HEADER    TRANSFERASE                             17-DEC-98   1B39              
TITLE     HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CELL DIVISION PROTEIN KINASE 2);                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: INTACT;                                                    
COMPND   5 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   6 EC: 2.7.1.37;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BACULOVIRUS                               
KEYWDS    PROTEIN KINASE, TRANSFERASE, SERINE/THREONINE PROTEIN KINASE, ATP-    
KEYWDS   2 BINDING, CELL CYCLE, CELL DIVISION, MITOSIS, PHOSPHORYLATION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.R.BROWN,M.E.M.NOBLE,A.M.LAWRIE,M.C.MORRIS,P.TUNNAH,G.DIVITA,        
AUTHOR   2 L.N.JOHNSON,J.A.ENDICOTT                                             
REVDAT   5   03-APR-24 1B39    1       REMARK LINK                              
REVDAT   4   24-FEB-09 1B39    1       VERSN                                    
REVDAT   3   01-APR-03 1B39    1       JRNL                                     
REVDAT   2   22-DEC-99 1B39    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   23-DEC-98 1B39    0                                                
JRNL        AUTH   N.R.BROWN,M.E.NOBLE,A.M.LAWRIE,M.C.MORRIS,P.TUNNAH,G.DIVITA, 
JRNL        AUTH 2 L.N.JOHNSON,J.A.ENDICOTT                                     
JRNL        TITL   EFFECTS OF PHOSPHORYLATION OF THREONINE 160 ON               
JRNL        TITL 2 CYCLIN-DEPENDENT KINASE 2 STRUCTURE AND ACTIVITY.            
JRNL        REF    J.BIOL.CHEM.                  V. 274  8746 1999              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10085115                                                     
JRNL        DOI    10.1074/JBC.274.13.8746                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   U.SCHULZE-GAHMEN,J.BRANDSEN,H.D.JONES,D.O.MORGAN,L.MEIJER,   
REMARK   1  AUTH 2 J.VESELY,S.H.KIM                                             
REMARK   1  TITL   MULTIPLE MODES OF LIGAND RECOGNITION: CRYSTAL STRUCTURES OF  
REMARK   1  TITL 2 CYCLIN-DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH ATP AND    
REMARK   1  TITL 3 TWO INHIBITORS, OLOMOUCINE AND ISOPENTENYLADENINE            
REMARK   1  REF    PROTEINS                      V.  22   378 1995              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15947                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE-R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM 5%                       
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2338                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.020 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.049 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.044 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.172 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1B39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE DEPOSITION ID IS D_1000008204.                                   
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                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.044                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15947                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: UNPUBLISHED                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: STREAK SEEDING FROM UNPHOSPHORYLATED     
REMARK 280  CDK2 CRYSTALS, USING PHOSPHORYLATED CDK2 PROTEIN PREEQUILIBRATED    
REMARK 280  AGAINST WELL SOLUTION. PROTEIN AT 10 MG/ML IN 50MM TRIS/HCL         
REMARK 280  PH7.5, 50MM NACL. WELL SOLUTION OF 12-16% PEG 3350, 0.1M TRIS/      
REMARK 280  HCL PH 7.5, 50MM AMMONIUM ACETATE., STREAK SEEDING                  
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       26.71000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.26000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.83000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.26000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.71000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.83000            
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     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   8   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    ARG A  22   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    LEU A  32   CA  -  CB  -  CG  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    LEU A  58   CB  -  CG  -  CD1 ANGL. DEV. = -12.0 DEGREES          
REMARK 500    LEU A  58   CB  -  CG  -  CD2 ANGL. DEV. =  17.6 DEGREES          
REMARK 500    GLN A  85   OE1 -  CD  -  NE2 ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD1 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    TYR A 107   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 122   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    LEU A 124   N   -  CA  -  CB  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    THR A 137   O   -  C   -  N   ANGL. DEV. = -10.2 DEGREES          
REMARK 500    GLU A 138   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    GLU A 138   OE1 -  CD  -  OE2 ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ARG A 150   CD  -  NE  -  CZ  ANGL. DEV. =  12.7 DEGREES          
REMARK 500    MET A 196   O   -  C   -  N   ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG A 200   CA  -  CB  -  CG  ANGL. DEV. =  24.6 DEGREES          
REMARK 500    ARG A 200   CG  -  CD  -  NE  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    SER A 207   N   -  CA  -  CB  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG A 217   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    SER A 232   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    SER A 232   N   -  CA  -  CB  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    MET A 233   CA  -  CB  -  CG  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TRP A 243   CA  -  CB  -  CG  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 245   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLU A 257   CG  -  CD  -  OE1 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ASP A 288   CB  -  CG  -  OD2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   8      146.72   -170.60                                   
REMARK 500    LEU A  25      -79.21    -87.22                                   
REMARK 500    ARG A 126      -15.37     77.55                                   
REMARK 500    TYR A 159      -58.05    -29.82                                   
REMARK 500    THR A 160       30.48    -82.34                                   
REMARK 500    HIS A 161      -33.37     82.69                                   
REMARK 500    SER A 181     -164.89   -108.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU A 138         11.59                                           
REMARK 500    TYR A 269        -10.29                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 382  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 132   OD1                                                    
REMARK 620 2 ASP A 145   OD2 103.2                                              
REMARK 620 3 ATP A 381   O1B  74.2 173.9                                        
REMARK 620 4 ATP A 381   O2A 170.2  86.4  96.0                                  
REMARK 620 5 ATP A 381   O2G  97.9  91.0  83.9  79.3                            
REMARK 620 6 HOH A 527   O    87.8  99.2  86.3  93.0 166.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 382                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 381                 
DBREF  1B39 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  299  ACE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU          
SEQRES   2 A  299  GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU          
SEQRES   3 A  299  THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP          
SEQRES   4 A  299  THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU          
SEQRES   5 A  299  ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL          
SEQRES   6 A  299  LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR          
SEQRES   7 A  299  LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE          
SEQRES   8 A  299  MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU          
SEQRES   9 A  299  ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA          
SEQRES  10 A  299  PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS          
SEQRES  11 A  299  PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS          
SEQRES  12 A  299  LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO          
SEQRES  13 A  299  VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR          
SEQRES  14 A  299  ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER          
SEQRES  15 A  299  THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA          
SEQRES  16 A  299  GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER          
SEQRES  17 A  299  GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY          
SEQRES  18 A  299  THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET          
SEQRES  19 A  299  PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN          
SEQRES  20 A  299  ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY          
SEQRES  21 A  299  ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN          
SEQRES  22 A  299  LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE          
SEQRES  23 A  299  PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU          
HET    ACE  A   0       3                                                       
HET     MG  A 382       1                                                       
HET    ATP  A 381      31                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4  HOH   *145(H2 O)                                                    
HELIX    1   1 SER A   46  GLU A   57  1                                  12    
HELIX    2   2 LEU A   87  ALA A   93  1                                   7    
HELIX    3   3 LEU A  101  HIS A  121  1                                  21    
HELIX    4   4 PRO A  130  ASN A  132  5                                   3    
HELIX    5   5 LEU A  148  PHE A  152  1                                   5    
HELIX    6   6 PRO A  171  LEU A  174  1                                   4    
HELIX    7   7 THR A  182  THR A  198  5                                  17    
HELIX    8   8 GLU A  208  LEU A  219  1                                  12    
HELIX    9   9 VAL A  230  SER A  232  5                                   3    
HELIX   10  10 PHE A  248  VAL A  251  1                                   4    
HELIX   11  11 GLU A  257  MET A  266  1                                  10    
HELIX   12  12 ALA A  277  ALA A  282  1                                   6    
HELIX   13  13 PRO A  284  ASP A  288  5                                   5    
SHEET    1   A 5 LEU A  66  THR A  72  0                                        
SHEET    2   A 5 LYS A  75  GLU A  81 -1  N  VAL A  79   O  LEU A  67           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  N  ILE A  35   O  LEU A  76           
SHEET    4   A 5 VAL A  17  ASN A  23 -1  N  ALA A  21   O  VAL A  30           
SHEET    5   A 5 PHE A   4  LYS A   9 -1  N  GLU A   8   O  LYS A  20           
SHEET    1   B 2 LEU A 133  ILE A 135  0                                        
SHEET    2   B 2 ILE A 141  LEU A 143 -1  N  LYS A 142   O  LEU A 134           
LINK         C   ACE A   0                 N   MET A   1     1555   1555  1.33  
LINK         OD1 ASN A 132                MG    MG A 382     1555   1555  2.04  
LINK         OD2 ASP A 145                MG    MG A 382     1555   1555  2.07  
LINK         O1B ATP A 381                MG    MG A 382     1555   1555  2.24  
LINK         O2A ATP A 381                MG    MG A 382     1555   1555  2.37  
LINK         O2G ATP A 381                MG    MG A 382     1555   1555  2.15  
LINK        MG    MG A 382                 O   HOH A 527     1555   1555  2.21  
SITE     1 AC1  4 ASN A 132  ASP A 145  ATP A 381  HOH A 527                    
SITE     1 AC2 22 ILE A  10  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC2 22 VAL A  18  ALA A  31  LYS A  33  GLU A  81                    
SITE     3 AC2 22 PHE A  82  LEU A  83  ASP A  86  ASP A 127                    
SITE     4 AC2 22 LYS A 129  GLN A 131  ASN A 132  LEU A 134                    
SITE     5 AC2 22 ASP A 145   MG A 382  HOH A 447  HOH A 453                    
SITE     6 AC2 22 HOH A 512  HOH A 527                                          
CRYST1   53.420   71.660   72.520  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      0.018719  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013955  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013789        0.00000                         
HETATM    1  C   ACE A   0     -14.518  33.352  -2.537  1.00 57.76           C  
HETATM    2  O   ACE A   0     -13.183  34.007  -2.646  1.00 55.99           O  
HETATM    3  CH3 ACE A   0     -15.603  33.993  -2.469  1.00 58.49           C  
ATOM      4  N   MET A   1     -14.446  32.026  -2.488  1.00 58.29           N  
ATOM      5  CA  MET A   1     -13.209  31.351  -2.140  1.00 58.98           C  
ATOM      6  C   MET A   1     -12.654  30.775  -3.438  1.00 58.41           C  
ATOM      7  O   MET A   1     -11.526  30.225  -3.442  1.00 59.83           O  
ATOM      8  CB  MET A   1     -13.270  30.275  -1.087  1.00 61.90           C  
ATOM      9  CG  MET A   1     -13.944  28.968  -1.370  1.00 64.83           C  
ATOM     10  SD  MET A   1     -12.963  27.718  -2.208  1.00 68.89           S  
ATOM     11  CE  MET A   1     -11.908  27.083  -0.902  1.00 68.01           C  
ATOM     12  N   GLU A   2     -13.393  30.987  -4.539  1.00 56.58           N  
ATOM     13  CA  GLU A   2     -12.937  30.530  -5.855  1.00 53.05           C  
ATOM     14  C   GLU A   2     -11.974  31.559  -6.418  1.00 49.24           C  
ATOM     15  O   GLU A   2     -11.450  31.401  -7.512  1.00 49.78           O  
ATOM     16  CB  GLU A   2     -14.051  30.386  -6.878  1.00 56.86           C  
ATOM     17  CG  GLU A   2     -14.744  31.692  -7.271  1.00 61.10           C  
ATOM     18  CD  GLU A   2     -15.961  31.950  -6.383  1.00 64.64           C  
ATOM     19  OE1 GLU A   2     -16.245  31.063  -5.522  1.00 65.99           O  
ATOM     20  OE2 GLU A   2     -16.620  33.015  -6.494  1.00 65.72           O  
ATOM     21  N   ASN A   3     -11.750  32.659  -5.702  1.00 43.24           N  
ATOM     22  CA  ASN A   3     -10.865  33.719  -6.097  1.00 39.69           C  
ATOM     23  C   ASN A   3      -9.426  33.301  -5.685  1.00 36.31           C  
ATOM     24  O   ASN A   3      -8.573  34.189  -5.704  1.00 37.01           O  
ATOM     25  CB  ASN A   3     -11.186  35.055  -5.443  1.00 38.13           C  
ATOM     26  CG  ASN A   3     -12.480  35.752  -5.701  1.00 38.87           C  
ATOM     27  OD1 ASN A   3     -13.480  35.724  -4.950  1.00 36.99           O  
ATOM     28  ND2 ASN A   3     -12.518  36.558  -6.771  1.00 37.41           N  
ATOM     29  N   PHE A   4      -9.163  32.087  -5.285  1.00 31.23           N  
ATOM     30  CA  PHE A   4      -7.860  31.654  -4.873  1.00 34.55           C  
ATOM     31  C   PHE A   4      -7.548  30.309  -5.540  1.00 35.13           C  
ATOM     32  O   PHE A   4      -8.417  29.455  -5.516  1.00 35.65           O  
ATOM     33  CB  PHE A   4      -7.646  31.357  -3.356  1.00 32.19           C  
ATOM     34  CG  PHE A   4      -7.890  32.588  -2.523  1.00 34.84           C  
ATOM     35  CD1 PHE A   4      -6.892  33.521  -2.277  1.00 32.41           C  
ATOM     36  CD2 PHE A   4      -9.174  32.829  -2.048  1.00 33.87           C  
ATOM     37  CE1 PHE A   4      -7.153  34.675  -1.590  1.00 34.52           C  
ATOM     38  CE2 PHE A   4      -9.445  33.982  -1.368  1.00 33.81           C  
ATOM     39  CZ  PHE A   4      -8.450  34.902  -1.137  1.00 35.73           C  
ATOM     40  N   GLN A   5      -6.319  30.127  -5.987  1.00 38.82           N  
ATOM     41  CA  GLN A   5      -5.830  28.849  -6.499  1.00 40.80           C  
ATOM     42  C   GLN A   5      -4.999  28.240  -5.376  1.00 39.80           C  
ATOM     43  O   GLN A   5      -4.072  28.916  -4.898  1.00 38.34           O  
ATOM     44  CB  GLN A   5      -4.917  29.089  -7.694  1.00 44.62           C  
ATOM     45  CG  GLN A   5      -4.440  27.909  -8.505  1.00 51.17           C  
ATOM     46  CD  GLN A   5      -4.794  28.037  -9.990  1.00 57.33           C  
ATOM     47  OE1 GLN A   5      -4.719  29.145 -10.580  1.00 59.54           O  
ATOM     48  NE2 GLN A   5      -5.206  26.934 -10.648  1.00 58.26           N  
ATOM     49  N   LYS A   6      -5.270  27.019  -4.998  1.00 40.30           N  
ATOM     50  CA  LYS A   6      -4.537  26.312  -3.969  1.00 42.81           C  
ATOM     51  C   LYS A   6      -3.208  25.781  -4.500  1.00 44.95           C  
ATOM     52  O   LYS A   6      -3.177  25.053  -5.472  1.00 46.92           O  
ATOM     53  CB  LYS A   6      -5.309  25.115  -3.410  1.00 44.23           C  
ATOM     54  CG  LYS A   6      -6.650  25.544  -2.797  1.00 46.54           C  
ATOM     55  CD  LYS A   6      -7.389  24.310  -2.281  1.00 46.50           C  
ATOM     56  CE  LYS A   6      -8.886  24.363  -2.490  1.00 46.44           C  
ATOM     57  NZ  LYS A   6      -9.686  24.357  -1.225  1.00 43.50           N  
ATOM     58  N   VAL A   7      -2.094  26.120  -3.871  1.00 44.39           N  
ATOM     59  CA  VAL A   7      -0.786  25.707  -4.283  1.00 44.35           C  
ATOM     60  C   VAL A   7      -0.382  24.442  -3.535  1.00 46.11           C  
ATOM     61  O   VAL A   7       0.422  23.674  -4.067  1.00 48.20           O  
ATOM     62  CB  VAL A   7       0.295  26.773  -3.854  1.00 41.52           C  
ATOM     63  CG1 VAL A   7       1.698  26.280  -4.121  1.00 39.06           C  
ATOM     64  CG2 VAL A   7      -0.013  28.082  -4.529  1.00 39.67           C  
ATOM     65  N   GLU A   8      -0.695  24.414  -2.241  1.00 45.90           N  
ATOM     66  CA  GLU A   8      -0.203  23.279  -1.462  1.00 46.44           C  
ATOM     67  C   GLU A   8      -0.875  23.344  -0.098  1.00 44.39           C  
ATOM     68  O   GLU A   8      -1.116  24.434   0.412  1.00 41.23           O  
ATOM     69  CB  GLU A   8       1.314  23.259  -1.370  1.00 50.18           C  
ATOM     70  CG  GLU A   8       2.179  24.317  -0.742  1.00 53.82           C  
ATOM     71  CD  GLU A   8       3.568  23.903  -0.289  1.00 56.70           C  
ATOM     72  OE1 GLU A   8       4.367  23.448  -1.135  1.00 59.36           O  
ATOM     73  OE2 GLU A   8       4.019  23.984   0.882  1.00 57.19           O  
ATOM     74  N   LYS A   9      -1.127  22.165   0.459  1.00 45.77           N  
ATOM     75  CA  LYS A   9      -1.725  21.988   1.782  1.00 45.76           C  
ATOM     76  C   LYS A   9      -0.692  22.289   2.846  1.00 45.20           C  
ATOM     77  O   LYS A   9       0.235  21.481   2.964  1.00 48.90           O  
ATOM     78  CB  LYS A   9      -2.222  20.567   1.973  1.00 46.81           C  
ATOM     79  CG  LYS A   9      -2.730  20.203   3.357  1.00 50.17           C  
ATOM     80  CD  LYS A   9      -3.831  19.127   3.276  1.00 51.64           C  
ATOM     81  CE  LYS A   9      -4.286  18.733   4.691  1.00 52.69           C  
ATOM     82  NZ  LYS A   9      -5.128  17.469   4.687  1.00 50.16           N  
ATOM     83  N   ILE A  10      -0.716  23.438   3.480  1.00 44.42           N  
ATOM     84  CA  ILE A  10       0.359  23.678   4.447  1.00 45.61           C  
ATOM     85  C   ILE A  10       0.105  22.701   5.580  1.00 46.12           C  
ATOM     86  O   ILE A  10       0.956  21.833   5.735  1.00 49.23           O  
ATOM     87  CB  ILE A  10       0.601  25.088   4.976  1.00 43.72           C  
ATOM     88  CG1 ILE A  10       0.864  26.047   3.820  1.00 41.88           C  
ATOM     89  CG2 ILE A  10       1.831  25.052   5.890  1.00 43.69           C  
ATOM     90  CD1 ILE A  10       0.674  27.490   4.227  1.00 40.71           C  
ATOM     91  N   GLY A  11      -1.045  22.752   6.236  1.00 46.47           N  
ATOM     92  CA  GLY A  11      -1.254  21.715   7.264  1.00 49.40           C  
ATOM     93  C   GLY A  11      -2.702  21.649   7.689  1.00 49.83           C  
ATOM     94  O   GLY A  11      -3.583  22.169   7.009  1.00 50.15           O  
ATOM     95  N   GLU A  12      -2.918  20.944   8.781  1.00 51.17           N  
ATOM     96  CA  GLU A  12      -4.269  20.805   9.322  1.00 53.84           C  
ATOM     97  C   GLU A  12      -4.096  21.019  10.814  1.00 53.91           C  
ATOM     98  O   GLU A  12      -2.941  21.014  11.292  1.00 54.98           O  
ATOM     99  CB  GLU A  12      -4.992  19.559   8.870  1.00 57.68           C  
ATOM    100  CG  GLU A  12      -4.268  18.252   9.062  1.00 62.72           C  
ATOM    101  CD  GLU A  12      -4.510  17.078   8.136  1.00 64.31           C  
ATOM    102  OE1 GLU A  12      -5.166  17.193   7.083  1.00 64.17           O  
ATOM    103  OE2 GLU A  12      -4.046  15.959   8.523  1.00 66.15           O  
ATOM    104  N   GLY A  13      -5.166  21.347  11.521  1.00 53.19           N  
ATOM    105  CA  GLY A  13      -5.008  21.655  12.936  1.00 52.36           C  
ATOM    106  C   GLY A  13      -6.341  21.813  13.645  1.00 52.28           C  
ATOM    107  O   GLY A  13      -7.355  21.349  13.156  1.00 49.07           O  
ATOM    108  N   THR A  14      -6.324  22.382  14.855  1.00 52.98           N  
ATOM    109  CA  THR A  14      -7.563  22.511  15.637  1.00 54.67           C  
