78           C  
ATOM    716  SD  MET A  91      15.342  46.053  18.669  1.00 53.14           S  
ATOM    717  CE  MET A  91      14.172  46.527  19.929  1.00 51.96           C  
ATOM    718  N   ASP A  92      13.161  49.166  14.375  1.00 45.13           N  
ATOM    719  CA  ASP A  92      12.712  50.483  13.931  1.00 47.00           C  
ATOM    720  C   ASP A  92      11.458  50.343  13.065  1.00 47.76           C  
ATOM    721  O   ASP A  92      10.530  51.141  13.171  1.00 49.45           O  
ATOM    722  CB  ASP A  92      13.805  51.196  13.124  1.00 45.22           C  
ATOM    723  CG  ASP A  92      15.016  51.551  13.961  1.00 45.71           C  
ATOM    724  OD1 ASP A  92      14.858  51.789  15.176  1.00 46.66           O  
ATOM    725  OD2 ASP A  92      16.128  51.612  13.398  1.00 47.07           O  
ATOM    726  N   ALA A  93      11.437  49.318  12.218  1.00 48.46           N  
ATOM    727  CA  ALA A  93      10.303  49.065  11.329  1.00 48.88           C  
ATOM    728  C   ALA A  93       9.084  48.523  12.072  1.00 49.27           C  
ATOM    729  O   ALA A  93       7.975  48.528  11.540  1.00 50.78           O  
ATOM    730  CB  ALA A  93      10.713  48.088  10.226  1.00 47.49           C  
ATOM    731  N   SER A  94       9.296  48.049  13.297  1.00 49.48           N  
ATOM    732  CA  SER A  94       8.221  47.502  14.119  1.00 48.02           C  
ATOM    733  C   SER A  94       7.811  48.517  15.181  1.00 49.13           C  
ATOM    734  O   SER A  94       6.888  48.281  15.949  1.00 49.77           O  
ATOM    735  CB  SER A  94       8.683  46.215  14.819  1.00 46.92           C  
ATOM    736  OG  SER A  94       9.038  45.190  13.900  1.00 47.38           O  
ATOM    737  N   ALA A  95       8.511  49.645  15.218  1.00 50.26           N  
ATOM    738  CA  ALA A  95       8.254  50.697  16.198  1.00 52.64           C  
ATOM    739  C   ALA A  95       6.783  50.999  16.506  1.00 54.44           C  
ATOM    740  O   ALA A  95       6.369  50.951  17.665  1.00 54.77           O  
ATOM    741  CB  ALA A  95       8.955  51.975  15.768  1.00 52.53           C  
ATOM    742  N   LEU A  96       6.000  51.311  15.477  1.00 55.29           N  
ATOM    743  CA  LEU A  96       4.593  51.654  15.668  1.00 56.82           C  
ATOM    744  C   LEU A  96       3.761  50.567  16.329  1.00 56.91           C  
ATOM    745  O   LEU A  96       3.006  50.838  17.263  1.00 58.38           O  
ATOM    746  CB  LEU A  96       3.946  52.035  14.333  1.00 58.22           C  
ATOM    747  CG  LEU A  96       4.535  53.235  13.586  1.00 60.45           C  
ATOM    748  CD1 LEU A  96       3.666  53.543  12.374  1.00 61.23           C  
ATOM    749  CD2 LEU A  96       4.608  54.446  14.506  1.00 60.92           C  
ATOM    750  N   THR A  97       3.892  49.341  15.841  1.00 56.14           N  
ATOM    751  CA  THR A  97       3.134  48.222  16.383  1.00 55.30           C  
ATOM    752  C   THR A  97       3.903  47.477  17.463  1.00 53.84           C  
ATOM    753  O   THR A  97       3.369  47.170  18.527  1.00 53.72           O  
ATOM    754  CB  THR A  97       2.784  47.213  15.281  1.00 56.59           C  
ATOM    755  OG1 THR A  97       3.990  46.630  14.771  1.00 56.50           O  
ATOM    756  CG2 THR A  97       2.045  47.902  14.147  1.00 58.12           C  
ATOM    757  N   GLY A  98       5.164  47.184  17.172  1.00 51.92           N  
ATOM    758  CA  GLY A  98       5.994  46.450  18.105  1.00 49.47           C  
ATOM    759  C   GLY A  98       6.083  45.005  17.656  1.00 47.66           C  
ATOM    760  O   GLY A  98       5.150  44.479  17.056  1.00 48.48           O  
ATOM    761  N   ILE A  99       7.210  44.364  17.935  1.00 46.53           N  
ATOM    762  CA  ILE A  99       7.408  42.973  17.555  1.00 44.22           C  
ATOM    763  C   ILE A  99       6.492  42.095  18.393  1.00 43.36           C  
ATOM    764  O   ILE A  99       6.451  42.225  19.613  1.00 44.19           O  
ATOM    765  CB  ILE A  99       8.869  42.537  17.796  1.00 43.90           C  
ATOM    766  CG1 ILE A  99       9.823  43.508  17.102  1.00 43.35           C  
ATOM    767  CG2 ILE A  99       9.091  41.131  17.273  1.00 44.01           C  
ATOM    768  CD1 ILE A  99      11.293  43.196  17.344  1.00 44.21           C  
ATOM    769  N   PRO A 100       5.730  41.198  17.748  1.00 42.62           N  
ATOM    770  CA  PRO A 100       4.820  40.309  18.480  1.00 41.76           C  
ATOM    771  C   PRO A 100       5.592  39.519  19.533  1.00 41.45           C  
ATOM    772  O   PRO A 100       6.738  39.129  19.297  1.00 39.74           O  
ATOM    773  CB  PRO A 100       4.266  39.401  17.381  1.00 42.18           C  
ATOM    774  CG  PRO A 100       4.293  40.279  16.172  1.00 41.77           C  
ATOM    775  CD  PRO A 100       5.629  40.974  16.295  1.00 42.76           C  
ATOM    776  N   LEU A 101       4.964  39.278  20.683  1.00 39.43           N  
ATOM    777  CA  LEU A 101       5.613  38.540  21.758  1.00 38.26           C  
ATOM    778  C   LEU A 101       6.080  37.145  21.340  1.00 37.47           C  
ATOM    779  O   LEU A 101       7.183  36.725  21.694  1.00 37.78           O  
ATOM    780  CB  LEU A 101       4.688  38.412  22.972  1.00 39.05           C  
ATOM    781  CG  LEU A 101       5.336  37.637  24.129  1.00 43.92           C  
ATOM    782  CD1 LEU A 101       6.483  38.465  24.712  1.00 43.19           C  
ATOM    783  CD2 LEU A 101       4.307  37.325  25.203  1.00 44.43           C  
ATOM    784  N   PRO A 102       5.241  36.398  20.599  1.00 33.99           N  
ATOM    785  CA  PRO A 102       5.691  35.063  20.196  1.00 30.68           C  
ATOM    786  C   PRO A 102       7.023  35.126  19.437  1.00 28.70           C  
ATOM    787  O   PRO A 102       7.853  34.231  19.552  1.00 26.25           O  
ATOM    788  CB  PRO A 102       4.536  34.555  19.322  1.00 29.70           C  
ATOM    789  CG  PRO A 102       3.317  35.216  19.969  1.00 31.01           C  
ATOM    790  CD  PRO A 102       3.833  36.630  20.219  1.00 31.14           C  
ATOM    791  N   LEU A 103       7.224  36.193  18.672  1.00 28.31           N  
ATOM    792  CA  LEU A 103       8.455  36.350  17.912  1.00 29.83           C  
ATOM    793  C   LEU A 103       9.597  36.751  18.832  1.00 29.87           C  
ATOM    794  O   LEU A 103      10.710  36.230  18.721  1.00 29.28           O  
ATOM    795  CB  LEU A 103       8.284  37.398  16.806  1.00 30.74           C  
ATOM    796  CG  LEU A 103       9.511  37.536  15.892  1.00 33.50           C  
ATOM    797  CD1 LEU A 103       9.900  36.162  15.378  1.00 33.11           C  
ATOM    798  CD2 LEU A 103       9.214  38.477  14.733  1.00 34.18           C  
ATOM    799  N   ILE A 104       9.320  37.682  19.739  1.00 29.54           N  
ATOM    800  CA  ILE A 104      10.337  38.109  20.684  1.00 30.38           C  
ATOM    801  C   ILE A 104      10.859  36.873  21.418  1.00 28.97           C  
ATOM    802  O   ILE A 104      12.064  36.672  21.535  1.00 28.38           O  
ATOM    803  CB  ILE A 104       9.769  39.112  21.717  1.00 31.54           C  
ATOM    804  CG1 ILE A 104       9.435  40.439  21.031  1.00 33.18           C  
ATOM    805  CG2 ILE A 104      10.775  39.329  22.839  1.00 33.93           C  
ATOM    806  CD1 ILE A 104       8.858  41.494  21.953  1.00 30.12           C  
ATOM    807  N   LYS A 105       9.939  36.033  21.879  1.00 28.43           N  
ATOM    808  CA  LYS A 105      10.297  34.830  22.623  1.00 29.37           C  
ATOM    809  C   LYS A 105      11.086  33.813  21.802  1.00 30.41           C  
ATOM    810  O   LYS A 105      11.975  33.132  22.326  1.00 30.33           O  
ATOM    811  CB  LYS A 105       9.033  34.174  23.198  1.00 29.37           C  
ATOM    812  CG  LYS A 105       9.317  33.084  24.222  1.00 30.85           C  
ATOM    813  CD  LYS A 105       8.046  32.455  24.764  1.00 29.72           C  
ATOM    814  CE  LYS A 105       7.182  33.462  25.517  1.00 27.92           C  
ATOM    815  NZ  LYS A 105       6.008  32.778  26.128  1.00 27.55           N  
ATOM    816  N   SER A 106      10.759  33.706  20.518  1.00 30.61           N  
ATOM    817  CA  SER A 106      11.458  32.782  19.624  1.00 27.51           C  
ATOM    818  C   SER A 106      12.888  33.279  19.428  1.00 25.38           C  
ATOM    819  O   SER A 106      13.845  32.497  19.446  1.00 26.57           O  
ATOM    820  CB  SER A 106      10.745  32.725  18.268  1.00 29.87           C  
ATOM    821  OG  SER A 106      11.507  31.992  17.322  1.00 28.71           O  
ATOM    822  N   TYR A 107      13.025  34.586  19.228  1.00 24.69           N  
ATOM    823  CA  TYR A 107      14.340  35.183  19.039  1.00 26.79           C  
ATOM    824  C   TYR A 107      15.224  34.992  20.259  1.00 25.11           C  
ATOM    825  O   TYR A 107      16.381  34.612  20.127  1.00 26.61           O  
ATOM    826  CB  TYR A 107      14.223  36.673  18.707  1.00 26.17           C  
ATOM    827  CG  TYR A 107      13.865  36.945  17.260  1.00 28.50           C  
ATOM    828  CD1 TYR A 107      13.868  35.919  16.307  1.00 26.45           C  
ATOM    829  CD2 TYR A 107      13.543  38.231  16.837  1.00 27.28           C  
ATOM    830  CE1 TYR A 107      13.554  36.178  14.974  1.00 27.05           C  
ATOM    831  CE2 TYR A 107      13.231  38.496  15.516  1.00 28.31           C  
ATOM    832  CZ  TYR A 107      13.232  37.471  14.590  1.00 26.39           C  
ATOM    833  OH  TYR A 107      12.859  37.746  13.300  1.00 27.67           O  
ATOM    834  N   LEU A 108      14.679  35.244  21.445  1.00 26.78           N  
ATOM    835  CA  LEU A 108      15.456  35.078  22.673  1.00 27.01           C  
ATOM    836  C   LEU A 108      15.918  33.621  22.830  1.00 26.14           C  
ATOM    837  O   LEU A 108      17.084  33.361  23.115  1.00 25.01           O  
ATOM    838  CB  LEU A 108      14.622  35.502  23.886  1.00 26.33           C  
ATOM    839  CG  LEU A 108      15.346  35.640  25.230  1.00 30.22           C  
ATOM    840  CD1 LEU A 108      16.517  36.634  25.107  1.00 27.02           C  
ATOM    841  CD2 LEU A 108      14.355  36.106  26.284  1.00 30.72           C  
ATOM    842  N   PHE A 109      14.999  32.682  22.613  1.00 28.17           N  
ATOM    843  CA  PHE A 109      15.289  31.250  22.730  1.00 28.05           C  
ATOM    844  C   PHE A 109      16.423  30.829  21.784  1.00 29.07           C  
ATOM    845  O   PHE A 109      17.311  30.063  22.162  1.00 29.11           O  
ATOM    846  CB  PHE A 109      14.016  30.442  22.417  1.00 29.12           C  
ATOM    847  CG  PHE A 109      14.130  28.969  22.713  1.00 29.52           C  
ATOM    848  CD1 PHE A 109      14.077  28.501  24.018  1.00 31.15           C  
ATOM    849  CD2 PHE A 109      14.266  28.047  21.682  1.00 34.20           C  
ATOM    850  CE1 PHE A 109      14.151  27.134  24.295  1.00 32.01           C  
ATOM    851  CE2 PHE A 109      14.345  26.676  21.947  1.00 35.09           C  
ATOM    852  CZ  PHE A 109      14.284  26.222  23.258  1.00 33.75           C  
ATOM    853  N   GLN A 110      16.388  31.346  20.556  1.00 30.08           N  
ATOM    854  CA  GLN A 110      17.412  31.031  19.561  1.00 29.01           C  
ATOM    855  C   GLN A 110      18.755  31.668  19.928  1.00 29.50           C  
ATOM    856  O   GLN A 110      19.808  31.039  19.789  1.00 30.15           O  
ATOM    857  CB  GLN A 110      16.978  31.516  18.166  1.00 28.00           C  
ATOM    858  CG  GLN A 110      15.780  30.777  17.533  1.00 23.79           C  
ATOM    859  CD  GLN A 110      15.455  31.315  16.149  1.00 23.30           C  
ATOM    860  OE1 GLN A 110      16.269  31.229  15.238  1.00 25.87           O  
ATOM    861  NE2 GLN A 110      14.265  31.887  15.993  1.00 23.55           N  
ATOM    862  N   LEU A 111      18.720  32.921  20.376  1.00 27.56           N  
ATOM    863  CA  LEU A 111      19.950  33.608  20.768  1.00 28.61           C  
ATOM    864  C   LEU A 111      20.596  32.874  21.945  1.00 27.12           C  
ATOM    865  O   LEU A 111      21.815  32.720  22.000  1.00 26.16           O  
ATOM    866  CB  LEU A 111      19.648  35.061  21.147  1.00 29.09           C  
ATOM    867  CG  LEU A 111      19.850  36.172  20.112  1.00 32.45           C  
ATOM    868  CD1 LEU A 111      20.077  35.608  18.725  1.00 32.83           C  
ATOM    869  CD2 LEU A 111      18.649  37.097  20.147  1.00 32.45           C  
ATOM    870  N   LEU A 112      19.761  32.423  22.879  1.00 25.70           N  
ATOM    871  CA  LEU A 112      20.231  31.687  24.042  1.00 27.96           C  
ATOM    872  C   LEU A 112      20.899  30.375  23.630  1.00 30.20           C  
ATOM    873  O   LEU A 112      21.900  29.964  24.242  1.00 28.52           O  
ATOM    874  CB  LEU A 112      19.069  31.396  25.003  1.00 27.64           C  
ATOM    875  CG  LEU A 112      18.531  32.575  25.817  1.00 29.49           C  
ATOM    876  CD1 LEU A 112      17.400  32.112  26.710  1.00 29.31           C  
ATOM    877  CD2 LEU A 112      19.661  33.176  26.660  1.00 26.90           C  
ATOM    878  N   GLN A 113      20.350  29.714  22.609  1.00 29.62           N  
ATOM    879  CA  GLN A 113      20.933  28.457  22.135  1.00 33.02           C  
ATOM    880  C   GLN A 113      22.313  28.768  21.590  1.00 33.04           C  
ATOM    881  O   GLN A 113      23.290  28.109  21.939  1.00 35.53           O  
ATOM    882  CB  GLN A 113      20.070  27.810  21.035  1.00 35.40           C  
ATOM    883  CG  GLN A 113      18.745  27.241  21.539  1.00 37.66           C  
ATOM    884  CD  GLN A 113      17.874  26.657  20.429  1.00 40.27           C  
ATOM    885  OE1 GLN A 113      18.105  25.543  19.955  1.00 43.42           O  
ATOM    886  NE2 GLN A 113      16.867  27.413  20.014  1.00 42.33           N  
ATOM    887  N   GLY A 114      22.378  29.785  20.735  1.00 33.55           N  
ATOM    888  CA  GLY A 114      23.642  30.202  20.163  1.00 30.36           C  
ATOM    889  C   GLY A 114      24.654  30.439  21.266  1.00 31.38           C  
ATOM    890  O   GLY A 114      25.777  29.935  21.211  1.00 30.66           O  
ATOM    891  N   LEU A 115      24.250  31.197  22.280  1.00 32.19           N  
ATOM    892  CA  LEU A 115      25.131  31.491  23.396  1.00 32.68           C  
ATOM    893  C   LEU A 115      25.551  30.218  24.132  1.00 31.95           C  
ATOM    894  O   LEU A 115      26.715  30.068  24.486  1.00 32.56           O  
ATOM    895  CB  LEU A 115      24.468  32.480  24.365  1.00 30.85           C  
ATOM    896  CG  LEU A 115      24.758  33.973  24.130  1.00 32.61           C  
ATOM    897  CD1 LEU A 115      24.307  34.387  22.751  1.00 33.50           C  
ATOM    898  CD2 LEU A 115      24.042  34.817  25.174  1.00 28.98           C  
ATOM    899  N   ALA A 116      24.609  29.304  24.353  1.00 32.10           N  
ATOM    900  CA  ALA A 116      24.915  28.051  25.040  1.00 32.29           C  
ATOM    901  C   ALA A 116      26.022  27.324  24.286  1.00 34.04           C  
ATOM    902  O   ALA A 116      26.962  26.806  24.887  1.00 35.82           O  
ATOM    903  CB  ALA A 116      23.674  27.168  25.114  1.00 29.99           C  
ATOM    904  N   PHE A 117      25.903  27.294  22.961  1.00 34.97           N  
ATOM    905  CA  PHE A 117      26.894  26.634  22.129  1.00 36.80           C  
ATOM    906  C   PHE A 117      28.270  27.295  22.258  1.00 37.02           C  
ATOM    907  O   PHE A 117      29.279  26.612  22.425  1.00 38.14           O  
ATOM    908  CB  PHE A 117      26.461  26.660  20.659  1.00 36.89           C  
ATOM    909  CG  PHE A 117      27.443  26.004  19.734  1.00 38.06           C  
ATOM    910  CD1 PHE A 117      27.421  24.622  19.533  1.00 39.59           C  
ATOM    911  CD2 PHE A 117      28.425  26.759  19.097  1.00 37.14           C  
ATOM    912  CE1 PHE A 117      28.370  24.002  18.709  1.00 37.33           C  
ATOM    913  CE2 PHE A 117      29.378  26.153  18.274  1.00 38.88           C  
ATOM    914  CZ  PHE A 117      29.348  24.769  18.081  1.00 38.35           C  
ATOM    915  N   CYS A 118      28.298  28.621  22.173  1.00 37.40           N  
ATOM    916  CA  CYS A 118      29.536  29.383  22.257  1.00 39.05           C  
ATOM    917  C   CYS A 118      30.179  29.295  23.623  1.00 39.52           C  
ATOM    918  O   CYS A 118      31.405  29.185  23.749  1.00 40.17           O  
ATOM    919  CB  CYS A 118      29.272  30.852  21.927  1.00 39.11           C  
ATOM    920  SG  CYS A 118      29.085  31.191  20.170  1.00 46.35           S  
ATOM    921  N   HIS A 119      29.341  29.359  24.647  1.00 38.39           N  
ATOM    922  CA  HIS A 119      29.814  29.292  26.015  1.00 39.39           C  
ATOM    923  C   HIS A 119      30.318  27.897  26.397  1.00 40.64           C  
ATOM    924  O   HIS A 119      31.166  27.768  27.271  1.00 39.50           O  
ATOM    925  CB  HIS A 119      28.701  29.745  26.967  1.00 35.98           C  
ATOM    926  CG  HIS A 119      28.325  31.189  26.808  1.00 36.12           C  
ATOM    927  ND1 HIS A 119      29.105  32.089  26.112  1.00 34.36           N  
ATOM    928  CD2 HIS A 119      27.271  31.894  27.280  1.00 34.27           C  
ATOM    929  CE1 HIS A 119      28.548  33.285  26.162  1.00 34.44           C  
ATOM    930  NE2 HIS A 119      27.433  33.194  26.865  1.00 37.01           N  
ATOM    931  N   SER A 120      29.808  26.856  25.742  1.00 42.23           N  
ATOM    932  CA  SER A 120      30.248  25.499  26.050  1.00 45.44           C  
ATOM    933  C   SER A 120      31.607  25.233  25.395  1.00 45.98           C  
ATOM    934  O   SER A 120      32.303  24.286  25.750  1.00 46.53           O  
ATOM    935  CB  SER A 120      29.213  24.465  25.576  1.00 45.05           C  
ATOM    936  OG  SER A 120      29.171  24.378  24.164  1.00 46.98           O  
ATOM    937  N   HIS A 121      31.977  26.085  24.443  1.00 48.13           N  
ATOM    938  CA  HIS A 121      33.259  25.967  23.751  1.00 49.39           C  
ATOM    939  C   HIS A 121      34.231  27.015  24.293  1.00 50.09           C  