ATOM    110  C   THR A  14      -8.784  22.912  14.836  1.00 54.91           C  
ATOM    111  O   THR A  14      -9.791  22.199  14.806  1.00 58.16           O  
ATOM    112  CB  THR A  14      -7.363  23.503  16.807  1.00 53.92           C  
ATOM    113  OG1 THR A  14      -6.136  23.150  17.440  1.00 53.37           O  
ATOM    114  CG2 THR A  14      -8.499  23.419  17.819  1.00 55.06           C  
ATOM    115  N   TYR A  15      -8.750  24.049  14.168  1.00 55.79           N  
ATOM    116  CA  TYR A  15      -9.817  24.663  13.448  1.00 55.17           C  
ATOM    117  C   TYR A  15     -10.026  24.284  12.005  1.00 54.56           C  
ATOM    118  O   TYR A  15     -11.155  24.548  11.523  1.00 55.58           O  
ATOM    119  CB  TYR A  15      -9.580  26.201  13.346  1.00 57.45           C  
ATOM    120  CG  TYR A  15      -9.356  26.765  14.730  1.00 59.32           C  
ATOM    121  CD1 TYR A  15     -10.157  26.331  15.777  1.00 60.12           C  
ATOM    122  CD2 TYR A  15      -8.344  27.686  14.979  1.00 60.86           C  
ATOM    123  CE1 TYR A  15      -9.951  26.784  17.062  1.00 61.58           C  
ATOM    124  CE2 TYR A  15      -8.133  28.146  16.272  1.00 61.66           C  
ATOM    125  CZ  TYR A  15      -8.944  27.702  17.286  1.00 61.60           C  
ATOM    126  OH  TYR A  15      -8.796  28.159  18.575  1.00 63.95           O  
ATOM    127  N   GLY A  16      -8.992  23.821  11.317  1.00 49.36           N  
ATOM    128  CA  GLY A  16      -9.346  23.558   9.906  1.00 46.48           C  
ATOM    129  C   GLY A  16      -8.058  23.243   9.159  1.00 43.91           C  
ATOM    130  O   GLY A  16      -7.101  22.869   9.844  1.00 41.07           O  
ATOM    131  N   VAL A  17      -8.124  23.518   7.859  1.00 38.32           N  
ATOM    132  CA  VAL A  17      -6.949  23.135   7.072  1.00 38.90           C  
ATOM    133  C   VAL A  17      -6.399  24.361   6.403  1.00 38.24           C  
ATOM    134  O   VAL A  17      -7.217  25.184   5.992  1.00 38.12           O  
ATOM    135  CB  VAL A  17      -7.377  22.008   6.129  1.00 39.60           C  
ATOM    136  CG1 VAL A  17      -8.590  22.557   5.364  1.00 41.28           C  
ATOM    137  CG2 VAL A  17      -6.243  21.520   5.282  1.00 40.44           C  
ATOM    138  N   VAL A  18      -5.064  24.463   6.418  1.00 36.78           N  
ATOM    139  CA  VAL A  18      -4.395  25.675   5.968  1.00 34.69           C  
ATOM    140  C   VAL A  18      -3.771  25.391   4.621  1.00 34.30           C  
ATOM    141  O   VAL A  18      -3.075  24.372   4.524  1.00 32.85           O  
ATOM    142  CB  VAL A  18      -3.238  26.126   6.859  1.00 36.06           C  
ATOM    143  CG1 VAL A  18      -2.651  27.467   6.386  1.00 37.51           C  
ATOM    144  CG2 VAL A  18      -3.528  26.335   8.342  1.00 35.01           C  
ATOM    145  N   TYR A  19      -4.128  26.197   3.613  1.00 33.70           N  
ATOM    146  CA  TYR A  19      -3.440  25.966   2.325  1.00 33.38           C  
ATOM    147  C   TYR A  19      -2.601  27.199   1.957  1.00 28.22           C  
ATOM    148  O   TYR A  19      -3.001  28.320   2.247  1.00 27.43           O  
ATOM    149  CB  TYR A  19      -4.383  25.761   1.144  1.00 38.11           C  
ATOM    150  CG  TYR A  19      -5.197  24.501   1.227  1.00 43.74           C  
ATOM    151  CD1 TYR A  19      -6.426  24.546   1.890  1.00 47.14           C  
ATOM    152  CD2 TYR A  19      -4.792  23.323   0.644  1.00 45.71           C  
ATOM    153  CE1 TYR A  19      -7.205  23.395   1.953  1.00 50.03           C  
ATOM    154  CE2 TYR A  19      -5.570  22.182   0.724  1.00 47.40           C  
ATOM    155  CZ  TYR A  19      -6.765  22.227   1.380  1.00 47.70           C  
ATOM    156  OH  TYR A  19      -7.567  21.120   1.482  1.00 51.42           O  
ATOM    157  N   LYS A  20      -1.582  26.981   1.176  1.00 25.87           N  
ATOM    158  CA  LYS A  20      -0.818  28.121   0.688  1.00 24.28           C  
ATOM    159  C   LYS A  20      -1.691  28.456  -0.542  1.00 24.95           C  
ATOM    160  O   LYS A  20      -1.985  27.502  -1.280  1.00 23.21           O  
ATOM    161  CB  LYS A  20       0.615  27.808   0.277  1.00 23.41           C  
ATOM    162  CG  LYS A  20       1.345  29.005  -0.372  1.00 25.02           C  
ATOM    163  CD  LYS A  20       2.785  28.609  -0.826  1.00 27.41           C  
ATOM    164  CE  LYS A  20       3.773  29.677  -1.171  1.00 25.76           C  
ATOM    165  NZ  LYS A  20       5.207  29.157  -1.410  1.00 25.15           N  
ATOM    166  N   ALA A  21      -1.967  29.742  -0.765  1.00 25.46           N  
ATOM    167  CA  ALA A  21      -2.741  29.951  -2.000  1.00 25.34           C  
ATOM    168  C   ALA A  21      -2.431  31.282  -2.642  1.00 25.15           C  
ATOM    169  O   ALA A  21      -1.792  32.128  -2.020  1.00 23.63           O  
ATOM    170  CB  ALA A  21      -4.203  29.756  -1.564  1.00 26.21           C  
ATOM    171  N   ARG A  22      -2.898  31.495  -3.874  1.00 27.85           N  
ATOM    172  CA  ARG A  22      -2.668  32.737  -4.600  1.00 33.17           C  
ATOM    173  C   ARG A  22      -3.947  33.459  -4.992  1.00 35.95           C  
ATOM    174  O   ARG A  22      -4.784  32.837  -5.631  1.00 34.63           O  
ATOM    175  CB  ARG A  22      -1.848  32.402  -5.885  1.00 34.43           C  
ATOM    176  CG  ARG A  22      -1.540  33.601  -6.765  1.00 37.61           C  
ATOM    177  CD  ARG A  22      -0.874  33.205  -8.113  1.00 41.67           C  
ATOM    178  NE  ARG A  22       0.341  32.505  -7.716  1.00 44.62           N  
ATOM    179  CZ  ARG A  22       1.471  33.179  -7.398  1.00 46.35           C  
ATOM    180  NH1 ARG A  22       1.567  34.527  -7.480  1.00 41.39           N  
ATOM    181  NH2 ARG A  22       2.408  32.299  -6.981  1.00 46.75           N  
ATOM    182  N   ASN A  23      -4.053  34.764  -4.745  1.00 39.56           N  
ATOM    183  CA  ASN A  23      -5.114  35.598  -5.211  1.00 44.25           C  
ATOM    184  C   ASN A  23      -5.150  35.687  -6.738  1.00 46.95           C  
ATOM    185  O   ASN A  23      -4.241  36.270  -7.326  1.00 49.95           O  
ATOM    186  CB  ASN A  23      -4.907  37.070  -4.801  1.00 46.72           C  
ATOM    187  CG  ASN A  23      -6.207  37.851  -5.019  1.00 48.45           C  
ATOM    188  OD1 ASN A  23      -6.703  37.972  -6.147  1.00 48.85           O  
ATOM    189  ND2 ASN A  23      -6.757  38.332  -3.899  1.00 47.89           N  
ATOM    190  N   LYS A  24      -6.229  35.277  -7.356  1.00 51.00           N  
ATOM    191  CA  LYS A  24      -6.439  35.303  -8.801  1.00 54.35           C  
ATOM    192  C   LYS A  24      -6.571  36.707  -9.372  1.00 55.92           C  
ATOM    193  O   LYS A  24      -6.337  36.864 -10.558  1.00 55.44           O  
ATOM    194  CB  LYS A  24      -7.653  34.475  -9.187  1.00 53.80           C  
ATOM    195  CG  LYS A  24      -7.422  33.017  -8.770  1.00 55.31           C  
ATOM    196  CD  LYS A  24      -8.218  32.134  -9.749  1.00 55.38           C  
ATOM    197  CE  LYS A  24      -8.608  30.821  -9.119  1.00 55.14           C  
ATOM    198  NZ  LYS A  24     -10.045  30.515  -9.243  1.00 55.49           N  
ATOM    199  N   LEU A  25      -6.868  37.691  -8.533  1.00 58.96           N  
ATOM    200  CA  LEU A  25      -6.849  39.091  -8.923  1.00 61.50           C  
ATOM    201  C   LEU A  25      -5.416  39.631  -8.727  1.00 60.84           C  
ATOM    202  O   LEU A  25      -4.666  39.743  -9.698  1.00 63.55           O  
ATOM    203  CB  LEU A  25      -7.829  39.979  -8.154  1.00 62.90           C  
ATOM    204  CG  LEU A  25      -8.233  41.318  -8.798  1.00 64.15           C  
ATOM    205  CD1 LEU A  25      -8.679  41.118 -10.248  1.00 66.01           C  
ATOM    206  CD2 LEU A  25      -9.331  42.029  -8.025  1.00 62.91           C  
ATOM    207  N   THR A  26      -5.031  39.955  -7.513  1.00 57.36           N  
ATOM    208  CA  THR A  26      -3.769  40.484  -7.141  1.00 54.11           C  
ATOM    209  C   THR A  26      -2.483  39.820  -7.671  1.00 50.52           C  
ATOM    210  O   THR A  26      -1.490  40.488  -7.994  1.00 49.23           O  
ATOM    211  CB  THR A  26      -3.493  40.359  -5.612  1.00 56.04           C  
ATOM    212  OG1 THR A  26      -4.540  40.663  -4.709  1.00 57.44           O  
ATOM    213  CG2 THR A  26      -2.272  41.267  -5.315  1.00 56.35           C  
ATOM    214  N   GLY A  27      -2.439  38.518  -7.440  1.00 45.65           N  
ATOM    215  CA  GLY A  27      -1.257  37.704  -7.527  1.00 39.79           C  
ATOM    216  C   GLY A  27      -0.697  37.543  -6.086  1.00 34.87           C  
ATOM    217  O   GLY A  27       0.312  36.851  -5.872  1.00 30.12           O  
ATOM    218  N   GLU A  28      -1.358  38.149  -5.083  1.00 31.17           N  
ATOM    219  CA  GLU A  28      -0.916  37.984  -3.701  1.00 33.91           C  
ATOM    220  C   GLU A  28      -0.910  36.538  -3.204  1.00 30.35           C  
ATOM    221  O   GLU A  28      -1.663  35.611  -3.612  1.00 28.44           O  
ATOM    222  CB  GLU A  28      -1.753  38.974  -2.904  1.00 37.63           C  
ATOM    223  CG  GLU A  28      -1.272  39.296  -1.494  1.00 42.54           C  
ATOM    224  CD  GLU A  28      -2.344  40.058  -0.732  1.00 45.71           C  
ATOM    225  OE1 GLU A  28      -3.558  39.934  -1.011  1.00 45.53           O  
ATOM    226  OE2 GLU A  28      -1.980  40.841   0.175  1.00 48.78           O  
ATOM    227  N   VAL A  29       0.154  36.191  -2.487  1.00 27.56           N  
ATOM    228  CA  VAL A  29       0.390  34.852  -1.951  1.00 26.86           C  
ATOM    229  C   VAL A  29      -0.040  34.917  -0.474  1.00 26.94           C  
ATOM    230  O   VAL A  29       0.281  35.827   0.270  1.00 25.68           O  
ATOM    231  CB  VAL A  29       1.754  34.229  -2.111  1.00 27.19           C  
ATOM    232  CG1 VAL A  29       1.999  33.024  -1.206  1.00 27.18           C  
ATOM    233  CG2 VAL A  29       1.959  33.781  -3.557  1.00 26.22           C  
ATOM    234  N   VAL A  30      -0.951  33.969  -0.148  1.00 26.52           N  
ATOM    235  CA  VAL A  30      -1.566  33.949   1.160  1.00 24.16           C  
ATOM    236  C   VAL A  30      -1.704  32.537   1.739  1.00 22.71           C  
ATOM    237  O   VAL A  30      -1.480  31.460   1.157  1.00 19.66           O  
ATOM    238  CB  VAL A  30      -2.971  34.598   1.210  1.00 25.68           C  
ATOM    239  CG1 VAL A  30      -3.035  36.029   0.696  1.00 25.79           C  
ATOM    240  CG2 VAL A  30      -3.928  33.728   0.384  1.00 18.90           C  
ATOM    241  N   ALA A  31      -2.021  32.631   3.068  1.00 20.82           N  
ATOM    242  CA  ALA A  31      -2.304  31.367   3.751  1.00 22.05           C  
ATOM    243  C   ALA A  31      -3.841  31.447   3.891  1.00 21.51           C  
ATOM    244  O   ALA A  31      -4.348  32.428   4.400  1.00 24.39           O  
ATOM    245  CB  ALA A  31      -1.628  31.105   5.080  1.00 22.24           C  
ATOM    246  N   LEU A  32      -4.519  30.448   3.421  1.00 21.67           N  
ATOM    247  CA  LEU A  32      -5.983  30.398   3.396  1.00 23.94           C  
ATOM    248  C   LEU A  32      -6.461  29.346   4.383  1.00 24.03           C  
ATOM    249  O   LEU A  32      -6.203  28.136   4.195  1.00 23.87           O  
ATOM    250  CB  LEU A  32      -6.491  30.005   2.001  1.00 26.46           C  
ATOM    251  CG  LEU A  32      -7.787  30.386   1.296  1.00 28.82           C  
ATOM    252  CD1 LEU A  32      -8.289  29.169   0.545  1.00 29.27           C  
ATOM    253  CD2 LEU A  32      -8.854  31.068   2.147  1.00 26.45           C  
ATOM    254  N   LYS A  33      -7.062  29.805   5.469  1.00 23.61           N  
ATOM    255  CA  LYS A  33      -7.525  28.742   6.377  1.00 28.25           C  
ATOM    256  C   LYS A  33      -8.992  28.376   6.144  1.00 29.94           C  
ATOM    257  O   LYS A  33      -9.915  29.203   6.205  1.00 29.16           O  
ATOM    258  CB  LYS A  33      -7.241  29.132   7.838  1.00 29.64           C  
ATOM    259  CG  LYS A  33      -7.569  27.988   8.823  1.00 30.69           C  
ATOM    260  CD  LYS A  33      -7.098  28.373  10.215  1.00 35.13           C  
ATOM    261  CE  LYS A  33      -5.679  27.881  10.535  1.00 37.27           C  
ATOM    262  NZ  LYS A  33      -5.558  27.700  12.055  1.00 38.22           N  
ATOM    263  N   LYS A  34      -9.254  27.091   5.891  1.00 33.93           N  
ATOM    264  CA  LYS A  34     -10.702  26.773   5.762  1.00 40.04           C  
ATOM    265  C   LYS A  34     -11.231  26.266   7.115  1.00 39.37           C  
ATOM    266  O   LYS A  34     -10.714  25.243   7.556  1.00 39.84           O  
ATOM    267  CB  LYS A  34     -10.998  25.882   4.576  1.00 44.78           C  
ATOM    268  CG  LYS A  34     -12.498  25.516   4.566  1.00 49.88           C  
ATOM    269  CD  LYS A  34     -12.790  24.361   3.606  1.00 51.99           C  
ATOM    270  CE  LYS A  34     -14.048  23.611   4.071  1.00 54.14           C  
ATOM    271  NZ  LYS A  34     -13.836  22.153   3.770  1.00 56.75           N  
ATOM    272  N   ILE A  35     -12.219  26.948   7.734  1.00 37.47           N  
ATOM    273  CA  ILE A  35     -12.654  26.562   9.077  1.00 37.99           C  
ATOM    274  C   ILE A  35     -13.698  25.435   8.974  1.00 39.70           C  
ATOM    275  O   ILE A  35     -14.666  25.752   8.218  1.00 41.05           O  
ATOM    276  CB  ILE A  35     -13.158  27.731   9.905  1.00 36.43           C  
ATOM    277  CG1 ILE A  35     -12.225  28.911  10.088  1.00 35.65           C  
ATOM    278  CG2 ILE A  35     -13.530  27.279  11.361  1.00 37.44           C  
ATOM    279  CD1 ILE A  35     -10.814  28.762  10.525  1.00 32.74           C  
ATOM    280  N   VAL A  44     -22.236  29.308   9.968  1.00 54.60           N  
ATOM    281  CA  VAL A  44     -21.246  29.846  10.898  1.00 56.90           C  
ATOM    282  C   VAL A  44     -21.891  30.697  11.992  1.00 57.18           C  
ATOM    283  O   VAL A  44     -22.767  31.501  11.737  1.00 55.69           O  
ATOM    284  CB  VAL A  44     -20.215  30.734  10.171  1.00 58.20           C  
ATOM    285  CG1 VAL A  44     -19.186  31.356  11.121  1.00 59.27           C  
ATOM    286  CG2 VAL A  44     -19.507  29.997   9.054  1.00 57.03           C  
ATOM    287  N   PRO A  45     -21.362  30.596  13.207  1.00 57.54           N  
ATOM    288  CA  PRO A  45     -21.866  31.317  14.354  1.00 55.57           C  
ATOM    289  C   PRO A  45     -21.733  32.829  14.213  1.00 53.97           C  
ATOM    290  O   PRO A  45     -20.627  33.313  13.912  1.00 51.46           O  
ATOM    291  CB  PRO A  45     -20.968  30.812  15.492  1.00 58.22           C  
ATOM    292  CG  PRO A  45     -20.513  29.434  15.056  1.00 58.12           C  
ATOM    293  CD  PRO A  45     -20.279  29.609  13.574  1.00 57.22           C  
ATOM    294  N   SER A  46     -22.841  33.561  14.489  1.00 49.84           N  
ATOM    295  CA  SER A  46     -22.782  35.004  14.333  1.00 47.56           C  
ATOM    296  C   SER A  46     -21.817  35.648  15.307  1.00 44.87           C  
ATOM    297  O   SER A  46     -21.085  36.540  14.893  1.00 41.64           O  
ATOM    298  CB  SER A  46     -24.147  35.674  14.389  1.00 50.16           C  
ATOM    299  OG  SER A  46     -24.167  36.857  15.173  1.00 50.78           O  
ATOM    300  N   THR A  47     -21.830  35.183  16.566  1.00 42.00           N  
ATOM    301  CA  THR A  47     -20.926  35.702  17.592  1.00 37.66           C  
ATOM    302  C   THR A  47     -19.473  35.540  17.123  1.00 32.85           C  
ATOM    303  O   THR A  47     -18.684  36.484  17.181  1.00 31.10           O  
ATOM    304  CB  THR A  47     -21.139  34.979  18.933  1.00 40.61           C  
ATOM    305  OG1 THR A  47     -20.167  35.473  19.917  1.00 44.15           O  
ATOM    306  CG2 THR A  47     -20.931  33.461  18.794  1.00 40.70           C  
ATOM    307  N   ALA A  48     -19.172  34.412  16.555  1.00 29.94           N  
ATOM    308  CA  ALA A  48     -17.887  34.064  15.960  1.00 32.35           C  
ATOM    309  C   ALA A  48     -17.540  34.930  14.745  1.00 31.79           C  
ATOM    310  O   ALA A  48     -16.389  35.382  14.690  1.00 28.68           O  
ATOM    311  CB  ALA A  48     -17.965  32.612  15.571  1.00 32.69           C  
ATOM    312  N   ILE A  49     -18.563  35.262  13.910  1.00 32.33           N  
ATOM    313  CA  ILE A  49     -18.294  36.241  12.872  1.00 33.32           C  
ATOM    314  C   ILE A  49     -17.962  37.631  13.413  1.00 28.83           C  
ATOM    315  O   ILE A  49     -16.953  38.208  12.974  1.00 26.20           O  
ATOM    316  CB  ILE A  49     -19.385  36.391  11.802  1.00 35.78           C  
ATOM    317  CG1 ILE A  49     -19.456  35.121  10.936  1.00 36.26           C  
ATOM    318  CG2 ILE A  49     -19.090  37.643  10.942  1.00 36.73           C  
ATOM    319  CD1 ILE A  49     -18.570  35.220   9.706  1.00 36.38           C  
ATOM    320  N   ARG A  50     -18.733  38.216  14.297  1.00 30.18           N  
ATOM    321  CA  ARG A  50     -18.362  39.544  14.740  1.00 33.96           C  
ATOM    322  C   ARG A  50     -16.996  39.527  15.428  1.00 37.08           C  
ATOM    323  O   ARG A  50     -16.168  40.345  14.999  1.00 36.30           O  
ATOM    324  CB  ARG A  50     -19.450  40.287  15.465  1.00 37.76           C  
ATOM    325  CG  ARG A  50     -20.804  39.541  15.437  1.00 44.89           C  
ATOM    326  CD  ARG A  50     -21.951  40.452  15.787  1.00 45.33           C  
ATOM    327  NE  ARG A  50     -23.292  40.185  15.258  1.00 47.46           N  
ATOM    328  CZ  ARG A  50     -24.173  39.496  16.008  1.00 49.84           C  
ATOM    329  NH1 ARG A  50     -23.735  39.009  17.201  1.00 51.39           N  
ATOM    330  NH2 ARG A  50     -25.411  39.267  15.627  1.00 46.90           N  
ATOM    331  N   GLU A  51     -16.665  38.548  16.278  1.00 39.00           N  
ATOM    332  CA  GLU A  51     -15.378  38.539  16.979  1.00 40.44           C  
ATOM    333  C   GLU A  51     -14.198  38.367  16.034  1.00 36.58           C  
ATOM    334  O   GLU A  51     -13.229  39.128  16.176  1.00 35.53           O  
ATOM    335  CB  GLU A  51     -15.283  37.439  18.029  1.00 46.53           C  
ATOM    336  CG  GLU A  51     -14.070  37.482  18.933  1.00 52.99           C  
ATOM    337  CD  GLU A  51     -14.382  38.039  20.316  1.00 58.93           C  
ATOM    338  OE1 GLU A  51     -14.416  39.282  20.490  1.00 60.01           O  
ATOM    339  OE2 GLU A  51     -14.604  37.218  21.247  1.00 61.38           O  
ATOM    340  N   ILE A  52     -14.308  37.490  15.069  1.00 33.87           N  
ATOM    341  CA  ILE A  52     -13.273  37.313  14.061  1.00 34.44           C  
ATOM    342  C   ILE A  52     -13.089  38.665  13.368  1.00 36.81           C  
ATOM    343  O   ILE A  52     -11.937  39.046  13.167  1.00 32.45           O  
ATOM    344  CB  ILE A  52     -13.523  36.312  12.933  1.00 34.91           C  
ATOM    345  CG1 ILE A  52     -13.843  34.902  13.491  1.00 35.99           C  
ATOM    346  CG2 ILE A  52     -12.317  36.027  12.021  1.00 34.94           C  
ATOM    347  CD1 ILE A  52     -12.756  34.204  14.213  1.00 35.97           C  
ATOM    348  N   SER A  53     -14.211  39.386  13.131  1.00 37.89           N  
ATOM    349  CA  SER A  53     -14.093  40.615  12.360  1.00 42.35           C  
ATOM    350  C   SER A  53     -13.409  41.740  13.063  1.00 44.20           C  
ATOM    351  O   SER A  53     -12.604  42.429  12.416  1.00 46.32           O  
ATOM    352  CB  SER A  53     -15.417  41.004  11.675  1.00 41.23           C  
ATOM    353  OG  SER A  53     -15.863  39.833  10.996  1.00 40.38           O  
ATOM    354  N   LEU A  54     -13.555  41.880  14.365  1.00 46.87           N  
ATOM    355  CA  LEU A  54     -12.822  42.913  15.100  1.00 46.82           C  
ATOM    356  C   LEU A  54     -11.341  42.546  15.220  1.00 46.75           C  
ATOM    357  O   LEU A  54     -10.493  43.422  15.477  1.00 46.64           O  
ATOM    358  CB  LEU A  54     -13.493  43.082  16.460  1.00 50.06           C  
ATOM    359  CG  LEU A  54     -14.946  42.579  16.576  1.00 53.23           C  
ATOM    360  CD1 LEU A  54     -15.561  42.937  17.938  1.00 51.67           C  
ATOM    361  CD2 LEU A  54     -15.846  43.133  15.467  1.00 51.13           C  
ATOM    362  N   LEU A  55     -10.954  41.273  14.967  1.00 43.67           N  
ATOM    363  CA  LEU A  55      -9.553  40.885  14.996  1.00 40.80           C  
ATOM    364  C   LEU A  55      -8.791  41.497  13.813  1.00 38.61           C  
ATOM    365  O   LEU A  55      -7.610  41.847  13.905  1.00 34.32           O  
ATOM    366  CB  LEU A  55      -9.305  39.397  15.072  1.00 40.57           C  
ATOM    367  CG  LEU A  55      -9.869  38.639  16.254  1.00 41.99           C  
ATOM    368  CD1 LEU A  55      -9.696  37.151  15.930  1.00 43.76           C  
ATOM    369  CD2 LEU A  55      -9.237  39.045  17.577  1.00 40.66           C  
ATOM    370  N   LYS A  56      -9.472  41.750  12.717  1.00 38.19           N  
ATOM    371  CA  LYS A  56      -8.978  42.430  11.543  1.00 40.43           C  
ATOM    372  C   LYS A  56      -8.367  43.813  11.807  1.00 38.56           C  
ATOM    373  O   LYS A  56      -7.653  44.385  10.976  1.00 39.25           O  
ATOM    374  CB  LYS A  56     -10.161  42.764  10.622  1.00 42.19           C  
ATOM    375  CG  LYS A  56     -10.261  41.941   9.367  1.00 45.57           C  
ATOM    376  CD  LYS A  56     -11.641  41.312   9.251  1.00 48.11           C  
ATOM    377  CE  LYS A  56     -12.741  42.336   9.013  1.00 48.66           C  
ATOM    378  NZ  LYS A  56     -13.112  42.328   7.559  1.00 49.26           N  
ATOM    379  N   GLU A  57      -8.781  44.450  12.898  1.00 37.14           N  
ATOM    380  CA  GLU A  57      -8.301  45.771  13.271  1.00 34.12           C  
ATOM    381  C   GLU A  57      -7.130  45.665  14.246  1.00 33.75           C  
ATOM    382  O   GLU A  57      -6.535  46.714  14.504  1.00 31.27           O  
ATOM    383  CB  GLU A  57      -9.474  46.564  13.796  1.00 38.17           C  
ATOM    384  CG  GLU A  57     -10.807  46.284  13.149  1.00 42.35           C  
ATOM    385  CD  GLU A  57     -11.884  47.340  13.185  1.00 45.98           C  
ATOM    386  OE1 GLU A  57     -12.240  47.744  14.327  1.00 50.28           O  
ATOM    387  OE2 GLU A  57     -12.440  47.793  12.134  1.00 48.44           O  
ATOM    388  N   LEU A  58      -6.783  44.488  14.742  1.00 30.52           N  
ATOM    389  CA  LEU A  58      -5.710  44.225  15.664  1.00 33.54           C  
ATOM    390  C   LEU A  58      -4.404  44.151  14.848  1.00 32.10           C  
ATOM    391  O   LEU A  58      -3.935  43.028  14.751  1.00 30.07           O  
ATOM    392  CB  LEU A  58      -5.843  42.789  16.324  1.00 37.79           C  
ATOM    393  CG  LEU A  58      -5.141  42.545  17.646  1.00 40.47           C  
ATOM    394  CD1 LEU A  58      -6.157  43.222  18.587  1.00 40.84           C  
ATOM    395  CD2 LEU A  58      -4.646  41.183  18.258  1.00 39.20           C  
ATOM    396  N   ASN A  59      -3.866  45.207  14.261  1.00 28.41           N  
ATOM    397  CA  ASN A  59      -2.651  45.055  13.490  1.00 29.74           C  
ATOM    398  C   ASN A  59      -1.372  45.439  14.231  1.00 25.08           C  
ATOM    399  O   ASN A  59      -1.345  46.468  14.896  1.00 27.32           O  
ATOM    400  CB  ASN A  59      -2.752  45.908  12.192  1.00 32.55           C  
ATOM    401  CG  ASN A  59      -3.853  45.302  11.335  1.00 35.11           C  
ATOM    402  OD1 ASN A  59      -4.604  45.931  10.628  1.00 35.96           O  
ATOM    403  ND2 ASN A  59      -4.063  43.984  11.371  1.00 37.47           N  
ATOM    404  N   HIS A  60      -0.323  44.666  14.095  1.00 23.05           N  
ATOM    405  CA  HIS A  60       0.927  45.000  14.807  1.00 23.30           C  
ATOM    406  C   HIS A  60       1.954  44.207  14.056  1.00 22.64           C  
ATOM    407  O   HIS A  60       1.700  43.059  13.632  1.00 25.79           O  
ATOM    408  CB  HIS A  60       0.725  44.573  16.328  1.00 19.07           C  
ATOM    409  CG  HIS A  60       2.006  44.737  17.035  1.00 15.84           C  
ATOM    410  ND1 HIS A  60       2.324  45.781  17.926  1.00 19.90           N  
ATOM    411  CD2 HIS A  60       3.100  44.004  16.967  1.00 12.68           C  
ATOM    412  CE1 HIS A  60       3.554  45.673  18.346  1.00 16.12           C  
ATOM    413  NE2 HIS A  60       4.076  44.568  17.761  1.00 18.35           N  
ATOM    414  N   PRO A  61       3.192  44.671  13.955  1.00 24.94           N  
ATOM    415  CA  PRO A  61       4.222  43.943  13.212  1.00 27.49           C  
ATOM    416  C   PRO A  61       4.616  42.548  13.689  1.00 26.84           C  
ATOM    417  O   PRO A  61       5.213  41.702  12.979  1.00 26.09           O  
ATOM    418  CB  PRO A  61       5.476  44.831  13.342  1.00 27.95           C  
ATOM    419  CG  PRO A  61       5.106  45.949  14.259  1.00 30.21           C  
ATOM    420  CD  PRO A  61       3.614  46.026  14.374  1.00 24.57           C  
ATOM    421  N   ASN A  62       4.304  42.185  14.955  1.00 23.83           N  
ATOM    422  CA  ASN A  62       4.639  40.883  15.464  1.00 20.38           C  
ATOM    423  C   ASN A  62       3.388  40.025  15.615  1.00 19.23           C  
ATOM    424  O   ASN A  62       3.438  38.927  16.250  1.00 16.16           O  
ATOM    425  CB  ASN A  62       5.436  41.001  16.796  1.00 20.99           C  
ATOM    426  CG  ASN A  62       6.753  41.652  16.602  1.00 18.36           C  
ATOM    427  OD1 ASN A  62       6.836  42.831  16.974  1.00 23.16           O  
ATOM    428  ND2 ASN A  62       7.687  40.919  16.051  1.00 13.98           N  
ATOM    429  N   ILE A  63       2.329  40.487  14.914  1.00 21.47           N  
ATOM    430  CA  ILE A  63       1.080  39.699  14.783  1.00 22.72           C  
ATOM    431  C   ILE A  63       0.771  39.385  13.315  1.00 22.04           C  
ATOM    432  O   ILE A  63       0.765  40.259  12.452  1.00 21.63           O  
ATOM    433  CB  ILE A  63      -0.109  40.458  15.392  1.00 24.48           C  
ATOM    434  CG1 ILE A  63       0.160  40.792  16.869  1.00 28.05           C  
ATOM    435  CG2 ILE A  63      -1.379  39.606  15.294  1.00 25.26           C  
ATOM    436  CD1 ILE A  63       0.004  39.630  17.837  1.00 28.67           C  
ATOM    437  N   VAL A  64       0.611  38.149  12.922  1.00 20.55           N  
ATOM    438  CA  VAL A  64       0.357  37.658  11.600  1.00 22.01           C  
ATOM    439  C   VAL A  64      -0.955  38.365  11.159  1.00 23.50           C  
ATOM    440  O   VAL A  64      -1.981  38.178  11.800  1.00 20.01           O  
ATOM    441  CB  VAL A  64       0.205  36.117  11.541  1.00 22.72           C  
ATOM    442  CG1 VAL A  64      -0.290  35.644  10.146  1.00 24.50           C  
ATOM    443  CG2 VAL A  64       1.475  35.292  11.791  1.00 18.86           C  
ATOM    444  N   LYS A  65      -0.949  39.187  10.127  1.00 23.52           N  
ATOM    445  CA  LYS A  65      -2.153  39.952   9.715  1.00 28.66           C  
ATOM    446  C   LYS A  65      -3.265  39.115   9.080  1.00 24.96           C  
ATOM    447  O   LYS A  65      -3.069  38.218   8.247  1.00 23.83           O  
ATOM    448  CB  LYS A  65      -1.658  41.080   8.737  1.00 32.92           C  
ATOM    449  CG  LYS A  65      -2.775  41.868   7.989  1.00 37.63           C  
ATOM    450  CD  LYS A  65      -2.083  42.884   7.082  1.00 36.96           C  
ATOM    451  CE  LYS A  65      -2.761  44.151   6.667  1.00 36.74           C  
ATOM    452  NZ  LYS A  65      -3.720  44.761   7.605  1.00 37.47           N  
ATOM    453  N   LEU A  66      -4.486  39.288   9.560  1.00 26.05           N  
ATOM    454  CA  LEU A  66      -5.713  38.649   9.097  1.00 25.38           C  
ATOM    455  C   LEU A  66      -6.181  39.617   7.976  1.00 31.08           C  
ATOM    456  O   LEU A  66      -6.449  40.830   8.095  1.00 26.38           O  
ATOM    457  CB  LEU A  66      -6.584  38.458  10.320  1.00 28.14           C  
ATOM    458  CG  LEU A  66      -8.107  38.336  10.135  1.00 30.10           C  
ATOM    459  CD1 LEU A  66      -8.375  37.075   9.280  1.00 29.35           C  
ATOM    460  CD2 LEU A  66      -8.974  38.270  11.388  1.00 27.77           C  
ATOM    461  N   LEU A  67      -5.902  39.111   6.740  1.00 31.98           N  
ATOM    462  CA  LEU A  67      -6.194  39.923   5.582  1.00 34.05           C  
ATOM    463  C   LEU A  67      -7.671  40.083   5.363  1.00 35.72           C  
ATOM    464  O   LEU A  67      -8.132  41.204   5.054  1.00 35.34           O  
ATOM    465  CB  LEU A  67      -5.427  39.392   4.356  1.00 34.40           C  
ATOM    466  CG  LEU A  67      -3.905  39.598   4.566  1.00 33.42           C  
ATOM    467  CD1 LEU A  67      -3.116  39.044   3.433  1.00 32.66           C  
ATOM    468  CD2 LEU A  67      -3.617  41.083   4.756  1.00 35.03           C  
ATOM    469  N   ASP A  68      -8.448  39.026   5.559  1.00 35.87           N  
ATOM    470  CA  ASP A  68      -9.847  39.046   5.197  1.00 34.55           C  
ATOM    471  C   ASP A  68     -10.552  37.803   5.687  1.00 34.41           C  
ATOM    472  O   ASP A  68      -9.947  36.779   5.958  1.00 29.92           O  
ATOM    473  CB  ASP A  68      -9.882  38.964   3.642  1.00 40.18           C  
ATOM    474  CG  ASP A  68     -10.127  40.335   3.031  1.00 42.30           C  
ATOM    475  OD1 ASP A  68     -11.149  40.900   3.455  1.00 46.05           O  
ATOM    476  OD2 ASP A  68      -9.270  40.786   2.264  1.00 42.26           O  
ATOM    477  N   VAL A  69     -11.859  37.946   5.822  1.00 35.74           N  
ATOM    478  CA  VAL A  69     -12.795  36.992   6.354  1.00 38.08           C  
ATOM    479  C   VAL A  69     -13.836  36.800   5.261  1.00 38.51           C  
ATOM    480  O   VAL A  69     -14.407  37.800   4.844  1.00 39.97           O  
ATOM    481  CB  VAL A  69     -13.535  37.525   7.621  1.00 38.27           C  
ATOM    482  CG1 VAL A  69     -14.260  36.389   8.298  1.00 37.06           C  
ATOM    483  CG2 VAL A  69     -12.555  38.142   8.579  1.00 39.53           C  
ATOM    484  N   ILE A  70     -13.914  35.616   4.723  1.00 39.54           N  
ATOM    485  CA  ILE A  70     -14.785  35.298   3.601  1.00 39.59           C  
ATOM    486  C   ILE A  70     -15.748  34.265   4.169  1.00 39.83           C  
ATOM    487  O   ILE A  70     -15.474  33.099   4.388  1.00 37.81           O  
ATOM    488  CB  ILE A  70     -14.025  34.741   2.394  1.00 36.46           C  
ATOM    489  CG1 ILE A  70     -12.997  35.736   1.875  1.00 36.55           C  
ATOM    490  CG2 ILE A  70     -14.859  34.363   1.186  1.00 39.46           C  
ATOM    491  CD1 ILE A  70     -11.987  35.160   0.898  1.00 34.82           C  
ATOM    492  N   HIS A  71     -16.944  34.749   4.434  1.00 43.84           N  
ATOM    493  CA  HIS A  71     -18.028  33.890   4.936  1.00 47.23           C  
ATOM    494  C   HIS A  71     -18.971  33.606   3.793  1.00 51.23           C  
ATOM    495  O   HIS A  71     -19.650  34.531   3.317  1.00 52.70           O  
ATOM    496  CB  HIS A  71     -18.691  34.688   6.070  1.00 47.01           C  
ATOM    497  CG  HIS A  71     -19.892  34.041   6.664  1.00 46.31           C  
ATOM    498  ND1 HIS A  71     -20.076  32.672   6.674  1.00 45.94           N  
ATOM    499  CD2 HIS A  71     -20.943  34.606   7.314  1.00 46.85           C  
ATOM    500  CE1 HIS A  71     -21.209  32.430   7.304  1.00 46.25           C  
ATOM    501  NE2 HIS A  71     -21.731  33.563   7.715  1.00 46.54           N  
ATOM    502  N   THR A  72     -19.050  32.374   3.333  1.00 55.48           N  
ATOM    503  CA  THR A  72     -19.893  31.917   2.246  1.00 56.32           C  
ATOM    504  C   THR A  72     -20.387  30.490   2.525  1.00 57.91           C  
ATOM    505  O   THR A  72     -19.657  29.679   3.063  1.00 56.44           O  
ATOM    506  CB  THR A  72     -19.187  31.827   0.882  1.00 56.75           C  
ATOM    507  OG1 THR A  72     -18.071  30.930   1.011  1.00 56.86           O  
ATOM    508  CG2 THR A  72     -18.713  33.123   0.258  1.00 56.93           C  
ATOM    509  N   GLU A  73     -21.613  30.178   2.109  1.00 59.93           N  
ATOM    510  CA  GLU A  73     -22.259  28.889   2.216  1.00 62.39           C  
ATOM    511  C   GLU A  73     -22.079  28.157   3.525  1.00 63.14           C  
ATOM    512  O   GLU A  73     -21.713  26.965   3.594  1.00 62.93           O  
ATOM    513  CB  GLU A  73     -21.796  27.937   1.098  1.00 65.37           C  
ATOM    514  CG  GLU A  73     -22.041  28.375  -0.339  1.00 67.54           C  
ATOM    515  CD  GLU A  73     -20.703  28.625  -1.030  1.00 69.05           C  
ATOM    516  OE1 GLU A  73     -19.981  29.517  -0.551  1.00 67.69           O  
ATOM    517  OE2 GLU A  73     -20.371  27.943  -2.039  1.00 70.75           O  
ATOM    518  N   ASN A  74     -22.261  28.824   4.674  1.00 63.49           N  
ATOM    519  CA  ASN A  74     -22.022  28.173   5.971  1.00 65.19           C  
ATOM    520  C   ASN A  74     -20.539  27.811   6.111  1.00 63.25           C  
ATOM    521  O   ASN A  74     -20.148  27.027   6.994  1.00 64.19           O  
ATOM    522  CB  ASN A  74     -22.886  26.930   6.187  1.00 68.06           C  
ATOM    523  CG  ASN A  74     -24.359  26.907   5.866  1.00 70.37           C  
ATOM    524  OD1 ASN A  74     -24.890  27.593   4.975  1.00 71.37           O  
ATOM    525  ND2 ASN A  74     -25.175  26.085   6.544  1.00 71.51           N  
ATOM    526  N   LYS A  75     -19.666  28.263   5.210  1.00 59.23           N  
ATOM    527  CA  LYS A  75     -18.243  27.999   5.218  1.00 55.34           C  
ATOM    528  C   LYS A  75     -17.533  29.323   5.549  1.00 48.49           C  
ATOM    529  O   LYS A  75     -17.972  30.404   5.157  1.00 45.87           O  
ATOM    530  CB  LYS A  75     -17.679  27.341   3.961  1.00 58.73           C  
ATOM    531  CG  LYS A  75     -18.665  26.862   2.914  1.00 62.01           C  
ATOM    532  CD  LYS A  75     -18.140  25.800   1.956  1.00 63.93           C  
ATOM    533  CE  LYS A  75     -19.264  24.892   1.452  1.00 65.43           C  
ATOM    534  NZ  LYS A  75     -19.769  23.884   2.439  1.00 65.37           N  
ATOM    535  N   LEU A  76     -16.510  29.199   6.383  1.00 43.03           N  
ATOM    536  CA  LEU A  76     -15.756  30.396   6.773  1.00 37.58           C  
ATOM    537  C   LEU A  76     -14.322  30.295   6.277  1.00 33.14           C  
ATOM    538  O   LEU A  76     -13.750  29.237   6.383  1.00 33.34           O  
ATOM    539  CB  LEU A  76     -15.906  30.551   8.278  1.00 34.19           C  
ATOM    540  CG  LEU A  76     -15.270  31.800   8.858  1.00 34.58           C  
ATOM    541  CD1 LEU A  76     -15.764  33.055   8.147  1.00 34.00           C  
ATOM    542  CD2 LEU A  76     -15.382  31.811  10.377  1.00 29.54           C  
ATOM    543  N   TYR A  77     -13.704  31.261   5.674  1.00 30.22           N  
ATOM    544  CA  TYR A  77     -12.330  31.195   5.136  1.00 30.58           C  
ATOM    545  C   TYR A  77     -11.532  32.389   5.686  1.00 29.15           C  
ATOM    546  O   TYR A  77     -12.111  33.489   5.664  1.00 29.46           O  
ATOM    547  CB  TYR A  77     -12.279  31.350   3.613  1.00 32.41           C  
ATOM    548  CG  TYR A  77     -12.949  30.164   2.969  1.00 37.84           C  
ATOM    549  CD1 TYR A  77     -12.287  28.969   2.816  1.00 39.46           C  
ATOM    550  CD2 TYR A  77     -14.267  30.264   2.574  1.00 39.11           C  
ATOM    551  CE1 TYR A  77     -12.936  27.887   2.224  1.00 43.68           C  
ATOM    552  CE2 TYR A  77     -14.907  29.180   1.996  1.00 42.61           C  
ATOM    553  CZ  TYR A  77     -14.238  27.991   1.831  1.00 43.59           C  
ATOM    554  OH  TYR A  77     -14.883  26.905   1.273  1.00 47.17           O  
ATOM    555  N   LEU A  78     -10.426  32.126   6.348  1.00 26.59           N  
ATOM    556  CA  LEU A  78      -9.609  33.210   6.918  1.00 27.01           C  
ATOM    557  C   LEU A  78      -8.360  33.338   6.049  1.00 23.38           C  
ATOM    558  O   LEU A  78      -7.711  32.310   5.776  1.00 21.92           O  
ATOM    559  CB  LEU A  78      -9.223  32.907   8.362  1.00 28.18           C  
ATOM    560  CG  LEU A  78     -10.344  32.729   9.406  1.00 32.52           C  
ATOM    561  CD1 LEU A  78      -9.811  32.625  10.839  1.00 30.43           C  
ATOM    562  CD2 LEU A  78     -11.345  33.910   9.358  1.00 29.67           C  
ATOM    563  N   VAL A  79      -8.142  34.503   5.509  1.00 21.01           N  
ATOM    564  CA  VAL A  79      -7.009  34.719   4.598  1.00 24.05           C  
ATOM    565  C   VAL A  79      -5.946  35.511   5.366  1.00 26.26           C  
ATOM    566  O   VAL A  79      -6.275  36.624   5.828  1.00 28.15           O  
ATOM    567  CB  VAL A  79      -7.461  35.624   3.409  1.00 24.37           C  
ATOM    568  CG1 VAL A  79      -6.254  35.798   2.468  1.00 24.87           C  
ATOM    569  CG2 VAL A  79      -8.745  35.167   2.739  1.00 22.96           C  
ATOM    570  N   PHE A  80      -4.825  34.890   5.630  1.00 26.81           N  
ATOM    571  CA  PHE A  80      -3.810  35.553   6.464  1.00 27.17           C  
ATOM    572  C   PHE A  80      -2.601  35.931   5.627  1.00 25.72           C  
ATOM    573  O   PHE A  80      -2.348  35.396   4.560  1.00 22.91           O  
ATOM    574  CB  PHE A  80      -3.356  34.595   7.610  1.00 26.58           C  
ATOM    575  CG  PHE A  80      -4.329  34.441   8.777  1.00 26.09           C  
ATOM    576  CD1 PHE A  80      -4.392  35.394   9.767  1.00 23.76           C  
ATOM    577  CD2 PHE A  80      -5.121  33.324   8.908  1.00 27.23           C  
ATOM    578  CE1 PHE A  80      -5.216  35.259  10.846  1.00 25.59           C  
ATOM    579  CE2 PHE A  80      -5.985  33.123  10.009  1.00 28.48           C  
ATOM    580  CZ  PHE A  80      -6.048  34.136  10.960  1.00 29.38           C  
ATOM    581  N   GLU A  81      -1.775  36.819   6.177  1.00 27.76           N  
ATOM    582  CA  GLU A  81      -0.438  37.081   5.551  1.00 26.52           C  
ATOM    583  C   GLU A  81       0.312  35.754   5.510  1.00 25.01           C  
ATOM    584  O   GLU A  81       0.216  34.896   6.433  1.00 20.96           O  
ATOM    585  CB  GLU A  81       0.191  37.984   6.599  1.00 26.13           C  
ATOM    586  CG  GLU A  81       1.667  38.204   6.521  1.00 27.28           C  
ATOM    587  CD  GLU A  81       2.151  39.085   7.678  1.00 27.68           C  
ATOM    588  OE1 GLU A  81       1.539  39.273   8.745  1.00 24.05           O  
ATOM    589  OE2 GLU A  81       3.249  39.628   7.457  1.00 29.15           O  
ATOM    590  N   PHE A  82       1.090  35.450   4.499  1.00 22.83           N  
ATOM    591  CA  PHE A  82       1.830  34.152   4.530  1.00 23.67           C  
ATOM    592  C   PHE A  82       3.271  34.366   4.957  1.00 23.48           C  
ATOM    593  O   PHE A  82       3.919  35.335   4.449  1.00 29.39           O  
ATOM    594  CB  PHE A  82       1.741  33.424   3.197  1.00 21.30           C  
ATOM    595  CG  PHE A  82       2.569  32.239   2.907  1.00 22.56           C  
ATOM    596  CD1 PHE A  82       3.865  32.335   2.435  1.00 25.68           C  
ATOM    597  CD2 PHE A  82       2.074  30.961   3.064  1.00 23.17           C  
ATOM    598  CE1 PHE A  82       4.649  31.231   2.217  1.00 23.26           C  
ATOM    599  CE2 PHE A  82       2.831  29.836   2.801  1.00 23.46           C  
ATOM    600  CZ  PHE A  82       4.121  29.948   2.371  1.00 22.60           C  
ATOM    601  N   LEU A  83       3.809  33.435   5.679  1.00 18.83           N  
ATOM    602  CA  LEU A  83       5.183  33.403   6.179  1.00 24.02           C  
ATOM    603  C   LEU A  83       5.802  32.049   5.752  1.00 26.43           C  
ATOM    604  O   LEU A  83       5.100  31.027   5.764  1.00 24.64           O  
ATOM    605  CB  LEU A  83       5.269  33.742   7.639  1.00 21.47           C  
ATOM    606  CG  LEU A  83       5.273  35.223   8.045  1.00 23.68           C  
ATOM    607  CD1 LEU A  83       3.919  35.507   8.720  1.00 23.28           C  
ATOM    608  CD2 LEU A  83       6.340  35.673   9.058  1.00 21.08           C  
ATOM    609  N   HIS A  84       7.095  32.008   5.404  1.00 28.56           N  
ATOM    610  CA  HIS A  84       7.619  30.744   4.907  1.00 28.82           C  
ATOM    611  C   HIS A  84       7.938  29.732   5.975  1.00 31.55           C  
ATOM    612  O   HIS A  84       7.954  28.573   5.547  1.00 30.65           O  
ATOM    613  CB  HIS A  84       8.798  30.862   3.966  1.00 29.47           C  
ATOM    614  CG  HIS A  84       8.429  31.673   2.731  1.00 28.75           C  
ATOM    615  ND1 HIS A  84       8.123  33.029   2.823  1.00 26.22           N  
ATOM    616  CD2 HIS A  84       8.329  31.295   1.438  1.00 28.72           C  
ATOM    617  CE1 HIS A  84       7.826  33.435   1.585  1.00 29.84           C  
ATOM    618  NE2 HIS A  84       7.975  32.404   0.722  1.00 28.11           N  
ATOM    619  N   GLN A  85       8.193  30.113   7.263  1.00 30.08           N  
ATOM    620  CA  GLN A  85       8.381  28.939   8.121  1.00 29.29           C  
ATOM    621  C   GLN A  85       7.835  29.076   9.520  1.00 26.74           C  
ATOM    622  O   GLN A  85       7.747  30.235   9.964  1.00 26.18           O  
ATOM    623  CB  GLN A  85       9.918  28.753   8.021  1.00 30.99           C  
ATOM    624  CG  GLN A  85      10.234  27.702   9.105  1.00 34.60           C  
ATOM    625  CD  GLN A  85      11.395  26.844   8.729  1.00 37.52           C  
ATOM    626  OE1 GLN A  85      11.038  25.918   7.958  1.00 42.54           O  
ATOM    627  NE2 GLN A  85      12.544  27.276   9.239  1.00 34.32           N  
ATOM    628  N   ASP A  86       7.579  28.000  10.258  1.00 24.86           N  
ATOM    629  CA  ASP A  86       7.168  28.091  11.664  1.00 24.50           C  
ATOM    630  C   ASP A  86       8.332  27.667  12.540  1.00 21.74           C  
ATOM    631  O   ASP A  86       9.345  27.111  12.098  1.00 19.41           O  
ATOM    632  CB  ASP A  86       5.913  27.331  12.129  1.00 24.02           C  
ATOM    633  CG  ASP A  86       6.181  25.855  12.067  1.00 30.49           C  
ATOM    634  OD1 ASP A  86       7.007  25.149  12.719  1.00 35.45           O  
ATOM    635  OD2 ASP A  86       5.550  25.229  11.221  1.00 34.94           O  
ATOM    636  N   LEU A  87       8.104  27.926  13.866  1.00 23.16           N  
ATOM    637  CA  LEU A  87       9.243  27.791  14.785  1.00 24.17           C  
ATOM    638  C   LEU A  87       9.580  26.318  15.074  1.00 24.73           C  
ATOM    639  O   LEU A  87      10.759  25.924  15.260  1.00 22.32           O  
ATOM    640  CB  LEU A  87       9.056  28.675  16.044  1.00 25.94           C  
ATOM    641  CG  LEU A  87      10.146  28.468  17.125  1.00 27.31           C  
ATOM    642  CD1 LEU A  87      11.386  29.348  16.842  1.00 26.43           C  
ATOM    643  CD2 LEU A  87       9.647  28.875  18.523  1.00 26.62           C  
ATOM    644  N   LYS A  88       8.550  25.500  14.925  1.00 25.23           N  
ATOM    645  CA  LYS A  88       8.761  24.068  15.120  1.00 26.79           C  
ATOM    646  C   LYS A  88       9.727  23.616  14.072  1.00 28.35           C  
ATOM    647  O   LYS A  88      10.804  23.100  14.404  1.00 28.83           O  
ATOM    648  CB  LYS A  88       7.399  23.414  15.175  1.00 23.86           C  
ATOM    649  CG  LYS A  88       7.391  21.912  15.260  1.00 28.42           C  