ATOM    940  O   HIS A 121      35.305  27.238  23.730  1.00 49.98           O  
ATOM    941  CB  HIS A 121      33.076  26.159  22.240  1.00 50.41           C  
ATOM    942  CG  HIS A 121      32.568  24.940  21.530  1.00 53.08           C  
ATOM    943  ND1 HIS A 121      31.382  24.322  21.863  1.00 55.38           N  
ATOM    944  CD2 HIS A 121      33.092  24.219  20.511  1.00 54.71           C  
ATOM    945  CE1 HIS A 121      31.198  23.273  21.081  1.00 54.92           C  
ATOM    946  NE2 HIS A 121      32.222  23.188  20.252  1.00 55.74           N  
ATOM    947  N   ARG A 122      33.838  27.654  25.392  1.00 50.40           N  
ATOM    948  CA  ARG A 122      34.657  28.675  26.034  1.00 51.92           C  
ATOM    949  C   ARG A 122      34.950  29.890  25.146  1.00 51.28           C  
ATOM    950  O   ARG A 122      36.063  30.418  25.134  1.00 52.88           O  
ATOM    951  CB  ARG A 122      35.961  28.045  26.532  1.00 54.56           C  
ATOM    952  CG  ARG A 122      35.764  27.153  27.751  1.00 57.83           C  
ATOM    953  CD  ARG A 122      36.904  26.162  27.951  1.00 61.83           C  
ATOM    954  NE  ARG A 122      36.527  24.814  27.530  1.00 65.26           N  
ATOM    955  CZ  ARG A 122      36.432  24.416  26.264  1.00 66.30           C  
ATOM    956  NH1 ARG A 122      36.693  25.262  25.277  1.00 66.38           N  
ATOM    957  NH2 ARG A 122      36.058  23.175  25.985  1.00 66.10           N  
ATOM    958  N   VAL A 123      33.936  30.329  24.410  1.00 49.30           N  
ATOM    959  CA  VAL A 123      34.052  31.493  23.539  1.00 46.97           C  
ATOM    960  C   VAL A 123      32.912  32.467  23.835  1.00 44.32           C  
ATOM    961  O   VAL A 123      31.741  32.087  23.836  1.00 43.52           O  
ATOM    962  CB  VAL A 123      33.995  31.084  22.048  1.00 47.30           C  
ATOM    963  CG1 VAL A 123      33.897  32.318  21.165  1.00 46.68           C  
ATOM    964  CG2 VAL A 123      35.236  30.290  21.689  1.00 48.98           C  
ATOM    965  N   LEU A 124      33.254  33.720  24.103  1.00 41.97           N  
ATOM    966  CA  LEU A 124      32.232  34.719  24.384  1.00 41.70           C  
ATOM    967  C   LEU A 124      32.225  35.822  23.331  1.00 39.94           C  
ATOM    968  O   LEU A 124      33.191  35.990  22.587  1.00 38.16           O  
ATOM    969  CB  LEU A 124      32.426  35.314  25.786  1.00 43.52           C  
ATOM    970  CG  LEU A 124      33.805  35.719  26.306  1.00 44.32           C  
ATOM    971  CD1 LEU A 124      33.650  36.425  27.655  1.00 43.85           C  
ATOM    972  CD2 LEU A 124      34.681  34.483  26.469  1.00 47.72           C  
ATOM    973  N   HIS A 125      31.124  36.564  23.249  1.00 36.88           N  
ATOM    974  CA  HIS A 125      31.044  37.635  22.265  1.00 35.64           C  
ATOM    975  C   HIS A 125      31.631  38.933  22.805  1.00 35.23           C  
ATOM    976  O   HIS A 125      32.454  39.564  22.150  1.00 35.18           O  
ATOM    977  CB  HIS A 125      29.599  37.880  21.836  1.00 34.04           C  
ATOM    978  CG  HIS A 125      29.476  38.844  20.697  1.00 33.23           C  
ATOM    979  ND1 HIS A 125      29.035  38.468  19.447  1.00 31.77           N  
ATOM    980  CD2 HIS A 125      29.783  40.160  20.609  1.00 31.54           C  
ATOM    981  CE1 HIS A 125      29.075  39.511  18.639  1.00 32.02           C  
ATOM    982  NE2 HIS A 125      29.527  40.550  19.318  1.00 31.39           N  
ATOM    983  N   ARG A 126      31.182  39.327  23.993  1.00 35.90           N  
ATOM    984  CA  ARG A 126      31.650  40.541  24.662  1.00 38.15           C  
ATOM    985  C   ARG A 126      31.022  41.839  24.162  1.00 36.98           C  
ATOM    986  O   ARG A 126      31.086  42.855  24.847  1.00 38.60           O  
ATOM    987  CB  ARG A 126      33.183  40.635  24.577  1.00 43.14           C  
ATOM    988  CG  ARG A 126      33.798  41.815  25.330  1.00 50.48           C  
ATOM    989  CD  ARG A 126      34.057  43.003  24.414  1.00 56.92           C  
ATOM    990  NE  ARG A 126      34.566  44.162  25.143  1.00 60.94           N  
ATOM    991  CZ  ARG A 126      33.809  45.004  25.840  1.00 62.31           C  
ATOM    992  NH1 ARG A 126      32.497  44.826  25.903  1.00 62.47           N  
ATOM    993  NH2 ARG A 126      34.366  46.026  26.478  1.00 63.58           N  
ATOM    994  N   ASP A 127      30.400  41.827  22.989  1.00 35.28           N  
ATOM    995  CA  ASP A 127      29.802  43.063  22.506  1.00 34.36           C  
ATOM    996  C   ASP A 127      28.473  42.899  21.773  1.00 31.23           C  
ATOM    997  O   ASP A 127      28.251  43.504  20.725  1.00 29.09           O  
ATOM    998  CB  ASP A 127      30.810  43.809  21.623  1.00 36.29           C  
ATOM    999  CG  ASP A 127      30.368  45.221  21.310  1.00 41.04           C  
ATOM   1000  OD1 ASP A 127      29.758  45.862  22.198  1.00 40.60           O  
ATOM   1001  OD2 ASP A 127      30.634  45.692  20.182  1.00 42.49           O  
ATOM   1002  N   LEU A 128      27.585  42.094  22.339  1.00 30.42           N  
ATOM   1003  CA  LEU A 128      26.276  41.868  21.741  1.00 30.59           C  
ATOM   1004  C   LEU A 128      25.467  43.163  21.692  1.00 30.84           C  
ATOM   1005  O   LEU A 128      25.470  43.948  22.644  1.00 27.82           O  
ATOM   1006  CB  LEU A 128      25.500  40.812  22.534  1.00 30.83           C  
ATOM   1007  CG  LEU A 128      26.047  39.382  22.533  1.00 33.13           C  
ATOM   1008  CD1 LEU A 128      25.125  38.468  23.345  1.00 33.36           C  
ATOM   1009  CD2 LEU A 128      26.154  38.887  21.090  1.00 33.38           C  
ATOM   1010  N   LYS A 129      24.781  43.382  20.575  1.00 29.24           N  
ATOM   1011  CA  LYS A 129      23.964  44.572  20.400  1.00 29.85           C  
ATOM   1012  C   LYS A 129      23.020  44.325  19.231  1.00 29.89           C  
ATOM   1013  O   LYS A 129      23.288  43.477  18.377  1.00 29.48           O  
ATOM   1014  CB  LYS A 129      24.846  45.792  20.128  1.00 31.71           C  
ATOM   1015  CG  LYS A 129      25.385  45.881  18.714  1.00 37.03           C  
ATOM   1016  CD  LYS A 129      26.519  46.888  18.605  1.00 40.45           C  
ATOM   1017  CE  LYS A 129      27.843  46.271  19.034  1.00 41.75           C  
ATOM   1018  NZ  LYS A 129      28.984  47.198  18.811  1.00 43.08           N  
ATOM   1019  N   PRO A 130      21.896  45.054  19.180  1.00 29.74           N  
ATOM   1020  CA  PRO A 130      20.930  44.879  18.093  1.00 31.05           C  
ATOM   1021  C   PRO A 130      21.555  44.846  16.699  1.00 31.46           C  
ATOM   1022  O   PRO A 130      21.080  44.120  15.830  1.00 31.52           O  
ATOM   1023  CB  PRO A 130      19.979  46.059  18.292  1.00 29.52           C  
ATOM   1024  CG  PRO A 130      19.957  46.189  19.790  1.00 27.15           C  
ATOM   1025  CD  PRO A 130      21.427  46.072  20.137  1.00 29.01           C  
ATOM   1026  N   GLN A 131      22.624  45.619  16.506  1.00 32.66           N  
ATOM   1027  CA  GLN A 131      23.326  45.697  15.216  1.00 33.44           C  
ATOM   1028  C   GLN A 131      24.070  44.424  14.790  1.00 31.75           C  
ATOM   1029  O   GLN A 131      24.386  44.268  13.618  1.00 33.11           O  
ATOM   1030  CB  GLN A 131      24.322  46.868  15.209  1.00 36.41           C  
ATOM   1031  CG  GLN A 131      23.711  48.269  15.317  1.00 42.09           C  
ATOM   1032  CD  GLN A 131      23.213  48.607  16.720  1.00 45.27           C  
ATOM   1033  OE1 GLN A 131      23.635  48.002  17.709  1.00 43.96           O  
ATOM   1034  NE2 GLN A 131      22.323  49.594  16.809  1.00 48.38           N  
ATOM   1035  N   ASN A 132      24.388  43.529  15.723  1.00 32.17           N  
ATOM   1036  CA  ASN A 132      25.058  42.296  15.313  1.00 32.49           C  
ATOM   1037  C   ASN A 132      24.198  41.069  15.550  1.00 29.40           C  
ATOM   1038  O   ASN A 132      24.692  39.980  15.801  1.00 27.43           O  
ATOM   1039  CB  ASN A 132      26.442  42.127  15.964  1.00 36.01           C  
ATOM   1040  CG  ASN A 132      26.420  42.273  17.466  1.00 38.60           C  
ATOM   1041  OD1 ASN A 132      25.580  41.691  18.154  1.00 37.97           O  
ATOM   1042  ND2 ASN A 132      27.377  43.035  17.988  1.00 38.70           N  
ATOM   1043  N   LEU A 133      22.893  41.279  15.472  1.00 29.43           N  
ATOM   1044  CA  LEU A 133      21.905  40.219  15.597  1.00 30.23           C  
ATOM   1045  C   LEU A 133      21.216  40.255  14.227  1.00 29.84           C  
ATOM   1046  O   LEU A 133      20.572  41.238  13.874  1.00 28.80           O  
ATOM   1047  CB  LEU A 133      20.927  40.539  16.734  1.00 30.65           C  
ATOM   1048  CG  LEU A 133      21.220  39.917  18.111  1.00 30.48           C  
ATOM   1049  CD1 LEU A 133      22.701  39.849  18.386  1.00 32.13           C  
ATOM   1050  CD2 LEU A 133      20.517  40.721  19.186  1.00 30.67           C  
ATOM   1051  N   LEU A 134      21.374  39.190  13.450  1.00 29.71           N  
ATOM   1052  CA  LEU A 134      20.815  39.135  12.099  1.00 29.33           C  
ATOM   1053  C   LEU A 134      19.672  38.142  11.920  1.00 27.64           C  
ATOM   1054  O   LEU A 134      19.733  37.014  12.391  1.00 27.20           O  
ATOM   1055  CB  LEU A 134      21.941  38.806  11.119  1.00 30.84           C  
ATOM   1056  CG  LEU A 134      23.176  39.688  11.351  1.00 35.71           C  
ATOM   1057  CD1 LEU A 134      24.400  38.933  10.932  1.00 39.58           C  
ATOM   1058  CD2 LEU A 134      23.047  41.008  10.596  1.00 36.35           C  
ATOM   1059  N   ILE A 135      18.632  38.567  11.215  1.00 27.21           N  
ATOM   1060  CA  ILE A 135      17.476  37.708  10.988  1.00 28.92           C  
ATOM   1061  C   ILE A 135      17.290  37.423   9.502  1.00 29.47           C  
ATOM   1062  O   ILE A 135      17.857  38.113   8.662  1.00 26.55           O  
ATOM   1063  CB  ILE A 135      16.179  38.358  11.530  1.00 29.28           C  
ATOM   1064  CG1 ILE A 135      15.948  39.709  10.849  1.00 28.01           C  
ATOM   1065  CG2 ILE A 135      16.267  38.517  13.049  1.00 29.18           C  
ATOM   1066  CD1 ILE A 135      14.624  40.353  11.212  1.00 29.09           C  
ATOM   1067  N   ASN A 136      16.507  36.394   9.189  1.00 31.54           N  
ATOM   1068  CA  ASN A 136      16.218  36.029   7.802  1.00 34.00           C  
ATOM   1069  C   ASN A 136      14.726  35.783   7.697  1.00 35.87           C  
ATOM   1070  O   ASN A 136      14.033  35.718   8.708  1.00 36.84           O  
ATOM   1071  CB  ASN A 136      16.967  34.754   7.379  1.00 32.25           C  
ATOM   1072  CG  ASN A 136      16.547  33.530   8.183  1.00 32.86           C  
ATOM   1073  OD1 ASN A 136      15.490  33.519   8.813  1.00 33.27           O  
ATOM   1074  ND2 ASN A 136      17.376  32.490   8.156  1.00 29.02           N  
ATOM   1075  N   THR A 137      14.238  35.633   6.472  1.00 38.02           N  
ATOM   1076  CA  THR A 137      12.823  35.387   6.229  1.00 38.88           C  
ATOM   1077  C   THR A 137      12.347  34.066   6.839  1.00 40.75           C  
ATOM   1078  O   THR A 137      11.150  33.796   6.882  1.00 42.08           O  
ATOM   1079  CB  THR A 137      12.530  35.347   4.717  1.00 39.89           C  
ATOM   1080  OG1 THR A 137      13.355  34.351   4.099  1.00 41.93           O  
ATOM   1081  CG2 THR A 137      12.818  36.690   4.076  1.00 38.52           C  
ATOM   1082  N   GLU A 138      13.281  33.245   7.308  1.00 42.34           N  
ATOM   1083  CA  GLU A 138      12.944  31.947   7.892  1.00 42.96           C  
ATOM   1084  C   GLU A 138      12.485  31.997   9.343  1.00 42.78           C  
ATOM   1085  O   GLU A 138      12.066  30.978   9.896  1.00 44.06           O  
ATOM   1086  CB  GLU A 138      14.142  30.996   7.792  1.00 46.45           C  
ATOM   1087  CG  GLU A 138      14.242  30.227   6.485  1.00 49.46           C  
ATOM   1088  CD  GLU A 138      14.080  31.114   5.274  1.00 52.29           C  
ATOM   1089  OE1 GLU A 138      14.818  32.114   5.161  1.00 52.62           O  
ATOM   1090  OE2 GLU A 138      13.210  30.806   4.434  1.00 53.67           O  
ATOM   1091  N   GLY A 139      12.559  33.169   9.963  1.00 39.61           N  
ATOM   1092  CA  GLY A 139      12.146  33.276  11.352  1.00 36.85           C  
ATOM   1093  C   GLY A 139      13.295  32.972  12.298  1.00 34.78           C  
ATOM   1094  O   GLY A 139      13.109  32.882  13.512  1.00 33.86           O  
ATOM   1095  N   ALA A 140      14.487  32.802  11.734  1.00 32.44           N  
ATOM   1096  CA  ALA A 140      15.684  32.525  12.516  1.00 31.63           C  
ATOM   1097  C   ALA A 140      16.452  33.824  12.797  1.00 30.63           C  
ATOM   1098  O   ALA A 140      16.351  34.788  12.043  1.00 30.49           O  
ATOM   1099  CB  ALA A 140      16.580  31.545  11.767  1.00 28.47           C  
ATOM   1100  N   ILE A 141      17.204  33.845  13.894  1.00 29.01           N  
ATOM   1101  CA  ILE A 141      18.003  35.017  14.250  1.00 29.96           C  
ATOM   1102  C   ILE A 141      19.412  34.535  14.577  1.00 30.69           C  
ATOM   1103  O   ILE A 141      19.577  33.492  15.206  1.00 29.37           O  
ATOM   1104  CB  ILE A 141      17.393  35.791  15.459  1.00 27.34           C  
ATOM   1105  CG1 ILE A 141      18.229  37.039  15.744  1.00 28.68           C  
ATOM   1106  CG2 ILE A 141      17.338  34.903  16.702  1.00 26.56           C  
ATOM   1107  CD1 ILE A 141      17.571  38.002  16.731  1.00 27.83           C  
ATOM   1108  N   LYS A 142      20.425  35.282  14.147  1.00 29.89           N  
ATOM   1109  CA  LYS A 142      21.804  34.871  14.390  1.00 31.69           C  
ATOM   1110  C   LYS A 142      22.741  35.916  14.991  1.00 29.54           C  
ATOM   1111  O   LYS A 142      22.596  37.118  14.764  1.00 27.26           O  
ATOM   1112  CB  LYS A 142      22.437  34.355  13.089  1.00 32.71           C  
ATOM   1113  CG  LYS A 142      21.688  33.210  12.430  1.00 34.43           C  
ATOM   1114  CD  LYS A 142      22.494  32.606  11.277  1.00 36.92           C  
ATOM   1115  CE  LYS A 142      21.678  31.561  10.510  1.00 39.00           C  
ATOM   1116  NZ  LYS A 142      22.470  30.841   9.478  1.00 39.21           N  
ATOM   1117  N   LEU A 143      23.721  35.412  15.739  1.00 31.71           N  
ATOM   1118  CA  LEU A 143      24.747  36.214  16.395  1.00 34.07           C  
ATOM   1119  C   LEU A 143      25.933  36.410  15.455  1.00 34.40           C  
ATOM   1120  O   LEU A 143      26.527  35.440  15.008  1.00 34.60           O  
ATOM   1121  CB  LEU A 143      25.242  35.493  17.642  1.00 34.63           C  
ATOM   1122  CG  LEU A 143      24.225  35.217  18.745  1.00 37.03           C  
ATOM   1123  CD1 LEU A 143      24.719  34.042  19.580  1.00 35.04           C  
ATOM   1124  CD2 LEU A 143      24.030  36.469  19.598  1.00 37.72           C  
ATOM   1125  N   ALA A 144      26.290  37.656  15.169  1.00 36.29           N  
ATOM   1126  CA  ALA A 144      27.421  37.923  14.285  1.00 37.89           C  
ATOM   1127  C   ALA A 144      28.574  38.579  15.045  1.00 39.66           C  
ATOM   1128  O   ALA A 144      28.359  39.227  16.063  1.00 39.22           O  
ATOM   1129  CB  ALA A 144      26.982  38.815  13.129  1.00 36.51           C  
ATOM   1130  N   ASP A 145      29.790  38.406  14.532  1.00 44.60           N  
ATOM   1131  CA  ASP A 145      31.008  38.964  15.132  1.00 47.60           C  
ATOM   1132  C   ASP A 145      31.417  38.295  16.437  1.00 47.19           C  
ATOM   1133  O   ASP A 145      31.982  38.932  17.318  1.00 47.55           O  
ATOM   1134  CB  ASP A 145      30.865  40.471  15.373  1.00 50.49           C  
ATOM   1135  CG  ASP A 145      30.794  41.260  14.084  1.00 54.38           C  
ATOM   1136  OD1 ASP A 145      31.518  40.901  13.134  1.00 56.84           O  
ATOM   1137  OD2 ASP A 145      30.025  42.243  14.023  1.00 57.67           O  
ATOM   1138  N   PHE A 146      31.140  37.003  16.546  1.00 49.20           N  
ATOM   1139  CA  PHE A 146      31.473  36.237  17.737  1.00 50.67           C  
ATOM   1140  C   PHE A 146      32.968  35.938  17.825  1.00 52.76           C  
ATOM   1141  O   PHE A 146      33.575  35.470  16.861  1.00 52.72           O  
ATOM   1142  CB  PHE A 146      30.695  34.921  17.738  1.00 50.33           C  
ATOM   1143  CG  PHE A 146      30.041  34.615  19.046  1.00 51.02           C  
ATOM   1144  CD1 PHE A 146      30.803  34.453  20.197  1.00 49.33           C  
ATOM   1145  CD2 PHE A 146      28.656  34.535  19.139  1.00 51.19           C  
ATOM   1146  CE1 PHE A 146      30.193  34.220  21.429  1.00 51.92           C  
ATOM   1147  CE2 PHE A 146      28.037  34.303  20.365  1.00 52.01           C  
ATOM   1148  CZ  PHE A 146      28.807  34.147  21.512  1.00 51.07           C  
ATOM   1149  N   GLY A 147      33.555  36.214  18.986  1.00 54.69           N  
ATOM   1150  CA  GLY A 147      34.969  35.951  19.192  1.00 57.02           C  
ATOM   1151  C   GLY A 147      35.927  37.009  18.685  1.00 59.55           C  
ATOM   1152  O   GLY A 147      37.132  36.910  18.914  1.00 60.22           O  
ATOM   1153  N   LEU A 148      35.409  38.024  17.999  1.00 61.91           N  
ATOM   1154  CA  LEU A 148      36.262  39.084  17.472  1.00 65.91           C  
ATOM   1155  C   LEU A 148      36.896  39.947  18.564  1.00 69.30           C  
ATOM   1156  O   LEU A 148      37.905  40.613  18.330  1.00 70.13           O  
ATOM   1157  CB  LEU A 148      35.471  39.967  16.503  1.00 65.77           C  
ATOM   1158  CG  LEU A 148      35.351  39.473  15.056  1.00 66.20           C  
ATOM   1159  CD1 LEU A 148      34.779  38.065  15.021  1.00 66.32           C  
ATOM   1160  CD2 LEU A 148      34.477  40.433  14.266  1.00 65.48           C  
ATOM   1161  N   ALA A 149      36.308  39.933  19.755  1.00 72.87           N  
ATOM   1162  CA  ALA A 149      36.834  40.717  20.868  1.00 77.22           C  
ATOM   1163  C   ALA A 149      38.136  40.109  21.380  1.00 80.03           C  
ATOM   1164  O   ALA A 149      39.104  40.820  21.647  1.00 79.99           O  
ATOM   1165  CB  ALA A 149      35.807  40.785  21.993  1.00 77.04           C  
ATOM   1166  N   ARG A 150      38.149  38.787  21.509  1.00 84.03           N  
ATOM   1167  CA  ARG A 150      39.326  38.066  21.977  1.00 88.75           C  
ATOM   1168  C   ARG A 150      40.427  38.158  20.922  1.00 91.74           C  
ATOM   1169  O   ARG A 150      41.578  37.804  21.175  1.00 91.97           O  
ATOM   1170  CB  ARG A 150      38.967  36.599  22.233  1.00 88.87           C  
ATOM   1171  CG  ARG A 150      40.062  35.781  22.895  1.00 89.90           C  
ATOM   1172  CD  ARG A 150      39.636  34.327  23.044  1.00 90.65           C  
ATOM   1173  NE  ARG A 150      40.643  33.523  23.733  1.00 91.54           N  
ATOM   1174  CZ  ARG A 150      40.554  32.209  23.916  1.00 91.56           C  
ATOM   1175  NH1 ARG A 150      39.502  31.544  23.458  1.00 92.32           N  
ATOM   1176  NH2 ARG A 150      41.516  31.560  24.556  1.00 90.67           N  
ATOM   1177  N   ALA A 151      40.059  38.636  19.737  1.00 95.52           N  
ATOM   1178  CA  ALA A 151      41.004  38.784  18.637  1.00 99.75           C  
ATOM   1179  C   ALA A 151      41.699  40.138  18.717  1.00102.94           C  
ATOM   1180  O   ALA A 151      42.890  40.252  18.434  1.00103.41           O  
ATOM   1181  CB  ALA A 151      40.278  38.647  17.308  1.00 99.36           C  
ATOM   1182  N   PHE A 152      40.945  41.161  19.104  1.00107.22           N  
ATOM   1183  CA  PHE A 152      41.482  42.511  19.231  1.00111.64           C  
ATOM   1184  C   PHE A 152      40.927  43.191  20.480  1.00114.99           C  
ATOM   1185  O   PHE A 152      41.488  43.058  21.568  1.00114.92           O  
ATOM   1186  CB  PHE A 152      41.132  43.337  17.990  1.00111.24           C  
ATOM   1187  CG  PHE A 152      41.682  42.773  16.715  1.00111.07           C  
ATOM   1188  CD1 PHE A 152      43.056  42.698  16.509  1.00111.20           C  
ATOM   1189  CD2 PHE A 152      40.827  42.304  15.723  1.00111.00           C  
ATOM   1190  CE1 PHE A 152      43.572  42.162  15.331  1.00111.48           C  
ATOM   1191  CE2 PHE A 152      41.332  41.765  14.542  1.00111.08           C  
ATOM   1192  CZ  PHE A 152      42.708  41.694  14.346  1.00111.28           C  
ATOM   1193  N   GLY A 153      39.823  43.914  20.320  1.00119.02           N  
ATOM   1194  CA  GLY A 153      39.220  44.595  21.451  1.00124.13           C  
ATOM   1195  C   GLY A 153      38.402  45.808  21.052  1.00127.80           C  
ATOM   1196  O   GLY A 153      38.790  46.562  20.160  1.00127.99           O  
ATOM   1197  N   VAL A 154      37.266  45.997  21.717  1.00131.43           N  
ATOM   1198  CA  VAL A 154      36.389  47.129  21.435  1.00135.03           C  
ATOM   1199  C   VAL A 154      36.658  48.285  22.396  1.00137.26           C  
ATOM   1200  O   VAL A 154      36.502  48.149  23.610  1.00137.42           O  
ATOM   1201  CB  VAL A 154      34.897  46.724  21.533  1.00135.37           C  
ATOM   1202  CG1 VAL A 154      34.604  46.132  22.901  1.00135.51           C  
ATOM   1203  CG2 VAL A 154      34.012  47.935  21.277  1.00135.54           C  
ATOM   1204  N   PRO A 155      37.074  49.441  21.857  1.00139.39           N  
ATOM   1205  CA  PRO A 155      37.371  50.635  22.653  1.00140.91           C  
ATOM   1206  C   PRO A 155      36.119  51.439  22.995  1.00142.37           C  
ATOM   1207  O   PRO A 155      35.042  50.880  23.204  1.00142.62           O  
ATOM   1208  CB  PRO A 155      38.318  51.409  21.748  1.00140.77           C  
ATOM   1209  CG  PRO A 155      37.738  51.139  20.397  1.00140.50           C  
ATOM   1210  CD  PRO A 155      37.454  49.648  20.446  1.00139.91           C  
ATOM   1211  N   VAL A 156      36.280  52.757  23.054  1.00143.84           N  
ATOM   1212  CA  VAL A 156      35.181  53.666  23.353  1.00145.24           C  
ATOM   1213  C   VAL A 156      35.093  54.667  22.202  1.00146.16           C  
ATOM   1214  O   VAL A 156      34.172  55.481  22.128  1.00146.30           O  
ATOM   1215  CB  VAL A 156      35.430  54.421  24.679  1.00145.14           C  
ATOM   1216  CG1 VAL A 156      36.644  55.326  24.548  1.00145.21           C  
ATOM   1217  CG2 VAL A 156      34.197  55.220  25.066  1.00145.32           C  
ATOM   1218  N   ARG A 157      36.070  54.587  21.303  1.00147.19           N  
ATOM   1219  CA  ARG A 157      36.141  55.457  20.134  1.00147.84           C  
ATOM   1220  C   ARG A 157      36.484  54.575  18.936  1.00147.42           C  
ATOM   1221  O   ARG A 157      37.357  53.713  19.024  1.00147.58           O  
ATOM   1222  CB  ARG A 157      37.231  56.512  20.330  1.00148.99           C  
ATOM   1223  CG  ARG A 157      37.147  57.689  19.372  1.00150.46           C  
ATOM   1224  CD  ARG A 157      35.934  58.548  19.682  1.00151.70           C  
ATOM   1225  NE  ARG A 157      35.947  59.801  18.936  1.00152.96           N  
ATOM   1226  CZ  ARG A 157      35.074  60.785  19.121  1.00153.61           C  
ATOM   1227  NH1 ARG A 157      34.115  60.660  20.028  1.00153.86           N  
ATOM   1228  NH2 ARG A 157      35.163  61.898  18.405  1.00154.13           N  
ATOM   1229  N   THR A 158      35.799  54.790  17.819  1.00146.61           N  
ATOM   1230  CA  THR A 158      36.032  53.992  16.622  1.00145.45           C  
ATOM   1231  C   THR A 158      36.654  54.762  15.459  1.00144.02           C  
ATOM   1232  O   THR A 158      36.535  55.985  15.370  1.00143.99           O  
ATOM   1233  CB  THR A 158      34.721  53.344  16.139  1.00145.98           C  
ATOM   1234  OG1 THR A 158      33.698  54.344  16.052  1.00146.35           O  
ATOM   1235  CG2 THR A 158      34.280  52.252  17.101  1.00146.16           C  
ATOM   1236  N   TYR A 159      37.319  54.025  14.572  1.00141.95           N  
ATOM   1237  CA  TYR A 159      37.965  54.608  13.400  1.00139.49           C  
ATOM   1238  C   TYR A 159      36.941  55.303  12.512  1.00136.90           C  
ATOM   1239  O   TYR A 159      37.266  56.260  11.808  1.00137.01           O  
ATOM   1240  CB  TYR A 159      38.703  53.518  12.611  1.00140.69           C  
ATOM   1241  CG  TYR A 159      39.186  53.945  11.239  1.00141.80           C  
ATOM   1242  CD1 TYR A 159      38.337  53.895  10.132  1.00142.36           C  
ATOM   1243  CD2 TYR A 159      40.488  54.407  11.048  1.00142.35           C  
ATOM   1244  CE1 TYR A 159      38.772  54.293   8.869  1.00142.79           C  
ATOM   1245  CE2 TYR A 159      40.933  54.809   9.788  1.00142.79           C  
ATOM   1246  CZ  TYR A 159      40.070  54.749   8.705  1.00142.90           C  
ATOM   1247  OH  TYR A 159      40.503  55.141   7.458  1.00142.93           O  
ATOM   1248  N   THR A 160      35.704  54.816  12.547  1.00133.25           N  
ATOM   1249  CA  THR A 160      34.633  55.408  11.753  1.00129.09           C  
ATOM   1250  C   THR A 160      34.340  56.808  12.279  1.00125.32           C  
ATOM   1251  O   THR A 160      33.418  57.482  11.819  1.00125.19           O  
ATOM   1252  CB  THR A 160      33.345  54.559  11.821  1.00129.86           C  
ATOM   1253  OG1 THR A 160      32.286  55.238  11.133  1.00130.01           O  
ATOM   1254  CG2 THR A 160      32.937  54.318  13.263  1.00129.99           C  
ATOM   1255  N   HIS A 161      35.139  57.229  13.255  1.00120.34           N  
ATOM   1256  CA  HIS A 161      35.009  58.546  13.861  1.00114.77           C  
ATOM   1257  C   HIS A 161      33.668  58.694  14.568  1.00110.52           C  
ATOM   1258  O   HIS A 161      33.306  59.786  15.008  1.00109.94           O  
ATOM   1259  CB  HIS A 161      35.162  59.626  12.788  1.00115.35           C  
ATOM   1260  CG  HIS A 161      36.317  59.393  11.863  1.00115.43           C  
ATOM   1261  ND1 HIS A 161      37.611  59.243  12.312  1.00115.50           N  
ATOM   1262  CD2 HIS A 161      36.369  59.271  10.516  1.00115.18           C  
ATOM   1263  CE1 HIS A 161      38.411  59.038  11.280  1.00115.24           C  
ATOM   1264  NE2 HIS A 161      37.683  59.050  10.179  1.00114.87           N  
ATOM   1265  N   GLU A 162      32.934  57.590  14.674  1.00105.27           N  
ATOM   1266  CA  GLU A 162      31.634  57.599  15.334  1.00 99.63           C  
ATOM   1267  C   GLU A 162      31.797  57.378  16.832  1.00 94.90           C  
ATOM   1268  O   GLU A 162      32.727  57.902  17.447  1.00 94.91           O  
ATOM   1269  CB  GLU A 162      30.725  56.515  14.750  1.00100.50           C  
ATOM   1270  CG  GLU A 162      30.491  56.634  13.256  1.00101.22           C  
ATOM   1271  CD  GLU A 162      29.388  55.717  12.770  1.00101.60           C  
ATOM   1272  OE1 GLU A 162      29.426  54.512  13.095  1.00102.00           O  
ATOM   1273  OE2 GLU A 162      28.484  56.203  12.058  1.00101.62           O  
ATOM   1274  N   VAL A 163      30.895  56.600  17.419  1.00 89.11           N  
ATOM   1275  CA  VAL A 163      30.947  56.333  18.850  1.00 82.86           C  
ATOM   1276  C   VAL A 163      30.566  54.898  19.199  1.00 78.26           C  
ATOM   1277  O   VAL A 163      29.638  54.326  18.622  1.00 76.98           O  
ATOM   1278  CB  VAL A 163      30.005  57.282  19.622  1.00 83.04           C  
ATOM   1279  CG1 VAL A 163      30.185  57.091  21.118  1.00 82.58           C  
ATOM   1280  CG2 VAL A 163      30.279  58.720  19.226  1.00 83.10           C  
ATOM   1281  N   VAL A 164      31.294  54.325  20.152  1.00 72.33           N  
ATOM   1282  CA  VAL A 164      31.033  52.968  20.609  1.00 66.43           C  
ATOM   1283  C   VAL A 164      29.847  53.020  21.568  1.00 61.11           C  
ATOM   1284  O   VAL A 164      29.758  53.915  22.406  1.00 59.72           O  
ATOM   1285  CB  VAL A 164      32.254  52.385  21.357  1.00 67.16           C  
ATOM   1286  CG1 VAL A 164      31.959  50.959  21.801  1.00 67.06           C  
ATOM   1287  CG2 VAL A 164      33.484  52.424  20.461  1.00 67.43           C  
ATOM   1288  N   THR A 165      28.932  52.068  21.439  1.00 55.37           N  
ATOM   1289  CA  THR A 165      27.763  52.037  22.309  1.00 50.80           C  
ATOM   1290  C   THR A 165      28.067  51.232  23.570  1.00 45.79           C  
ATOM   1291  O   THR A 165      28.666  50.161  23.506  1.00 43.97           O  
ATOM   1292  CB  THR A 165      26.549  51.417  21.586  1.00 51.50           C  
ATOM   1293  OG1 THR A 165      25.380  51.556  22.402  1.00 53.46           O  
ATOM   1294  CG2 THR A 165      26.793  49.941  21.307  1.00 52.09           C  
ATOM   1295  N   LEU A 166      27.665  51.759  24.719  1.00 40.45           N  
ATOM   1296  CA  LEU A 166      27.899  51.081  25.986  1.00 35.91           C  
ATOM   1297  C   LEU A 166      26.583  50.611  26.593  1.00 32.72           C  
ATOM   1298  O   LEU A 166      26.562  50.047  27.681  1.00 31.24           O  
ATOM   1299  CB  LEU A 166      28.593  52.029  26.965  1.00 39.15           C  
ATOM   1300  CG  LEU A 166      30.021  52.499  26.670  1.00 40.87           C  
ATOM   1301  CD1 LEU A 166      30.072  53.316  25.394  1.00 41.93           C  
ATOM   1302  CD2 LEU A 166      30.507  53.329  27.844  1.00 41.38           C  
ATOM   1303  N   TRP A 167      25.492  50.839  25.865  1.00 30.33           N  
ATOM   1304  CA  TRP A 167      24.143  50.494  26.314  1.00 26.58           C  
ATOM   1305  C   TRP A 167      23.913  49.058  26.765  1.00 24.96           C  
ATOM   1306  O   TRP A 167      23.003  48.789  27.546  1.00 21.79           O  
ATOM   1307  CB  TRP A 167      23.135  50.826  25.209  1.00 29.60           C  
ATOM   1308  CG  TRP A 167      23.104  52.277  24.775  1.00 32.38           C  
ATOM   1309  CD1 TRP A 167      23.840  53.306  25.285  1.00 35.58           C  
ATOM   1310  CD2 TRP A 167      22.261  52.849  23.766  1.00 33.35           C  
ATOM   1311  NE1 TRP A 167      23.505  54.487  24.661  1.00 36.83           N  
ATOM   1312  CE2 TRP A 167      22.537  54.233  23.726  1.00 36.66           C  
ATOM   1313  CE3 TRP A 167      21.295  52.326  22.895  1.00 34.04           C  
ATOM   1314  CZ2 TRP A 167      21.880  55.104  22.846  1.00 36.06           C  
ATOM   1315  CZ3 TRP A 167      20.640  53.193  22.020  1.00 35.54           C  
ATOM   1316  CH2 TRP A 167      20.937  54.566  22.005  1.00 36.12           C  
ATOM   1317  N   TYR A 168      24.745  48.137  26.294  1.00 24.33           N  
ATOM   1318  CA  TYR A 168      24.573  46.724  26.617  1.00 23.89           C  
ATOM   1319  C   TYR A 168      25.745  46.158  27.388  1.00 23.29           C  
ATOM   1320  O   TYR A 168      25.864  44.946  27.566  1.00 25.15           O  
ATOM   1321  CB  TYR A 168      24.394  45.937  25.312  1.00 23.23           C  
ATOM   1322  CG  TYR A 168      23.370  46.563  24.397  1.00 21.71           C  
ATOM   1323  CD1 TYR A 168      22.012  46.287  24.539  1.00 22.59           C  
ATOM   1324  CD2 TYR A 168      23.755  47.513  23.446  1.00 24.01           C  
ATOM   1325  CE1 TYR A 168      21.055  46.953  23.757  1.00 21.98           C  
ATOM   1326  CE2 TYR A 168      22.818  48.179  22.671  1.00 21.15           C  
ATOM   1327  CZ  TYR A 168      21.472  47.899  22.831  1.00 22.57           C  
ATOM   1328  OH  TYR A 168      20.553  48.586  22.071  1.00 21.21           O  
ATOM   1329  N   ARG A 169      26.613  47.035  27.853  1.00 24.32           N  
ATOM   1330  CA  ARG A 169      27.791  46.585  28.576  1.00 25.56           C  
ATOM   1331  C   ARG A 169      27.453  46.208  30.022  1.00 24.51           C  
ATOM   1332  O   ARG A 169      26.792  46.965  30.741  1.00 23.48           O  
ATOM   1333  CB  ARG A 169      28.858  47.681  28.517  1.00 27.94           C  
ATOM   1334  CG  ARG A 169      30.253  47.220  28.825  1.00 34.84           C  
ATOM   1335  CD  ARG A 169      31.279  48.184  28.253  1.00 37.78           C  
ATOM   1336  NE  ARG A 169      31.369  48.122  26.798  1.00 38.51           N  
ATOM   1337  CZ  ARG A 169      32.201  48.868  26.074  1.00 44.20           C  
ATOM   1338  NH1 ARG A 169      33.010  49.735  26.682  1.00 41.35           N  
ATOM   1339  NH2 ARG A 169      32.235  48.740  24.748  1.00 40.12           N  
ATOM   1340  N   ALA A 170      27.900  45.022  30.428  1.00 21.75           N  
ATOM   1341  CA  ALA A 170      27.667  44.506  31.777  1.00 22.63           C  
ATOM   1342  C   ALA A 170      28.406  45.355  32.822  1.00 22.96           C  
ATOM   1343  O   ALA A 170      29.500  45.844  32.565  1.00 21.42           O  
ATOM   1344  CB  ALA A 170      28.126  43.026  31.858  1.00 17.60           C  
ATOM   1345  N   PRO A 171      27.810  45.530  34.015  1.00 23.73           N  
ATOM   1346  CA  PRO A 171      28.437  46.329  35.073  1.00 25.37           C  
ATOM   1347  C   PRO A 171      29.855  45.899  35.469  1.00 25.85           C  
ATOM   1348  O   PRO A 171      30.694  46.752  35.752  1.00 27.29           O  
ATOM   1349  CB  PRO A 171      27.431  46.241  36.227  1.00 24.44           C  
ATOM   1350  CG  PRO A 171      26.701  44.957  35.969  1.00 24.16           C  
ATOM   1351  CD  PRO A 171      26.526  44.972  34.468  1.00 25.14           C  
ATOM   1352  N   GLU A 172      30.140  44.597  35.484  1.00 25.21           N  
ATOM   1353  CA  GLU A 172      31.489  44.174  35.836  1.00 25.07           C  
ATOM   1354  C   GLU A 172      32.504  44.746  34.839  1.00 25.60           C  
ATOM   1355  O   GLU A 172      33.635  45.011  35.202  1.00 26.05           O  
ATOM   1356  CB  GLU A 172      31.620  42.643  35.911  1.00 26.51           C  
ATOM   1357  CG  GLU A 172      31.232  41.893  34.655  1.00 28.47           C  
ATOM   1358  CD  GLU A 172      29.776  41.506  34.652  1.00 26.83           C  
ATOM   1359  OE1 GLU A 172      28.940  42.337  35.060  1.00 26.28           O  
ATOM   1360  OE2 GLU A 172      29.472  40.371  34.243  1.00 28.98           O  
ATOM   1361  N   ILE A 173      32.109  44.956  33.588  1.00 27.26           N  
ATOM   1362  CA  ILE A 173      33.053  45.534  32.629  1.00 28.63           C  
ATOM   1363  C   ILE A 173      33.226  47.032  32.908  1.00 30.36           C  
ATOM   1364  O   ILE A 173      34.341  47.557  32.885  1.00 30.73           O  
ATOM   1365  CB  ILE A 173      32.589  45.375  31.162  1.00 29.55           C  
ATOM   1366  CG1 ILE A 173      32.465  43.887  30.802  1.00 27.83           C  
ATOM   1367  CG2 ILE A 173      33.597  46.069  30.229  1.00 27.07           C  
ATOM   1368  CD1 ILE A 173      32.009  43.636  29.363  1.00 29.67           C  
ATOM   1369  N   LEU A 174      32.117  47.716  33.169  1.00 28.10           N  
ATOM   1370  CA  LEU A 174      32.162  49.147  33.461  1.00 27.30           C  
ATOM   1371  C   LEU A 174      32.910  49.440  34.759  1.00 28.38           C  
ATOM   1372  O   LEU A 174      33.434  50.532  34.937  1.00 29.00           O  
ATOM   1373  CB  LEU A 174      30.747  49.703  33.585  1.00 25.88           C  
ATOM   1374  CG  LEU A 174      29.981  50.226  32.367  1.00 27.85           C  
ATOM   1375  CD1 LEU A 174      30.714  49.983  31.078  1.00 26.59           C  
ATOM   1376  CD2 LEU A 174      28.628  49.573  32.367  1.00 22.81           C  
ATOM   1377  N   LEU A 175      32.941  48.466  35.666  1.00 28.18           N  
ATOM   1378  CA  LEU A 175      33.611  48.634  36.945  1.00 29.75           C  
ATOM   1379  C   LEU A 175      35.085  48.219  36.929  1.00 31.49           C  
ATOM   1380  O   LEU A 175      35.734  48.158  37.976  1.00 32.51           O  
ATOM   1381  CB  LEU A 175      32.848  47.866  38.037  1.00 29.70           C  
ATOM   1382  CG  LEU A 175      31.485  48.485  38.391  1.00 27.50           C  
ATOM   1383  CD1 LEU A 175      30.781  47.682  39.464  1.00 24.95           C  
ATOM   1384  CD2 LEU A 175      31.706  49.920  38.850  1.00 27.41           C  
ATOM   1385  N   GLY A 176      35.608  47.916  35.744  1.00 33.65           N  
ATOM   1386  CA  GLY A 176      37.018  47.571  35.637  1.00 35.48           C  
ATOM   1387  C   GLY A 176      37.443  46.118  35.714  1.00 37.55           C  
ATOM   1388  O   GLY A 176      38.638  45.837  35.615  1.00 35.69           O  