ATOM    650  CD  LYS A  88       8.327  21.473  16.376  1.00 32.47           C  
ATOM    651  CE  LYS A  88       7.656  21.764  17.719  1.00 38.35           C  
ATOM    652  NZ  LYS A  88       8.648  22.125  18.832  1.00 39.25           N  
ATOM    653  N   LYS A  89       9.395  23.819  12.770  1.00 31.18           N  
ATOM    654  CA  LYS A  89      10.385  23.470  11.728  1.00 27.95           C  
ATOM    655  C   LYS A  89      11.731  24.119  11.869  1.00 26.14           C  
ATOM    656  O   LYS A  89      12.727  23.453  11.639  1.00 28.07           O  
ATOM    657  CB  LYS A  89       9.809  23.915  10.345  1.00 30.29           C  
ATOM    658  CG  LYS A  89       8.487  23.215  10.111  1.00 39.34           C  
ATOM    659  CD  LYS A  89       8.021  23.261   8.630  1.00 41.49           C  
ATOM    660  CE  LYS A  89       6.647  22.553   8.647  1.00 43.08           C  
ATOM    661  NZ  LYS A  89       6.169  22.407   7.213  1.00 44.80           N  
ATOM    662  N   PHE A  90      11.920  25.404  12.235  1.00 25.49           N  
ATOM    663  CA  PHE A  90      13.197  26.050  12.438  1.00 26.39           C  
ATOM    664  C   PHE A  90      13.980  25.324  13.579  1.00 28.30           C  
ATOM    665  O   PHE A  90      15.197  25.121  13.584  1.00 23.49           O  
ATOM    666  CB  PHE A  90      13.107  27.505  12.859  1.00 23.82           C  
ATOM    667  CG  PHE A  90      14.392  28.305  12.928  1.00 28.00           C  
ATOM    668  CD1 PHE A  90      15.299  28.223  11.911  1.00 25.41           C  
ATOM    669  CD2 PHE A  90      14.633  29.225  13.984  1.00 26.59           C  
ATOM    670  CE1 PHE A  90      16.487  28.992  11.933  1.00 27.03           C  
ATOM    671  CE2 PHE A  90      15.813  29.947  13.946  1.00 28.03           C  
ATOM    672  CZ  PHE A  90      16.767  29.903  12.915  1.00 21.65           C  
ATOM    673  N   MET A  91      13.212  24.922  14.596  1.00 29.96           N  
ATOM    674  CA  MET A  91      13.808  24.194  15.730  1.00 30.58           C  
ATOM    675  C   MET A  91      14.323  22.818  15.317  1.00 32.16           C  
ATOM    676  O   MET A  91      15.457  22.459  15.637  1.00 29.64           O  
ATOM    677  CB  MET A  91      12.845  24.103  16.919  1.00 30.06           C  
ATOM    678  CG  MET A  91      12.993  25.325  17.838  1.00 32.55           C  
ATOM    679  SD  MET A  91      12.200  25.343  19.460  1.00 34.16           S  
ATOM    680  CE  MET A  91      10.582  24.746  18.825  1.00 25.07           C  
ATOM    681  N   ASP A  92      13.562  22.026  14.599  1.00 33.37           N  
ATOM    682  CA  ASP A  92      13.922  20.736  14.090  1.00 36.40           C  
ATOM    683  C   ASP A  92      15.109  20.973  13.164  1.00 40.37           C  
ATOM    684  O   ASP A  92      16.177  20.444  13.537  1.00 43.62           O  
ATOM    685  CB  ASP A  92      12.832  19.982  13.357  1.00 38.41           C  
ATOM    686  CG  ASP A  92      11.717  19.463  14.223  1.00 40.54           C  
ATOM    687  OD1 ASP A  92      11.905  19.237  15.454  1.00 42.05           O  
ATOM    688  OD2 ASP A  92      10.591  19.262  13.677  1.00 40.36           O  
ATOM    689  N   ALA A  93      15.053  21.886  12.193  1.00 39.98           N  
ATOM    690  CA  ALA A  93      16.277  22.198  11.449  1.00 39.58           C  
ATOM    691  C   ALA A  93      17.504  22.573  12.232  1.00 39.82           C  
ATOM    692  O   ALA A  93      18.594  22.430  11.632  1.00 43.33           O  
ATOM    693  CB  ALA A  93      16.071  23.388  10.480  1.00 38.11           C  
ATOM    694  N   SER A  94      17.502  23.206  13.369  1.00 39.38           N  
ATOM    695  CA  SER A  94      18.600  23.660  14.178  1.00 38.85           C  
ATOM    696  C   SER A  94      18.966  22.716  15.341  1.00 40.09           C  
ATOM    697  O   SER A  94      19.798  23.046  16.220  1.00 40.25           O  
ATOM    698  CB  SER A  94      18.243  24.941  14.941  1.00 39.37           C  
ATOM    699  OG  SER A  94      17.902  26.089  14.255  1.00 42.81           O  
ATOM    700  N   ALA A  95      18.329  21.571  15.473  1.00 41.23           N  
ATOM    701  CA  ALA A  95      18.603  20.654  16.556  1.00 42.69           C  
ATOM    702  C   ALA A  95      20.072  20.421  16.932  1.00 42.65           C  
ATOM    703  O   ALA A  95      20.411  20.486  18.112  1.00 43.64           O  
ATOM    704  CB  ALA A  95      17.967  19.308  16.245  1.00 39.98           C  
ATOM    705  N   LEU A  96      20.944  20.037  16.022  1.00 44.33           N  
ATOM    706  CA  LEU A  96      22.330  19.726  16.193  1.00 43.16           C  
ATOM    707  C   LEU A  96      23.106  20.853  16.823  1.00 40.82           C  
ATOM    708  O   LEU A  96      23.913  20.617  17.704  1.00 42.06           O  
ATOM    709  CB  LEU A  96      23.033  19.541  14.804  1.00 48.13           C  
ATOM    710  CG  LEU A  96      23.710  18.163  14.622  1.00 49.32           C  
ATOM    711  CD1 LEU A  96      22.721  17.014  14.786  1.00 49.34           C  
ATOM    712  CD2 LEU A  96      24.414  18.072  13.277  1.00 50.12           C  
ATOM    713  N   THR A  97      22.823  22.045  16.371  1.00 38.96           N  
ATOM    714  CA  THR A  97      23.490  23.272  16.709  1.00 41.68           C  
ATOM    715  C   THR A  97      22.774  24.122  17.751  1.00 40.97           C  
ATOM    716  O   THR A  97      23.459  24.788  18.543  1.00 37.06           O  
ATOM    717  CB  THR A  97      23.696  24.121  15.423  1.00 44.83           C  
ATOM    718  OG1 THR A  97      22.429  24.450  14.770  1.00 47.58           O  
ATOM    719  CG2 THR A  97      24.492  23.357  14.369  1.00 43.25           C  
ATOM    720  N   GLY A  98      21.434  24.093  17.790  1.00 39.69           N  
ATOM    721  CA  GLY A  98      20.767  24.998  18.768  1.00 35.11           C  
ATOM    722  C   GLY A  98      20.609  26.392  18.128  1.00 34.48           C  
ATOM    723  O   GLY A  98      21.272  26.696  17.131  1.00 36.04           O  
ATOM    724  N   ILE A  99      19.625  27.177  18.507  1.00 29.74           N  
ATOM    725  CA  ILE A  99      19.367  28.515  18.076  1.00 28.89           C  
ATOM    726  C   ILE A  99      20.334  29.400  18.838  1.00 27.57           C  
ATOM    727  O   ILE A  99      20.228  29.272  20.039  1.00 26.28           O  
ATOM    728  CB  ILE A  99      17.915  28.917  18.374  1.00 29.03           C  
ATOM    729  CG1 ILE A  99      16.987  27.922  17.651  1.00 30.11           C  
ATOM    730  CG2 ILE A  99      17.731  30.357  17.854  1.00 28.70           C  
ATOM    731  CD1 ILE A  99      15.530  28.228  18.081  1.00 33.82           C  
ATOM    732  N   PRO A 100      21.149  30.241  18.199  1.00 25.19           N  
ATOM    733  CA  PRO A 100      22.046  31.087  18.943  1.00 27.18           C  
ATOM    734  C   PRO A 100      21.278  31.927  19.961  1.00 28.67           C  
ATOM    735  O   PRO A 100      20.258  32.546  19.622  1.00 27.36           O  
ATOM    736  CB  PRO A 100      22.756  31.931  17.874  1.00 28.04           C  
ATOM    737  CG  PRO A 100      22.366  31.377  16.555  1.00 28.39           C  
ATOM    738  CD  PRO A 100      21.247  30.364  16.752  1.00 27.39           C  
ATOM    739  N   LEU A 101      21.823  32.221  21.139  1.00 27.54           N  
ATOM    740  CA  LEU A 101      21.194  32.994  22.170  1.00 26.22           C  
ATOM    741  C   LEU A 101      20.697  34.354  21.720  1.00 24.44           C  
ATOM    742  O   LEU A 101      19.560  34.702  22.119  1.00 18.51           O  
ATOM    743  CB  LEU A 101      21.976  33.147  23.500  1.00 28.23           C  
ATOM    744  CG  LEU A 101      21.116  33.807  24.611  1.00 36.82           C  
ATOM    745  CD1 LEU A 101      20.151  32.852  25.366  1.00 35.14           C  
ATOM    746  CD2 LEU A 101      21.921  34.568  25.656  1.00 38.73           C  
ATOM    747  N   PRO A 102      21.502  35.191  21.029  1.00 21.71           N  
ATOM    748  CA  PRO A 102      21.048  36.471  20.584  1.00 20.13           C  
ATOM    749  C   PRO A 102      19.814  36.320  19.692  1.00 18.77           C  
ATOM    750  O   PRO A 102      19.032  37.276  19.707  1.00 19.48           O  
ATOM    751  CB  PRO A 102      22.202  37.105  19.757  1.00 19.27           C  
ATOM    752  CG  PRO A 102      23.425  36.351  20.256  1.00 23.05           C  
ATOM    753  CD  PRO A 102      22.876  34.898  20.529  1.00 23.95           C  
ATOM    754  N   LEU A 103      19.591  35.253  18.948  1.00 16.55           N  
ATOM    755  CA  LEU A 103      18.332  35.179  18.144  1.00 19.81           C  
ATOM    756  C   LEU A 103      17.115  34.779  18.998  1.00 20.55           C  
ATOM    757  O   LEU A 103      15.957  35.284  18.968  1.00 20.11           O  
ATOM    758  CB  LEU A 103      18.610  34.105  17.055  1.00 19.66           C  
ATOM    759  CG  LEU A 103      17.459  34.049  16.047  1.00 19.86           C  
ATOM    760  CD1 LEU A 103      17.128  35.462  15.485  1.00 18.51           C  
ATOM    761  CD2 LEU A 103      17.644  33.025  14.982  1.00 19.60           C  
ATOM    762  N   ILE A 104      17.389  33.881  19.960  1.00 17.10           N  
ATOM    763  CA  ILE A 104      16.358  33.458  20.925  1.00 20.67           C  
ATOM    764  C   ILE A 104      15.837  34.686  21.616  1.00 20.00           C  
ATOM    765  O   ILE A 104      14.688  35.080  21.819  1.00 21.58           O  
ATOM    766  CB  ILE A 104      17.048  32.483  21.953  1.00 21.67           C  
ATOM    767  CG1 ILE A 104      17.434  31.122  21.284  1.00 20.86           C  
ATOM    768  CG2 ILE A 104      16.136  32.221  23.165  1.00 19.92           C  
ATOM    769  CD1 ILE A 104      18.058  30.108  22.252  1.00 14.15           C  
ATOM    770  N   LYS A 105      16.799  35.528  22.025  1.00 22.41           N  
ATOM    771  CA  LYS A 105      16.571  36.783  22.715  1.00 22.36           C  
ATOM    772  C   LYS A 105      15.764  37.728  21.865  1.00 20.24           C  
ATOM    773  O   LYS A 105      14.820  38.401  22.336  1.00 20.72           O  
ATOM    774  CB  LYS A 105      17.832  37.424  23.335  1.00 21.14           C  
ATOM    775  CG  LYS A 105      17.627  38.654  24.211  1.00 25.88           C  
ATOM    776  CD  LYS A 105      18.892  39.348  24.802  1.00 24.34           C  
ATOM    777  CE  LYS A 105      19.621  38.387  25.767  1.00 26.34           C  
ATOM    778  NZ  LYS A 105      20.742  39.056  26.489  1.00 24.88           N  
ATOM    779  N   SER A 106      16.156  37.907  20.610  1.00 18.35           N  
ATOM    780  CA  SER A 106      15.370  38.795  19.713  1.00 15.85           C  
ATOM    781  C   SER A 106      13.956  38.306  19.567  1.00 14.94           C  
ATOM    782  O   SER A 106      12.970  39.029  19.583  1.00 15.75           O  
ATOM    783  CB  SER A 106      16.136  38.617  18.304  1.00 18.02           C  
ATOM    784  OG  SER A 106      15.529  39.595  17.436  1.00 21.02           O  
ATOM    785  N   TYR A 107      13.794  36.979  19.378  1.00 14.51           N  
ATOM    786  CA  TYR A 107      12.543  36.296  19.221  1.00 17.66           C  
ATOM    787  C   TYR A 107      11.651  36.551  20.453  1.00 17.76           C  
ATOM    788  O   TYR A 107      10.498  37.018  20.303  1.00 22.88           O  
ATOM    789  CB  TYR A 107      12.731  34.809  18.818  1.00 17.02           C  
ATOM    790  CG  TYR A 107      13.091  34.570  17.319  1.00 17.08           C  
ATOM    791  CD1 TYR A 107      13.048  35.557  16.319  1.00 18.69           C  
ATOM    792  CD2 TYR A 107      13.419  33.324  16.908  1.00 18.94           C  
ATOM    793  CE1 TYR A 107      13.371  35.298  14.977  1.00 18.81           C  
ATOM    794  CE2 TYR A 107      13.701  33.001  15.594  1.00 18.01           C  
ATOM    795  CZ  TYR A 107      13.658  33.995  14.624  1.00 17.86           C  
ATOM    796  OH  TYR A 107      14.079  33.601  13.386  1.00 19.71           O  
ATOM    797  N   LEU A 108      12.078  36.336  21.655  1.00 18.71           N  
ATOM    798  CA  LEU A 108      11.319  36.485  22.915  1.00 16.86           C  
ATOM    799  C   LEU A 108      10.831  37.936  23.131  1.00 16.76           C  
ATOM    800  O   LEU A 108       9.666  38.266  23.422  1.00 14.05           O  
ATOM    801  CB  LEU A 108      12.190  36.092  24.104  1.00 16.62           C  
ATOM    802  CG  LEU A 108      11.463  36.160  25.459  1.00 18.03           C  
ATOM    803  CD1 LEU A 108      10.275  35.197  25.460  1.00 20.65           C  
ATOM    804  CD2 LEU A 108      12.492  35.833  26.535  1.00 19.84           C  
ATOM    805  N   PHE A 109      11.727  38.858  22.852  1.00 14.52           N  
ATOM    806  CA  PHE A 109      11.520  40.282  22.901  1.00 18.15           C  
ATOM    807  C   PHE A 109      10.435  40.678  21.907  1.00 17.82           C  
ATOM    808  O   PHE A 109       9.581  41.476  22.327  1.00 16.92           O  
ATOM    809  CB  PHE A 109      12.818  41.054  22.524  1.00 20.83           C  
ATOM    810  CG  PHE A 109      12.667  42.551  22.678  1.00 21.63           C  
ATOM    811  CD1 PHE A 109      12.778  43.137  23.909  1.00 22.87           C  
ATOM    812  CD2 PHE A 109      12.538  43.394  21.595  1.00 24.12           C  
ATOM    813  CE1 PHE A 109      12.690  44.512  24.130  1.00 22.23           C  
ATOM    814  CE2 PHE A 109      12.410  44.755  21.790  1.00 23.85           C  
ATOM    815  CZ  PHE A 109      12.484  45.327  23.071  1.00 23.03           C  
ATOM    816  N   GLN A 110      10.586  40.191  20.656  1.00 14.55           N  
ATOM    817  CA  GLN A 110       9.477  40.602  19.722  1.00 16.42           C  
ATOM    818  C   GLN A 110       8.118  39.980  20.071  1.00 16.02           C  
ATOM    819  O   GLN A 110       7.014  40.533  19.909  1.00 18.77           O  
ATOM    820  CB  GLN A 110       9.876  40.135  18.272  1.00 16.02           C  
ATOM    821  CG  GLN A 110      11.055  40.876  17.605  1.00 17.27           C  
ATOM    822  CD  GLN A 110      11.342  40.208  16.271  1.00 19.80           C  
ATOM    823  OE1 GLN A 110      10.497  40.127  15.362  1.00 17.50           O  
ATOM    824  NE2 GLN A 110      12.529  39.629  16.202  1.00 15.66           N  
ATOM    825  N   LEU A 111       8.087  38.703  20.495  1.00 15.91           N  
ATOM    826  CA  LEU A 111       6.843  38.061  20.934  1.00 16.70           C  
ATOM    827  C   LEU A 111       6.248  38.783  22.132  1.00 17.30           C  
ATOM    828  O   LEU A 111       5.003  38.915  22.207  1.00 14.84           O  
ATOM    829  CB  LEU A 111       7.112  36.564  21.330  1.00 14.47           C  
ATOM    830  CG  LEU A 111       7.581  35.869  20.050  1.00 19.90           C  
ATOM    831  CD1 LEU A 111       8.064  34.446  20.305  1.00 21.29           C  
ATOM    832  CD2 LEU A 111       6.538  35.874  18.928  1.00 15.61           C  
ATOM    833  N   LEU A 112       7.134  39.209  23.103  1.00 14.98           N  
ATOM    834  CA  LEU A 112       6.647  40.044  24.170  1.00 16.77           C  
ATOM    835  C   LEU A 112       6.054  41.365  23.617  1.00 21.01           C  
ATOM    836  O   LEU A 112       5.055  41.872  24.244  1.00 21.52           O  
ATOM    837  CB  LEU A 112       7.723  40.344  25.238  1.00 17.64           C  
ATOM    838  CG  LEU A 112       7.997  39.045  26.110  1.00 17.81           C  
ATOM    839  CD1 LEU A 112       9.301  39.306  26.875  1.00 21.06           C  
ATOM    840  CD2 LEU A 112       6.897  38.620  27.034  1.00 16.33           C  
ATOM    841  N   GLN A 113       6.585  41.995  22.551  1.00 15.79           N  
ATOM    842  CA  GLN A 113       5.935  43.241  22.099  1.00 21.54           C  
ATOM    843  C   GLN A 113       4.540  42.918  21.545  1.00 19.96           C  
ATOM    844  O   GLN A 113       3.582  43.639  21.860  1.00 20.98           O  
ATOM    845  CB  GLN A 113       6.780  43.892  20.970  1.00 23.07           C  
ATOM    846  CG  GLN A 113       8.000  44.648  21.489  1.00 31.79           C  
ATOM    847  CD  GLN A 113       8.985  44.873  20.380  1.00 36.69           C  
ATOM    848  OE1 GLN A 113       9.997  44.241  20.136  1.00 40.73           O  
ATOM    849  NE2 GLN A 113       8.658  45.776  19.476  1.00 42.23           N  
ATOM    850  N   GLY A 114       4.464  41.783  20.838  1.00 20.57           N  
ATOM    851  CA  GLY A 114       3.172  41.315  20.273  1.00 20.52           C  
ATOM    852  C   GLY A 114       2.150  41.125  21.413  1.00 21.98           C  
ATOM    853  O   GLY A 114       1.029  41.622  21.330  1.00 18.66           O  
ATOM    854  N   LEU A 115       2.552  40.418  22.470  1.00 20.23           N  
ATOM    855  CA  LEU A 115       1.674  40.215  23.621  1.00 22.02           C  
ATOM    856  C   LEU A 115       1.313  41.525  24.345  1.00 20.57           C  
ATOM    857  O   LEU A 115       0.101  41.666  24.611  1.00 22.06           O  
ATOM    858  CB  LEU A 115       2.110  39.223  24.659  1.00 19.94           C  
ATOM    859  CG  LEU A 115       2.402  37.791  24.143  1.00 22.95           C  
ATOM    860  CD1 LEU A 115       2.763  36.891  25.318  1.00 21.63           C  
ATOM    861  CD2 LEU A 115       1.179  37.225  23.410  1.00 23.15           C  
ATOM    862  N   ALA A 116       2.180  42.481  24.452  1.00 19.57           N  
ATOM    863  CA  ALA A 116       1.917  43.716  25.174  1.00 21.17           C  
ATOM    864  C   ALA A 116       0.834  44.449  24.374  1.00 22.82           C  
ATOM    865  O   ALA A 116      -0.185  44.856  24.911  1.00 23.50           O  
ATOM    866  CB  ALA A 116       3.073  44.616  25.445  1.00 18.30           C  
ATOM    867  N   PHE A 117       1.007  44.490  23.050  1.00 26.21           N  
ATOM    868  CA  PHE A 117      -0.008  45.023  22.198  1.00 24.17           C  
ATOM    869  C   PHE A 117      -1.369  44.380  22.377  1.00 22.89           C  
ATOM    870  O   PHE A 117      -2.348  45.093  22.606  1.00 21.83           O  
ATOM    871  CB  PHE A 117       0.427  44.935  20.714  1.00 26.76           C  
ATOM    872  CG  PHE A 117      -0.622  45.539  19.816  1.00 27.55           C  
ATOM    873  CD1 PHE A 117      -0.776  46.921  19.774  1.00 30.31           C  
ATOM    874  CD2 PHE A 117      -1.446  44.760  19.069  1.00 28.08           C  
ATOM    875  CE1 PHE A 117      -1.745  47.497  18.951  1.00 31.52           C  
ATOM    876  CE2 PHE A 117      -2.438  45.317  18.242  1.00 30.71           C  
ATOM    877  CZ  PHE A 117      -2.589  46.693  18.207  1.00 32.08           C  
ATOM    878  N   CYS A 118      -1.509  43.068  22.203  1.00 22.95           N  
ATOM    879  CA  CYS A 118      -2.818  42.423  22.197  1.00 23.93           C  
ATOM    880  C   CYS A 118      -3.419  42.508  23.602  1.00 23.86           C  
ATOM    881  O   CYS A 118      -4.633  42.799  23.740  1.00 24.29           O  
ATOM    882  CB  CYS A 118      -2.632  40.918  21.789  1.00 25.89           C  
ATOM    883  SG  CYS A 118      -2.229  40.634  20.019  1.00 37.21           S  
ATOM    884  N   HIS A 119      -2.531  42.304  24.613  1.00 18.07           N  
ATOM    885  CA  HIS A 119      -3.038  42.336  25.983  1.00 21.34           C  
ATOM    886  C   HIS A 119      -3.541  43.723  26.363  1.00 24.24           C  
ATOM    887  O   HIS A 119      -4.502  43.733  27.118  1.00 25.64           O  
ATOM    888  CB  HIS A 119      -2.035  41.868  27.061  1.00 22.07           C  
ATOM    889  CG  HIS A 119      -1.741  40.390  26.904  1.00 19.72           C  
ATOM    890  ND1 HIS A 119      -0.667  39.788  27.465  1.00 19.04           N  
ATOM    891  CD2 HIS A 119      -2.365  39.438  26.152  1.00 19.88           C  
ATOM    892  CE1 HIS A 119      -0.671  38.484  27.146  1.00 19.56           C  
ATOM    893  NE2 HIS A 119      -1.706  38.232  26.337  1.00 20.58           N  
ATOM    894  N   SER A 120      -2.977  44.789  25.778  1.00 24.61           N  
ATOM    895  CA  SER A 120      -3.412  46.135  26.077  1.00 30.06           C  
ATOM    896  C   SER A 120      -4.799  46.333  25.468  1.00 31.14           C  
ATOM    897  O   SER A 120      -5.521  47.086  26.075  1.00 33.14           O  
ATOM    898  CB  SER A 120      -2.430  47.244  25.627  1.00 29.46           C  
ATOM    899  OG  SER A 120      -2.478  47.254  24.199  1.00 31.29           O  
ATOM    900  N   HIS A 121      -5.204  45.581  24.446  1.00 33.92           N  
ATOM    901  CA  HIS A 121      -6.559  45.631  23.873  1.00 36.06           C  
ATOM    902  C   HIS A 121      -7.468  44.555  24.443  1.00 35.63           C  
ATOM    903  O   HIS A 121      -8.533  44.255  23.907  1.00 36.59           O  
ATOM    904  CB  HIS A 121      -6.508  45.456  22.341  1.00 36.51           C  
ATOM    905  CG  HIS A 121      -6.011  46.725  21.687  1.00 39.07           C  
ATOM    906  ND1 HIS A 121      -4.683  46.981  21.520  1.00 40.91           N  
ATOM    907  CD2 HIS A 121      -6.627  47.809  21.193  1.00 39.16           C  
ATOM    908  CE1 HIS A 121      -4.456  48.140  20.948  1.00 41.29           C  
ATOM    909  NE2 HIS A 121      -5.661  48.655  20.747  1.00 42.78           N  
ATOM    910  N   ARG A 122      -6.982  43.873  25.501  1.00 36.97           N  
ATOM    911  CA  ARG A 122      -7.696  42.786  26.139  1.00 36.66           C  
ATOM    912  C   ARG A 122      -7.877  41.524  25.313  1.00 35.02           C  
ATOM    913  O   ARG A 122      -8.894  40.816  25.481  1.00 32.15           O  
ATOM    914  CB  ARG A 122      -9.085  43.329  26.562  1.00 40.56           C  
ATOM    915  CG  ARG A 122      -8.973  44.229  27.788  1.00 45.78           C  
ATOM    916  CD  ARG A 122      -8.241  43.404  28.880  1.00 51.95           C  
ATOM    917  NE  ARG A 122      -6.952  44.047  29.117  1.00 54.57           N  
ATOM    918  CZ  ARG A 122      -6.565  44.629  30.242  1.00 56.71           C  
ATOM    919  NH1 ARG A 122      -7.363  44.649  31.311  1.00 56.76           N  
ATOM    920  NH2 ARG A 122      -5.345  45.177  30.183  1.00 57.99           N  
ATOM    921  N   VAL A 123      -6.940  41.197  24.397  1.00 31.14           N  
ATOM    922  CA  VAL A 123      -7.141  39.992  23.608  1.00 30.56           C  
ATOM    923  C   VAL A 123      -6.132  38.939  24.019  1.00 27.19           C  
ATOM    924  O   VAL A 123      -4.981  39.345  24.042  1.00 27.38           O  
ATOM    925  CB  VAL A 123      -7.064  40.307  22.103  1.00 31.79           C  
ATOM    926  CG1 VAL A 123      -7.082  39.044  21.222  1.00 33.30           C  
ATOM    927  CG2 VAL A 123      -8.159  41.287  21.762  1.00 34.36           C  
ATOM    928  N   LEU A 124      -6.470  37.702  24.214  1.00 25.68           N  
ATOM    929  CA  LEU A 124      -5.583  36.670  24.599  1.00 31.04           C  
ATOM    930  C   LEU A 124      -5.465  35.659  23.457  1.00 29.59           C  
ATOM    931  O   LEU A 124      -6.394  35.485  22.713  1.00 29.20           O  
ATOM    932  CB  LEU A 124      -5.866  35.733  25.785  1.00 33.38           C  
ATOM    933  CG  LEU A 124      -6.943  36.083  26.774  1.00 37.89           C  
ATOM    934  CD1 LEU A 124      -6.975  35.205  28.019  1.00 36.43           C  
ATOM    935  CD2 LEU A 124      -6.756  37.513  27.284  1.00 40.96           C  
ATOM    936  N   HIS A 125      -4.271  35.047  23.451  1.00 27.47           N  
ATOM    937  CA  HIS A 125      -4.181  33.965  22.429  1.00 26.02           C  
ATOM    938  C   HIS A 125      -4.769  32.699  23.037  1.00 26.44           C  
ATOM    939  O   HIS A 125      -5.684  32.117  22.426  1.00 25.95           O  
ATOM    940  CB  HIS A 125      -2.721  33.852  21.977  1.00 25.57           C  
ATOM    941  CG  HIS A 125      -2.599  32.852  20.859  1.00 27.13           C  
ATOM    942  ND1 HIS A 125      -2.146  33.105  19.576  1.00 27.55           N  
ATOM    943  CD2 HIS A 125      -2.885  31.555  20.876  1.00 27.48           C  
ATOM    944  CE1 HIS A 125      -2.165  32.004  18.896  1.00 27.63           C  
ATOM    945  NE2 HIS A 125      -2.623  31.008  19.639  1.00 29.20           N  
ATOM    946  N   ARG A 126      -4.334  32.232  24.213  1.00 25.04           N  
ATOM    947  CA  ARG A 126      -4.810  31.045  24.848  1.00 27.83           C  
ATOM    948  C   ARG A 126      -4.278  29.740  24.287  1.00 26.82           C  
ATOM    949  O   ARG A 126      -4.235  28.702  24.978  1.00 28.33           O  
ATOM    950  CB  ARG A 126      -6.355  30.961  24.802  1.00 33.60           C  
ATOM    951  CG  ARG A 126      -6.857  30.008  25.894  1.00 41.26           C  
ATOM    952  CD  ARG A 126      -7.854  28.995  25.251  1.00 46.75           C  
ATOM    953  NE  ARG A 126      -7.052  27.747  25.277  1.00 52.26           N  
ATOM    954  CZ  ARG A 126      -7.497  26.738  26.030  1.00 55.39           C  
ATOM    955  NH1 ARG A 126      -8.657  26.802  26.672  1.00 56.58           N  
ATOM    956  NH2 ARG A 126      -6.803  25.625  26.130  1.00 56.37           N  
ATOM    957  N   ASP A 127      -3.695  29.783  23.105  1.00 24.49           N  
ATOM    958  CA  ASP A 127      -3.097  28.578  22.575  1.00 25.82           C  
ATOM    959  C   ASP A 127      -1.673  28.676  22.021  1.00 25.07           C  
ATOM    960  O   ASP A 127      -1.342  28.217  20.889  1.00 28.10           O  
ATOM    961  CB  ASP A 127      -4.124  28.072  21.546  1.00 30.51           C  
ATOM    962  CG  ASP A 127      -3.725  26.617  21.370  1.00 36.51           C  
ATOM    963  OD1 ASP A 127      -3.075  26.107  22.335  1.00 42.42           O  
ATOM    964  OD2 ASP A 127      -3.957  26.055  20.302  1.00 37.61           O  
ATOM    965  N   LEU A 128      -0.796  29.464  22.634  1.00 24.45           N  
ATOM    966  CA  LEU A 128       0.551  29.573  22.063  1.00 26.54           C  
ATOM    967  C   LEU A 128       1.285  28.237  21.999  1.00 24.05           C  
ATOM    968  O   LEU A 128       1.179  27.489  22.970  1.00 23.71           O  
ATOM    969  CB  LEU A 128       1.430  30.612  22.734  1.00 26.57           C  
ATOM    970  CG  LEU A 128       0.854  32.029  22.588  1.00 31.91           C  
ATOM    971  CD1 LEU A 128       1.798  33.052  23.213  1.00 32.28           C  
ATOM    972  CD2 LEU A 128       0.733  32.327  21.087  1.00 34.64           C  
ATOM    973  N   LYS A 129       1.987  27.989  20.917  1.00 18.56           N  
ATOM    974  CA  LYS A 129       2.824  26.814  20.713  1.00 19.58           C  
ATOM    975  C   LYS A 129       3.744  27.053  19.532  1.00 18.22           C  
ATOM    976  O   LYS A 129       3.494  28.049  18.844  1.00 18.48           O  
ATOM    977  CB  LYS A 129       2.048  25.547  20.478  1.00 22.88           C  
ATOM    978  CG  LYS A 129       1.000  25.676  19.373  1.00 30.81           C  
ATOM    979  CD  LYS A 129       0.020  24.482  19.566  1.00 34.99           C  
ATOM    980  CE  LYS A 129      -0.860  24.455  18.296  1.00 35.71           C  
ATOM    981  NZ  LYS A 129      -2.239  24.723  18.687  1.00 39.01           N  
ATOM    982  N   PRO A 130       4.896  26.413  19.429  1.00 20.37           N  
ATOM    983  CA  PRO A 130       5.869  26.646  18.383  1.00 20.48           C  
ATOM    984  C   PRO A 130       5.282  26.650  16.994  1.00 23.25           C  
ATOM    985  O   PRO A 130       5.630  27.614  16.306  1.00 23.19           O  
ATOM    986  CB  PRO A 130       6.913  25.568  18.658  1.00 22.54           C  
ATOM    987  CG  PRO A 130       6.899  25.498  20.174  1.00 23.28           C  
ATOM    988  CD  PRO A 130       5.410  25.363  20.370  1.00 20.80           C  
ATOM    989  N   GLN A 131       4.331  25.838  16.574  1.00 24.19           N  
ATOM    990  CA  GLN A 131       3.656  25.915  15.287  1.00 26.73           C  
ATOM    991  C   GLN A 131       2.855  27.202  15.082  1.00 25.46           C  
ATOM    992  O   GLN A 131       2.458  27.399  13.966  1.00 24.81           O  
ATOM    993  CB  GLN A 131       2.599  24.801  15.130  1.00 33.37           C  
ATOM    994  CG  GLN A 131       3.055  23.429  15.563  1.00 38.85           C  
ATOM    995  CD  GLN A 131       2.956  23.259  17.089  1.00 45.19           C  
ATOM    996  OE1 GLN A 131       3.743  23.571  17.993  1.00 40.50           O  
ATOM    997  NE2 GLN A 131       1.796  22.651  17.421  1.00 50.99           N  
ATOM    998  N   ASN A 132       2.456  27.935  16.104  1.00 21.81           N  
ATOM    999  CA  ASN A 132       1.738  29.211  15.944  1.00 22.51           C  
ATOM   1000  C   ASN A 132       2.698  30.388  15.911  1.00 16.42           C  
ATOM   1001  O   ASN A 132       2.307  31.563  16.109  1.00 19.93           O  
ATOM   1002  CB  ASN A 132       0.675  29.336  17.071  1.00 27.55           C  
ATOM   1003  CG  ASN A 132      -0.585  28.537  16.706  1.00 34.08           C  
ATOM   1004  OD1 ASN A 132      -0.814  28.180  15.541  1.00 34.32           O  
ATOM   1005  ND2 ASN A 132      -1.403  28.180  17.683  1.00 32.61           N  
ATOM   1006  N   LEU A 133       3.991  30.239  15.791  1.00 15.57           N  
ATOM   1007  CA  LEU A 133       4.991  31.330  15.800  1.00 16.61           C  
ATOM   1008  C   LEU A 133       5.695  31.238  14.406  1.00 19.12           C  
ATOM   1009  O   LEU A 133       6.252  30.182  14.125  1.00 16.42           O  
ATOM   1010  CB  LEU A 133       5.981  31.106  16.923  1.00 15.75           C  
ATOM   1011  CG  LEU A 133       5.327  31.125  18.345  1.00 16.52           C  
ATOM   1012  CD1 LEU A 133       6.382  31.131  19.448  1.00 12.31           C  
ATOM   1013  CD2 LEU A 133       4.506  32.380  18.561  1.00 19.43           C  
ATOM   1014  N   LEU A 134       5.525  32.259  13.605  1.00 14.80           N  
ATOM   1015  CA  LEU A 134       5.947  32.235  12.242  1.00 16.99           C  
ATOM   1016  C   LEU A 134       7.141  33.194  12.049  1.00 18.07           C  
ATOM   1017  O   LEU A 134       7.059  34.287  12.562  1.00 17.40           O  
ATOM   1018  CB  LEU A 134       4.800  32.698  11.280  1.00 19.37           C  
ATOM   1019  CG  LEU A 134       3.498  31.867  11.336  1.00 25.53           C  
ATOM   1020  CD1 LEU A 134       2.560  32.125  10.165  1.00 24.20           C  
ATOM   1021  CD2 LEU A 134       3.770  30.359  11.468  1.00 22.19           C  
ATOM   1022  N   ILE A 135       8.160  32.794  11.274  1.00 20.24           N  
ATOM   1023  CA  ILE A 135       9.359  33.618  11.125  1.00 21.08           C  
ATOM   1024  C   ILE A 135       9.682  33.883   9.642  1.00 21.48           C  
ATOM   1025  O   ILE A 135       9.220  33.123   8.774  1.00 18.49           O  
ATOM   1026  CB  ILE A 135      10.618  32.872  11.605  1.00 24.52           C  
ATOM   1027  CG1 ILE A 135      10.701  31.491  10.902  1.00 23.27           C  
ATOM   1028  CG2 ILE A 135      10.626  32.686  13.138  1.00 23.76           C  
ATOM   1029  CD1 ILE A 135      12.124  30.905  11.179  1.00 23.84           C  
ATOM   1030  N   ASN A 136      10.309  34.988   9.348  1.00 20.22           N  
ATOM   1031  CA  ASN A 136      10.807  35.244   7.969  1.00 21.52           C  
ATOM   1032  C   ASN A 136      12.316  35.316   7.889  1.00 24.33           C  
ATOM   1033  O   ASN A 136      13.161  35.130   8.825  1.00 23.14           O  
ATOM   1034  CB  ASN A 136      10.104  36.480   7.415  1.00 18.07           C  
ATOM   1035  CG  ASN A 136      10.338  37.718   8.215  1.00 19.00           C  
ATOM   1036  OD1 ASN A 136      11.386  37.891   8.920  1.00 19.34           O  
ATOM   1037  ND2 ASN A 136       9.389  38.623   8.062  1.00 17.52           N  
ATOM   1038  N   THR A 137      12.817  35.754   6.694  1.00 26.09           N  
ATOM   1039  CA  THR A 137      14.265  35.906   6.479  1.00 24.65           C  
ATOM   1040  C   THR A 137      14.862  37.165   7.106  1.00 27.67           C  
ATOM   1041  O   THR A 137      16.099  37.328   7.295  1.00 27.20           O  
ATOM   1042  CB  THR A 137      14.487  35.918   4.938  1.00 27.14           C  
ATOM   1043  OG1 THR A 137      13.622  36.926   4.350  1.00 26.92           O  
ATOM   1044  CG2 THR A 137      14.037  34.617   4.232  1.00 22.19           C  
ATOM   1045  N   GLU A 138      14.148  38.236   7.454  1.00 25.33           N  
ATOM   1046  CA  GLU A 138      14.753  39.405   8.055  1.00 29.62           C  
ATOM   1047  C   GLU A 138      14.950  39.339   9.611  1.00 27.31           C  
ATOM   1048  O   GLU A 138      15.061  40.445  10.205  1.00 24.76           O  
ATOM   1049  CB  GLU A 138      13.652  40.505   8.044  1.00 31.20           C  
ATOM   1050  CG  GLU A 138      13.911  41.641   7.079  1.00 38.28           C  
ATOM   1051  CD  GLU A 138      13.221  41.094   5.829  1.00 42.12           C  
ATOM   1052  OE1 GLU A 138      11.976  41.175   5.998  1.00 43.76           O  
ATOM   1053  OE2 GLU A 138      14.005  40.613   5.018  1.00 43.20           O  
ATOM   1054  N   GLY A 139      14.581  38.233  10.235  1.00 21.57           N  
ATOM   1055  CA  GLY A 139      14.639  38.179  11.676  1.00 22.90           C  
ATOM   1056  C   GLY A 139      13.386  38.485  12.479  1.00 23.49           C  
ATOM   1057  O   GLY A 139      13.508  38.703  13.697  1.00 23.54           O  
ATOM   1058  N   ALA A 140      12.217  38.581  11.835  1.00 21.07           N  
ATOM   1059  CA  ALA A 140      10.994  38.866  12.513  1.00 18.26           C  
ATOM   1060  C   ALA A 140      10.311  37.559  12.948  1.00 19.16           C  
ATOM   1061  O   ALA A 140      10.506  36.546  12.298  1.00 17.02           O  
ATOM   1062  CB  ALA A 140      10.013  39.615  11.601  1.00 18.45           C  
ATOM   1063  N   ILE A 141       9.428  37.613  13.988  1.00 20.29           N  
ATOM   1064  CA  ILE A 141       8.722  36.403  14.433  1.00 18.51           C  
ATOM   1065  C   ILE A 141       7.311  36.892  14.776  1.00 15.39           C  
ATOM   1066  O   ILE A 141       7.256  38.082  15.165  1.00 16.75           O  
ATOM   1067  CB  ILE A 141       9.382  35.630  15.595  1.00 18.97           C  
ATOM   1068  CG1 ILE A 141       8.595  34.381  15.958  1.00 21.53           C  
ATOM   1069  CG2 ILE A 141       9.600  36.543  16.824  1.00 17.62           C  
ATOM   1070  CD1 ILE A 141       9.284  33.225  16.675  1.00 16.13           C  
ATOM   1071  N   LYS A 142       6.264  36.189  14.381  1.00 15.59           N  
ATOM   1072  CA  LYS A 142       4.947  36.847  14.533  1.00 19.09           C  
ATOM   1073  C   LYS A 142       3.993  35.865  15.206  1.00 17.14           C  
ATOM   1074  O   LYS A 142       4.172  34.692  14.893  1.00 16.83           O  
ATOM   1075  CB  LYS A 142       4.374  37.118  13.103  1.00 20.50           C  
ATOM   1076  CG  LYS A 142       5.206  38.123  12.307  1.00 20.84           C  
ATOM   1077  CD  LYS A 142       4.380  38.929  11.350  1.00 22.52           C  
ATOM   1078  CE  LYS A 142       5.309  39.626  10.306  1.00 27.63           C  
ATOM   1079  NZ  LYS A 142       4.603  40.925   9.856  1.00 27.09           N  
ATOM   1080  N   LEU A 143       3.060  36.295  15.984  1.00 15.88           N  
ATOM   1081  CA  LEU A 143       2.113  35.260  16.524  1.00 20.60           C  
ATOM   1082  C   LEU A 143       0.991  34.865  15.625  1.00 19.70           C  
ATOM   1083  O   LEU A 143       0.409  35.873  15.146  1.00 20.75           O  
ATOM   1084  CB  LEU A 143       1.480  35.955  17.782  1.00 22.67           C  
ATOM   1085  CG  LEU A 143       2.672  36.158  18.762  1.00 26.28           C  
ATOM   1086  CD1 LEU A 143       2.630  37.561  19.350  1.00 26.24           C  
ATOM   1087  CD2 LEU A 143       2.491  35.028  19.801  1.00 24.79           C  
ATOM   1088  N   ALA A 144       0.694  33.686  15.207  1.00 18.26           N  
ATOM   1089  CA  ALA A 144      -0.368  33.371  14.247  1.00 18.78           C  
ATOM   1090  C   ALA A 144      -1.612  32.841  15.000  1.00 22.49           C  
ATOM   1091  O   ALA A 144      -1.416  32.300  16.112  1.00 19.46           O  
ATOM   1092  CB  ALA A 144       0.125  32.160  13.480  1.00 16.75           C  
ATOM   1093  N   ASP A 145      -2.828  33.065  14.558  1.00 26.61           N  
ATOM   1094  CA  ASP A 145      -4.023  32.513  15.176  1.00 29.57           C  
ATOM   1095  C   ASP A 145      -4.412  33.144  16.494  1.00 29.48           C  
ATOM   1096  O   ASP A 145      -5.141  32.500  17.247  1.00 33.23           O  
ATOM   1097  CB  ASP A 145      -4.019  30.977  15.415  1.00 29.15           C  
ATOM   1098  CG  ASP A 145      -3.991  30.309  14.066  1.00 34.09           C  
ATOM   1099  OD1 ASP A 145      -4.642  30.872  13.127  1.00 34.61           O  
ATOM   1100  OD2 ASP A 145      -3.370  29.248  13.896  1.00 34.32           O  
ATOM   1101  N   PHE A 146      -3.998  34.366  16.732  1.00 29.69           N  
ATOM   1102  CA  PHE A 146      -4.349  35.102  17.917  1.00 31.48           C  
ATOM   1103  C   PHE A 146      -5.852  35.348  17.954  1.00 30.39           C  
ATOM   1104  O   PHE A 146      -6.406  35.842  16.970  1.00 27.16           O  
ATOM   1105  CB  PHE A 146      -3.733  36.525  17.763  1.00 33.53           C  
ATOM   1106  CG  PHE A 146      -3.088  36.938  19.034  1.00 36.50           C  
ATOM   1107  CD1 PHE A 146      -3.828  37.352  20.098  1.00 38.37           C  
ATOM   1108  CD2 PHE A 146      -1.708  36.854  19.160  1.00 37.51           C  
ATOM   1109  CE1 PHE A 146      -3.222  37.709  21.285  1.00 39.68           C  
ATOM   1110  CE2 PHE A 146      -1.081  37.165  20.333  1.00 40.61           C  
ATOM   1111  CZ  PHE A 146      -1.851  37.615  21.395  1.00 40.74           C  
ATOM   1112  N   GLY A 147      -6.529  35.211  19.055  1.00 29.68           N  
ATOM   1113  CA  GLY A 147      -7.976  35.538  19.126  1.00 28.31           C  
ATOM   1114  C   GLY A 147      -8.854  34.415  18.709  1.00 26.53           C  
ATOM   1115  O   GLY A 147      -9.994  34.315  19.153  1.00 29.46           O  
ATOM   1116  N   LEU A 148      -8.469  33.498  17.860  1.00 31.44           N  
ATOM   1117  CA  LEU A 148      -9.341  32.435  17.370  1.00 29.58           C  
ATOM   1118  C   LEU A 148      -9.919  31.516  18.433  1.00 33.24           C  
ATOM   1119  O   LEU A 148     -11.107  31.148  18.228  1.00 33.87           O  
ATOM   1120  CB  LEU A 148      -8.646  31.664  16.272  1.00 30.43           C  
ATOM   1121  CG  LEU A 148      -8.148  32.491  15.062  1.00 32.05           C  
ATOM   1122  CD1 LEU A 148      -7.824  31.520  13.954  1.00 32.81           C  
ATOM   1123  CD2 LEU A 148      -9.163  33.539  14.584  1.00 34.57           C  
ATOM   1124  N   ALA A 149      -9.238  31.119  19.493  1.00 30.31           N  
ATOM   1125  CA  ALA A 149      -9.733  30.237  20.512  1.00 33.57           C  
ATOM   1126  C   ALA A 149     -10.984  30.807  21.183  1.00 36.15           C  
ATOM   1127  O   ALA A 149     -12.009  30.085  21.285  1.00 37.22           O  
ATOM   1128  CB  ALA A 149      -8.679  29.898  21.589  1.00 32.50           C  
ATOM   1129  N   ARG A 150     -10.992  32.078  21.536  1.00 38.28           N  
ATOM   1130  CA  ARG A 150     -12.193  32.646  22.129  1.00 45.75           C  
ATOM   1131  C   ARG A 150     -13.290  32.809  21.065  1.00 47.23           C  
ATOM   1132  O   ARG A 150     -14.476  32.717  21.463  1.00 46.47           O  
ATOM   1133  CB  ARG A 150     -12.031  33.993  22.811  1.00 49.73           C  
ATOM   1134  CG  ARG A 150     -12.924  35.151  22.434  1.00 54.36           C  
ATOM   1135  CD  ARG A 150     -12.774  36.346  23.392  1.00 58.33           C  
ATOM   1136  NE  ARG A 150     -13.853  36.346  24.355  1.00 61.52           N  
ATOM   1137  CZ  ARG A 150     -14.325  37.183  25.256  1.00 63.38           C  
ATOM   1138  NH1 ARG A 150     -13.793  38.384  25.463  1.00 63.43           N  
ATOM   1139  NH2 ARG A 150     -15.388  36.787  25.975  1.00 64.11           N  
ATOM   1140  N   ALA A 151     -12.853  33.070  19.812  1.00 46.18           N  
ATOM   1141  CA  ALA A 151     -13.926  33.279  18.840  1.00 48.03           C  
ATOM   1142  C   ALA A 151     -14.552  31.980  18.424  1.00 48.53           C  
ATOM   1143  O   ALA A 151     -15.742  32.127  18.177  1.00 51.01           O  
ATOM   1144  CB  ALA A 151     -13.546  34.204  17.716  1.00 48.17           C  
ATOM   1145  N   PHE A 152     -14.043  30.797  18.464  1.00 52.46           N  
ATOM   1146  CA  PHE A 152     -14.711  29.587  18.052  1.00 57.87           C  
ATOM   1147  C   PHE A 152     -14.755  28.404  19.002  1.00 63.73           C  
ATOM   1148  O   PHE A 152     -15.416  27.439  18.587  1.00 64.74           O  
ATOM   1149  CB  PHE A 152     -13.981  28.914  16.860  1.00 54.82           C  
ATOM   1150  CG  PHE A 152     -13.878  29.692  15.610  1.00 55.24           C  
ATOM   1151  CD1 PHE A 152     -14.993  30.055  14.872  1.00 55.24           C  
ATOM   1152  CD2 PHE A 152     -12.625  30.082  15.151  1.00 55.52           C  
ATOM   1153  CE1 PHE A 152     -14.853  30.789  13.712  1.00 55.97           C  
ATOM   1154  CE2 PHE A 152     -12.458  30.816  13.999  1.00 55.95           C  
ATOM   1155  CZ  PHE A 152     -13.594  31.157  13.274  1.00 57.08           C  
ATOM   1156  N   GLY A 153     -13.953  28.334  20.070  1.00 70.42           N  
ATOM   1157  CA  GLY A 153     -13.808  27.184  20.951  1.00 74.60           C  
ATOM   1158  C   GLY A 153     -12.450  26.506  20.743  1.00 80.06           C  
ATOM   1159  O   GLY A 153     -11.883  26.488  19.639  1.00 79.26           O  
ATOM   1160  N   VAL A 154     -11.870  25.876  21.771  1.00 86.11           N  
ATOM   1161  CA  VAL A 154     -10.607  25.147  21.673  1.00 91.05           C  
ATOM   1162  C   VAL A 154     -10.760  23.643  21.984  1.00 94.87           C  
ATOM   1163  O   VAL A 154     -10.487  23.207  23.110  1.00 94.62           O  
ATOM   1164  CB  VAL A 154      -9.459  25.531  22.646  1.00 90.43           C  
ATOM   1165  CG1 VAL A 154      -8.152  25.108  21.972  1.00 90.73           C  
ATOM   1166  CG2 VAL A 154      -9.456  26.962  23.110  1.00 90.09           C  
ATOM   1167  N   PRO A 155     -11.117  22.842  20.989  1.00 97.68           N  
ATOM   1168  CA  PRO A 155     -11.357  21.427  21.141  1.00 99.98           C  
ATOM   1169  C   PRO A 155     -10.274  20.532  21.712  1.00102.33           C  
ATOM   1170  O   PRO A 155      -9.074  20.810  21.675  1.00103.15           O  
ATOM   1171  CB  PRO A 155     -11.690  20.966  19.710  1.00 99.64           C  
ATOM   1172  CG  PRO A 155     -12.336  22.182  19.122  1.00 99.28           C  
ATOM   1173  CD  PRO A 155     -11.469  23.314  19.625  1.00 98.35           C  
ATOM   1174  N   VAL A 156     -10.726  19.374  22.221  1.00104.30           N  
ATOM   1175  CA  VAL A 156      -9.825  18.365  22.772  1.00105.93           C  
ATOM   1176  C   VAL A 156      -8.929  17.866  21.628  1.00106.96           C  
ATOM   1177  O   VAL A 156      -7.710  17.992  21.588  1.00106.91           O  
ATOM   1178  CB  VAL A 156     -10.568  17.146  23.337  1.00105.71           C  
ATOM   1179  CG1 VAL A 156      -9.570  16.086  23.787  1.00106.07           C  
ATOM   1180  CG2 VAL A 156     -11.494  17.548  24.472  1.00105.62           C  
ATOM   1181  N   ARG A 157      -9.670  17.306  20.674  1.00108.16           N  
ATOM   1182  CA  ARG A 157      -9.110  16.763  19.454  1.00108.95           C  
ATOM   1183  C   ARG A 157      -9.123  17.758  18.301  1.00109.51           C  
ATOM   1184  O   ARG A 157     -10.224  18.120  17.877  1.00109.83           O  
ATOM   1185  CB  ARG A 157      -9.926  15.528  19.043  1.00108.68           C  
ATOM   1186  CG  ARG A 157      -9.073  14.339  18.647  1.00108.72           C  
ATOM   1187  CD  ARG A 157      -7.856  14.181  19.540  1.00108.31           C  
ATOM   1188  NE  ARG A 157      -8.057  13.283  20.655  1.00108.37           N  
ATOM   1189  CZ  ARG A 157      -8.262  11.975  20.535  1.00108.52           C  