ATOM   1389  N   CYS A 177      36.498  45.197  35.897  1.00 39.20           N  
ATOM   1390  CA  CYS A 177      36.846  43.781  35.970  1.00 41.86           C  
ATOM   1391  C   CYS A 177      37.453  43.405  34.620  1.00 43.63           C  
ATOM   1392  O   CYS A 177      36.797  43.507  33.583  1.00 43.11           O  
ATOM   1393  CB  CYS A 177      35.598  42.932  36.251  1.00 42.95           C  
ATOM   1394  SG  CYS A 177      35.922  41.216  36.743  1.00 41.86           S  
ATOM   1395  N   LYS A 178      38.709  42.976  34.636  1.00 44.54           N  
ATOM   1396  CA  LYS A 178      39.403  42.615  33.410  1.00 47.26           C  
ATOM   1397  C   LYS A 178      39.249  41.151  33.012  1.00 47.13           C  
ATOM   1398  O   LYS A 178      39.573  40.774  31.892  1.00 46.57           O  
ATOM   1399  CB  LYS A 178      40.887  42.974  33.533  1.00 49.31           C  
ATOM   1400  CG  LYS A 178      41.566  42.402  34.762  1.00 50.13           C  
ATOM   1401  CD  LYS A 178      42.985  42.930  34.907  1.00 52.72           C  
ATOM   1402  CE  LYS A 178      43.004  44.437  35.116  1.00 52.55           C  
ATOM   1403  NZ  LYS A 178      42.300  44.843  36.365  1.00 54.27           N  
ATOM   1404  N   TYR A 179      38.746  40.326  33.921  1.00 48.47           N  
ATOM   1405  CA  TYR A 179      38.564  38.914  33.614  1.00 49.73           C  
ATOM   1406  C   TYR A 179      37.095  38.521  33.683  1.00 49.28           C  
ATOM   1407  O   TYR A 179      36.702  37.664  34.479  1.00 49.01           O  
ATOM   1408  CB  TYR A 179      39.396  38.069  34.578  1.00 51.69           C  
ATOM   1409  CG  TYR A 179      40.863  38.421  34.523  1.00 55.26           C  
ATOM   1410  CD1 TYR A 179      41.574  38.323  33.327  1.00 55.07           C  
ATOM   1411  CD2 TYR A 179      41.530  38.899  35.651  1.00 55.68           C  
ATOM   1412  CE1 TYR A 179      42.910  38.697  33.251  1.00 57.72           C  
ATOM   1413  CE2 TYR A 179      42.870  39.277  35.586  1.00 56.96           C  
ATOM   1414  CZ  TYR A 179      43.551  39.175  34.382  1.00 58.51           C  
ATOM   1415  OH  TYR A 179      44.869  39.563  34.303  1.00 60.19           O  
ATOM   1416  N   TYR A 180      36.285  39.157  32.842  1.00 47.12           N  
ATOM   1417  CA  TYR A 180      34.857  38.875  32.811  1.00 47.30           C  
ATOM   1418  C   TYR A 180      34.569  37.552  32.110  1.00 45.02           C  
ATOM   1419  O   TYR A 180      35.385  37.051  31.339  1.00 44.36           O  
ATOM   1420  CB  TYR A 180      34.096  40.015  32.133  1.00 48.88           C  
ATOM   1421  CG  TYR A 180      34.731  40.499  30.860  1.00 51.34           C  
ATOM   1422  CD1 TYR A 180      35.607  41.584  30.865  1.00 53.63           C  
ATOM   1423  CD2 TYR A 180      34.475  39.862  29.649  1.00 52.57           C  
ATOM   1424  CE1 TYR A 180      36.213  42.025  29.689  1.00 55.78           C  
ATOM   1425  CE2 TYR A 180      35.074  40.292  28.471  1.00 55.63           C  
ATOM   1426  CZ  TYR A 180      35.940  41.374  28.498  1.00 56.57           C  
ATOM   1427  OH  TYR A 180      36.528  41.805  27.331  1.00 61.37           O  
ATOM   1428  N   SER A 181      33.392  37.003  32.382  1.00 42.13           N  
ATOM   1429  CA  SER A 181      32.992  35.718  31.840  1.00 37.71           C  
ATOM   1430  C   SER A 181      31.858  35.745  30.814  1.00 34.31           C  
ATOM   1431  O   SER A 181      31.448  36.796  30.321  1.00 34.26           O  
ATOM   1432  CB  SER A 181      32.568  34.814  32.995  1.00 39.01           C  
ATOM   1433  OG  SER A 181      31.387  35.318  33.597  1.00 36.98           O  
ATOM   1434  N   THR A 182      31.360  34.550  30.518  1.00 31.18           N  
ATOM   1435  CA  THR A 182      30.262  34.351  29.587  1.00 28.95           C  
ATOM   1436  C   THR A 182      29.036  35.136  30.058  1.00 26.94           C  
ATOM   1437  O   THR A 182      28.138  35.422  29.277  1.00 29.49           O  
ATOM   1438  CB  THR A 182      29.884  32.860  29.516  1.00 28.49           C  
ATOM   1439  OG1 THR A 182      29.611  32.379  30.837  1.00 30.00           O  
ATOM   1440  CG2 THR A 182      31.023  32.042  28.925  1.00 27.56           C  
ATOM   1441  N   ALA A 183      29.022  35.487  31.340  1.00 26.03           N  
ATOM   1442  CA  ALA A 183      27.913  36.219  31.936  1.00 25.34           C  
ATOM   1443  C   ALA A 183      27.692  37.598  31.331  1.00 25.27           C  
ATOM   1444  O   ALA A 183      26.589  38.138  31.399  1.00 24.48           O  
ATOM   1445  CB  ALA A 183      28.112  36.332  33.450  1.00 23.57           C  
ATOM   1446  N   VAL A 184      28.733  38.180  30.745  1.00 25.32           N  
ATOM   1447  CA  VAL A 184      28.555  39.489  30.138  1.00 25.36           C  
ATOM   1448  C   VAL A 184      27.634  39.413  28.913  1.00 24.37           C  
ATOM   1449  O   VAL A 184      26.908  40.363  28.623  1.00 24.35           O  
ATOM   1450  CB  VAL A 184      29.920  40.140  29.765  1.00 24.88           C  
ATOM   1451  CG1 VAL A 184      30.849  40.079  30.972  1.00 21.98           C  
ATOM   1452  CG2 VAL A 184      30.535  39.462  28.564  1.00 25.17           C  
ATOM   1453  N   ASP A 185      27.646  38.284  28.208  1.00 23.01           N  
ATOM   1454  CA  ASP A 185      26.777  38.142  27.038  1.00 24.45           C  
ATOM   1455  C   ASP A 185      25.324  38.000  27.469  1.00 24.33           C  
ATOM   1456  O   ASP A 185      24.419  38.463  26.781  1.00 24.66           O  
ATOM   1457  CB  ASP A 185      27.184  36.935  26.185  1.00 24.71           C  
ATOM   1458  CG  ASP A 185      28.537  37.123  25.530  1.00 25.29           C  
ATOM   1459  OD1 ASP A 185      28.949  38.295  25.370  1.00 24.61           O  
ATOM   1460  OD2 ASP A 185      29.178  36.107  25.165  1.00 24.72           O  
ATOM   1461  N   ILE A 186      25.114  37.356  28.614  1.00 23.45           N  
ATOM   1462  CA  ILE A 186      23.776  37.174  29.152  1.00 23.01           C  
ATOM   1463  C   ILE A 186      23.203  38.531  29.535  1.00 22.23           C  
ATOM   1464  O   ILE A 186      22.016  38.805  29.313  1.00 24.90           O  
ATOM   1465  CB  ILE A 186      23.790  36.240  30.387  1.00 21.88           C  
ATOM   1466  CG1 ILE A 186      24.018  34.792  29.942  1.00 24.35           C  
ATOM   1467  CG2 ILE A 186      22.483  36.326  31.131  1.00 20.63           C  
ATOM   1468  CD1 ILE A 186      22.902  34.236  29.034  1.00 23.55           C  
ATOM   1469  N   TRP A 187      24.044  39.388  30.104  1.00 20.37           N  
ATOM   1470  CA  TRP A 187      23.590  40.722  30.486  1.00 19.94           C  
ATOM   1471  C   TRP A 187      23.133  41.492  29.240  1.00 18.78           C  
ATOM   1472  O   TRP A 187      22.050  42.071  29.223  1.00 19.64           O  
ATOM   1473  CB  TRP A 187      24.707  41.496  31.200  1.00 20.41           C  
ATOM   1474  CG  TRP A 187      24.322  42.922  31.530  1.00 20.19           C  
ATOM   1475  CD1 TRP A 187      24.280  43.983  30.674  1.00 21.75           C  
ATOM   1476  CD2 TRP A 187      23.873  43.415  32.799  1.00 19.49           C  
ATOM   1477  NE1 TRP A 187      23.829  45.106  31.328  1.00 19.74           N  
ATOM   1478  CE2 TRP A 187      23.570  44.783  32.633  1.00 21.25           C  
ATOM   1479  CE3 TRP A 187      23.701  42.831  34.060  1.00 21.85           C  
ATOM   1480  CZ2 TRP A 187      23.098  45.577  33.683  1.00 22.73           C  
ATOM   1481  CZ3 TRP A 187      23.235  43.620  35.105  1.00 22.15           C  
ATOM   1482  CH2 TRP A 187      22.937  44.980  34.908  1.00 22.45           C  
ATOM   1483  N   SER A 188      23.968  41.488  28.206  1.00 19.15           N  
ATOM   1484  CA  SER A 188      23.651  42.172  26.955  1.00 19.97           C  
ATOM   1485  C   SER A 188      22.333  41.647  26.375  1.00 20.10           C  
ATOM   1486  O   SER A 188      21.445  42.417  26.024  1.00 21.25           O  
ATOM   1487  CB  SER A 188      24.772  41.942  25.938  1.00 20.46           C  
ATOM   1488  OG  SER A 188      26.006  42.391  26.441  1.00 19.30           O  
ATOM   1489  N   LEU A 189      22.203  40.327  26.294  1.00 18.80           N  
ATOM   1490  CA  LEU A 189      20.985  39.747  25.744  1.00 21.40           C  
ATOM   1491  C   LEU A 189      19.763  40.175  26.560  1.00 21.38           C  
ATOM   1492  O   LEU A 189      18.672  40.363  26.017  1.00 22.36           O  
ATOM   1493  CB  LEU A 189      21.106  38.223  25.696  1.00 21.94           C  
ATOM   1494  CG  LEU A 189      20.034  37.474  24.905  1.00 23.74           C  
ATOM   1495  CD1 LEU A 189      19.987  38.007  23.474  1.00 23.93           C  
ATOM   1496  CD2 LEU A 189      20.350  35.973  24.915  1.00 26.61           C  
ATOM   1497  N   GLY A 190      19.955  40.329  27.867  1.00 22.65           N  
ATOM   1498  CA  GLY A 190      18.866  40.761  28.726  1.00 19.35           C  
ATOM   1499  C   GLY A 190      18.443  42.172  28.350  1.00 20.59           C  
ATOM   1500  O   GLY A 190      17.248  42.463  28.226  1.00 23.67           O  
ATOM   1501  N   CYS A 191      19.426  43.052  28.158  1.00 19.36           N  
ATOM   1502  CA  CYS A 191      19.149  44.428  27.768  1.00 19.85           C  
ATOM   1503  C   CYS A 191      18.437  44.463  26.419  1.00 20.53           C  
ATOM   1504  O   CYS A 191      17.540  45.282  26.201  1.00 21.66           O  
ATOM   1505  CB  CYS A 191      20.453  45.241  27.680  1.00 17.87           C  
ATOM   1506  SG  CYS A 191      21.363  45.382  29.243  1.00 24.09           S  
ATOM   1507  N   ILE A 192      18.835  43.573  25.512  1.00 20.94           N  
ATOM   1508  CA  ILE A 192      18.215  43.522  24.188  1.00 21.57           C  
ATOM   1509  C   ILE A 192      16.786  43.004  24.314  1.00 21.77           C  
ATOM   1510  O   ILE A 192      15.869  43.512  23.674  1.00 22.74           O  
ATOM   1511  CB  ILE A 192      19.025  42.620  23.228  1.00 22.99           C  
ATOM   1512  CG1 ILE A 192      20.423  43.216  23.017  1.00 24.87           C  
ATOM   1513  CG2 ILE A 192      18.320  42.518  21.886  1.00 23.10           C  
ATOM   1514  CD1 ILE A 192      21.320  42.401  22.089  1.00 22.01           C  
ATOM   1515  N   PHE A 193      16.610  42.000  25.165  1.00 21.80           N  
ATOM   1516  CA  PHE A 193      15.308  41.405  25.418  1.00 22.55           C  
ATOM   1517  C   PHE A 193      14.345  42.507  25.863  1.00 24.73           C  
ATOM   1518  O   PHE A 193      13.263  42.670  25.292  1.00 25.06           O  
ATOM   1519  CB  PHE A 193      15.469  40.328  26.505  1.00 24.96           C  
ATOM   1520  CG  PHE A 193      14.188  39.662  26.931  1.00 23.25           C  
ATOM   1521  CD1 PHE A 193      13.053  39.680  26.123  1.00 23.96           C  
ATOM   1522  CD2 PHE A 193      14.140  38.967  28.140  1.00 24.26           C  
ATOM   1523  CE1 PHE A 193      11.887  39.017  26.511  1.00 24.58           C  
ATOM   1524  CE2 PHE A 193      12.983  38.300  28.540  1.00 24.75           C  
ATOM   1525  CZ  PHE A 193      11.851  38.324  27.723  1.00 24.48           C  
ATOM   1526  N   ALA A 194      14.757  43.272  26.871  1.00 25.33           N  
ATOM   1527  CA  ALA A 194      13.936  44.358  27.393  1.00 26.03           C  
ATOM   1528  C   ALA A 194      13.638  45.397  26.315  1.00 26.40           C  
ATOM   1529  O   ALA A 194      12.536  45.939  26.257  1.00 27.62           O  
ATOM   1530  CB  ALA A 194      14.637  45.030  28.586  1.00 22.52           C  
ATOM   1531  N   GLU A 195      14.616  45.670  25.458  1.00 28.06           N  
ATOM   1532  CA  GLU A 195      14.429  46.657  24.400  1.00 27.60           C  
ATOM   1533  C   GLU A 195      13.356  46.204  23.400  1.00 29.12           C  
ATOM   1534  O   GLU A 195      12.496  46.989  23.000  1.00 28.12           O  
ATOM   1535  CB  GLU A 195      15.755  46.927  23.686  1.00 28.09           C  
ATOM   1536  CG  GLU A 195      15.800  48.267  22.970  1.00 31.15           C  
ATOM   1537  CD  GLU A 195      17.149  48.559  22.345  1.00 33.91           C  
ATOM   1538  OE1 GLU A 195      18.176  48.150  22.925  1.00 36.68           O  
ATOM   1539  OE2 GLU A 195      17.184  49.214  21.282  1.00 36.20           O  
ATOM   1540  N   MET A 196      13.391  44.935  23.011  1.00 29.41           N  
ATOM   1541  CA  MET A 196      12.382  44.418  22.087  1.00 30.09           C  
ATOM   1542  C   MET A 196      10.979  44.615  22.672  1.00 30.47           C  
ATOM   1543  O   MET A 196      10.068  45.073  21.987  1.00 33.10           O  
ATOM   1544  CB  MET A 196      12.618  42.926  21.812  1.00 29.14           C  
ATOM   1545  CG  MET A 196      13.952  42.610  21.146  1.00 30.05           C  
ATOM   1546  SD  MET A 196      13.979  40.948  20.402  1.00 35.91           S  
ATOM   1547  CE  MET A 196      14.503  39.915  21.794  1.00 32.85           C  
ATOM   1548  N   VAL A 197      10.820  44.282  23.947  1.00 30.48           N  
ATOM   1549  CA  VAL A 197       9.534  44.403  24.617  1.00 31.00           C  
ATOM   1550  C   VAL A 197       9.009  45.835  24.759  1.00 31.49           C  
ATOM   1551  O   VAL A 197       7.836  46.098  24.482  1.00 31.12           O  
ATOM   1552  CB  VAL A 197       9.588  43.759  26.018  1.00 31.73           C  
ATOM   1553  CG1 VAL A 197       8.261  43.930  26.724  1.00 34.07           C  
ATOM   1554  CG2 VAL A 197       9.920  42.292  25.896  1.00 33.36           C  
ATOM   1555  N   THR A 198       9.865  46.765  25.170  1.00 31.61           N  
ATOM   1556  CA  THR A 198       9.422  48.146  25.366  1.00 32.10           C  
ATOM   1557  C   THR A 198       9.601  49.090  24.178  1.00 33.74           C  
ATOM   1558  O   THR A 198       9.014  50.170  24.165  1.00 32.74           O  
ATOM   1559  CB  THR A 198      10.143  48.803  26.572  1.00 31.70           C  
ATOM   1560  OG1 THR A 198      11.505  49.073  26.225  1.00 30.56           O  
ATOM   1561  CG2 THR A 198      10.094  47.882  27.804  1.00 28.59           C  
ATOM   1562  N   ARG A 199      10.421  48.696  23.203  1.00 34.44           N  
ATOM   1563  CA  ARG A 199      10.689  49.514  22.024  1.00 36.92           C  
ATOM   1564  C   ARG A 199      11.490  50.745  22.414  1.00 38.54           C  
ATOM   1565  O   ARG A 199      11.356  51.812  21.812  1.00 41.27           O  
ATOM   1566  CB  ARG A 199       9.390  49.958  21.351  1.00 36.91           C  
ATOM   1567  CG  ARG A 199       8.370  48.848  21.162  1.00 40.82           C  
ATOM   1568  CD  ARG A 199       7.152  49.385  20.438  1.00 41.21           C  
ATOM   1569  NE  ARG A 199       5.932  48.732  20.881  1.00 42.87           N  
ATOM   1570  CZ  ARG A 199       4.716  49.183  20.601  1.00 42.74           C  
ATOM   1571  NH1 ARG A 199       4.579  50.286  19.874  1.00 39.36           N  
ATOM   1572  NH2 ARG A 199       3.644  48.540  21.057  1.00 42.11           N  
ATOM   1573  N   ARG A 200      12.327  50.586  23.427  1.00 39.23           N  
ATOM   1574  CA  ARG A 200      13.164  51.667  23.912  1.00 37.49           C  
ATOM   1575  C   ARG A 200      14.345  51.026  24.638  1.00 34.18           C  
ATOM   1576  O   ARG A 200      14.175  50.050  25.358  1.00 32.33           O  
ATOM   1577  CB  ARG A 200      12.351  52.552  24.856  1.00 41.13           C  
ATOM   1578  CG  ARG A 200      12.982  53.886  25.167  1.00 49.02           C  
ATOM   1579  CD  ARG A 200      11.989  54.808  25.854  1.00 53.71           C  
ATOM   1580  NE  ARG A 200      12.566  56.125  26.114  1.00 59.50           N  
ATOM   1581  CZ  ARG A 200      11.901  57.143  26.652  1.00 63.16           C  
ATOM   1582  NH1 ARG A 200      10.627  57.003  26.993  1.00 64.15           N  
ATOM   1583  NH2 ARG A 200      12.511  58.306  26.848  1.00 65.97           N  
ATOM   1584  N   ALA A 201      15.538  51.564  24.427  1.00 31.12           N  
ATOM   1585  CA  ALA A 201      16.731  51.031  25.061  1.00 31.20           C  
ATOM   1586  C   ALA A 201      16.575  51.052  26.582  1.00 30.96           C  
ATOM   1587  O   ALA A 201      16.056  52.010  27.147  1.00 32.07           O  
ATOM   1588  CB  ALA A 201      17.952  51.847  24.633  1.00 28.30           C  
ATOM   1589  N   LEU A 202      17.020  49.988  27.238  1.00 30.55           N  
ATOM   1590  CA  LEU A 202      16.915  49.892  28.685  1.00 30.09           C  
ATOM   1591  C   LEU A 202      17.797  50.935  29.372  1.00 28.93           C  
ATOM   1592  O   LEU A 202      17.323  51.722  30.177  1.00 29.29           O  
ATOM   1593  CB  LEU A 202      17.337  48.498  29.157  1.00 29.70           C  
ATOM   1594  CG  LEU A 202      16.469  47.767  30.184  1.00 31.86           C  
ATOM   1595  CD1 LEU A 202      17.341  46.782  30.956  1.00 28.25           C  
ATOM   1596  CD2 LEU A 202      15.802  48.750  31.130  1.00 30.33           C  
ATOM   1597  N   PHE A 203      19.085  50.921  29.036  1.00 29.51           N  
ATOM   1598  CA  PHE A 203      20.075  51.828  29.620  1.00 27.16           C  
ATOM   1599  C   PHE A 203      20.859  52.587  28.545  1.00 28.89           C  
ATOM   1600  O   PHE A 203      21.988  52.209  28.223  1.00 28.77           O  
ATOM   1601  CB  PHE A 203      21.078  51.027  30.454  1.00 25.98           C  
ATOM   1602  CG  PHE A 203      20.447  50.097  31.454  1.00 25.06           C  
ATOM   1603  CD1 PHE A 203      19.590  50.587  32.447  1.00 22.79           C  
ATOM   1604  CD2 PHE A 203      20.750  48.732  31.436  1.00 19.82           C  
ATOM   1605  CE1 PHE A 203      19.047  49.730  33.404  1.00 19.63           C  
ATOM   1606  CE2 PHE A 203      20.211  47.867  32.392  1.00 18.29           C  
ATOM   1607  CZ  PHE A 203      19.358  48.369  33.378  1.00 17.81           C  
ATOM   1608  N   PRO A 204      20.290  53.668  27.990  1.00 29.11           N  
ATOM   1609  CA  PRO A 204      20.978  54.440  26.951  1.00 32.68           C  
ATOM   1610  C   PRO A 204      22.015  55.440  27.475  1.00 35.38           C  
ATOM   1611  O   PRO A 204      21.828  56.649  27.369  1.00 38.12           O  
ATOM   1612  CB  PRO A 204      19.823  55.125  26.215  1.00 29.92           C  
ATOM   1613  CG  PRO A 204      18.874  55.406  27.304  1.00 29.79           C  