ATOM   1190  NH1 ARG A 157      -8.293  11.399  19.341  1.00108.24           N  
ATOM   1191  NH2 ARG A 157      -8.420  11.269  21.650  1.00109.08           N  
ATOM   1192  N   THR A 158      -7.944  18.154  17.822  1.00109.63           N  
ATOM   1193  CA  THR A 158      -7.879  19.040  16.672  1.00109.75           C  
ATOM   1194  C   THR A 158      -8.641  18.392  15.508  1.00109.93           C  
ATOM   1195  O   THR A 158      -8.613  17.166  15.371  1.00110.37           O  
ATOM   1196  CB  THR A 158      -6.485  19.332  16.109  1.00109.63           C  
ATOM   1197  OG1 THR A 158      -6.094  18.299  15.191  1.00108.64           O  
ATOM   1198  CG2 THR A 158      -5.458  19.543  17.199  1.00110.09           C  
ATOM   1199  N   TYR A 159      -9.223  19.221  14.661  1.00109.42           N  
ATOM   1200  CA  TYR A 159     -10.018  18.763  13.528  1.00108.87           C  
ATOM   1201  C   TYR A 159      -9.636  17.423  12.916  1.00108.18           C  
ATOM   1202  O   TYR A 159     -10.479  16.505  12.890  1.00107.79           O  
ATOM   1203  CB  TYR A 159     -10.101  19.934  12.528  1.00108.59           C  
ATOM   1204  CG  TYR A 159     -10.078  19.495  11.082  1.00108.31           C  
ATOM   1205  CD1 TYR A 159     -11.215  18.978  10.478  1.00108.34           C  
ATOM   1206  CD2 TYR A 159      -8.905  19.572  10.349  1.00108.26           C  
ATOM   1207  CE1 TYR A 159     -11.193  18.556   9.165  1.00108.47           C  
ATOM   1208  CE2 TYR A 159      -8.892  19.165   9.029  1.00108.58           C  
ATOM   1209  CZ  TYR A 159     -10.023  18.641   8.446  1.00108.39           C  
ATOM   1210  OH  TYR A 159      -9.980  18.231   7.135  1.00108.54           O  
ATOM   1211  N   THR A 160      -8.408  17.220  12.438  1.00107.11           N  
ATOM   1212  CA  THR A 160      -7.950  16.016  11.796  1.00105.67           C  
ATOM   1213  C   THR A 160      -7.504  14.856  12.643  1.00104.69           C  
ATOM   1214  O   THR A 160      -6.692  13.981  12.282  1.00104.60           O  
ATOM   1215  CB  THR A 160      -6.695  16.243  10.894  1.00105.72           C  
ATOM   1216  OG1 THR A 160      -5.798  17.148  11.526  1.00105.17           O  
ATOM   1217  CG2 THR A 160      -7.232  16.613   9.533  1.00105.67           C  
ATOM   1218  N   HIS A 161      -8.083  14.714  13.818  1.00103.33           N  
ATOM   1219  CA  HIS A 161      -7.852  13.706  14.840  1.00101.39           C  
ATOM   1220  C   HIS A 161      -6.647  14.158  15.640  1.00 99.96           C  
ATOM   1221  O   HIS A 161      -6.658  13.964  16.861  1.00100.30           O  
ATOM   1222  CB  HIS A 161      -7.879  12.249  14.352  1.00101.40           C  
ATOM   1223  CG  HIS A 161      -9.046  12.071  13.406  1.00101.65           C  
ATOM   1224  ND1 HIS A 161     -10.263  12.674  13.652  1.00102.05           N  
ATOM   1225  CD2 HIS A 161      -9.153  11.543  12.178  1.00101.81           C  
ATOM   1226  CE1 HIS A 161     -11.081  12.450  12.641  1.00102.20           C  
ATOM   1227  NE2 HIS A 161     -10.425  11.761  11.729  1.00102.01           N  
ATOM   1228  N   GLU A 162      -5.660  14.824  15.060  1.00 97.94           N  
ATOM   1229  CA  GLU A 162      -4.523  15.346  15.796  1.00 95.19           C  
ATOM   1230  C   GLU A 162      -5.030  15.938  17.112  1.00 91.60           C  
ATOM   1231  O   GLU A 162      -6.115  16.504  17.200  1.00 90.55           O  
ATOM   1232  CB  GLU A 162      -3.743  16.368  14.966  1.00 96.82           C  
ATOM   1233  CG  GLU A 162      -2.289  16.458  15.405  1.00 99.08           C  
ATOM   1234  CD  GLU A 162      -1.513  17.631  14.853  1.00100.66           C  
ATOM   1235  OE1 GLU A 162      -2.027  18.436  14.044  1.00101.40           O  
ATOM   1236  OE2 GLU A 162      -0.329  17.774  15.249  1.00101.38           O  
ATOM   1237  N   VAL A 163      -4.228  15.783  18.148  1.00 87.96           N  
ATOM   1238  CA  VAL A 163      -4.522  16.237  19.496  1.00 82.76           C  
ATOM   1239  C   VAL A 163      -3.757  17.530  19.762  1.00 79.56           C  
ATOM   1240  O   VAL A 163      -2.511  17.570  19.652  1.00 79.34           O  
ATOM   1241  CB  VAL A 163      -4.066  15.187  20.538  1.00 82.48           C  
ATOM   1242  CG1 VAL A 163      -4.831  15.328  21.840  1.00 82.31           C  
ATOM   1243  CG2 VAL A 163      -4.205  13.767  20.004  1.00 82.01           C  
ATOM   1244  N   VAL A 164      -4.522  18.578  20.103  1.00 74.27           N  
ATOM   1245  CA  VAL A 164      -3.825  19.813  20.460  1.00 67.86           C  
ATOM   1246  C   VAL A 164      -2.893  19.444  21.638  1.00 62.88           C  
ATOM   1247  O   VAL A 164      -3.078  18.651  22.574  1.00 61.28           O  
ATOM   1248  CB  VAL A 164      -4.647  21.029  20.892  1.00 68.98           C  
ATOM   1249  CG1 VAL A 164      -3.770  22.238  21.279  1.00 68.52           C  
ATOM   1250  CG2 VAL A 164      -5.649  21.479  19.833  1.00 69.06           C  
ATOM   1251  N   THR A 165      -1.777  20.171  21.549  1.00 56.42           N  
ATOM   1252  CA  THR A 165      -0.819  20.113  22.631  1.00 50.28           C  
ATOM   1253  C   THR A 165      -1.301  20.730  23.925  1.00 42.94           C  
ATOM   1254  O   THR A 165      -1.894  21.776  23.956  1.00 40.02           O  
ATOM   1255  CB  THR A 165       0.388  20.873  22.065  1.00 50.34           C  
ATOM   1256  OG1 THR A 165       0.793  19.888  21.069  1.00 55.37           O  
ATOM   1257  CG2 THR A 165       1.399  21.083  23.129  1.00 49.27           C  
ATOM   1258  N   LEU A 166      -0.969  20.146  25.041  1.00 36.13           N  
ATOM   1259  CA  LEU A 166      -1.154  20.575  26.393  1.00 29.29           C  
ATOM   1260  C   LEU A 166       0.136  21.057  27.010  1.00 23.67           C  
ATOM   1261  O   LEU A 166       0.094  21.576  28.158  1.00 15.90           O  
ATOM   1262  CB  LEU A 166      -1.533  19.277  27.134  1.00 33.59           C  
ATOM   1263  CG  LEU A 166      -2.890  18.742  26.656  1.00 37.14           C  
ATOM   1264  CD1 LEU A 166      -3.340  17.733  27.729  1.00 37.27           C  
ATOM   1265  CD2 LEU A 166      -3.943  19.846  26.470  1.00 37.41           C  
ATOM   1266  N   TRP A 167       1.275  20.799  26.290  1.00 19.79           N  
ATOM   1267  CA  TRP A 167       2.612  21.091  26.860  1.00 18.63           C  
ATOM   1268  C   TRP A 167       2.858  22.518  27.305  1.00 17.64           C  
ATOM   1269  O   TRP A 167       3.658  22.866  28.206  1.00 18.76           O  
ATOM   1270  CB  TRP A 167       3.607  20.818  25.680  1.00 23.88           C  
ATOM   1271  CG  TRP A 167       3.692  19.411  25.167  1.00 20.67           C  
ATOM   1272  CD1 TRP A 167       3.018  18.332  25.665  1.00 24.78           C  
ATOM   1273  CD2 TRP A 167       4.518  18.910  24.132  1.00 23.92           C  
ATOM   1274  NE1 TRP A 167       3.413  17.191  25.048  1.00 27.32           N  
ATOM   1275  CE2 TRP A 167       4.307  17.517  24.053  1.00 25.54           C  
ATOM   1276  CE3 TRP A 167       5.511  19.513  23.296  1.00 19.69           C  
ATOM   1277  CZ2 TRP A 167       4.989  16.654  23.165  1.00 23.94           C  
ATOM   1278  CZ3 TRP A 167       6.133  18.657  22.408  1.00 24.25           C  
ATOM   1279  CH2 TRP A 167       5.915  17.254  22.355  1.00 24.38           C  
ATOM   1280  N   TYR A 168       2.099  23.458  26.718  1.00 16.62           N  
ATOM   1281  CA  TYR A 168       2.199  24.870  26.899  1.00 18.19           C  
ATOM   1282  C   TYR A 168       1.016  25.420  27.712  1.00 18.14           C  
ATOM   1283  O   TYR A 168       0.891  26.657  27.903  1.00 14.42           O  
ATOM   1284  CB  TYR A 168       2.280  25.719  25.538  1.00 17.21           C  
ATOM   1285  CG  TYR A 168       3.366  25.045  24.674  1.00 17.00           C  
ATOM   1286  CD1 TYR A 168       4.701  25.272  24.900  1.00 17.21           C  
ATOM   1287  CD2 TYR A 168       2.970  24.053  23.764  1.00 15.56           C  
ATOM   1288  CE1 TYR A 168       5.683  24.591  24.184  1.00 17.64           C  
ATOM   1289  CE2 TYR A 168       3.944  23.356  23.066  1.00 18.02           C  
ATOM   1290  CZ  TYR A 168       5.299  23.636  23.284  1.00 17.10           C  
ATOM   1291  OH  TYR A 168       6.239  22.960  22.502  1.00 16.47           O  
ATOM   1292  N   ARG A 169       0.243  24.507  28.275  1.00 17.57           N  
ATOM   1293  CA  ARG A 169      -0.918  25.100  29.037  1.00 18.66           C  
ATOM   1294  C   ARG A 169      -0.659  25.528  30.462  1.00 16.14           C  
ATOM   1295  O   ARG A 169      -0.001  24.824  31.265  1.00 14.63           O  
ATOM   1296  CB  ARG A 169      -2.024  24.064  28.842  1.00 24.98           C  
ATOM   1297  CG  ARG A 169      -3.410  24.549  29.156  1.00 32.72           C  
ATOM   1298  CD  ARG A 169      -4.446  23.724  28.384  1.00 37.33           C  
ATOM   1299  NE  ARG A 169      -4.720  24.092  27.014  1.00 37.53           N  
ATOM   1300  CZ  ARG A 169      -5.419  23.272  26.237  1.00 43.06           C  
ATOM   1301  NH1 ARG A 169      -5.898  22.148  26.788  1.00 44.50           N  
ATOM   1302  NH2 ARG A 169      -5.669  23.601  24.959  1.00 43.22           N  
ATOM   1303  N   ALA A 170      -1.036  26.742  30.796  1.00 14.67           N  
ATOM   1304  CA  ALA A 170      -0.855  27.281  32.141  1.00 16.46           C  
ATOM   1305  C   ALA A 170      -1.587  26.387  33.165  1.00 19.35           C  
ATOM   1306  O   ALA A 170      -2.696  25.846  32.923  1.00 16.39           O  
ATOM   1307  CB  ALA A 170      -1.380  28.757  32.287  1.00  9.54           C  
ATOM   1308  N   PRO A 171      -1.023  26.343  34.371  1.00 17.85           N  
ATOM   1309  CA  PRO A 171      -1.657  25.563  35.458  1.00 17.37           C  
ATOM   1310  C   PRO A 171      -3.021  26.091  35.855  1.00 16.12           C  
ATOM   1311  O   PRO A 171      -3.863  25.311  36.211  1.00 17.15           O  
ATOM   1312  CB  PRO A 171      -0.658  25.638  36.614  1.00 18.17           C  
ATOM   1313  CG  PRO A 171       0.204  26.853  36.314  1.00 17.61           C  
ATOM   1314  CD  PRO A 171       0.215  27.038  34.778  1.00 17.06           C  
ATOM   1315  N   GLU A 172      -3.403  27.368  35.882  1.00 14.34           N  
ATOM   1316  CA  GLU A 172      -4.790  27.696  36.262  1.00 16.19           C  
ATOM   1317  C   GLU A 172      -5.789  27.103  35.244  1.00 17.60           C  
ATOM   1318  O   GLU A 172      -6.911  26.777  35.664  1.00 14.49           O  
ATOM   1319  CB  GLU A 172      -4.985  29.214  36.427  1.00 15.72           C  
ATOM   1320  CG  GLU A 172      -4.596  30.049  35.187  1.00 17.31           C  
ATOM   1321  CD  GLU A 172      -3.153  30.480  35.010  1.00 17.49           C  
ATOM   1322  OE1 GLU A 172      -2.220  29.760  35.430  1.00 15.47           O  
ATOM   1323  OE2 GLU A 172      -2.817  31.575  34.411  1.00 17.93           O  
ATOM   1324  N   ILE A 173      -5.472  27.035  33.919  1.00 19.79           N  
ATOM   1325  CA  ILE A 173      -6.443  26.431  32.980  1.00 20.30           C  
ATOM   1326  C   ILE A 173      -6.563  24.929  33.319  1.00 20.98           C  
ATOM   1327  O   ILE A 173      -7.649  24.347  33.380  1.00 22.34           O  
ATOM   1328  CB  ILE A 173      -5.979  26.542  31.518  1.00 20.84           C  
ATOM   1329  CG1 ILE A 173      -5.912  28.052  31.198  1.00 21.07           C  
ATOM   1330  CG2 ILE A 173      -6.852  25.779  30.479  1.00 18.80           C  
ATOM   1331  CD1 ILE A 173      -5.246  28.195  29.820  1.00 22.98           C  
ATOM   1332  N   LEU A 174      -5.482  24.254  33.656  1.00 18.74           N  
ATOM   1333  CA  LEU A 174      -5.487  22.831  33.941  1.00 18.74           C  
ATOM   1334  C   LEU A 174      -6.215  22.435  35.188  1.00 20.34           C  
ATOM   1335  O   LEU A 174      -6.726  21.329  35.333  1.00 23.21           O  
ATOM   1336  CB  LEU A 174      -4.028  22.321  34.003  1.00 20.65           C  
ATOM   1337  CG  LEU A 174      -3.213  22.187  32.731  1.00 19.77           C  
ATOM   1338  CD1 LEU A 174      -1.753  21.958  33.095  1.00 23.33           C  
ATOM   1339  CD2 LEU A 174      -3.740  21.040  31.841  1.00 19.79           C  
ATOM   1340  N   LEU A 175      -6.327  23.348  36.148  1.00 20.32           N  
ATOM   1341  CA  LEU A 175      -6.961  23.237  37.410  1.00 23.14           C  
ATOM   1342  C   LEU A 175      -8.420  23.715  37.291  1.00 22.97           C  
ATOM   1343  O   LEU A 175      -9.085  23.649  38.323  1.00 25.94           O  
ATOM   1344  CB  LEU A 175      -6.203  24.034  38.518  1.00 19.44           C  
ATOM   1345  CG  LEU A 175      -4.862  23.386  38.983  1.00 20.30           C  
ATOM   1346  CD1 LEU A 175      -4.175  24.288  40.020  1.00 19.00           C  
ATOM   1347  CD2 LEU A 175      -5.021  21.954  39.485  1.00 16.12           C  
ATOM   1348  N   GLY A 176      -8.853  24.072  36.106  1.00 22.02           N  
ATOM   1349  CA  GLY A 176     -10.248  24.375  35.786  1.00 21.92           C  
ATOM   1350  C   GLY A 176     -10.646  25.808  36.085  1.00 24.41           C  
ATOM   1351  O   GLY A 176     -11.846  26.007  36.346  1.00 23.70           O  
ATOM   1352  N   CYS A 177      -9.742  26.744  36.218  1.00 21.93           N  
ATOM   1353  CA  CYS A 177     -10.061  28.126  36.404  1.00 29.00           C  
ATOM   1354  C   CYS A 177     -10.874  28.558  35.164  1.00 29.86           C  
ATOM   1355  O   CYS A 177     -10.457  28.345  34.021  1.00 32.19           O  
ATOM   1356  CB  CYS A 177      -8.899  29.090  36.608  1.00 30.94           C  
ATOM   1357  SG  CYS A 177      -9.413  30.814  36.887  1.00 38.81           S  
ATOM   1358  N   LYS A 178     -12.059  29.152  35.418  1.00 30.31           N  
ATOM   1359  CA  LYS A 178     -12.918  29.434  34.284  1.00 32.52           C  
ATOM   1360  C   LYS A 178     -12.645  30.736  33.571  1.00 29.98           C  
ATOM   1361  O   LYS A 178     -12.894  30.927  32.383  1.00 29.00           O  
ATOM   1362  CB  LYS A 178     -14.371  29.422  34.856  1.00 37.00           C  
ATOM   1363  CG  LYS A 178     -15.173  28.287  34.224  1.00 42.36           C  
ATOM   1364  CD  LYS A 178     -14.443  26.940  34.177  1.00 45.87           C  
ATOM   1365  CE  LYS A 178     -14.913  26.051  33.037  1.00 48.00           C  
ATOM   1366  NZ  LYS A 178     -15.608  24.796  33.490  1.00 51.40           N  
ATOM   1367  N   TYR A 179     -12.168  31.688  34.346  1.00 27.68           N  
ATOM   1368  CA  TYR A 179     -11.955  33.024  33.884  1.00 31.31           C  
ATOM   1369  C   TYR A 179     -10.477  33.349  33.825  1.00 29.52           C  
ATOM   1370  O   TYR A 179     -10.174  34.414  34.310  1.00 28.31           O  
ATOM   1371  CB  TYR A 179     -12.724  33.967  34.840  1.00 34.55           C  
ATOM   1372  CG  TYR A 179     -14.186  33.614  34.934  1.00 38.35           C  
ATOM   1373  CD1 TYR A 179     -14.977  33.779  33.806  1.00 37.72           C  
ATOM   1374  CD2 TYR A 179     -14.796  33.161  36.092  1.00 41.12           C  
ATOM   1375  CE1 TYR A 179     -16.317  33.493  33.816  1.00 39.86           C  
ATOM   1376  CE2 TYR A 179     -16.164  32.843  36.138  1.00 41.15           C  
ATOM   1377  CZ  TYR A 179     -16.897  33.014  34.971  1.00 42.45           C  
ATOM   1378  OH  TYR A 179     -18.231  32.737  34.895  1.00 45.51           O  
ATOM   1379  N   TYR A 180      -9.655  32.538  33.242  1.00 31.18           N  
ATOM   1380  CA  TYR A 180      -8.184  32.857  33.288  1.00 33.32           C  
ATOM   1381  C   TYR A 180      -7.898  34.126  32.463  1.00 33.48           C  
ATOM   1382  O   TYR A 180      -8.704  34.484  31.605  1.00 33.96           O  
ATOM   1383  CB  TYR A 180      -7.459  31.536  32.923  1.00 31.88           C  
ATOM   1384  CG  TYR A 180      -7.943  31.160  31.536  1.00 31.85           C  
ATOM   1385  CD1 TYR A 180      -7.583  31.938  30.434  1.00 35.25           C  
ATOM   1386  CD2 TYR A 180      -8.820  30.145  31.323  1.00 32.67           C  
ATOM   1387  CE1 TYR A 180      -8.053  31.721  29.177  1.00 36.07           C  
ATOM   1388  CE2 TYR A 180      -9.336  29.890  30.069  1.00 35.38           C  
ATOM   1389  CZ  TYR A 180      -8.932  30.678  29.021  1.00 38.41           C  
ATOM   1390  OH  TYR A 180      -9.442  30.394  27.747  1.00 43.91           O  
ATOM   1391  N   SER A 181      -6.830  34.881  32.670  1.00 28.65           N  
ATOM   1392  CA  SER A 181      -6.486  36.189  32.140  1.00 24.95           C  
ATOM   1393  C   SER A 181      -5.341  36.111  31.127  1.00 22.40           C  
ATOM   1394  O   SER A 181      -4.752  35.090  30.777  1.00 21.38           O  
ATOM   1395  CB  SER A 181      -5.884  36.953  33.382  1.00 23.42           C  
ATOM   1396  OG  SER A 181      -4.520  36.494  33.691  1.00 21.20           O  
ATOM   1397  N   THR A 182      -4.735  37.260  30.810  1.00 21.89           N  
ATOM   1398  CA  THR A 182      -3.674  37.380  29.844  1.00 22.81           C  
ATOM   1399  C   THR A 182      -2.391  36.689  30.356  1.00 20.98           C  
ATOM   1400  O   THR A 182      -1.479  36.321  29.583  1.00 21.34           O  
ATOM   1401  CB  THR A 182      -3.385  38.859  29.495  1.00 22.74           C  
ATOM   1402  OG1 THR A 182      -2.931  39.416  30.697  1.00 23.90           O  
ATOM   1403  CG2 THR A 182      -4.539  39.621  28.883  1.00 24.04           C  
ATOM   1404  N   ALA A 183      -2.284  36.419  31.637  1.00 16.98           N  
ATOM   1405  CA  ALA A 183      -1.161  35.688  32.237  1.00 17.85           C  
ATOM   1406  C   ALA A 183      -0.988  34.279  31.630  1.00 15.71           C  
ATOM   1407  O   ALA A 183       0.166  33.818  31.630  1.00 15.13           O  
ATOM   1408  CB  ALA A 183      -1.224  35.479  33.741  1.00 12.62           C  
ATOM   1409  N   VAL A 184      -1.978  33.612  31.105  1.00 15.43           N  
ATOM   1410  CA  VAL A 184      -1.843  32.288  30.520  1.00 16.00           C  
ATOM   1411  C   VAL A 184      -0.916  32.358  29.276  1.00 14.43           C  
ATOM   1412  O   VAL A 184      -0.279  31.337  29.086  1.00 14.68           O  
ATOM   1413  CB  VAL A 184      -3.165  31.568  30.124  1.00 15.18           C  
ATOM   1414  CG1 VAL A 184      -4.181  31.612  31.295  1.00 17.30           C  
ATOM   1415  CG2 VAL A 184      -3.783  32.245  28.906  1.00 16.05           C  
ATOM   1416  N   ASP A 185      -0.859  33.427  28.502  1.00 15.20           N  
ATOM   1417  CA  ASP A 185       0.007  33.511  27.322  1.00 15.66           C  
ATOM   1418  C   ASP A 185       1.447  33.717  27.786  1.00 16.83           C  
ATOM   1419  O   ASP A 185       2.356  33.249  27.151  1.00 14.85           O  
ATOM   1420  CB  ASP A 185      -0.342  34.763  26.411  1.00 16.80           C  
ATOM   1421  CG  ASP A 185      -1.661  34.481  25.670  1.00 17.11           C  
ATOM   1422  OD1 ASP A 185      -2.148  33.296  25.597  1.00 16.51           O  
ATOM   1423  OD2 ASP A 185      -2.242  35.486  25.246  1.00 16.69           O  
ATOM   1424  N   ILE A 186       1.629  34.396  28.958  1.00 16.69           N  
ATOM   1425  CA  ILE A 186       2.985  34.571  29.445  1.00 17.50           C  
ATOM   1426  C   ILE A 186       3.580  33.223  29.941  1.00 17.23           C  
ATOM   1427  O   ILE A 186       4.768  32.962  29.717  1.00 12.83           O  
ATOM   1428  CB  ILE A 186       3.023  35.568  30.609  1.00 15.51           C  
ATOM   1429  CG1 ILE A 186       2.606  36.918  30.117  1.00 13.98           C  
ATOM   1430  CG2 ILE A 186       4.405  35.495  31.293  1.00 10.97           C  
ATOM   1431  CD1 ILE A 186       3.729  37.671  29.292  1.00 21.45           C  
ATOM   1432  N   TRP A 187       2.767  32.338  30.463  1.00 15.44           N  
ATOM   1433  CA  TRP A 187       3.144  30.990  30.917  1.00 15.49           C  
ATOM   1434  C   TRP A 187       3.616  30.202  29.706  1.00 14.35           C  
ATOM   1435  O   TRP A 187       4.733  29.675  29.645  1.00 14.41           O  
ATOM   1436  CB  TRP A 187       1.930  30.230  31.587  1.00 15.16           C  
ATOM   1437  CG  TRP A 187       2.366  28.792  31.861  1.00 16.68           C  
ATOM   1438  CD1 TRP A 187       2.373  27.691  31.062  1.00  9.84           C  
ATOM   1439  CD2 TRP A 187       2.864  28.376  33.135  1.00 14.80           C  
ATOM   1440  NE1 TRP A 187       2.906  26.612  31.733  1.00 13.90           N  
ATOM   1441  CE2 TRP A 187       3.219  27.015  33.007  1.00 15.48           C  
ATOM   1442  CE3 TRP A 187       3.070  29.037  34.356  1.00 17.03           C  
ATOM   1443  CZ2 TRP A 187       3.750  26.274  34.079  1.00 14.28           C  
ATOM   1444  CZ3 TRP A 187       3.576  28.308  35.410  1.00 16.37           C  
ATOM   1445  CH2 TRP A 187       3.928  26.940  35.221  1.00 13.38           C  
ATOM   1446  N   SER A 188       2.743  30.168  28.677  1.00 15.97           N  
ATOM   1447  CA  SER A 188       3.081  29.453  27.407  1.00 13.64           C  
ATOM   1448  C   SER A 188       4.364  29.960  26.752  1.00 13.76           C  
ATOM   1449  O   SER A 188       5.196  29.128  26.337  1.00 12.81           O  
ATOM   1450  CB  SER A 188       1.956  29.647  26.356  1.00 16.88           C  
ATOM   1451  OG  SER A 188       0.666  29.170  26.909  1.00 14.99           O  
ATOM   1452  N   LEU A 189       4.557  31.269  26.592  1.00 13.86           N  
ATOM   1453  CA  LEU A 189       5.786  31.750  25.946  1.00 17.09           C  
ATOM   1454  C   LEU A 189       7.022  31.425  26.814  1.00 19.39           C  
ATOM   1455  O   LEU A 189       8.130  31.191  26.290  1.00 17.83           O  
ATOM   1456  CB  LEU A 189       5.625  33.267  25.717  1.00 16.41           C  
ATOM   1457  CG  LEU A 189       6.840  33.900  25.008  1.00 17.55           C  
ATOM   1458  CD1 LEU A 189       6.974  33.536  23.549  1.00 16.64           C  
ATOM   1459  CD2 LEU A 189       6.704  35.432  25.149  1.00 21.50           C  
ATOM   1460  N   GLY A 190       6.874  31.385  28.163  1.00 16.58           N  
ATOM   1461  CA  GLY A 190       7.938  30.957  29.048  1.00 14.00           C  
ATOM   1462  C   GLY A 190       8.370  29.521  28.754  1.00 17.45           C  
ATOM   1463  O   GLY A 190       9.570  29.174  28.719  1.00 14.56           O  
ATOM   1464  N   CYS A 191       7.410  28.612  28.555  1.00 15.46           N  
ATOM   1465  CA  CYS A 191       7.652  27.229  28.222  1.00 15.11           C  
ATOM   1466  C   CYS A 191       8.313  27.188  26.818  1.00 19.50           C  
ATOM   1467  O   CYS A 191       9.231  26.322  26.628  1.00 18.51           O  
ATOM   1468  CB  CYS A 191       6.355  26.375  28.104  1.00 12.18           C  
ATOM   1469  SG  CYS A 191       5.448  26.153  29.692  1.00 16.57           S  
ATOM   1470  N   ILE A 192       7.898  28.090  25.914  1.00 14.47           N  
ATOM   1471  CA  ILE A 192       8.570  28.006  24.559  1.00 16.29           C  
ATOM   1472  C   ILE A 192      10.022  28.463  24.683  1.00 14.30           C  
ATOM   1473  O   ILE A 192      10.848  27.967  23.972  1.00 14.04           O  
ATOM   1474  CB  ILE A 192       7.793  28.936  23.588  1.00 16.30           C  
ATOM   1475  CG1 ILE A 192       6.430  28.278  23.331  1.00 17.18           C  
ATOM   1476  CG2 ILE A 192       8.541  29.342  22.259  1.00 13.46           C  
ATOM   1477  CD1 ILE A 192       5.307  28.765  22.536  1.00 17.63           C  
ATOM   1478  N   PHE A 193      10.267  29.562  25.465  1.00 12.92           N  
ATOM   1479  CA  PHE A 193      11.540  30.174  25.696  1.00 16.26           C  
ATOM   1480  C   PHE A 193      12.488  29.117  26.228  1.00 15.36           C  
ATOM   1481  O   PHE A 193      13.602  29.006  25.656  1.00 15.95           O  
ATOM   1482  CB  PHE A 193      11.434  31.394  26.636  1.00 19.29           C  
ATOM   1483  CG  PHE A 193      12.657  32.016  27.222  1.00 18.68           C  
ATOM   1484  CD1 PHE A 193      13.829  32.020  26.452  1.00 18.64           C  
ATOM   1485  CD2 PHE A 193      12.633  32.661  28.459  1.00 17.07           C  
ATOM   1486  CE1 PHE A 193      14.956  32.664  26.978  1.00 17.76           C  
ATOM   1487  CE2 PHE A 193      13.748  33.284  28.958  1.00 18.37           C  
ATOM   1488  CZ  PHE A 193      14.956  33.267  28.233  1.00 19.74           C  
ATOM   1489  N   ALA A 194      12.122  28.469  27.339  1.00 16.95           N  
ATOM   1490  CA  ALA A 194      12.853  27.341  27.887  1.00 15.22           C  
ATOM   1491  C   ALA A 194      13.195  26.314  26.759  1.00 18.50           C  
ATOM   1492  O   ALA A 194      14.251  25.649  26.703  1.00 18.01           O  
ATOM   1493  CB  ALA A 194      11.932  26.529  28.828  1.00 16.61           C  
ATOM   1494  N   GLU A 195      12.231  25.908  25.968  1.00 17.41           N  
ATOM   1495  CA  GLU A 195      12.425  24.865  24.883  1.00 18.31           C  
ATOM   1496  C   GLU A 195      13.391  25.346  23.815  1.00 18.45           C  
ATOM   1497  O   GLU A 195      14.155  24.544  23.311  1.00 16.92           O  
ATOM   1498  CB  GLU A 195      11.075  24.504  24.315  1.00 17.37           C  
ATOM   1499  CG  GLU A 195      11.089  23.398  23.255  1.00 21.92           C  
ATOM   1500  CD  GLU A 195       9.730  22.997  22.755  1.00 22.27           C  
ATOM   1501  OE1 GLU A 195       8.632  23.235  23.319  1.00 20.92           O  
ATOM   1502  OE2 GLU A 195       9.705  22.439  21.637  1.00 23.56           O  
ATOM   1503  N   MET A 196      13.415  26.643  23.427  1.00 16.57           N  
ATOM   1504  CA  MET A 196      14.373  27.151  22.456  1.00 15.51           C  
ATOM   1505  C   MET A 196      15.775  27.006  22.997  1.00 19.35           C  
ATOM   1506  O   MET A 196      16.805  26.679  22.430  1.00 19.65           O  
ATOM   1507  CB  MET A 196      14.052  28.627  22.264  1.00 17.99           C  
ATOM   1508  CG  MET A 196      12.826  28.969  21.365  1.00 19.47           C  
ATOM   1509  SD  MET A 196      12.930  30.593  20.593  1.00 24.97           S  
ATOM   1510  CE  MET A 196      12.183  31.578  21.943  1.00 23.89           C  
ATOM   1511  N   VAL A 197      15.952  27.226  24.303  1.00 17.45           N  
ATOM   1512  CA  VAL A 197      17.219  27.210  24.962  1.00 15.85           C  
ATOM   1513  C   VAL A 197      17.734  25.782  25.037  1.00 18.22           C  
ATOM   1514  O   VAL A 197      18.879  25.594  24.706  1.00 19.19           O  
ATOM   1515  CB  VAL A 197      17.166  27.777  26.367  1.00 21.17           C  
ATOM   1516  CG1 VAL A 197      18.493  27.464  27.085  1.00 20.24           C  
ATOM   1517  CG2 VAL A 197      16.816  29.284  26.428  1.00 20.42           C  
ATOM   1518  N   THR A 198      16.995  24.794  25.462  1.00 15.79           N  
ATOM   1519  CA  THR A 198      17.446  23.468  25.718  1.00 17.37           C  
ATOM   1520  C   THR A 198      17.271  22.532  24.584  1.00 18.02           C  
ATOM   1521  O   THR A 198      17.836  21.477  24.687  1.00 19.85           O  
ATOM   1522  CB  THR A 198      16.663  22.714  26.898  1.00 18.52           C  
ATOM   1523  OG1 THR A 198      15.334  22.494  26.468  1.00 17.18           O  
ATOM   1524  CG2 THR A 198      16.807  23.516  28.178  1.00 20.13           C  
ATOM   1525  N   ARG A 199      16.370  22.856  23.623  1.00 19.86           N  
ATOM   1526  CA  ARG A 199      16.169  22.020  22.482  1.00 22.24           C  
ATOM   1527  C   ARG A 199      15.315  20.839  22.918  1.00 24.99           C  
ATOM   1528  O   ARG A 199      15.242  19.830  22.170  1.00 25.69           O  
ATOM   1529  CB  ARG A 199      17.371  21.505  21.651  1.00 26.75           C  
ATOM   1530  CG  ARG A 199      18.295  22.657  21.192  1.00 29.08           C  
ATOM   1531  CD  ARG A 199      19.559  22.032  20.534  1.00 31.54           C  
ATOM   1532  NE  ARG A 199      20.742  22.608  21.151  1.00 31.16           N  
ATOM   1533  CZ  ARG A 199      21.965  22.161  20.848  1.00 33.85           C  
ATOM   1534  NH1 ARG A 199      22.186  21.163  20.018  1.00 30.52           N  
ATOM   1535  NH2 ARG A 199      22.913  22.823  21.527  1.00 37.23           N  
ATOM   1536  N   ARG A 200      14.513  21.094  23.967  1.00 23.22           N  
ATOM   1537  CA  ARG A 200      13.614  19.972  24.300  1.00 24.61           C  
ATOM   1538  C   ARG A 200      12.487  20.590  25.149  1.00 20.70           C  
ATOM   1539  O   ARG A 200      12.697  21.578  25.810  1.00 16.65           O  
ATOM   1540  CB  ARG A 200      14.268  18.772  24.817  1.00 29.79           C  
ATOM   1541  CG  ARG A 200      14.591  18.173  26.135  1.00 35.18           C  
ATOM   1542  CD  ARG A 200      14.387  16.695  25.822  1.00 44.04           C  
ATOM   1543  NE  ARG A 200      15.263  15.575  26.035  1.00 50.28           N  
ATOM   1544  CZ  ARG A 200      15.004  14.673  27.023  1.00 53.54           C  
ATOM   1545  NH1 ARG A 200      13.949  14.833  27.814  1.00 54.30           N  
ATOM   1546  NH2 ARG A 200      15.751  13.624  27.319  1.00 52.46           N  
ATOM   1547  N   ALA A 201      11.327  20.065  24.803  1.00 18.70           N  
ATOM   1548  CA  ALA A 201      10.113  20.571  25.498  1.00 19.28           C  
ATOM   1549  C   ALA A 201      10.283  20.542  27.003  1.00 19.49           C  
ATOM   1550  O   ALA A 201      10.826  19.601  27.648  1.00 20.85           O  
ATOM   1551  CB  ALA A 201       8.862  19.820  25.013  1.00 20.59           C  
ATOM   1552  N   LEU A 202       9.761  21.575  27.622  1.00 17.53           N  
ATOM   1553  CA  LEU A 202       9.904  21.597  29.094  1.00 17.83           C  
ATOM   1554  C   LEU A 202       8.946  20.602  29.733  1.00 20.61           C  
ATOM   1555  O   LEU A 202       9.381  19.926  30.713  1.00 17.65           O  
ATOM   1556  CB  LEU A 202       9.564  22.975  29.592  1.00 18.37           C  
ATOM   1557  CG  LEU A 202       9.704  23.265  31.117  1.00 22.95           C  
ATOM   1558  CD1 LEU A 202      11.144  22.982  31.615  1.00 20.85           C  
ATOM   1559  CD2 LEU A 202       9.363  24.752  31.361  1.00 20.46           C  
ATOM   1560  N   PHE A 203       7.639  20.696  29.367  1.00 16.27           N  
ATOM   1561  CA  PHE A 203       6.656  19.827  30.020  1.00 21.03           C  
ATOM   1562  C   PHE A 203       5.783  19.091  28.974  1.00 20.35           C  
ATOM   1563  O   PHE A 203       4.688  19.500  28.627  1.00 20.56           O  
ATOM   1564  CB  PHE A 203       5.803  20.737  30.916  1.00 19.76           C  
ATOM   1565  CG  PHE A 203       6.419  21.645  31.953  1.00 20.78           C  
ATOM   1566  CD1 PHE A 203       7.303  21.117  32.934  1.00 16.61           C  
ATOM   1567  CD2 PHE A 203       6.064  22.990  32.007  1.00 18.70           C  
ATOM   1568  CE1 PHE A 203       7.814  21.960  33.904  1.00 14.86           C  
ATOM   1569  CE2 PHE A 203       6.575  23.784  33.048  1.00 15.38           C  
ATOM   1570  CZ  PHE A 203       7.488  23.283  33.981  1.00 12.92           C  
ATOM   1571  N   PRO A 204       6.311  17.998  28.439  1.00 19.38           N  
ATOM   1572  CA  PRO A 204       5.690  17.186  27.473  1.00 20.00           C  
ATOM   1573  C   PRO A 204       4.574  16.303  28.001  1.00 22.01           C  
ATOM   1574  O   PRO A 204       4.588  15.075  27.787  1.00 24.00           O  
ATOM   1575  CB  PRO A 204       6.840  16.317  26.874  1.00 19.10           C  
ATOM   1576  CG  PRO A 204       7.917  16.337  27.885  1.00 19.35           C  
ATOM   1577  CD  PRO A 204       7.695  17.504  28.788  1.00 18.17           C  
ATOM   1578  N   GLY A 205       3.472  16.817  28.596  1.00 22.64           N  
ATOM   1579  CA  GLY A 205       2.552  15.799  29.098  1.00 25.65           C  
ATOM   1580  C   GLY A 205       1.827  15.023  27.995  1.00 29.44           C  
ATOM   1581  O   GLY A 205       1.539  15.555  26.902  1.00 29.31           O  
ATOM   1582  N   ASP A 206       1.367  13.808  28.295  1.00 30.57           N  
ATOM   1583  CA  ASP A 206       0.487  13.226  27.265  1.00 34.16           C  
ATOM   1584  C   ASP A 206      -0.926  13.105  27.793  1.00 34.13           C  
ATOM   1585  O   ASP A 206      -1.706  12.308  27.259  1.00 36.43           O  
ATOM   1586  CB  ASP A 206       1.003  11.894  26.727  1.00 38.56           C  
ATOM   1587  CG  ASP A 206       1.130  10.843  27.812  1.00 38.44           C  
ATOM   1588  OD1 ASP A 206       0.949  11.194  28.977  1.00 38.83           O  
ATOM   1589  OD2 ASP A 206       1.433   9.677  27.498  1.00 40.46           O  
ATOM   1590  N   SER A 207      -1.270  13.784  28.862  1.00 32.68           N  
ATOM   1591  CA  SER A 207      -2.608  13.879  29.420  1.00 31.13           C  
ATOM   1592  C   SER A 207      -2.621  15.034  30.456  1.00 29.99           C  
ATOM   1593  O   SER A 207      -1.581  15.683  30.615  1.00 27.04           O  
ATOM   1594  CB  SER A 207      -3.270  12.688  30.039  1.00 30.63           C  
ATOM   1595  OG  SER A 207      -2.492  12.318  31.154  1.00 34.94           O  
ATOM   1596  N   GLU A 208      -3.851  15.358  30.861  1.00 25.40           N  
ATOM   1597  CA  GLU A 208      -4.001  16.473  31.744  1.00 28.03           C  
ATOM   1598  C   GLU A 208      -3.387  16.193  33.111  1.00 24.29           C  
ATOM   1599  O   GLU A 208      -2.819  17.180  33.598  1.00 27.93           O  
ATOM   1600  CB  GLU A 208      -5.490  16.905  31.933  1.00 28.18           C  
ATOM   1601  CG  GLU A 208      -6.053  17.356  30.585  1.00 32.20           C  
ATOM   1602  CD  GLU A 208      -7.245  18.267  30.729  1.00 33.40           C  
ATOM   1603  OE1 GLU A 208      -7.466  18.847  31.800  1.00 35.39           O  
ATOM   1604  OE2 GLU A 208      -7.982  18.482  29.765  1.00 37.10           O  
ATOM   1605  N   ILE A 209      -3.430  14.967  33.620  1.00 21.05           N  
ATOM   1606  CA  ILE A 209      -2.864  14.747  34.945  1.00 18.83           C  
ATOM   1607  C   ILE A 209      -1.377  14.640  34.764  1.00 20.08           C  
ATOM   1608  O   ILE A 209      -0.723  15.236  35.589  1.00 18.30           O  
ATOM   1609  CB  ILE A 209      -3.476  13.551  35.717  1.00 18.76           C  
ATOM   1610  CG1 ILE A 209      -3.198  13.628  37.215  1.00 18.65           C  
ATOM   1611  CG2 ILE A 209      -2.982  12.244  35.113  1.00 21.00           C  
ATOM   1612  CD1 ILE A 209      -3.820  14.901  37.900  1.00 18.03           C  
ATOM   1613  N   ASP A 210      -0.887  14.000  33.712  1.00 19.69           N  
ATOM   1614  CA  ASP A 210       0.541  13.923  33.456  1.00 21.53           C  
ATOM   1615  C   ASP A 210       1.091  15.332  33.237  1.00 20.81           C  
ATOM   1616  O   ASP A 210       2.246  15.544  33.563  1.00 21.96           O  
ATOM   1617  CB  ASP A 210       0.823  12.979  32.283  1.00 22.48           C  
ATOM   1618  CG  ASP A 210       2.313  12.844  31.917  1.00 26.33           C  
ATOM   1619  OD1 ASP A 210       2.985  12.272  32.781  1.00 24.56           O  
ATOM   1620  OD2 ASP A 210       2.719  13.401  30.872  1.00 23.90           O  
ATOM   1621  N   GLN A 211       0.282  16.203  32.568  1.00 18.54           N  
ATOM   1622  CA  GLN A 211       0.800  17.542  32.292  1.00 19.38           C  
ATOM   1623  C   GLN A 211       1.078  18.270  33.615  1.00 19.05           C  
ATOM   1624  O   GLN A 211       2.103  18.861  33.894  1.00 18.93           O  
ATOM   1625  CB  GLN A 211      -0.209  18.320  31.466  1.00 16.78           C  
ATOM   1626  CG  GLN A 211       0.364  19.654  31.033  1.00 16.85           C  
ATOM   1627  CD  GLN A 211       1.578  19.604  30.142  1.00 21.04           C  
ATOM   1628  OE1 GLN A 211       1.751  18.695  29.291  1.00 21.61           O  
ATOM   1629  NE2 GLN A 211       2.410  20.660  30.396  1.00 18.27           N  
ATOM   1630  N   LEU A 212       0.088  18.298  34.485  1.00 18.56           N  
ATOM   1631  CA  LEU A 212       0.107  18.850  35.797  1.00 20.53           C  
ATOM   1632  C   LEU A 212       1.257  18.311  36.653  1.00 20.13           C  
ATOM   1633  O   LEU A 212       1.873  19.103  37.370  1.00 17.57           O  
ATOM   1634  CB  LEU A 212      -1.190  18.474  36.551  1.00 19.23           C  
ATOM   1635  CG  LEU A 212      -2.041  19.571  37.155  1.00 24.66           C  
ATOM   1636  CD1 LEU A 212      -1.767  21.025  36.794  1.00 24.21           C  
ATOM   1637  CD2 LEU A 212      -3.493  19.234  36.888  1.00 27.15           C  
ATOM   1638  N   PHE A 213       1.374  16.979  36.567  1.00 19.19           N  
ATOM   1639  CA  PHE A 213       2.314  16.313  37.472  1.00 21.19           C  
ATOM   1640  C   PHE A 213       3.745  16.559  36.955  1.00 19.95           C  
ATOM   1641  O   PHE A 213       4.604  16.740  37.785  1.00 17.77           O  
ATOM   1642  CB  PHE A 213       1.926  14.852  37.678  1.00 24.53           C  
ATOM   1643  CG  PHE A 213       0.790  14.579  38.659  1.00 27.99           C  
ATOM   1644  CD1 PHE A 213       0.091  15.566  39.292  1.00 26.36           C  
ATOM   1645  CD2 PHE A 213       0.451  13.252  38.952  1.00 30.38           C  
ATOM   1646  CE1 PHE A 213      -0.918  15.253  40.228  1.00 29.87           C  
ATOM   1647  CE2 PHE A 213      -0.555  12.913  39.850  1.00 29.12           C  
ATOM   1648  CZ  PHE A 213      -1.257  13.948  40.491  1.00 28.06           C  
ATOM   1649  N   ARG A 214       3.950  16.751  35.666  1.00 18.67           N  
ATOM   1650  CA  ARG A 214       5.252  17.215  35.159  1.00 18.09           C  
ATOM   1651  C   ARG A 214       5.575  18.637  35.577  1.00 17.95           C  
ATOM   1652  O   ARG A 214       6.701  18.823  36.045  1.00 18.72           O  
ATOM   1653  CB  ARG A 214       5.246  17.148  33.616  1.00 19.18           C  
ATOM   1654  CG  ARG A 214       5.483  15.695  33.077  1.00 16.53           C  
ATOM   1655  CD  ARG A 214       5.345  15.814  31.505  1.00 23.67           C  
ATOM   1656  NE  ARG A 214       5.410  14.425  30.974  1.00 24.09           N  
ATOM   1657  CZ  ARG A 214       6.628  13.943  30.727  1.00 29.55           C  
ATOM   1658  NH1 ARG A 214       7.695  14.723  30.983  1.00 29.27           N  
ATOM   1659  NH2 ARG A 214       6.788  12.725  30.226  1.00 28.41           N  
ATOM   1660  N   ILE A 215       4.609  19.540  35.668  1.00 18.52           N  
ATOM   1661  CA  ILE A 215       4.832  20.910  36.182  1.00 19.41           C  
ATOM   1662  C   ILE A 215       5.143  20.822  37.682  1.00 22.64           C  
ATOM   1663  O   ILE A 215       6.120  21.489  38.184  1.00 17.94           O  
ATOM   1664  CB  ILE A 215       3.547  21.792  35.957  1.00 16.06           C  
ATOM   1665  CG1 ILE A 215       3.123  21.891  34.480  1.00 16.51           C  
ATOM   1666  CG2 ILE A 215       3.508  23.086  36.659  1.00 11.19           C  
ATOM   1667  CD1 ILE A 215       1.809  22.708  34.306  1.00 11.08           C  
ATOM   1668  N   PHE A 216       4.359  19.933  38.357  1.00 22.51           N  
ATOM   1669  CA  PHE A 216       4.619  19.853  39.834  1.00 24.86           C  
ATOM   1670  C   PHE A 216       6.032  19.328  40.190  1.00 23.46           C  
ATOM   1671  O   PHE A 216       6.620  19.767  41.171  1.00 23.47           O  
ATOM   1672  CB  PHE A 216       3.571  19.048  40.630  1.00 23.11           C  
ATOM   1673  CG  PHE A 216       2.115  19.540  40.509  1.00 24.06           C  
ATOM   1674  CD1 PHE A 216       1.760  20.756  39.997  1.00 21.91           C  
ATOM   1675  CD2 PHE A 216       1.095  18.772  41.055  1.00 21.15           C  
ATOM   1676  CE1 PHE A 216       0.441  21.200  39.933  1.00 24.34           C  
ATOM   1677  CE2 PHE A 216      -0.234  19.165  41.024  1.00 22.08           C  
ATOM   1678  CZ  PHE A 216      -0.550  20.370  40.424  1.00 24.61           C  
ATOM   1679  N   ARG A 217       6.537  18.328  39.498  1.00 22.75           N  
ATOM   1680  CA  ARG A 217       7.841  17.789  39.758  1.00 26.28           C  
ATOM   1681  C   ARG A 217       8.982  18.748  39.449  1.00 25.84           C  
ATOM   1682  O   ARG A 217      10.097  18.515  39.950  1.00 29.02           O  
ATOM   1683  CB  ARG A 217       8.043  16.536  38.900  1.00 30.37           C  
ATOM   1684  CG  ARG A 217       7.321  15.323  39.439  1.00 37.17           C  
ATOM   1685  CD  ARG A 217       7.632  14.119  38.540  1.00 44.48           C  
ATOM   1686  NE  ARG A 217       6.606  13.739  37.610  1.00 47.28           N  
ATOM   1687  CZ  ARG A 217       6.564  13.405  36.324  1.00 50.25           C  
ATOM   1688  NH1 ARG A 217       7.675  13.355  35.583  1.00 49.68           N  
ATOM   1689  NH2 ARG A 217       5.368  13.105  35.767  1.00 48.99           N  
ATOM   1690  N   THR A 218       8.863  19.746  38.573  1.00 24.13           N  
ATOM   1691  CA  THR A 218       9.956  20.728  38.382  1.00 24.41           C  
ATOM   1692  C   THR A 218       9.799  21.925  39.300  1.00 23.45           C  
ATOM   1693  O   THR A 218      10.749  22.517  39.864  1.00 27.86           O  
ATOM   1694  CB  THR A 218       9.895  21.264  36.895  1.00 23.97           C  
ATOM   1695  OG1 THR A 218       9.882  20.111  36.067  1.00 23.23           O  
ATOM   1696  CG2 THR A 218      10.949  22.121  36.377  1.00 23.08           C  
ATOM   1697  N   LEU A 219       8.625  22.489  39.427  1.00 19.99           N  
ATOM   1698  CA  LEU A 219       8.359  23.744  40.099  1.00 20.65           C  
ATOM   1699  C   LEU A 219       7.767  23.514  41.520  1.00 20.17           C  
ATOM   1700  O   LEU A 219       7.657  24.477  42.207  1.00 15.66           O  
ATOM   1701  CB  LEU A 219       7.352  24.620  39.323  1.00 20.43           C  
ATOM   1702  CG  LEU A 219       7.757  24.971  37.857  1.00 24.11           C  
ATOM   1703  CD1 LEU A 219       6.684  25.817  37.197  1.00 23.81           C  
ATOM   1704  CD2 LEU A 219       9.062  25.782  37.865  1.00 21.23           C  
ATOM   1705  N   GLY A 220       7.472  22.324  41.924  1.00 21.40           N  
ATOM   1706  CA  GLY A 220       6.955  21.958  43.216  1.00 21.85           C  
ATOM   1707  C   GLY A 220       5.419  21.980  43.170  1.00 24.24           C  
ATOM   1708  O   GLY A 220       4.819  22.703  42.332  1.00 19.24           O  
ATOM   1709  N   THR A 221       4.854  21.075  43.967  1.00 22.56           N  
ATOM   1710  CA  THR A 221       3.348  21.178  44.057  1.00 20.29           C  
ATOM   1711  C   THR A 221       2.999  22.500  44.641  1.00 19.90           C  
ATOM   1712  O   THR A 221       3.365  22.859  45.769  1.00 20.54           O  
ATOM   1713  CB  THR A 221       2.805  20.012  44.893  1.00 22.00           C  
ATOM   1714  OG1 THR A 221       3.430  18.866  44.311  1.00 19.14           O  
ATOM   1715  CG2 THR A 221       1.274  19.878  44.808  1.00 23.43           C  
ATOM   1716  N   PRO A 222       2.059  23.251  44.030  1.00 22.02           N  
ATOM   1717  CA  PRO A 222       1.672  24.564  44.554  1.00 19.93           C  
ATOM   1718  C   PRO A 222       0.784  24.423  45.794  1.00 23.46           C  
ATOM   1719  O   PRO A 222       0.150  23.366  45.989  1.00 23.18           O  
ATOM   1720  CB  PRO A 222       0.954  25.200  43.337  1.00 21.68           C  
ATOM   1721  CG  PRO A 222       0.257  24.005  42.720  1.00 20.25           C  
ATOM   1722  CD  PRO A 222       1.417  22.962  42.726  1.00 19.99           C  
ATOM   1723  N   ASP A 223       0.846  25.362  46.710  1.00 17.62           N  
ATOM   1724  CA  ASP A 223       0.023  25.284  47.893  1.00 19.78           C  
ATOM   1725  C   ASP A 223      -0.434  26.698  48.153  1.00 19.42           C  
ATOM   1726  O   ASP A 223      -0.166  27.647  47.381  1.00 15.80           O  
ATOM   1727  CB  ASP A 223       0.807  24.683  49.081  1.00 25.54           C  
ATOM   1728  CG  ASP A 223       2.008  25.572  49.338  1.00 28.24           C  