ATOM   1614  CD  PRO A 204      18.910  54.152  28.180  1.00 30.31           C  
ATOM   1615  N   GLY A 205      23.112  54.930  28.024  1.00 36.24           N  
ATOM   1616  CA  GLY A 205      24.146  55.802  28.550  1.00 38.49           C  
ATOM   1617  C   GLY A 205      24.947  56.496  27.464  1.00 39.65           C  
ATOM   1618  O   GLY A 205      25.153  55.940  26.389  1.00 40.36           O  
ATOM   1619  N   ASP A 206      25.397  57.716  27.740  1.00 40.65           N  
ATOM   1620  CA  ASP A 206      26.185  58.465  26.766  1.00 42.23           C  
ATOM   1621  C   ASP A 206      27.652  58.559  27.175  1.00 41.12           C  
ATOM   1622  O   ASP A 206      28.439  59.241  26.528  1.00 43.27           O  
ATOM   1623  CB  ASP A 206      25.608  59.870  26.574  1.00 44.06           C  
ATOM   1624  CG  ASP A 206      25.624  60.679  27.843  1.00 48.58           C  
ATOM   1625  OD1 ASP A 206      26.722  60.903  28.395  1.00 52.49           O  
ATOM   1626  OD2 ASP A 206      24.537  61.090  28.291  1.00 53.24           O  
ATOM   1627  N   SER A 207      28.006  57.881  28.263  1.00 38.76           N  
ATOM   1628  CA  SER A 207      29.376  57.842  28.762  1.00 36.67           C  
ATOM   1629  C   SER A 207      29.438  56.656  29.711  1.00 35.80           C  
ATOM   1630  O   SER A 207      28.408  56.087  30.067  1.00 36.26           O  
ATOM   1631  CB  SER A 207      29.750  59.131  29.505  1.00 35.50           C  
ATOM   1632  OG  SER A 207      29.149  59.193  30.784  1.00 40.98           O  
ATOM   1633  N   GLU A 208      30.638  56.292  30.136  1.00 35.06           N  
ATOM   1634  CA  GLU A 208      30.790  55.150  31.018  1.00 36.33           C  
ATOM   1635  C   GLU A 208      30.130  55.308  32.374  1.00 35.96           C  
ATOM   1636  O   GLU A 208      29.485  54.377  32.861  1.00 35.48           O  
ATOM   1637  CB  GLU A 208      32.269  54.813  31.190  1.00 39.76           C  
ATOM   1638  CG  GLU A 208      32.935  54.398  29.889  1.00 46.63           C  
ATOM   1639  CD  GLU A 208      34.221  53.629  30.110  1.00 49.98           C  
ATOM   1640  OE1 GLU A 208      34.167  52.572  30.768  1.00 52.17           O  
ATOM   1641  OE2 GLU A 208      35.281  54.076  29.627  1.00 55.65           O  
ATOM   1642  N   ILE A 209      30.282  56.478  32.984  1.00 35.61           N  
ATOM   1643  CA  ILE A 209      29.688  56.709  34.289  1.00 35.77           C  
ATOM   1644  C   ILE A 209      28.198  56.972  34.148  1.00 33.32           C  
ATOM   1645  O   ILE A 209      27.411  56.612  35.017  1.00 33.07           O  
ATOM   1646  CB  ILE A 209      30.344  57.899  35.027  1.00 36.74           C  
ATOM   1647  CG1 ILE A 209      29.940  57.850  36.498  1.00 38.86           C  
ATOM   1648  CG2 ILE A 209      29.918  59.216  34.405  1.00 37.73           C  
ATOM   1649  CD1 ILE A 209      30.388  59.032  37.291  1.00 46.03           C  
ATOM   1650  N   ASP A 210      27.818  57.611  33.050  1.00 31.95           N  
ATOM   1651  CA  ASP A 210      26.413  57.867  32.795  1.00 33.10           C  
ATOM   1652  C   ASP A 210      25.734  56.506  32.575  1.00 33.17           C  
ATOM   1653  O   ASP A 210      24.575  56.305  32.945  1.00 33.16           O  
ATOM   1654  CB  ASP A 210      26.252  58.743  31.549  1.00 32.29           C  
ATOM   1655  CG  ASP A 210      24.799  58.996  31.201  1.00 35.18           C  
ATOM   1656  OD1 ASP A 210      24.091  59.625  32.014  1.00 37.44           O  
ATOM   1657  OD2 ASP A 210      24.362  58.558  30.113  1.00 40.04           O  
ATOM   1658  N   GLN A 211      26.477  55.572  31.986  1.00 30.83           N  
ATOM   1659  CA  GLN A 211      25.962  54.232  31.713  1.00 29.36           C  
ATOM   1660  C   GLN A 211      25.789  53.464  33.018  1.00 25.91           C  
ATOM   1661  O   GLN A 211      24.776  52.806  33.250  1.00 25.79           O  
ATOM   1662  CB  GLN A 211      26.927  53.488  30.789  1.00 30.07           C  
ATOM   1663  CG  GLN A 211      26.519  52.068  30.438  1.00 31.06           C  
ATOM   1664  CD  GLN A 211      25.255  52.005  29.606  1.00 32.27           C  
ATOM   1665  OE1 GLN A 211      25.058  52.811  28.696  1.00 34.28           O  
ATOM   1666  NE2 GLN A 211      24.395  51.029  29.903  1.00 31.03           N  
ATOM   1667  N   LEU A 212      26.791  53.569  33.873  1.00 27.06           N  
ATOM   1668  CA  LEU A 212      26.776  52.908  35.162  1.00 28.11           C  
ATOM   1669  C   LEU A 212      25.660  53.479  36.047  1.00 26.86           C  
ATOM   1670  O   LEU A 212      24.934  52.732  36.715  1.00 26.74           O  
ATOM   1671  CB  LEU A 212      28.140  53.096  35.825  1.00 28.40           C  
ATOM   1672  CG  LEU A 212      28.563  52.144  36.929  1.00 32.59           C  
ATOM   1673  CD1 LEU A 212      28.479  50.698  36.436  1.00 30.54           C  
ATOM   1674  CD2 LEU A 212      29.983  52.497  37.357  1.00 34.49           C  
ATOM   1675  N   PHE A 213      25.508  54.799  36.041  1.00 26.64           N  
ATOM   1676  CA  PHE A 213      24.468  55.417  36.862  1.00 31.82           C  
ATOM   1677  C   PHE A 213      23.039  55.153  36.385  1.00 30.64           C  
ATOM   1678  O   PHE A 213      22.112  55.198  37.184  1.00 32.56           O  
ATOM   1679  CB  PHE A 213      24.726  56.926  37.010  1.00 32.55           C  
ATOM   1680  CG  PHE A 213      25.863  57.258  37.954  1.00 35.79           C  
ATOM   1681  CD1 PHE A 213      26.701  56.259  38.445  1.00 36.60           C  
ATOM   1682  CD2 PHE A 213      26.097  58.572  38.350  1.00 38.18           C  
ATOM   1683  CE1 PHE A 213      27.752  56.561  39.314  1.00 37.43           C  
ATOM   1684  CE2 PHE A 213      27.145  58.885  39.218  1.00 36.11           C  
ATOM   1685  CZ  PHE A 213      27.974  57.878  39.700  1.00 37.24           C  
ATOM   1686  N   ARG A 214      22.843  54.892  35.095  1.00 31.49           N  
ATOM   1687  CA  ARG A 214      21.495  54.575  34.609  1.00 31.39           C  
ATOM   1688  C   ARG A 214      21.138  53.170  35.094  1.00 28.89           C  
ATOM   1689  O   ARG A 214      19.999  52.909  35.472  1.00 30.31           O  
ATOM   1690  CB  ARG A 214      21.420  54.635  33.080  1.00 32.81           C  
ATOM   1691  CG  ARG A 214      21.242  56.042  32.535  1.00 34.91           C  
ATOM   1692  CD  ARG A 214      21.390  56.051  31.024  1.00 39.14           C  
ATOM   1693  NE  ARG A 214      21.113  57.362  30.454  1.00 42.96           N  
ATOM   1694  CZ  ARG A 214      19.893  57.863  30.290  1.00 43.36           C  
ATOM   1695  NH1 ARG A 214      18.825  57.160  30.650  1.00 42.55           N  
ATOM   1696  NH2 ARG A 214      19.745  59.067  29.762  1.00 42.45           N  
ATOM   1697  N   ILE A 215      22.117  52.271  35.081  1.00 26.40           N  
ATOM   1698  CA  ILE A 215      21.905  50.906  35.563  1.00 27.44           C  
ATOM   1699  C   ILE A 215      21.513  50.984  37.045  1.00 29.35           C  
ATOM   1700  O   ILE A 215      20.520  50.380  37.480  1.00 28.63           O  
ATOM   1701  CB  ILE A 215      23.199  50.059  35.438  1.00 24.38           C  
ATOM   1702  CG1 ILE A 215      23.638  49.995  33.973  1.00 22.93           C  
ATOM   1703  CG2 ILE A 215      22.976  48.654  36.005  1.00 21.63           C  
ATOM   1704  CD1 ILE A 215      24.858  49.130  33.749  1.00 20.48           C  
ATOM   1705  N   PHE A 216      22.306  51.738  37.807  1.00 29.46           N  
ATOM   1706  CA  PHE A 216      22.074  51.929  39.238  1.00 30.39           C  
ATOM   1707  C   PHE A 216      20.684  52.501  39.513  1.00 30.93           C  
ATOM   1708  O   PHE A 216      19.960  52.012  40.383  1.00 31.85           O  
ATOM   1709  CB  PHE A 216      23.133  52.872  39.832  1.00 29.80           C  
ATOM   1710  CG  PHE A 216      24.534  52.310  39.832  1.00 30.41           C  
ATOM   1711  CD1 PHE A 216      24.801  51.038  39.327  1.00 31.26           C  
ATOM   1712  CD2 PHE A 216      25.593  53.070  40.325  1.00 31.43           C  
ATOM   1713  CE1 PHE A 216      26.099  50.529  39.311  1.00 30.36           C  
ATOM   1714  CE2 PHE A 216      26.898  52.574  40.316  1.00 29.72           C  
ATOM   1715  CZ  PHE A 216      27.152  51.298  39.807  1.00 32.22           C  
ATOM   1716  N   ARG A 217      20.306  53.533  38.772  1.00 33.72           N  
ATOM   1717  CA  ARG A 217      18.994  54.157  38.958  1.00 38.83           C  
ATOM   1718  C   ARG A 217      17.822  53.174  38.827  1.00 39.48           C  
ATOM   1719  O   ARG A 217      16.804  53.323  39.501  1.00 40.78           O  
ATOM   1720  CB  ARG A 217      18.817  55.308  37.959  1.00 41.67           C  
ATOM   1721  CG  ARG A 217      19.688  56.531  38.248  1.00 48.92           C  
ATOM   1722  CD  ARG A 217      19.820  57.431  37.015  1.00 53.06           C  
ATOM   1723  NE  ARG A 217      20.611  58.630  37.281  1.00 57.09           N  
ATOM   1724  CZ  ARG A 217      21.122  59.417  36.337  1.00 60.06           C  
ATOM   1725  NH1 ARG A 217      20.929  59.131  35.056  1.00 59.83           N  
ATOM   1726  NH2 ARG A 217      21.819  60.496  36.674  1.00 59.87           N  
ATOM   1727  N   THR A 218      17.972  52.170  37.966  1.00 40.10           N  
ATOM   1728  CA  THR A 218      16.917  51.183  37.739  1.00 39.31           C  
ATOM   1729  C   THR A 218      17.011  49.939  38.626  1.00 39.01           C  
ATOM   1730  O   THR A 218      16.012  49.505  39.204  1.00 40.20           O  
ATOM   1731  CB  THR A 218      16.904  50.728  36.263  1.00 39.47           C  
ATOM   1732  OG1 THR A 218      16.696  51.864  35.419  1.00 38.69           O  
ATOM   1733  CG2 THR A 218      15.790  49.712  36.020  1.00 38.91           C  
ATOM   1734  N   LEU A 219      18.205  49.363  38.724  1.00 35.67           N  
ATOM   1735  CA  LEU A 219      18.412  48.166  39.535  1.00 33.66           C  
ATOM   1736  C   LEU A 219      18.923  48.482  40.942  1.00 32.75           C  
ATOM   1737  O   LEU A 219      19.036  47.592  41.782  1.00 30.43           O  
ATOM   1738  CB  LEU A 219      19.409  47.239  38.843  1.00 34.20           C  
ATOM   1739  CG  LEU A 219      19.008  46.383  37.633  1.00 33.64           C  
ATOM   1740  CD1 LEU A 219      17.829  46.966  36.872  1.00 33.61           C  
ATOM   1741  CD2 LEU A 219      20.238  46.254  36.743  1.00 31.55           C  
ATOM   1742  N   GLY A 220      19.229  49.746  41.199  1.00 32.42           N  
ATOM   1743  CA  GLY A 220      19.737  50.116  42.502  1.00 32.91           C  
ATOM   1744  C   GLY A 220      21.247  49.968  42.567  1.00 33.46           C  
ATOM   1745  O   GLY A 220      21.826  49.070  41.944  1.00 31.20           O  
ATOM   1746  N   THR A 221      21.892  50.849  43.324  1.00 32.69           N  
ATOM   1747  CA  THR A 221      23.339  50.811  43.463  1.00 31.97           C  
ATOM   1748  C   THR A 221      23.753  49.501  44.108  1.00 31.75           C  
ATOM   1749  O   THR A 221      23.273  49.142  45.178  1.00 34.41           O  
ATOM   1750  CB  THR A 221      23.848  51.984  44.319  1.00 32.07           C  
ATOM   1751  OG1 THR A 221      23.343  53.207  43.780  1.00 30.79           O  
ATOM   1752  CG2 THR A 221      25.376  52.045  44.303  1.00 32.07           C  
ATOM   1753  N   PRO A 222      24.647  48.760  43.449  1.00 31.76           N  
ATOM   1754  CA  PRO A 222      25.113  47.482  43.978  1.00 30.89           C  
ATOM   1755  C   PRO A 222      25.958  47.650  45.238  1.00 34.49           C  
ATOM   1756  O   PRO A 222      26.705  48.622  45.380  1.00 35.83           O  
ATOM   1757  CB  PRO A 222      25.910  46.905  42.818  1.00 30.32           C  
ATOM   1758  CG  PRO A 222      26.481  48.142  42.177  1.00 30.21           C  
ATOM   1759  CD  PRO A 222      25.300  49.073  42.165  1.00 29.47           C  
ATOM   1760  N   ASP A 223      25.820  46.697  46.150  1.00 35.14           N  
ATOM   1761  CA  ASP A 223      26.565  46.696  47.395  1.00 37.99           C  
ATOM   1762  C   ASP A 223      27.063  45.276  47.632  1.00 36.57           C  
ATOM   1763  O   ASP A 223      26.826  44.386  46.817  1.00 35.66           O  
ATOM   1764  CB  ASP A 223      25.668  47.141  48.553  1.00 41.96           C  
ATOM   1765  CG  ASP A 223      24.356  46.386  48.590  1.00 43.95           C  
ATOM   1766  OD1 ASP A 223      24.383  45.139  48.535  1.00 47.19           O  
ATOM   1767  OD2 ASP A 223      23.297  47.041  48.673  1.00 47.31           O  
ATOM   1768  N   GLU A 224      27.757  45.073  48.745  1.00 36.84           N  
ATOM   1769  CA  GLU A 224      28.297  43.763  49.096  1.00 38.34           C  
ATOM   1770  C   GLU A 224      27.203  42.736  49.397  1.00 38.72           C  
ATOM   1771  O   GLU A 224      27.436  41.530  49.327  1.00 39.17           O  
ATOM   1772  CB  GLU A 224      29.229  43.895  50.304  1.00 40.07           C  
ATOM   1773  CG  GLU A 224      30.551  44.604  50.011  1.00 39.78           C  
ATOM   1774  CD  GLU A 224      31.433  43.817  49.056  1.00 40.18           C  
ATOM   1775  OE1 GLU A 224      31.479  42.579  49.180  1.00 38.58           O  
ATOM   1776  OE2 GLU A 224      32.088  44.433  48.190  1.00 40.22           O  
ATOM   1777  N   VAL A 225      26.012  43.211  49.743  1.00 40.35           N  
ATOM   1778  CA  VAL A 225      24.906  42.309  50.033  1.00 40.67           C  
ATOM   1779  C   VAL A 225      24.496  41.585  48.750  1.00 41.84           C  
ATOM   1780  O   VAL A 225      24.501  40.356  48.687  1.00 43.78           O  
ATOM   1781  CB  VAL A 225      23.674  43.076  50.581  1.00 41.30           C  
ATOM   1782  CG1 VAL A 225      22.480  42.135  50.703  1.00 42.05           C  
ATOM   1783  CG2 VAL A 225      24.000  43.690  51.937  1.00 39.96           C  
ATOM   1784  N   VAL A 226      24.156  42.358  47.726  1.00 39.84           N  
ATOM   1785  CA  VAL A 226      23.726  41.796  46.453  1.00 39.64           C  
ATOM   1786  C   VAL A 226      24.861  41.405  45.507  1.00 38.98           C  
ATOM   1787  O   VAL A 226      24.664  40.608  44.593  1.00 39.58           O  
ATOM   1788  CB  VAL A 226      22.776  42.770  45.724  1.00 41.14           C  
ATOM   1789  CG1 VAL A 226      21.517  42.983  46.556  1.00 40.45           C  
ATOM   1790  CG2 VAL A 226      23.474  44.096  45.473  1.00 40.78           C  
ATOM   1791  N   TRP A 227      26.050  41.950  45.731  1.00 37.75           N  
ATOM   1792  CA  TRP A 227      27.195  41.638  44.875  1.00 36.14           C  
ATOM   1793  C   TRP A 227      28.486  41.598  45.688  1.00 37.17           C  
ATOM   1794  O   TRP A 227      29.231  42.583  45.747  1.00 37.91           O  
ATOM   1795  CB  TRP A 227      27.326  42.692  43.770  1.00 32.63           C  
ATOM   1796  CG  TRP A 227      28.356  42.371  42.727  1.00 29.95           C  
ATOM   1797  CD1 TRP A 227      29.266  41.344  42.744  1.00 29.04           C  
ATOM   1798  CD2 TRP A 227      28.584  43.089  41.511  1.00 29.03           C  
ATOM   1799  NE1 TRP A 227      30.043  41.382  41.611  1.00 29.41           N  
ATOM   1800  CE2 TRP A 227      29.647  42.445  40.837  1.00 29.24           C  
ATOM   1801  CE3 TRP A 227      27.993  44.217  40.924  1.00 29.20           C  
ATOM   1802  CZ2 TRP A 227      30.130  42.891  39.603  1.00 28.23           C  
ATOM   1803  CZ3 TRP A 227      28.474  44.661  39.695  1.00 30.82           C  
ATOM   1804  CH2 TRP A 227      29.532  43.998  39.049  1.00 28.85           C  
ATOM   1805  N   PRO A 228      28.774  40.454  46.320  1.00 39.10           N  
ATOM   1806  CA  PRO A 228      29.992  40.327  47.123  1.00 37.63           C  
ATOM   1807  C   PRO A 228      31.239  40.646  46.306  1.00 38.06           C  
ATOM   1808  O   PRO A 228      31.460  40.057  45.245  1.00 38.33           O  
ATOM   1809  CB  PRO A 228      29.964  38.863  47.565  1.00 37.98           C  
ATOM   1810  CG  PRO A 228      28.488  38.543  47.588  1.00 38.64           C  
ATOM   1811  CD  PRO A 228      28.016  39.190  46.312  1.00 39.11           C  
ATOM   1812  N   GLY A 229      32.046  41.582  46.805  1.00 38.01           N  
ATOM   1813  CA  GLY A 229      33.276  41.950  46.125  1.00 37.97           C  
ATOM   1814  C   GLY A 229      33.168  43.143  45.198  1.00 37.25           C  
ATOM   1815  O   GLY A 229      34.171  43.600  44.653  1.00 40.32           O  
ATOM   1816  N   VAL A 230      31.955  43.649  45.013  1.00 36.12           N  
ATOM   1817  CA  VAL A 230      31.741  44.793  44.140  1.00 35.66           C  
ATOM   1818  C   VAL A 230      32.581  45.993  44.565  1.00 36.78           C  
ATOM   1819  O   VAL A 230      33.173  46.673  43.727  1.00 33.96           O  
ATOM   1820  CB  VAL A 230      30.247  45.205  44.123  1.00 35.88           C  
ATOM   1821  CG1 VAL A 230      29.794  45.581  45.521  1.00 34.70           C  
ATOM   1822  CG2 VAL A 230      30.033  46.362  43.173  1.00 35.79           C  
ATOM   1823  N   THR A 231      32.628  46.249  45.872  1.00 37.63           N  
ATOM   1824  CA  THR A 231      33.378  47.381  46.411  1.00 38.32           C  
ATOM   1825  C   THR A 231      34.875  47.229  46.187  1.00 40.76           C  
ATOM   1826  O   THR A 231      35.633  48.170  46.395  1.00 41.48           O  
ATOM   1827  CB  THR A 231      33.131  47.569  47.939  1.00 38.32           C  
ATOM   1828  OG1 THR A 231      33.582  46.406  48.646  1.00 37.20           O  
ATOM   1829  CG2 THR A 231      31.636  47.814  48.230  1.00 33.74           C  
ATOM   1830  N   SER A 232      35.305  46.045  45.764  1.00 43.14           N  
ATOM   1831  CA  SER A 232      36.723  45.810  45.515  1.00 44.50           C  
ATOM   1832  C   SER A 232      37.071  45.946  44.036  1.00 44.86           C  
ATOM   1833  O   SER A 232      38.231  45.796  43.649  1.00 45.71           O  
ATOM   1834  CB  SER A 232      37.129  44.422  46.012  1.00 45.53           C  
ATOM   1835  OG  SER A 232      37.014  44.341  47.421  1.00 50.11           O  
ATOM   1836  N   MET A 233      36.067  46.227  43.210  1.00 43.94           N  
ATOM   1837  CA  MET A 233      36.293  46.386  41.776  1.00 43.34           C  
ATOM   1838  C   MET A 233      37.232  47.574  41.551  1.00 41.02           C  
ATOM   1839  O   MET A 233      37.192  48.556  42.292  1.00 40.70           O  
ATOM   1840  CB  MET A 233      34.961  46.627  41.054  1.00 45.82           C  
ATOM   1841  CG  MET A 233      33.967  45.461  41.136  1.00 49.42           C  
ATOM   1842  SD  MET A 233      34.169  44.245  39.836  1.00 55.00           S  
ATOM   1843  CE  MET A 233      35.554  43.296  40.469  1.00 57.72           C  
ATOM   1844  N   PRO A 234      38.091  47.497  40.526  1.00 40.43           N  
ATOM   1845  CA  PRO A 234      39.042  48.573  40.215  1.00 39.44           C  
ATOM   1846  C   PRO A 234      38.463  49.992  40.113  1.00 39.25           C  
ATOM   1847  O   PRO A 234      39.065  50.942  40.613  1.00 40.58           O  
ATOM   1848  CB  PRO A 234      39.661  48.109  38.903  1.00 38.33           C  
ATOM   1849  CG  PRO A 234      39.691  46.626  39.072  1.00 40.03           C  
ATOM   1850  CD  PRO A 234      38.319  46.333  39.649  1.00 39.64           C  
ATOM   1851  N   ASP A 235      37.304  50.138  39.473  1.00 37.21           N  
ATOM   1852  CA  ASP A 235      36.699  51.457  39.304  1.00 36.27           C  
ATOM   1853  C   ASP A 235      35.518  51.749  40.212  1.00 36.47           C  
ATOM   1854  O   ASP A 235      34.801  52.729  39.995  1.00 35.38           O  
ATOM   1855  CB  ASP A 235      36.262  51.667  37.853  1.00 37.86           C  
ATOM   1856  CG  ASP A 235      37.411  51.558  36.878  1.00 40.46           C  
ATOM   1857  OD1 ASP A 235      38.452  52.208  37.111  1.00 43.21           O  
ATOM   1858  OD2 ASP A 235      37.273  50.828  35.877  1.00 44.52           O  
ATOM   1859  N   TYR A 236      35.297  50.906  41.218  1.00 35.48           N  
ATOM   1860  CA  TYR A 236      34.191  51.147  42.133  1.00 35.65           C  
ATOM   1861  C   TYR A 236      34.573  52.354  42.978  1.00 35.95           C  
ATOM   1862  O   TYR A 236      35.689  52.428  43.478  1.00 34.63           O  
ATOM   1863  CB  TYR A 236      33.952  49.948  43.051  1.00 36.17           C  
ATOM   1864  CG  TYR A 236      32.886  50.221  44.095  1.00 37.70           C  
ATOM   1865  CD1 TYR A 236      31.531  50.075  43.800  1.00 40.93           C  
ATOM   1866  CD2 TYR A 236      33.234  50.691  45.359  1.00 40.79           C  
ATOM   1867  CE1 TYR A 236      30.552  50.398  44.743  1.00 42.00           C  
ATOM   1868  CE2 TYR A 236      32.270  51.016  46.300  1.00 41.20           C  
ATOM   1869  CZ  TYR A 236      30.935  50.872  45.992  1.00 41.60           C  
ATOM   1870  OH  TYR A 236      29.989  51.226  46.927  1.00 44.14           O  
ATOM   1871  N   LYS A 237      33.650  53.299  43.128  1.00 35.43           N  
ATOM   1872  CA  LYS A 237      33.915  54.487  43.924  1.00 37.15           C  
ATOM   1873  C   LYS A 237      32.962  54.528  45.110  1.00 37.61           C  
ATOM   1874  O   LYS A 237      31.741  54.550  44.934  1.00 36.61           O  
ATOM   1875  CB  LYS A 237      33.736  55.753  43.083  1.00 38.92           C  
ATOM   1876  CG  LYS A 237      34.619  55.814  41.848  1.00 41.90           C  
ATOM   1877  CD  LYS A 237      36.091  55.856  42.222  1.00 44.64           C  
ATOM   1878  CE  LYS A 237      36.976  55.909  40.990  1.00 45.01           C  
ATOM   1879  NZ  LYS A 237      38.413  55.756  41.350  1.00 47.87           N  
ATOM   1880  N   PRO A 238      33.511  54.525  46.337  1.00 36.36           N  
ATOM   1881  CA  PRO A 238      32.695  54.567  47.552  1.00 35.36           C  
ATOM   1882  C   PRO A 238      31.720  55.735  47.494  1.00 35.79           C  
ATOM   1883  O   PRO A 238      30.673  55.719  48.141  1.00 36.04           O  
ATOM   1884  CB  PRO A 238      33.735  54.735  48.656  1.00 36.87           C  
ATOM   1885  CG  PRO A 238      34.905  53.963  48.127  1.00 34.65           C  
ATOM   1886  CD  PRO A 238      34.942  54.409  46.673  1.00 37.08           C  
ATOM   1887  N   SER A 239      32.067  56.738  46.692  1.00 34.69           N  
ATOM   1888  CA  SER A 239      31.237  57.923  46.539  1.00 36.87           C  
ATOM   1889  C   SER A 239      30.078  57.776  45.538  1.00 38.52           C  
ATOM   1890  O   SER A 239      29.390  58.755  45.246  1.00 38.65           O  
ATOM   1891  CB  SER A 239      32.110  59.114  46.136  1.00 37.62           C  
ATOM   1892  OG  SER A 239      32.855  58.821  44.966  1.00 38.81           O  
ATOM   1893  N   PHE A 240      29.867  56.578  44.996  1.00 37.02           N  
ATOM   1894  CA  PHE A 240      28.757  56.392  44.066  1.00 36.99           C  
ATOM   1895  C   PHE A 240      27.456  56.765  44.773  1.00 37.39           C  
ATOM   1896  O   PHE A 240      27.237  56.374  45.918  1.00 38.87           O  
ATOM   1897  CB  PHE A 240      28.608  54.929  43.623  1.00 36.44           C  
ATOM   1898  CG  PHE A 240      29.593  54.485  42.580  1.00 34.78           C  
ATOM   1899  CD1 PHE A 240      30.174  55.392  41.705  1.00 35.45           C  
ATOM   1900  CD2 PHE A 240      29.905  53.137  42.454  1.00 34.69           C  
ATOM   1901  CE1 PHE A 240      31.055  54.962  40.714  1.00 36.22           C  
ATOM   1902  CE2 PHE A 240      30.783  52.697  41.469  1.00 37.73           C  
ATOM   1903  CZ  PHE A 240      31.359  53.615  40.596  1.00 37.61           C  
ATOM   1904  N   PRO A 241      26.584  57.532  44.107  1.00 36.95           N  
ATOM   1905  CA  PRO A 241      25.313  57.905  44.732  1.00 39.90           C  
ATOM   1906  C   PRO A 241      24.564  56.619  45.064  1.00 42.95           C  
ATOM   1907  O   PRO A 241      24.693  55.627  44.350  1.00 43.65           O  
ATOM   1908  CB  PRO A 241      24.618  58.704  43.639  1.00 38.22           C  
ATOM   1909  CG  PRO A 241      25.768  59.407  42.992  1.00 39.22           C  
ATOM   1910  CD  PRO A 241      26.811  58.307  42.877  1.00 38.15           C  
ATOM   1911  N   LYS A 242      23.791  56.628  46.142  1.00 45.07           N  
ATOM   1912  CA  LYS A 242      23.047  55.438  46.538  1.00 47.38           C  
ATOM   1913  C   LYS A 242      21.591  55.468  46.080  1.00 47.55           C  
ATOM   1914  O   LYS A 242      20.750  56.141  46.675  1.00 46.91           O  
ATOM   1915  CB  LYS A 242      23.128  55.257  48.057  1.00 49.99           C  
ATOM   1916  CG  LYS A 242      24.130  54.194  48.492  1.00 52.96           C  
ATOM   1917  CD  LYS A 242      25.458  54.351  47.766  1.00 57.02           C  
ATOM   1918  CE  LYS A 242      26.336  53.126  47.952  1.00 58.41           C  
ATOM   1919  NZ  LYS A 242      27.590  53.212  47.148  1.00 59.80           N  
ATOM   1920  N   TRP A 243      21.305  54.730  45.014  1.00 46.76           N  
ATOM   1921  CA  TRP A 243      19.959  54.664  44.460  1.00 47.13           C  
ATOM   1922  C   TRP A 243      19.220  53.398  44.882  1.00 47.23           C  
ATOM   1923  O   TRP A 243      19.815  52.324  45.019  1.00 45.14           O  
ATOM   1924  CB  TRP A 243      20.015  54.739  42.931  1.00 49.34           C  
ATOM   1925  CG  TRP A 243      20.116  56.135  42.391  1.00 52.46           C  
ATOM   1926  CD1 TRP A 243      19.158  57.105  42.449  1.00 52.87           C  
ATOM   1927  CD2 TRP A 243      21.227  56.711  41.686  1.00 52.60           C  
ATOM   1928  NE1 TRP A 243      19.598  58.245  41.822  1.00 53.54           N  
ATOM   1929  CE2 TRP A 243      20.864  58.032  41.345  1.00 53.16           C  
ATOM   1930  CE3 TRP A 243      22.492  56.238  41.311  1.00 51.68           C  
ATOM   1931  CZ2 TRP A 243      21.721  58.889  40.642  1.00 53.14           C  
ATOM   1932  CZ3 TRP A 243      23.345  57.091  40.612  1.00 51.76           C  
ATOM   1933  CH2 TRP A 243      22.953  58.401  40.286  1.00 52.35           C  
ATOM   1934  N   ALA A 244      17.916  53.541  45.097  1.00 47.69           N  
ATOM   1935  CA  ALA A 244      17.071  52.419  45.488  1.00 48.32           C  
ATOM   1936  C   ALA A 244      16.650  51.674  44.227  1.00 48.10           C  
ATOM   1937  O   ALA A 244      16.505  52.278  43.165  1.00 47.19           O  
ATOM   1938  CB  ALA A 244      15.844  52.924  46.229  1.00 47.72           C  
ATOM   1939  N   ARG A 245      16.459  50.365  44.350  1.00 48.34           N  
ATOM   1940  CA  ARG A 245      16.053  49.539  43.220  1.00 50.15           C  
ATOM   1941  C   ARG A 245      14.603  49.827  42.831  1.00 51.67           C  
ATOM   1942  O   ARG A 245      13.808  50.279  43.655  1.00 50.27           O  
ATOM   1943  CB  ARG A 245      16.209  48.059  43.577  1.00 51.06           C  
ATOM   1944  CG  ARG A 245      15.930  47.101  42.438  1.00 52.43           C  
ATOM   1945  CD  ARG A 245      15.840  45.678  42.958  1.00 55.29           C  
ATOM   1946  NE  ARG A 245      15.627  44.705  41.892  1.00 56.68           N  
ATOM   1947  CZ  ARG A 245      16.540  44.381  40.982  1.00 58.45           C  
ATOM   1948  NH1 ARG A 245      17.738  44.954  41.003  1.00 56.64           N  
ATOM   1949  NH2 ARG A 245      16.260  43.474  40.056  1.00 59.19           N  
ATOM   1950  N   GLN A 246      14.271  49.566  41.569  1.00 54.09           N  
ATOM   1951  CA  GLN A 246      12.924  49.784  41.055  1.00 55.52           C  
ATOM   1952  C   GLN A 246      12.312  48.476  40.575  1.00 56.86           C  
ATOM   1953  O   GLN A 246      12.990  47.649  39.964  1.00 56.78           O  
ATOM   1954  CB  GLN A 246      12.953  50.795  39.909  1.00 56.88           C  
ATOM   1955  CG  GLN A 246      13.410  52.170  40.350  1.00 59.92           C  
ATOM   1956  CD  GLN A 246      12.532  52.747  41.449  1.00 62.76           C  
ATOM   1957  OE1 GLN A 246      13.000  53.512  42.296  1.00 63.41           O  
ATOM   1958  NE2 GLN A 246      11.247  52.391  41.432  1.00 63.16           N  
ATOM   1959  N   ASP A 247      11.022  48.302  40.846  1.00 58.20           N  
ATOM   1960  CA  ASP A 247      10.305  47.091  40.470  1.00 58.46           C  
ATOM   1961  C   ASP A 247      10.364  46.832  38.969  1.00 57.23           C  
ATOM   1962  O   ASP A 247      10.247  47.758  38.168  1.00 58.75           O  
ATOM   1963  CB  ASP A 247       8.846  47.190  40.920  1.00 62.06           C  
ATOM   1964  CG  ASP A 247       8.153  45.844  40.951  1.00 64.80           C  
ATOM   1965  OD1 ASP A 247       8.067  45.187  39.892  1.00 67.45           O  
ATOM   1966  OD2 ASP A 247       7.690  45.441  42.038  1.00 68.51           O  
ATOM   1967  N   PHE A 248      10.544  45.567  38.596  1.00 54.23           N  
ATOM   1968  CA  PHE A 248      10.615  45.176  37.191  1.00 51.84           C  
ATOM   1969  C   PHE A 248       9.295  45.365  36.470  1.00 50.31           C  
ATOM   1970  O   PHE A 248       9.249  45.392  35.236  1.00 49.20           O  
ATOM   1971  CB  PHE A 248      11.047  43.713  37.058  1.00 49.82           C  
ATOM   1972  CG  PHE A 248      12.508  43.544  36.816  1.00 48.30           C  
ATOM   1973  CD1 PHE A 248      13.435  43.929  37.779  1.00 49.11           C  
ATOM   1974  CD2 PHE A 248      12.967  43.044  35.605  1.00 48.08           C  
ATOM   1975  CE1 PHE A 248      14.799  43.819  37.537  1.00 47.67           C  
ATOM   1976  CE2 PHE A 248      14.327  42.933  35.355  1.00 47.36           C  
ATOM   1977  CZ  PHE A 248      15.245  43.322  36.321  1.00 47.63           C  
ATOM   1978  N   SER A 249       8.217  45.475  37.239  1.00 48.79           N  
ATOM   1979  CA  SER A 249       6.902  45.671  36.650  1.00 48.07           C  
ATOM   1980  C   SER A 249       6.870  47.032  35.949  1.00 46.80           C  
ATOM   1981  O   SER A 249       6.072  47.254  35.038  1.00 45.05           O  
ATOM   1982  CB  SER A 249       5.816  45.584  37.730  1.00 48.80           C  
ATOM   1983  OG  SER A 249       6.082  46.461  38.810  1.00 49.12           O  
ATOM   1984  N   LYS A 250       7.757  47.931  36.366  1.00 45.78           N  
ATOM   1985  CA  LYS A 250       7.834  49.259  35.766  1.00 47.91           C  
ATOM   1986  C   LYS A 250       8.945  49.319  34.723  1.00 47.87           C  
ATOM   1987  O   LYS A 250       8.962  50.199  33.864  1.00 46.81           O  
ATOM   1988  CB  LYS A 250       8.092  50.319  36.840  1.00 48.77           C  
ATOM   1989  CG  LYS A 250       8.130  51.738  36.294  1.00 51.20           C  
ATOM   1990  CD  LYS A 250       8.204  52.775  37.402  1.00 52.13           C  
ATOM   1991  CE  LYS A 250       7.903  54.166  36.859  1.00 54.31           C  
ATOM   1992  NZ  LYS A 250       7.792  55.186  37.939  1.00 55.35           N  
ATOM   1993  N   VAL A 251       9.873  48.375  34.807  1.00 48.41           N  
ATOM   1994  CA  VAL A 251      10.993  48.324  33.878  1.00 48.85           C  
ATOM   1995  C   VAL A 251      10.612  47.771  32.507  1.00 47.19           C  
ATOM   1996  O   VAL A 251      11.000  48.330  31.482  1.00 47.15           O  
ATOM   1997  CB  VAL A 251      12.149  47.466  34.447  1.00 50.25           C  
ATOM   1998  CG1 VAL A 251      13.240  47.296  33.399  1.00 52.07           C  
ATOM   1999  CG2 VAL A 251      12.715  48.121  35.695  1.00 49.39           C  
ATOM   2000  N   VAL A 252       9.853  46.681  32.483  1.00 44.79           N  
ATOM   2001  CA  VAL A 252       9.482  46.082  31.214  1.00 44.00           C  
ATOM   2002  C   VAL A 252       8.050  45.603  31.040  1.00 45.67           C  
ATOM   2003  O   VAL A 252       7.802  44.411  30.853  1.00 47.02           O  
ATOM   2004  CB  VAL A 252      10.428  44.908  30.862  1.00 43.56           C  
ATOM   2005  CG1 VAL A 252      11.831  45.445  30.583  1.00 41.19           C  
ATOM   2006  CG2 VAL A 252      10.459  43.898  32.006  1.00 40.09           C  
ATOM   2007  N   PRO A 253       7.079  46.526  31.116  1.00 46.14           N  
ATOM   2008  CA  PRO A 253       5.680  46.125  30.938  1.00 47.09           C  
ATOM   2009  C   PRO A 253       5.418  46.163  29.428  1.00 47.88           C  
ATOM   2010  O   PRO A 253       6.089  46.891  28.703  1.00 48.89           O  
ATOM   2011  CB  PRO A 253       4.923  47.213  31.676  1.00 46.17           C  
ATOM   2012  CG  PRO A 253       5.761  48.430  31.395  1.00 44.79           C  
ATOM   2013  CD  PRO A 253       7.178  47.925  31.572  1.00 44.53           C  
ATOM   2014  N   PRO A 254       4.436  45.395  28.938  1.00 47.83           N  
ATOM   2015  CA  PRO A 254       3.560  44.505  29.697  1.00 47.82           C  
ATOM   2016  C   PRO A 254       4.061  43.067  29.678  1.00 45.99           C  
ATOM   2017  O   PRO A 254       3.264  42.130  29.634  1.00 47.43           O  
ATOM   2018  CB  PRO A 254       2.235  44.661  28.971  1.00 48.29           C  
ATOM   2019  CG  PRO A 254       2.686  44.675  27.544  1.00 47.90           C  
ATOM   2020  CD  PRO A 254       3.951  45.535  27.552  1.00 48.21           C  
ATOM   2021  N   LEU A 255       5.379  42.897  29.698  1.00 42.51           N  
ATOM   2022  CA  LEU A 255       5.956  41.558  29.697  1.00 39.83           C  
ATOM   2023  C   LEU A 255       5.316  40.765  30.834  1.00 38.37           C  
ATOM   2024  O   LEU A 255       5.107  41.291  31.932  1.00 37.58           O  
ATOM   2025  CB  LEU A 255       7.475  41.625  29.894  1.00 37.33           C  
ATOM   2026  CG  LEU A 255       8.259  40.329  29.707  1.00 35.28           C  
ATOM   2027  CD1 LEU A 255       8.088  39.826  28.265  1.00 34.82           C  
ATOM   2028  CD2 LEU A 255       9.732  40.574  30.006  1.00 34.58           C  
ATOM   2029  N   ASP A 256       4.987  39.507  30.570  1.00 38.23           N  
ATOM   2030  CA  ASP A 256       4.369  38.681  31.593  1.00 38.40           C  
ATOM   2031  C   ASP A 256       5.395  38.318  32.665  1.00 37.30           C  
ATOM   2032  O   ASP A 256       6.600  38.458  32.459  1.00 36.04           O  
ATOM   2033  CB  ASP A 256       3.757  37.416  30.976  1.00 39.88           C  
ATOM   2034  CG  ASP A 256       4.799  36.439  30.481  1.00 42.20           C  
ATOM   2035  OD1 ASP A 256       5.677  36.051  31.279  1.00 42.16           O  
ATOM   2036  OD2 ASP A 256       4.737  36.054  29.293  1.00 48.76           O  
ATOM   2037  N   GLU A 257       4.904  37.838  33.801  1.00 35.93           N  
ATOM   2038  CA  GLU A 257       5.752  37.494  34.926  1.00 35.63           C  
ATOM   2039  C   GLU A 257       6.831  36.458  34.637  1.00 33.23           C  
ATOM   2040  O   GLU A 257       7.897  36.523  35.231  1.00 32.00           O  
ATOM   2041  CB  GLU A 257       4.887  37.043  36.102  1.00 39.54           C  
ATOM   2042  CG  GLU A 257       5.629  36.909  37.431  1.00 44.64           C  
ATOM   2043  CD  GLU A 257       6.194  38.228  37.915  1.00 47.48           C  
ATOM   2044  OE1 GLU A 257       5.440  39.224  37.949  1.00 49.80           O  
ATOM   2045  OE2 GLU A 257       7.391  38.267  38.266  1.00 51.38           O  
ATOM   2046  N   ASP A 258       6.565  35.491  33.758  1.00 31.26           N  
ATOM   2047  CA  ASP A 258       7.603  34.512  33.424  1.00 31.21           C  
ATOM   2048  C   ASP A 258       8.752  35.275  32.747  1.00 29.59           C  
ATOM   2049  O   ASP A 258       9.918  35.094  33.074  1.00 29.62           O  
ATOM   2050  CB  ASP A 258       7.086  33.437  32.452  1.00 31.77           C  
ATOM   2051  CG  ASP A 258       6.304  32.328  33.149  1.00 36.59           C  
ATOM   2052  OD1 ASP A 258       6.820  31.747  34.130  1.00 37.16           O  
ATOM   2053  OD2 ASP A 258       5.176  32.024  32.704  1.00 38.86           O  
ATOM   2054  N   GLY A 259       8.397  36.136  31.802  1.00 26.72           N  
ATOM   2055  CA  GLY A 259       9.399  36.912  31.105  1.00 27.73           C  
ATOM   2056  C   GLY A 259      10.144  37.825  32.056  1.00 28.78           C  
ATOM   2057  O   GLY A 259      11.366  37.935  31.989  1.00 30.77           O  
ATOM   2058  N   ARG A 260       9.402  38.473  32.946  1.00 27.92           N  
ATOM   2059  CA  ARG A 260       9.990  39.383  33.920  1.00 29.15           C  
ATOM   2060  C   ARG A 260      10.944  38.631  34.826  1.00 27.50           C  
ATOM   2061  O   ARG A 260      11.998  39.138  35.195  1.00 24.74           O  
ATOM   2062  CB  ARG A 260       8.908  40.041  34.779  1.00 32.13           C  
ATOM   2063  CG  ARG A 260       8.163  41.168  34.111  1.00 39.20           C  
ATOM   2064  CD  ARG A 260       7.276  41.898  35.123  1.00 43.15           C  
ATOM   2065  NE  ARG A 260       6.030  41.187  35.404  1.00 48.10           N  
ATOM   2066  CZ  ARG A 260       5.192  41.506  36.385  1.00 51.80           C  
ATOM   2067  NH1 ARG A 260       5.466  42.524  37.193  1.00 56.58           N  
ATOM   2068  NH2 ARG A 260       4.074  40.819  36.558  1.00 53.20           N  
ATOM   2069  N   SER A 261      10.548  37.420  35.190  1.00 27.71           N  
ATOM   2070  CA  SER A 261      11.355  36.566  36.043  1.00 29.05           C  
ATOM   2071  C   SER A 261      12.671  36.222  35.351  1.00 28.19           C  
ATOM   2072  O   SER A 261      13.741  36.331  35.952  1.00 26.89           O  
ATOM   2073  CB  SER A 261      10.591  35.280  36.370  1.00 29.83           C  
ATOM   2074  OG  SER A 261      11.451  34.311  36.942  1.00 33.10           O  
ATOM   2075  N   LEU A 262      12.584  35.815  34.088  1.00 27.26           N  
ATOM   2076  CA  LEU A 262      13.777  35.466  33.316  1.00 26.89           C  
ATOM   2077  C   LEU A 262      14.694  36.674  33.143  1.00 26.08           C  
ATOM   2078  O   LEU A 262      15.894  36.580  33.382  1.00 26.55           O  
ATOM   2079  CB  LEU A 262      13.385  34.907  31.942  1.00 26.09           C  
ATOM   2080  CG  LEU A 262      14.491  34.684  30.902  1.00 25.90           C  
ATOM   2081  CD1 LEU A 262      15.592  33.776  31.469  1.00 23.21           C  
ATOM   2082  CD2 LEU A 262      13.868  34.049  29.645  1.00 23.79           C  
ATOM   2083  N   LEU A 263      14.122  37.806  32.733  1.00 24.22           N  
ATOM   2084  CA  LEU A 263      14.913  39.023  32.533  1.00 25.21           C  
ATOM   2085  C   LEU A 263      15.674  39.392  33.805  1.00 26.94           C  
ATOM   2086  O   LEU A 263      16.837  39.799  33.754  1.00 27.25           O  
ATOM   2087  CB  LEU A 263      14.015  40.196  32.143  1.00 21.63           C  
ATOM   2088  CG  LEU A 263      14.737  41.551  32.076  1.00 27.03           C  
ATOM   2089  CD1 LEU A 263      15.745  41.547  30.918  1.00 21.09           C  
ATOM   2090  CD2 LEU A 263      13.721  42.675  31.901  1.00 24.04           C  
ATOM   2091  N   SER A 264      15.000  39.242  34.941  1.00 25.45           N  
ATOM   2092  CA  SER A 264      15.580  39.570  36.232  1.00 29.37           C  
ATOM   2093  C   SER A 264      16.808  38.717  36.528  1.00 27.32           C  
ATOM   2094  O   SER A 264      17.801  39.199  37.071  1.00 28.88           O  
ATOM   2095  CB  SER A 264      14.536  39.377  37.336  1.00 29.59           C  
ATOM   2096  OG  SER A 264      15.069  39.725  38.595  1.00 39.30           O  
ATOM   2097  N   GLN A 265      16.733  37.446  36.160  1.00 25.71           N  
ATOM   2098  CA  GLN A 265      17.841  36.538  36.380  1.00 25.26           C  
ATOM   2099  C   GLN A 265      18.987  36.791  35.403  1.00 25.74           C  
ATOM   2100  O   GLN A 265      20.131  36.435  35.680  1.00 26.65           O  
ATOM   2101  CB  GLN A 265      17.347  35.095  36.298  1.00 23.97           C  
ATOM   2102  CG  GLN A 265      16.426  34.757  37.457  1.00 29.77           C  
ATOM   2103  CD  GLN A 265      16.045  33.292  37.525  1.00 30.54           C  
ATOM   2104  OE1 GLN A 265      15.257  32.806  36.724  1.00 33.34           O  
ATOM   2105  NE2 GLN A 265      16.606  32.585  38.494  1.00 34.64           N  
ATOM   2106  N   MET A 266      18.677  37.425  34.274  1.00 23.88           N  
ATOM   2107  CA  MET A 266      19.684  37.750  33.273  1.00 25.30           C  
ATOM   2108  C   MET A 266      20.341  39.074  33.650  1.00 26.12           C  
ATOM   2109  O   MET A 266      21.436  39.391  33.187  1.00 26.37           O  
ATOM   2110  CB  MET A 266      19.052  37.891  31.880  1.00 24.73           C  
ATOM   2111  CG  MET A 266      18.406  36.624  31.331  1.00 23.84           C  
ATOM   2112  SD  MET A 266      17.631  36.892  29.719  1.00 29.96           S  
ATOM   2113  CE  MET A 266      19.076  36.748  28.591  1.00 19.97           C  
ATOM   2114  N   LEU A 267      19.668  39.844  34.498  1.00 26.94           N  
ATOM   2115  CA  LEU A 267      20.180  41.144  34.914  1.00 27.38           C  
ATOM   2116  C   LEU A 267      20.714  41.202  36.350  1.00 26.65           C  
ATOM   2117  O   LEU A 267      20.798  42.274  36.941  1.00 26.38           O  
ATOM   2118  CB  LEU A 267      19.091  42.204  34.714  1.00 29.62           C  
ATOM   2119  CG  LEU A 267      19.113  43.112  33.476  1.00 33.29           C  
ATOM   2120  CD1 LEU A 267      19.695  42.414  32.258  1.00 30.90           C  
ATOM   2121  CD2 LEU A 267      17.695  43.576  33.218  1.00 32.52           C  
ATOM   2122  N   HIS A 268      21.071  40.055  36.911  1.00 25.98           N  
ATOM   2123  CA  HIS A 268      21.632  40.036  38.261  1.00 29.30           C  
ATOM   2124  C   HIS A 268      23.018  40.670  38.220  1.00 28.93           C  
ATOM   2125  O   HIS A 268      23.828  40.359  37.342  1.00 28.11           O  
ATOM   2126  CB  HIS A 268      21.756  38.601  38.779  1.00 31.50           C  
ATOM   2127  CG  HIS A 268      20.496  38.060  39.375  1.00 36.63           C  
ATOM   2128  ND1 HIS A 268      20.273  36.710  39.543  1.00 38.60           N  
ATOM   2129  CD2 HIS A 268      19.395  38.687  39.855  1.00 37.85           C  
ATOM   2130  CE1 HIS A 268      19.088  36.529  40.099  1.00 38.60           C  
ATOM   2131  NE2 HIS A 268      18.536  37.711  40.299  1.00 38.15           N  
ATOM   2132  N   TYR A 269      23.285  41.561  39.167  1.00 28.42           N  
ATOM   2133  CA  TYR A 269      24.581  42.229  39.242  1.00 29.07           C  
ATOM   2134  C   TYR A 269      25.740  41.239  39.312  1.00 29.43           C  
ATOM   2135  O   TYR A 269      26.670  41.302  38.518  1.00 30.43           O  
ATOM   2136  CB  TYR A 269      24.637  43.145  40.464  1.00 26.59           C  
ATOM   2137  CG  TYR A 269      24.082  44.530  40.232  1.00 23.96           C  
ATOM   2138  CD1 TYR A 269      24.688  45.400  39.326  1.00 24.96           C  
ATOM   2139  CD2 TYR A 269      22.963  44.979  40.933  1.00 25.70           C  
ATOM   2140  CE1 TYR A 269      24.199  46.680  39.127  1.00 24.39           C  
ATOM   2141  CE2 TYR A 269      22.464  46.260  40.740  1.00 27.10           C  
ATOM   2142  CZ  TYR A 269      23.084  47.106  39.837  1.00 26.09           C  
ATOM   2143  OH  TYR A 269      22.584  48.373  39.636  1.00 29.04           O  
ATOM   2144  N   ASP A 270      25.673  40.324  40.270  1.00 31.47           N  
ATOM   2145  CA  ASP A 270      26.723  39.334  40.469  1.00 30.60           C  
ATOM   2146  C   ASP A 270      26.789  38.357  39.310  1.00 31.71           C  
ATOM   2147  O   ASP A 270      25.889  37.531  39.139  1.00 31.14           O  
ATOM   2148  CB  ASP A 270      26.471  38.559  41.761  1.00 31.76           C  
ATOM   2149  CG  ASP A 270      27.638  37.664  42.143  1.00 30.37           C  
ATOM   2150  OD1 ASP A 270      28.345  37.173  41.242  1.00 30.14           O  
ATOM   2151  OD2 ASP A 270      27.834  37.444  43.355  1.00 35.15           O  
ATOM   2152  N   PRO A 271      27.875  38.414  38.517  1.00 32.81           N  
ATOM   2153  CA  PRO A 271      28.065  37.531  37.360  1.00 33.52           C  
ATOM   2154  C   PRO A 271      27.845  36.059  37.703  1.00 37.11           C  
ATOM   2155  O   PRO A 271      27.417  35.274  36.858  1.00 39.19           O  
ATOM   2156  CB  PRO A 271      29.509  37.808  36.942  1.00 32.34           C  
ATOM   2157  CG  PRO A 271      29.757  39.204  37.411  1.00 30.16           C  
ATOM   2158  CD  PRO A 271      29.078  39.233  38.752  1.00 31.17           C  
ATOM   2159  N   ASN A 272      28.134  35.694  38.947  1.00 39.01           N  
ATOM   2160  CA  ASN A 272      27.981  34.312  39.400  1.00 41.01           C  
ATOM   2161  C   ASN A 272      26.531  33.918  39.641  1.00 41.14           C  
ATOM   2162  O   ASN A 272      26.181  32.744  39.541  1.00 43.17           O  
ATOM   2163  CB  ASN A 272      28.782  34.091  40.682  1.00 45.56           C  
ATOM   2164  CG  ASN A 272      30.253  34.380  40.500  1.00 49.24           C  
ATOM   2165  OD1 ASN A 272      30.657  35.531  40.331  1.00 53.81           O  
ATOM   2166  ND2 ASN A 272      31.065  33.332  40.523  1.00 53.00           N  
ATOM   2167  N   LYS A 273      25.693  34.897  39.973  1.00 40.05           N  
ATOM   2168  CA  LYS A 273      24.271  34.647  40.219  1.00 38.83           C  
ATOM   2169  C   LYS A 273      23.473  34.777  38.920  1.00 36.46           C  
ATOM   2170  O   LYS A 273      22.311  34.376  38.846  1.00 34.14           O  
ATOM   2171  CB  LYS A 273      23.711  35.658  41.220  1.00 40.72           C  
ATOM   2172  CG  LYS A 273      24.276  35.589  42.625  1.00 45.02           C  
ATOM   2173  CD  LYS A 273      23.583  36.630  43.513  1.00 46.84           C  
ATOM   2174  CE  LYS A 273      24.020  36.539  44.969  1.00 48.62           C  
ATOM   2175  NZ  LYS A 273      25.493  36.712  45.127  1.00 49.11           N  
ATOM   2176  N   ARG A 274      24.101  35.358  37.903  1.00 34.39           N  
ATOM   2177  CA  ARG A 274      23.443  35.568  36.622  1.00 30.48           C  
ATOM   2178  C   ARG A 274      23.219  34.217  35.954  1.00 29.31           C  
ATOM   2179  O   ARG A 274      24.148  33.424  35.785  1.00 29.33           O  
ATOM   2180  CB  ARG A 274      24.303  36.488  35.753  1.00 29.08           C  
ATOM   2181  CG  ARG A 274      23.535  37.311  34.724  1.00 26.70           C  
ATOM   2182  CD  ARG A 274      24.464  38.302  34.028  1.00 25.16           C  
ATOM   2183  NE  ARG A 274      24.954  39.333  34.940  1.00 24.06           N  
ATOM   2184  CZ  ARG A 274      26.100  39.994  34.789  1.00 26.25           C  
ATOM   2185  NH1 ARG A 274      26.890  39.732  33.757  1.00 24.22           N  
ATOM   2186  NH2 ARG A 274      26.460  40.924  35.668  1.00 25.57           N  
ATOM   2187  N   ILE A 275      21.976  33.950  35.584  1.00 27.95           N  
ATOM   2188  CA  ILE A 275      21.637  32.684  34.962  1.00 26.35           C  
ATOM   2189  C   ILE A 275      22.464  32.436  33.702  1.00 25.95           C  
ATOM   2190  O   ILE A 275      22.835  33.367  32.994  1.00 24.21           O  
ATOM   2191  CB  ILE A 275      20.131  32.634  34.634  1.00 28.07           C  
ATOM   2192  CG1 ILE A 275      19.723  31.207  34.258  1.00 27.15           C  
ATOM   2193  CG2 ILE A 275      19.810  33.617  33.507  1.00 29.47           C  
ATOM   2194  CD1 ILE A 275      18.224  31.023  34.141  1.00 25.62           C  
ATOM   2195  N   SER A 276      22.771  31.169  33.446  1.00 26.91           N  
ATOM   2196  CA  SER A 276      23.546  30.777  32.275  1.00 27.72           C  
ATOM   2197  C   SER A 276      22.619  30.625  31.062  1.00 28.13           C  
ATOM   2198  O   SER A 276      21.400  30.596  31.208  1.00 28.53           O  
ATOM   2199  CB  SER A 276      24.248  29.450  32.545  1.00 27.63           C  
ATOM   2200  OG  SER A 276      23.294  28.424  32.760  1.00 33.92           O  
ATOM   2201  N   ALA A 277      23.200  30.522  29.870  1.00 27.91           N  
ATOM   2202  CA  ALA A 277      22.406  30.366  28.655  1.00 29.35           C  
ATOM   2203  C   ALA A 277      21.642  29.044  28.676  1.00 30.05           C  
ATOM   2204  O   ALA A 277      20.470  28.979  28.303  1.00 29.08           O  
ATOM   2205  CB  ALA A 277      23.309  30.424  27.428  1.00 25.84           C  
ATOM   2206  N   LYS A 278      22.317  27.994  29.125  1.00 32.66           N  
ATOM   2207  CA  LYS A 278      21.723  26.667  29.193  1.00 34.63           C  
ATOM   2208  C   LYS A 278      20.539  26.649  30.160  1.00 34.07           C  
ATOM   2209  O   LYS A 278      19.473  26.137  29.831  1.00 34.71           O  
ATOM   2210  CB  LYS A 278      22.790  25.658  29.629  1.00 38.67           C  
ATOM   2211  CG  LYS A 278      22.449  24.210  29.349  1.00 43.28           C  
ATOM   2212  CD  LYS A 278      23.722  23.375  29.241  1.00 46.28           C  
ATOM   2213  CE  LYS A 278      23.408  21.919  28.943  1.00 48.81           C  
ATOM   2214  NZ  LYS A 278      22.512  21.778  27.761  1.00 51.92           N  
ATOM   2215  N   ALA A 279      20.729  27.221  31.346  1.00 34.52           N  
ATOM   2216  CA  ALA A 279      19.665  27.260  32.343  1.00 34.00           C  
ATOM   2217  C   ALA A 279      18.505  28.134  31.878  1.00 33.32           C  
ATOM   2218  O   ALA A 279      17.340  27.823  32.121  1.00 34.22           O  
ATOM   2219  CB  ALA A 279      20.209  27.775  33.672  1.00 34.68           C  
ATOM   2220  N   ALA A 280      18.830  29.230  31.207  1.00 31.26           N  
ATOM   2221  CA  ALA A 280      17.806  30.130  30.707  1.00 30.55           C  
ATOM   2222  C   ALA A 280      16.860  29.373  29.777  1.00 31.35           C  
ATOM   2223  O   ALA A 280      15.664  29.657  29.739  1.00 29.90           O  
ATOM   2224  CB  ALA A 280      18.448  31.287  29.970  1.00 25.92           C  
ATOM   2225  N   LEU A 281      17.406  28.408  29.039  1.00 30.61           N  
ATOM   2226  CA  LEU A 281      16.622  27.613  28.100  1.00 31.95           C  
ATOM   2227  C   LEU A 281      15.582  26.722  28.768  1.00 31.51           C  
ATOM   2228  O   LEU A 281      14.604  26.335  28.141  1.00 31.97           O  
ATOM   2229  CB  LEU A 281      17.541  26.744  27.236  1.00 31.09           C  
ATOM   2230  CG  LEU A 281      18.400  27.463  26.195  1.00 30.19           C  
ATOM   2231  CD1 LEU A 281      19.324  26.462  25.525  1.00 30.43           C  
ATOM   2232  CD2 LEU A 281      17.504  28.141  25.166  1.00 29.28           C  
ATOM   2233  N   ALA A 282      15.796  26.396  30.038  1.00 31.83           N  
ATOM   2234  CA  ALA A 282      14.859  25.549  30.767  1.00 29.04           C  
ATOM   2235  C   ALA A 282      13.823  26.380  31.527  1.00 29.82           C  
ATOM   2236  O   ALA A 282      12.958  25.841  32.215  1.00 30.08           O  
ATOM   2237  CB  ALA A 282      15.623  24.665  31.732  1.00 30.27           C  
ATOM   2238  N   HIS A 283      13.910  27.698  31.395  1.00 28.72           N  
ATOM   2239  CA  HIS A 283      12.981  28.587  32.085  1.00 30.18           C  
ATOM   2240  C   HIS A 283      11.541  28.409  31.586  1.00 30.88           C  
ATOM   2241  O   HIS A 283      11.312  28.216  30.402  1.00 30.53           O  
ATOM   2242  CB  HIS A 283      13.434  30.029  31.894  1.00 27.17           C  
ATOM   2243  CG  HIS A 283      12.798  30.992  32.841  1.00 26.14           C  
ATOM   2244  ND1 HIS A 283      11.520  31.474  32.668  1.00 29.08           N  
ATOM   2245  CD2 HIS A 283      13.272  31.576  33.968  1.00 26.89           C  
ATOM   2246  CE1 HIS A 283      11.235  32.318  33.645  1.00 27.07           C  
ATOM   2247  NE2 HIS A 283      12.281  32.398  34.446  1.00 25.35           N  
ATOM   2248  N   PRO A 284      10.552  28.481  32.496  1.00 32.42           N  
ATOM   2249  CA  PRO A 284       9.134  28.325  32.145  1.00 32.95           C  
ATOM   2250  C   PRO A 284       8.646  29.322  31.099  1.00 33.19           C  
ATOM   2251  O   PRO A 284       7.567  29.159  30.537  1.00 35.40           O  
ATOM   2252  CB  PRO A 284       8.420  28.511  33.485  1.00 33.45           C  
ATOM   2253  CG  PRO A 284       9.434  28.024  34.481  1.00 33.43           C  
ATOM   2254  CD  PRO A 284      10.714  28.634  33.954  1.00 32.17           C  
ATOM   2255  N   PHE A 285       9.431  30.363  30.847  1.00 33.01           N  
ATOM   2256  CA  PHE A 285       9.052  31.359  29.852  1.00 31.78           C  
ATOM   2257  C   PHE A 285       9.008  30.742  28.449  1.00 32.51           C  
ATOM   2258  O   PHE A 285       8.249  31.192  27.589  1.00 31.42           O  
ATOM   2259  CB  PHE A 285      10.044  32.533  29.865  1.00 30.40           C  
ATOM   2260  CG  PHE A 285       9.678  33.651  28.917  1.00 27.97           C  
ATOM   2261  CD1 PHE A 285       8.454  34.306  29.035  1.00 28.92           C  
ATOM   2262  CD2 PHE A 285      10.566  34.059  27.920  1.00 26.18           C  
ATOM   2263  CE1 PHE A 285       8.115  35.352  28.178  1.00 26.24           C  
ATOM   2264  CE2 PHE A 285      10.241  35.105  27.057  1.00 26.09           C  
ATOM   2265  CZ  PHE A 285       9.013  35.757  27.182  1.00 26.69           C  
ATOM   2266  N   PHE A 286       9.819  29.708  28.231  1.00 32.71           N  
ATOM   2267  CA  PHE A 286       9.884  29.043  26.936  1.00 36.47           C  
ATOM   2268  C   PHE A 286       9.044  27.776  26.890  1.00 40.01           C  
ATOM   2269  O   PHE A 286       9.150  26.986  25.953  1.00 40.19           O  
ATOM   2270  CB  PHE A 286      11.344  28.705  26.593  1.00 34.13           C  
ATOM   2271  CG  PHE A 286      12.235  29.913  26.516  1.00 32.46           C  
ATOM   2272  CD1 PHE A 286      11.969  30.926  25.604  1.00 28.07           C  
ATOM   2273  CD2 PHE A 286      13.311  30.059  27.388  1.00 30.88           C  
ATOM   2274  CE1 PHE A 286      12.760  32.076  25.558  1.00 29.28           C  
ATOM   2275  CE2 PHE A 286      14.107  31.203  27.351  1.00 32.29           C  
ATOM   2276  CZ  PHE A 286      13.831  32.216  26.433  1.00 28.54           C  
ATOM   2277  N   GLN A 287       8.207  27.576  27.898  1.00 42.34           N  
ATOM   2278  CA  GLN A 287       7.378  26.386  27.925  1.00 45.71           C  
ATOM   2279  C   GLN A 287       6.482  26.360  26.685  1.00 46.41           C  
ATOM   2280  O   GLN A 287       6.275  25.308  26.080  1.00 46.25           O  
ATOM   2281  CB  GLN A 287       6.523  26.360  29.191  1.00 48.60           C  
ATOM   2282  CG  GLN A 287       5.982  24.982  29.527  1.00 52.89           C  
ATOM   2283  CD  GLN A 287       7.079  24.006  29.923  1.00 56.63           C  
ATOM   2284  OE1 GLN A 287       6.839  22.805  30.053  1.00 58.15           O  
ATOM   2285  NE2 GLN A 287       8.289  24.522  30.127  1.00 57.56           N  
ATOM   2286  N   ASP A 288       5.969  27.525  26.299  1.00 45.46           N  
ATOM   2287  CA  ASP A 288       5.098  27.622  25.130  1.00 46.45           C  
ATOM   2288  C   ASP A 288       5.793  28.335  23.973  1.00 44.94           C  
ATOM   2289  O   ASP A 288       5.180  29.146  23.275  1.00 46.33           O  
ATOM   2290  CB  ASP A 288       3.815  28.375  25.493  1.00 47.80           C  
ATOM   2291  CG  ASP A 288       4.040  29.864  25.644  1.00 50.55           C  
ATOM   2292  OD1 ASP A 288       5.067  30.253  26.243  1.00 49.78           O  
ATOM   2293  OD2 ASP A 288       3.185  30.645  25.171  1.00 52.77           O  
ATOM   2294  N   VAL A 289       7.069  28.033  23.765  1.00 41.44           N  
ATOM   2295  CA  VAL A 289       7.803  28.675  22.688  1.00 39.91           C  
ATOM   2296  C   VAL A 289       7.508  28.051  21.326  1.00 39.42           C  
ATOM   2297  O   VAL A 289       7.345  26.840  21.198  1.00 40.68           O  
ATOM   2298  CB  VAL A 289       9.339  28.638  22.939  1.00 38.50           C  
ATOM   2299  CG1 VAL A 289       9.836  27.206  22.987  1.00 36.05           C  
ATOM   2300  CG2 VAL A 289      10.060  29.422  21.855  1.00 34.38           C  
ATOM   2301  N   THR A 290       7.435  28.902  20.314  1.00 39.92           N  
ATOM   2302  CA  THR A 290       7.179  28.468  18.951  1.00 38.19           C  
ATOM   2303  C   THR A 290       8.145  29.228  18.069  1.00 40.31           C  
ATOM   2304  O   THR A 290       9.009  29.952  18.561  1.00 42.30           O  
ATOM   2305  CB  THR A 290       5.752  28.811  18.505  1.00 37.45           C  
ATOM   2306  OG1 THR A 290       5.556  30.230  18.594  1.00 35.19           O  
ATOM   2307  CG2 THR A 290       4.730  28.106  19.380  1.00 36.27           C  
ATOM   2308  N   LYS A 291       7.994  29.070  16.761  1.00 41.65           N  
ATOM   2309  CA  LYS A 291       8.862  29.757  15.826  1.00 41.70           C  
ATOM   2310  C   LYS A 291       8.025  30.450  14.758  1.00 41.56           C  
ATOM   2311  O   LYS A 291       7.742  29.880  13.708  1.00 42.59           O  
ATOM   2312  CB  LYS A 291       9.831  28.762  15.195  1.00 41.57           C  
ATOM   2313  CG  LYS A 291      10.888  29.398  14.319  1.00 44.36           C  
ATOM   2314  CD  LYS A 291      12.041  28.438  14.103  1.00 47.84           C  
ATOM   2315  CE  LYS A 291      13.117  29.064  13.239  1.00 49.15           C  
ATOM   2316  NZ  LYS A 291      14.403  28.332  13.376  1.00 51.88           N  
ATOM   2317  N   PRO A 292       7.604  31.695  15.027  1.00 40.33           N  
ATOM   2318  CA  PRO A 292       6.793  32.453  14.073  1.00 40.81           C  
ATOM   2319  C   PRO A 292       7.642  32.912  12.895  1.00 41.94           C  
ATOM   2320  O   PRO A 292       8.850  32.701  12.873  1.00 41.50           O  
ATOM   2321  CB  PRO A 292       6.283  33.640  14.901  1.00 39.40           C  
ATOM   2322  CG  PRO A 292       6.424  33.184  16.329  1.00 40.38           C  
ATOM   2323  CD  PRO A 292       7.711  32.414  16.305  1.00 40.67           C  
ATOM   2324  N   VAL A 293       6.999  33.543  11.921  1.00 44.04           N  
ATOM   2325  CA  VAL A 293       7.690  34.054  10.747  1.00 45.85           C  
ATOM   2326  C   VAL A 293       7.635  35.575  10.804  1.00 45.29           C  
ATOM   2327  O   VAL A 293       6.570  36.152  11.015  1.00 46.32           O  
ATOM   2328  CB  VAL A 293       7.003  33.596   9.445  1.00 47.38           C  
ATOM   2329  CG1 VAL A 293       7.814  34.051   8.245  1.00 49.25           C  
ATOM   2330  CG2 VAL A 293       6.841  32.086   9.446  1.00 49.73           C  
ATOM   2331  N   PRO A 294       8.781  36.245  10.627  1.00 45.17           N  
ATOM   2332  CA  PRO A 294       8.783  37.707  10.672  1.00 46.78           C  
ATOM   2333  C   PRO A 294       8.247  38.283   9.367  1.00 48.84           C  
ATOM   2334  O   PRO A 294       8.376  37.668   8.311  1.00 47.59           O  
ATOM   2335  CB  PRO A 294      10.259  38.034  10.871  1.00 44.36           C  
ATOM   2336  CG  PRO A 294      10.915  37.003  10.019  1.00 44.26           C  
ATOM   2337  CD  PRO A 294      10.140  35.732  10.372  1.00 45.90           C  
ATOM   2338  N   HIS A 295       7.635  39.457   9.446  1.00 51.20           N  
ATOM   2339  CA  HIS A 295       7.118  40.113   8.255  1.00 54.40           C  
ATOM   2340  C   HIS A 295       8.183  41.114   7.836  1.00 53.82           C  
ATOM   2341  O   HIS A 295       8.065  42.306   8.105  1.00 52.62           O  
ATOM   2342  CB  HIS A 295       5.806  40.839   8.561  1.00 59.42           C  
ATOM   2343  CG  HIS A 295       5.333  41.716   7.444  1.00 65.24           C  
ATOM   2344  ND1 HIS A 295       5.091  41.237   6.174  1.00 67.23           N  
ATOM   2345  CD2 HIS A 295       5.080  43.045   7.400  1.00 68.17           C  
ATOM   2346  CE1 HIS A 295       4.710  42.235   5.396  1.00 69.54           C  
ATOM   2347  NE2 HIS A 295       4.695  43.343   6.115  1.00 69.69           N  
ATOM   2348  N   LEU A 296       9.223  40.613   7.175  1.00 53.47           N  
ATOM   2349  CA  LEU A 296      10.335  41.445   6.749  1.00 54.26           C  
ATOM   2350  C   LEU A 296      10.139  42.164   5.434  1.00 56.12           C  
ATOM   2351  O   LEU A 296       9.481  41.667   4.520  1.00 56.92           O  
ATOM   2352  CB  LEU A 296      11.617  40.613   6.662  1.00 52.62           C  
ATOM   2353  CG  LEU A 296      12.062  39.930   7.953  1.00 52.44           C  
ATOM   2354  CD1 LEU A 296      13.429  39.297   7.743  1.00 51.43           C  
ATOM   2355  CD2 LEU A 296      12.121  40.947   9.081  1.00 52.14           C  
ATOM   2356  N   ARG A 297      10.729  43.349   5.354  1.00 58.22           N  
ATOM   2357  CA  ARG A 297      10.669  44.158   4.155  1.00 60.39           C  
ATOM   2358  C   ARG A 297      12.105  44.308   3.684  1.00 60.71           C  
ATOM   2359  O   ARG A 297      12.957  44.816   4.415  1.00 60.58           O  
ATOM   2360  CB  ARG A 297      10.077  45.530   4.460  1.00 62.67           C  
ATOM   2361  CG  ARG A 297       9.470  46.207   3.249  1.00 66.89           C  
ATOM   2362  CD  ARG A 297       8.286  45.401   2.737  1.00 70.35           C  
ATOM   2363  NE  ARG A 297       7.513  46.123   1.733  1.00 73.83           N  
ATOM   2364  CZ  ARG A 297       6.348  45.706   1.248  1.00 75.25           C  
ATOM   2365  NH1 ARG A 297       5.821  44.566   1.676  1.00 76.17           N  
ATOM   2366  NH2 ARG A 297       5.707  46.429   0.339  1.00 75.30           N  
ATOM   2367  N   LEU A 298      12.370  43.851   2.466  1.00 60.43           N  
ATOM   2368  CA  LEU A 298      13.705  43.924   1.895  1.00 59.47           C  
ATOM   2369  C   LEU A 298      13.686  44.745   0.614  1.00 60.90           C  
ATOM   2370  O   LEU A 298      14.002  45.935   0.628  1.00 61.75           O  
ATOM   2371  CB  LEU A 298      14.218  42.512   1.607  1.00 57.39           C  
ATOM   2372  CG  LEU A 298      14.194  41.568   2.816  1.00 57.19           C  
ATOM   2373  CD1 LEU A 298      14.654  40.182   2.395  1.00 55.53           C  
ATOM   2374  CD2 LEU A 298      15.088  42.126   3.930  1.00 54.96           C  
ATOM   2375  OXT LEU A 298      13.298  44.172  -0.428  1.00 62.96           O  
TER    2376      LEU A 298                                                      
HETATM 2377  C6 ACK8 A 500      25.840  38.933   7.693  0.80 29.83           C  
HETATM 2378  N1 ACK8 A 500      24.807  39.625   7.158  0.80 30.94           N  
HETATM 2379  C2 ACK8 A 500      24.634  40.889   7.540  0.80 29.47           C  
HETATM 2380  N3 ACK8 A 500      25.407  41.531   8.414  0.80 31.43           N  
HETATM 2381  C4 ACK8 A 500      26.458  40.912   8.987  0.80 31.01           C  
HETATM 2382  C5 ACK8 A 500      26.726  39.530   8.638  0.80 30.70           C  
HETATM 2383  C5AACK8 A 500      27.230  41.703   9.921  0.80 33.64           C  
HETATM 2384  C1AACK8 A 500      28.488  41.558  10.551  0.80 34.14           C  
HETATM 2385  N2AACK8 A 500      28.838  42.588  11.393  0.80 36.15           N  
HETATM 2386  C3AACK8 A 500      27.880  43.516  11.423  0.80 36.09           C  
HETATM 2387  S4AACK8 A 500      26.520  43.212  10.451  0.80 34.67           S  
HETATM 2388  C6AACK8 A 500      29.486  40.414  10.409  0.80 33.40           C  
HETATM 2389  C7AACK8 A 500      27.950  44.781  12.254  0.80 37.07           C  
HETATM 2390  N7 ACK8 A 500      23.522  41.571   6.943  0.80 30.24           N  
HETATM 2391  C1BACK8 A 500      22.931  42.898   7.044  0.80 31.63           C  
HETATM 2392  C2BACK8 A 500      23.427  43.911   7.925  0.80 33.44           C  
HETATM 2393  C3BACK8 A 500      22.812  45.181   7.976  0.80 34.50           C  
HETATM 2394  C4BACK8 A 500      21.676  45.489   7.147  0.80 33.85           C  
HETATM 2395  C5BACK8 A 500      21.190  44.454   6.271  0.80 31.68           C  
HETATM 2396  C6BACK8 A 500      21.807  43.183   6.225  0.80 32.13           C  
HETATM 2397  N7BACK8 A 500      21.026  46.845   7.198  0.80 35.82           N  
HETATM 2398  C8BACK8 A 500      19.847  47.208   6.356  0.80 39.03           C  
HETATM 2399  C9BACK8 A 500      21.513  47.936   8.096  0.80 35.97           C  
HETATM 2400  O  BHOH A 501      26.565  38.455   7.864  0.20 33.44           O  
HETATM 2401  O  BHOH A 502      25.223  40.113   6.473  0.20 53.65           O  
HETATM 2402  O  BHOH A 503      28.320  39.272   9.799  0.20 33.23           O  
HETATM 2403  O  BHOH A 504      29.786  38.115  11.742  0.20 34.17           O  
HETATM 2404  O  BHOH A 505      22.717  42.725   5.599  0.20 64.97           O  
HETATM 2405  O  BHOH A 506      27.016  41.620  10.531  0.20 54.03           O  
HETATM 2406  O  BHOH A 507      25.635  42.838   8.550  0.20 34.60           O  
HETATM 2407  O  BHOH A 508      28.487  45.137  11.679  0.20 52.93           O  
HETATM 2408  O  BHOH A 509      26.584  43.231  12.398  0.20 30.90           O  
HETATM 2409  O   HOH A 510      22.680  47.635   5.135  0.20 49.57           O  
HETATM 2410  O   HOH A 512      24.306  47.901  30.209  1.00 27.52           O  
HETATM 2411  O   HOH A 513      31.659  38.321  33.973  1.00 27.56           O  
HETATM 2412  O   HOH A 514      18.349  48.040  25.775  1.00 18.54           O  
HETATM 2413  O   HOH A 515      20.299  49.206  27.454  1.00 25.68           O  
HETATM 2414  O   HOH A 516      30.376  47.111  24.583  1.00 42.19           O  
HETATM 2415  O   HOH A 517      25.647  33.985  32.956  1.00 27.07           O  
HETATM 2416  O   HOH A 518      20.850  41.315  41.496  1.00 32.97           O  
HETATM 2417  O   HOH A 519      27.338  48.211  24.539  1.00 25.31           O  
HETATM 2418  O   HOH A 520      25.435  33.605   2.191  1.00 42.20           O  
HETATM 2419  O   HOH A 521      28.042  41.022  25.038  1.00 27.07           O  
HETATM 2420  O   HOH A 522      27.620  45.084  23.804  1.00 34.38           O  
HETATM 2421  O   HOH A 523      15.818  53.758  21.921  1.00 43.68           O  
HETATM 2422  O   HOH A 524       6.843  31.754  20.471  1.00 39.26           O  
HETATM 2423  O   HOH A 525      28.517  42.948  28.278  1.00 26.44           O  
HETATM 2424  O   HOH A 526      22.693  38.599  47.509  1.00 35.62           O  
HETATM 2425  O   HOH A 527      20.180  46.168  43.768  1.00 38.49           O  
HETATM 2426  O   HOH A 528      19.539  46.395  -0.204  1.00 39.09           O  
HETATM 2427  O   HOH A 529      34.982  43.257  48.339  1.00 37.81           O  
HETATM 2428  O   HOH A 530      12.112  29.010  18.182  1.00 47.05           O  
HETATM 2429  O   HOH A 531      25.852  30.771  29.554  1.00 40.49           O  
HETATM 2430  O   HOH A 532      11.803  44.816   8.052  1.00 36.84           O  
HETATM 2431  O   HOH A 533      25.229  27.940  29.168  1.00 31.93           O  
HETATM 2432  O   HOH A 534      20.095  43.735   0.906  1.00 36.55           O  
HETATM 2433  O   HOH A 535       5.052  45.426  41.966  1.00 54.90           O  
HETATM 2434  O   HOH A 536       4.913  38.518  28.161  1.00 51.89           O  
HETATM 2435  O   HOH A 537       5.458  49.012  39.085  1.00 32.41           O  
HETATM 2436  O   HOH A 538      15.610  47.206  -0.881  1.00 53.48           O  
HETATM 2437  O   HOH A 539      32.990  31.986  31.401  1.00 51.75           O  
HETATM 2438  O   HOH A 540       7.829  47.624  -1.162  1.00 47.67           O  
HETATM 2439  O   HOH A 541       8.017  27.530  13.090  1.00 57.49           O  
HETATM 2440  O   HOH A 542      16.244  54.395  41.955  1.00 33.11           O  
HETATM 2441  O   HOH A 543       2.174  40.508  20.546  1.00 51.69           O  
HETATM 2442  O   HOH A 544      27.532  50.597  47.365  1.00 45.76           O  
HETATM 2443  O   HOH A 545       6.494  40.221  12.419  1.00 42.53           O  
HETATM 2444  O   HOH A 546      26.745  54.344  24.878  1.00 49.08           O  
HETATM 2445  O   HOH A 547      27.472  55.385  15.844  1.00 54.64           O  
HETATM 2446  O   HOH A 548       3.145  31.218  18.011  1.00 43.86           O  
HETATM 2447  O   HOH A 549      29.022  44.264  25.986  1.00 32.27           O  
HETATM 2448  O   HOH A 550       9.275  44.365   8.774  1.00 51.16           O  
HETATM 2449  O   HOH A 551      33.064  22.293  13.324  1.00 46.08           O  
HETATM 2450  O   HOH A 552      10.801  32.692  14.762  1.00 35.60           O  
HETATM 2451  O   HOH A 553      23.408  58.878  47.987  1.00 40.42           O  
HETATM 2452  O   HOH A 554      18.588  60.978  32.383  1.00 53.35           O  
HETATM 2453  O   HOH A 555      27.831  29.125  12.449  1.00 38.54           O  
HETATM 2454  O   HOH A 556      20.718  49.919  19.539  1.00 45.58           O  
HETATM 2455  O   HOH A 557       8.754  41.007  38.650  1.00 49.88           O  
HETATM 2456  O   HOH A 558      30.811  33.780  36.268  1.00 59.17           O  
HETATM 2457  O   HOH A 560      27.129  32.117  31.911  1.00 33.34           O  
HETATM 2458  O   HOH A 561      17.322  33.635  41.007  1.00 51.36           O  
HETATM 2459  O   HOH A 562       4.910  31.576  22.243  1.00 38.00           O  
HETATM 2460  O   HOH A 563      17.093  45.093   5.108  1.00 42.75           O  
HETATM 2461  O   HOH A 564      10.412  42.370   0.911  1.00 40.18           O  
HETATM 2462  O   HOH A 565      26.702  26.587  27.538  1.00 34.55           O  
HETATM 2463  O   HOH A 566      15.445  55.254  26.208  1.00 54.44           O  
HETATM 2464  O   HOH A 567      26.627  33.354  35.404  1.00 47.16           O  
HETATM 2465  O   HOH A 581       1.372   6.968   3.273  1.00 59.54           O  
HETATM 2466  O   HOH A 588       1.543  34.980  28.837  1.00 64.48           O  
HETATM 2467  O   HOH A 589       0.405   4.231  -1.782  1.00 53.88           O  
HETATM 2468  O   HOH A 592       3.659   3.739   0.770  1.00 61.51           O  
HETATM 2469  O   HOH A 593       2.379   5.432  -0.315  1.00 55.81           O  
HETATM 2470  O   HOH A 595       1.822  38.803  27.926  1.00 52.21           O  
HETATM 2471  O   HOH A 596      13.904  36.024  11.545  1.00 32.14           O  
HETATM 2472  O   HOH A 597      22.704  29.503  35.920  1.00 44.60           O  
HETATM 2473  O   HOH A 598      20.016  43.475  39.264  1.00 53.71           O  
HETATM 2474  O   HOH A 599      34.520  21.280  15.575  1.00 59.21           O  
HETATM 2475  O   HOH A 600      27.510  30.425  34.032  1.00 46.56           O  
HETATM 2476  O   HOH A 601       2.414  31.787  20.998  1.00 42.23           O  
HETATM 2477  O   HOH A 602      18.830  23.535  28.672  1.00 39.78           O  
HETATM 2478  O   HOH A 603       2.688  33.448  16.577  1.00 47.96           O  
HETATM 2479  O   HOH A 604      10.640  44.238  -0.892  1.00 58.39           O  
HETATM 2480  O   HOH A 605      11.546  25.418  28.959  1.00 48.52           O  
HETATM 2481  O   HOH A 606      16.901  35.741  42.409  1.00 55.19           O  
HETATM 2482  O   HOH A 607      24.617  46.227  11.440  1.00 45.71           O  
HETATM 2483  O   HOH A 608      18.890  55.006  16.509  1.00 57.13           O  
HETATM 2484  O   HOH A 609       4.313  34.529  27.230  1.00 49.83           O  
HETATM 2485  O   HOH A 610      30.475  60.064  24.553  1.00 55.49           O  
HETATM 2486  O   HOH A 611      23.112  40.078  42.324  1.00 42.82           O  
CONECT 2377 2378 2382                                                           
CONECT 2378 2377 2379                                                           
CONECT 2379 2378 2380 2390                                                      
CONECT 2380 2379 2381                                                           
CONECT 2381 2380 2382 2383                                                      
CONECT 2382 2377 2381                                                           
CONECT 2383 2381 2384 2387                                                      
CONECT 2384 2383 2385 2388                                                      
CONECT 2385 2384 2386                                                           
CONECT 2386 2385 2387 2389                                                      
CONECT 2387 2383 2386                                                           
CONECT 2388 2384                                                                
CONECT 2389 2386                                                                
CONECT 2390 2379 2391                                                           
CONECT 2391 2390 2392 2396                                                      
CONECT 2392 2391 2393                                                           
CONECT 2393 2392 2394                                                           
CONECT 2394 2393 2395 2397                                                      
CONECT 2395 2394 2396                                                           
CONECT 2396 2391 2395                                                           
CONECT 2397 2394 2398 2399                                                      
CONECT 2398 2397                                                                
CONECT 2399 2397                                                                
MASTER      353    0    1   12    8    0    6    6 2476    1   23   23          
END                                                                             