ATOM   1729  OD1 ASP A 223       2.202  26.777  48.972  1.00 30.79           O  
ATOM   1730  OD2 ASP A 223       2.929  24.949  49.863  1.00 34.29           O  
ATOM   1731  N   GLU A 224      -1.145  26.894  49.284  1.00 19.94           N  
ATOM   1732  CA  GLU A 224      -1.641  28.183  49.689  1.00 20.70           C  
ATOM   1733  C   GLU A 224      -0.541  29.189  49.979  1.00 21.24           C  
ATOM   1734  O   GLU A 224      -0.800  30.389  49.881  1.00 20.90           O  
ATOM   1735  CB  GLU A 224      -2.580  28.008  50.933  1.00 24.47           C  
ATOM   1736  CG  GLU A 224      -3.947  27.429  50.530  1.00 23.58           C  
ATOM   1737  CD  GLU A 224      -4.778  28.267  49.618  1.00 22.09           C  
ATOM   1738  OE1 GLU A 224      -4.721  29.515  49.556  1.00 22.71           O  
ATOM   1739  OE2 GLU A 224      -5.596  27.660  48.842  1.00 23.14           O  
ATOM   1740  N   VAL A 225       0.679  28.769  50.230  1.00 23.13           N  
ATOM   1741  CA  VAL A 225       1.790  29.693  50.422  1.00 26.73           C  
ATOM   1742  C   VAL A 225       2.139  30.327  49.058  1.00 27.38           C  
ATOM   1743  O   VAL A 225       2.101  31.564  48.917  1.00 27.48           O  
ATOM   1744  CB  VAL A 225       3.038  28.993  50.952  1.00 28.24           C  
ATOM   1745  CG1 VAL A 225       4.184  30.026  51.093  1.00 30.12           C  
ATOM   1746  CG2 VAL A 225       2.794  28.337  52.292  1.00 27.37           C  
ATOM   1747  N   VAL A 226       2.533  29.540  48.066  1.00 27.58           N  
ATOM   1748  CA  VAL A 226       2.927  30.183  46.786  1.00 27.15           C  
ATOM   1749  C   VAL A 226       1.785  30.746  45.946  1.00 25.62           C  
ATOM   1750  O   VAL A 226       1.953  31.702  45.165  1.00 24.29           O  
ATOM   1751  CB  VAL A 226       3.759  29.186  45.930  1.00 30.28           C  
ATOM   1752  CG1 VAL A 226       3.072  27.876  45.592  1.00 28.50           C  
ATOM   1753  CG2 VAL A 226       4.166  29.799  44.582  1.00 32.15           C  
ATOM   1754  N   TRP A 227       0.558  30.258  46.155  1.00 20.81           N  
ATOM   1755  CA  TRP A 227      -0.603  30.531  45.394  1.00 19.81           C  
ATOM   1756  C   TRP A 227      -1.912  30.499  46.221  1.00 21.48           C  
ATOM   1757  O   TRP A 227      -2.715  29.564  46.263  1.00 20.46           O  
ATOM   1758  CB  TRP A 227      -0.656  29.516  44.210  1.00 17.31           C  
ATOM   1759  CG  TRP A 227      -1.655  29.807  43.120  1.00 21.24           C  
ATOM   1760  CD1 TRP A 227      -2.540  30.864  43.096  1.00 19.64           C  
ATOM   1761  CD2 TRP A 227      -1.889  29.049  41.929  1.00 20.11           C  
ATOM   1762  NE1 TRP A 227      -3.327  30.790  41.928  1.00 24.43           N  
ATOM   1763  CE2 TRP A 227      -2.936  29.686  41.216  1.00 22.98           C  
ATOM   1764  CE3 TRP A 227      -1.371  27.882  41.410  1.00 19.63           C  
ATOM   1765  CZ2 TRP A 227      -3.428  29.231  40.001  1.00 22.29           C  
ATOM   1766  CZ3 TRP A 227      -1.838  27.440  40.200  1.00 21.63           C  
ATOM   1767  CH2 TRP A 227      -2.846  28.087  39.488  1.00 20.33           C  
ATOM   1768  N   PRO A 228      -2.243  31.675  46.764  1.00 23.65           N  
ATOM   1769  CA  PRO A 228      -3.479  31.864  47.508  1.00 24.02           C  
ATOM   1770  C   PRO A 228      -4.691  31.571  46.614  1.00 25.50           C  
ATOM   1771  O   PRO A 228      -4.862  32.214  45.588  1.00 24.44           O  
ATOM   1772  CB  PRO A 228      -3.460  33.327  47.902  1.00 24.94           C  
ATOM   1773  CG  PRO A 228      -1.971  33.648  47.959  1.00 26.57           C  
ATOM   1774  CD  PRO A 228      -1.401  32.929  46.755  1.00 22.73           C  
ATOM   1775  N   GLY A 229      -5.489  30.601  47.048  1.00 25.74           N  
ATOM   1776  CA  GLY A 229      -6.757  30.292  46.362  1.00 25.44           C  
ATOM   1777  C   GLY A 229      -6.556  29.021  45.577  1.00 23.88           C  
ATOM   1778  O   GLY A 229      -7.579  28.436  45.262  1.00 29.43           O  
ATOM   1779  N   VAL A 230      -5.343  28.494  45.428  1.00 20.95           N  
ATOM   1780  CA  VAL A 230      -5.147  27.281  44.617  1.00 20.48           C  
ATOM   1781  C   VAL A 230      -5.934  26.084  45.057  1.00 19.65           C  
ATOM   1782  O   VAL A 230      -6.568  25.312  44.306  1.00 17.08           O  
ATOM   1783  CB  VAL A 230      -3.635  26.937  44.519  1.00 22.84           C  
ATOM   1784  CG1 VAL A 230      -3.084  26.236  45.791  1.00 20.15           C  
ATOM   1785  CG2 VAL A 230      -3.296  26.075  43.328  1.00 23.16           C  
ATOM   1786  N   THR A 231      -5.945  25.774  46.339  1.00 23.07           N  
ATOM   1787  CA  THR A 231      -6.612  24.596  46.934  1.00 23.13           C  
ATOM   1788  C   THR A 231      -8.118  24.697  46.807  1.00 24.04           C  
ATOM   1789  O   THR A 231      -8.825  23.699  46.880  1.00 26.14           O  
ATOM   1790  CB  THR A 231      -6.203  24.250  48.402  1.00 24.12           C  
ATOM   1791  OG1 THR A 231      -6.787  25.197  49.311  1.00 20.33           O  
ATOM   1792  CG2 THR A 231      -4.691  24.088  48.529  1.00 23.35           C  
ATOM   1793  N   SER A 232      -8.719  25.777  46.292  1.00 25.28           N  
ATOM   1794  CA  SER A 232     -10.187  25.681  46.104  1.00 27.87           C  
ATOM   1795  C   SER A 232     -10.606  25.857  44.627  1.00 30.47           C  
ATOM   1796  O   SER A 232     -11.735  26.010  44.116  1.00 29.21           O  
ATOM   1797  CB  SER A 232     -10.679  26.591  47.222  1.00 28.42           C  
ATOM   1798  OG  SER A 232     -10.673  27.896  46.672  1.00 32.24           O  
ATOM   1799  N   MET A 233      -9.620  25.624  43.765  1.00 25.80           N  
ATOM   1800  CA  MET A 233      -9.805  25.501  42.319  1.00 28.61           C  
ATOM   1801  C   MET A 233     -10.539  24.193  42.077  1.00 25.55           C  
ATOM   1802  O   MET A 233     -10.321  23.138  42.714  1.00 21.63           O  
ATOM   1803  CB  MET A 233      -8.434  25.570  41.580  1.00 29.70           C  
ATOM   1804  CG  MET A 233      -8.420  27.114  41.313  1.00 34.06           C  
ATOM   1805  SD  MET A 233      -7.031  27.653  40.395  1.00 38.87           S  
ATOM   1806  CE  MET A 233      -7.351  29.374  40.071  1.00 35.65           C  
ATOM   1807  N   PRO A 234     -11.328  24.232  41.024  1.00 23.08           N  
ATOM   1808  CA  PRO A 234     -12.189  23.055  40.773  1.00 24.67           C  
ATOM   1809  C   PRO A 234     -11.543  21.720  40.593  1.00 26.23           C  
ATOM   1810  O   PRO A 234     -12.171  20.757  41.043  1.00 29.09           O  
ATOM   1811  CB  PRO A 234     -12.910  23.480  39.499  1.00 22.80           C  
ATOM   1812  CG  PRO A 234     -13.008  24.942  39.593  1.00 23.71           C  
ATOM   1813  CD  PRO A 234     -11.622  25.338  40.136  1.00 22.51           C  
ATOM   1814  N   ASP A 235     -10.367  21.536  39.983  1.00 23.90           N  
ATOM   1815  CA  ASP A 235      -9.797  20.219  39.710  1.00 22.25           C  
ATOM   1816  C   ASP A 235      -8.594  19.955  40.610  1.00 23.95           C  
ATOM   1817  O   ASP A 235      -7.828  18.990  40.474  1.00 22.49           O  
ATOM   1818  CB  ASP A 235      -9.389  20.163  38.233  1.00 23.08           C  
ATOM   1819  CG  ASP A 235     -10.577  20.231  37.280  1.00 28.89           C  
ATOM   1820  OD1 ASP A 235     -11.683  19.740  37.572  1.00 31.01           O  
ATOM   1821  OD2 ASP A 235     -10.446  20.833  36.219  1.00 29.93           O  
ATOM   1822  N   TYR A 236      -8.509  20.848  41.636  1.00 22.38           N  
ATOM   1823  CA  TYR A 236      -7.448  20.651  42.642  1.00 21.53           C  
ATOM   1824  C   TYR A 236      -7.839  19.449  43.522  1.00 23.61           C  
ATOM   1825  O   TYR A 236      -9.029  19.379  43.904  1.00 21.90           O  
ATOM   1826  CB  TYR A 236      -7.381  21.928  43.498  1.00 21.05           C  
ATOM   1827  CG  TYR A 236      -6.250  21.709  44.506  1.00 27.62           C  
ATOM   1828  CD1 TYR A 236      -4.905  21.925  44.291  1.00 27.64           C  
ATOM   1829  CD2 TYR A 236      -6.639  21.172  45.732  1.00 31.49           C  
ATOM   1830  CE1 TYR A 236      -3.987  21.665  45.273  1.00 29.18           C  
ATOM   1831  CE2 TYR A 236      -5.734  20.871  46.711  1.00 31.78           C  
ATOM   1832  CZ  TYR A 236      -4.404  21.105  46.466  1.00 31.00           C  
ATOM   1833  OH  TYR A 236      -3.569  20.764  47.506  1.00 30.90           O  
ATOM   1834  N   LYS A 237      -6.927  18.591  43.896  1.00 23.83           N  
ATOM   1835  CA  LYS A 237      -7.241  17.415  44.726  1.00 26.14           C  
ATOM   1836  C   LYS A 237      -6.242  17.359  45.868  1.00 27.06           C  
ATOM   1837  O   LYS A 237      -5.063  17.387  45.542  1.00 28.47           O  
ATOM   1838  CB  LYS A 237      -7.081  16.116  43.978  1.00 27.98           C  
ATOM   1839  CG  LYS A 237      -7.853  15.912  42.696  1.00 29.91           C  
ATOM   1840  CD  LYS A 237      -9.355  15.998  42.936  1.00 32.00           C  
ATOM   1841  CE  LYS A 237     -10.000  16.210  41.565  1.00 32.60           C  
ATOM   1842  NZ  LYS A 237     -11.442  16.031  41.572  1.00 30.87           N  
ATOM   1843  N   PRO A 238      -6.653  17.325  47.131  1.00 28.31           N  
ATOM   1844  CA  PRO A 238      -5.816  17.182  48.298  1.00 26.02           C  
ATOM   1845  C   PRO A 238      -4.944  15.937  48.269  1.00 27.01           C  
ATOM   1846  O   PRO A 238      -3.805  16.007  48.820  1.00 24.52           O  
ATOM   1847  CB  PRO A 238      -6.765  17.220  49.455  1.00 28.55           C  
ATOM   1848  CG  PRO A 238      -7.996  17.883  48.944  1.00 27.64           C  
ATOM   1849  CD  PRO A 238      -8.082  17.317  47.529  1.00 29.32           C  
ATOM   1850  N   SER A 239      -5.346  14.918  47.452  1.00 22.27           N  
ATOM   1851  CA  SER A 239      -4.512  13.748  47.272  1.00 23.15           C  
ATOM   1852  C   SER A 239      -3.328  13.974  46.321  1.00 22.58           C  
ATOM   1853  O   SER A 239      -2.603  12.982  46.053  1.00 18.79           O  
ATOM   1854  CB  SER A 239      -5.408  12.575  46.785  1.00 21.95           C  
ATOM   1855  OG  SER A 239      -6.094  13.028  45.618  1.00 19.02           O  
ATOM   1856  N   PHE A 240      -3.171  15.193  45.767  1.00 22.19           N  
ATOM   1857  CA  PHE A 240      -2.022  15.353  44.824  1.00 25.95           C  
ATOM   1858  C   PHE A 240      -0.705  15.098  45.638  1.00 25.61           C  
ATOM   1859  O   PHE A 240      -0.593  15.510  46.779  1.00 25.50           O  
ATOM   1860  CB  PHE A 240      -1.894  16.750  44.239  1.00 21.60           C  
ATOM   1861  CG  PHE A 240      -2.812  17.256  43.175  1.00 22.12           C  
ATOM   1862  CD1 PHE A 240      -3.459  16.466  42.263  1.00 24.06           C  
ATOM   1863  CD2 PHE A 240      -3.085  18.627  43.161  1.00 23.94           C  
ATOM   1864  CE1 PHE A 240      -4.382  16.940  41.335  1.00 25.00           C  
ATOM   1865  CE2 PHE A 240      -3.970  19.180  42.213  1.00 24.26           C  
ATOM   1866  CZ  PHE A 240      -4.603  18.343  41.341  1.00 26.29           C  
ATOM   1867  N   PRO A 241       0.241  14.402  45.065  1.00 25.90           N  
ATOM   1868  CA  PRO A 241       1.548  14.179  45.687  1.00 28.84           C  
ATOM   1869  C   PRO A 241       2.238  15.524  45.874  1.00 31.11           C  
ATOM   1870  O   PRO A 241       2.030  16.532  45.184  1.00 30.32           O  
ATOM   1871  CB  PRO A 241       2.264  13.227  44.797  1.00 27.96           C  
ATOM   1872  CG  PRO A 241       1.169  12.579  43.999  1.00 29.94           C  
ATOM   1873  CD  PRO A 241       0.114  13.677  43.769  1.00 28.34           C  
ATOM   1874  N   LYS A 242       2.917  15.631  46.997  1.00 33.06           N  
ATOM   1875  CA  LYS A 242       3.690  16.784  47.383  1.00 36.44           C  
ATOM   1876  C   LYS A 242       5.157  16.652  46.968  1.00 36.25           C  
ATOM   1877  O   LYS A 242       5.891  15.961  47.657  1.00 35.36           O  
ATOM   1878  CB  LYS A 242       3.529  17.006  48.895  1.00 36.79           C  
ATOM   1879  CG  LYS A 242       2.089  17.488  49.144  1.00 41.43           C  
ATOM   1880  CD  LYS A 242       1.745  17.894  50.569  1.00 39.39           C  
ATOM   1881  CE  LYS A 242       0.690  16.920  51.042  1.00 41.69           C  
ATOM   1882  NZ  LYS A 242      -0.694  17.424  51.328  1.00 41.86           N  
ATOM   1883  N   TRP A 243       5.608  17.368  45.938  1.00 35.50           N  
ATOM   1884  CA  TRP A 243       6.960  17.312  45.430  1.00 33.74           C  
ATOM   1885  C   TRP A 243       7.642  18.662  45.628  1.00 34.51           C  
ATOM   1886  O   TRP A 243       7.040  19.720  45.480  1.00 29.99           O  
ATOM   1887  CB  TRP A 243       7.072  16.923  43.984  1.00 36.13           C  
ATOM   1888  CG  TRP A 243       6.664  15.641  43.384  1.00 41.97           C  
ATOM   1889  CD1 TRP A 243       7.396  14.473  43.399  1.00 45.04           C  
ATOM   1890  CD2 TRP A 243       5.484  15.315  42.610  1.00 42.99           C  
ATOM   1891  NE1 TRP A 243       6.706  13.463  42.759  1.00 45.21           N  
ATOM   1892  CE2 TRP A 243       5.540  13.964  42.262  1.00 43.39           C  
ATOM   1893  CE3 TRP A 243       4.346  16.037  42.264  1.00 42.63           C  
ATOM   1894  CZ2 TRP A 243       4.539  13.324  41.532  1.00 44.47           C  
ATOM   1895  CZ3 TRP A 243       3.346  15.423  41.540  1.00 41.88           C  
ATOM   1896  CH2 TRP A 243       3.450  14.082  41.178  1.00 43.33           C  
ATOM   1897  N   ALA A 244       8.950  18.633  45.960  1.00 35.54           N  
ATOM   1898  CA  ALA A 244       9.712  19.862  46.136  1.00 36.53           C  
ATOM   1899  C   ALA A 244      10.066  20.539  44.799  1.00 36.34           C  
ATOM   1900  O   ALA A 244      10.269  19.730  43.886  1.00 35.03           O  
ATOM   1901  CB  ALA A 244      11.112  19.530  46.719  1.00 39.43           C  
ATOM   1902  N   ARG A 245      10.270  21.847  44.790  1.00 30.75           N  
ATOM   1903  CA  ARG A 245      10.745  22.501  43.589  1.00 32.63           C  
ATOM   1904  C   ARG A 245      12.200  22.083  43.358  1.00 37.38           C  
ATOM   1905  O   ARG A 245      12.895  21.765  44.299  1.00 35.14           O  
ATOM   1906  CB  ARG A 245      10.614  23.981  43.771  1.00 30.77           C  
ATOM   1907  CG  ARG A 245      11.173  25.027  42.855  1.00 30.00           C  
ATOM   1908  CD  ARG A 245      10.632  26.445  43.298  1.00 28.38           C  
ATOM   1909  NE  ARG A 245      10.921  27.379  42.257  1.00 30.12           N  
ATOM   1910  CZ  ARG A 245      10.133  27.842  41.277  1.00 32.97           C  
ATOM   1911  NH1 ARG A 245       8.821  27.552  41.110  1.00 26.20           N  
ATOM   1912  NH2 ARG A 245      10.718  28.679  40.399  1.00 33.54           N  
ATOM   1913  N   GLN A 246      12.679  22.129  42.108  1.00 41.77           N  
ATOM   1914  CA  GLN A 246      13.990  21.918  41.574  1.00 42.70           C  
ATOM   1915  C   GLN A 246      14.566  23.291  41.190  1.00 44.95           C  
ATOM   1916  O   GLN A 246      13.727  24.168  41.014  1.00 43.47           O  
ATOM   1917  CB  GLN A 246      13.982  21.079  40.296  1.00 44.14           C  
ATOM   1918  CG  GLN A 246      13.146  19.826  40.387  1.00 48.61           C  
ATOM   1919  CD  GLN A 246      13.620  18.809  41.390  1.00 50.20           C  
ATOM   1920  OE1 GLN A 246      14.704  18.280  41.061  1.00 55.06           O  
ATOM   1921  NE2 GLN A 246      12.989  18.485  42.499  1.00 48.76           N  
ATOM   1922  N   ASP A 247      15.893  23.492  41.022  1.00 43.73           N  
ATOM   1923  CA  ASP A 247      16.394  24.815  40.733  1.00 42.53           C  
ATOM   1924  C   ASP A 247      16.356  25.141  39.266  1.00 39.48           C  
ATOM   1925  O   ASP A 247      16.758  24.237  38.550  1.00 41.75           O  
ATOM   1926  CB  ASP A 247      17.886  24.887  40.992  1.00 48.53           C  
ATOM   1927  CG  ASP A 247      18.442  24.632  42.353  1.00 51.77           C  
ATOM   1928  OD1 ASP A 247      18.002  25.300  43.319  1.00 53.33           O  
ATOM   1929  OD2 ASP A 247      19.354  23.766  42.368  1.00 54.12           O  
ATOM   1930  N   PHE A 248      16.183  26.317  38.767  1.00 38.10           N  
ATOM   1931  CA  PHE A 248      16.259  26.642  37.337  1.00 36.36           C  
ATOM   1932  C   PHE A 248      17.559  26.362  36.651  1.00 35.62           C  
ATOM   1933  O   PHE A 248      17.679  26.245  35.413  1.00 33.77           O  
ATOM   1934  CB  PHE A 248      16.004  28.203  37.199  1.00 37.62           C  
ATOM   1935  CG  PHE A 248      14.495  28.290  37.150  1.00 38.34           C  
ATOM   1936  CD1 PHE A 248      13.743  27.691  38.132  1.00 38.97           C  
ATOM   1937  CD2 PHE A 248      13.851  28.831  36.083  1.00 39.89           C  
ATOM   1938  CE1 PHE A 248      12.356  27.695  38.051  1.00 42.23           C  
ATOM   1939  CE2 PHE A 248      12.477  28.813  35.998  1.00 39.72           C  
ATOM   1940  CZ  PHE A 248      11.709  28.257  36.983  1.00 37.39           C  
ATOM   1941  N   SER A 249      18.623  26.347  37.511  1.00 32.36           N  
ATOM   1942  CA  SER A 249      19.960  26.099  36.938  1.00 33.24           C  
ATOM   1943  C   SER A 249      20.007  24.685  36.382  1.00 31.18           C  
ATOM   1944  O   SER A 249      20.674  24.454  35.379  1.00 32.25           O  
ATOM   1945  CB  SER A 249      21.039  26.451  38.018  1.00 33.48           C  
ATOM   1946  OG  SER A 249      20.792  25.509  39.102  1.00 30.05           O  
ATOM   1947  N   LYS A 250      19.227  23.757  36.910  1.00 30.27           N  
ATOM   1948  CA  LYS A 250      19.089  22.428  36.371  1.00 32.95           C  
ATOM   1949  C   LYS A 250      18.071  22.378  35.210  1.00 36.46           C  
ATOM   1950  O   LYS A 250      18.138  21.536  34.308  1.00 36.56           O  
ATOM   1951  CB  LYS A 250      18.568  21.567  37.516  1.00 35.67           C  
ATOM   1952  CG  LYS A 250      18.160  20.155  37.174  1.00 35.70           C  
ATOM   1953  CD  LYS A 250      19.200  19.250  37.804  1.00 38.34           C  
ATOM   1954  CE  LYS A 250      19.191  17.851  37.171  1.00 40.07           C  
ATOM   1955  NZ  LYS A 250      18.376  16.972  38.060  1.00 37.81           N  
ATOM   1956  N   VAL A 251      17.078  23.276  35.247  1.00 33.37           N  
ATOM   1957  CA  VAL A 251      16.001  23.289  34.271  1.00 33.14           C  
ATOM   1958  C   VAL A 251      16.367  23.755  32.866  1.00 31.46           C  
ATOM   1959  O   VAL A 251      16.011  23.208  31.808  1.00 30.55           O  
ATOM   1960  CB  VAL A 251      14.812  24.168  34.763  1.00 33.18           C  
ATOM   1961  CG1 VAL A 251      13.684  23.996  33.720  1.00 35.74           C  
ATOM   1962  CG2 VAL A 251      14.246  23.760  36.127  1.00 33.47           C  
ATOM   1963  N   VAL A 252      17.087  24.909  32.780  1.00 27.12           N  
ATOM   1964  CA  VAL A 252      17.440  25.433  31.467  1.00 29.44           C  
ATOM   1965  C   VAL A 252      18.922  25.790  31.437  1.00 31.36           C  
ATOM   1966  O   VAL A 252      19.211  26.961  31.184  1.00 35.68           O  
ATOM   1967  CB  VAL A 252      16.561  26.657  31.120  1.00 26.02           C  
ATOM   1968  CG1 VAL A 252      15.104  26.170  31.047  1.00 26.12           C  
ATOM   1969  CG2 VAL A 252      16.594  27.768  32.171  1.00 25.31           C  
ATOM   1970  N   PRO A 253      19.834  24.851  31.717  1.00 28.97           N  
ATOM   1971  CA  PRO A 253      21.185  25.076  32.099  1.00 30.26           C  
ATOM   1972  C   PRO A 253      22.051  26.149  31.527  1.00 36.09           C  
ATOM   1973  O   PRO A 253      22.701  26.981  32.215  1.00 40.01           O  
ATOM   1974  CB  PRO A 253      21.909  23.750  31.944  1.00 26.78           C  
ATOM   1975  CG  PRO A 253      20.868  22.731  31.954  1.00 25.60           C  
ATOM   1976  CD  PRO A 253      19.534  23.428  31.984  1.00 26.40           C  
ATOM   1977  N   PRO A 254      22.113  26.144  30.190  1.00 34.19           N  
ATOM   1978  CA  PRO A 254      23.039  27.123  29.640  1.00 35.05           C  
ATOM   1979  C   PRO A 254      22.582  28.508  30.024  1.00 33.64           C  
ATOM   1980  O   PRO A 254      23.447  29.329  30.271  1.00 32.65           O  
ATOM   1981  CB  PRO A 254      23.154  26.713  28.188  1.00 36.35           C  
ATOM   1982  CG  PRO A 254      21.861  25.991  27.930  1.00 38.29           C  
ATOM   1983  CD  PRO A 254      21.499  25.219  29.238  1.00 35.16           C  
ATOM   1984  N   LEU A 255      21.308  28.826  30.122  1.00 31.84           N  
ATOM   1985  CA  LEU A 255      20.828  30.203  30.296  1.00 30.50           C  
ATOM   1986  C   LEU A 255      21.536  30.943  31.416  1.00 27.90           C  
ATOM   1987  O   LEU A 255      21.636  30.466  32.523  1.00 25.11           O  
ATOM   1988  CB  LEU A 255      19.291  30.114  30.360  1.00 30.81           C  
ATOM   1989  CG  LEU A 255      18.354  31.288  30.297  1.00 31.51           C  
ATOM   1990  CD1 LEU A 255      18.663  32.099  29.010  1.00 35.73           C  
ATOM   1991  CD2 LEU A 255      16.889  30.894  30.410  1.00 27.26           C  
ATOM   1992  N   ASP A 256      21.961  32.180  31.196  1.00 25.60           N  
ATOM   1993  CA  ASP A 256      22.509  33.030  32.225  1.00 27.17           C  
ATOM   1994  C   ASP A 256      21.506  33.473  33.259  1.00 26.10           C  
ATOM   1995  O   ASP A 256      20.277  33.308  33.077  1.00 26.41           O  
ATOM   1996  CB  ASP A 256      23.274  34.159  31.526  1.00 28.04           C  
ATOM   1997  CG  ASP A 256      22.397  35.179  30.851  1.00 31.64           C  
ATOM   1998  OD1 ASP A 256      21.517  35.829  31.506  1.00 31.40           O  
ATOM   1999  OD2 ASP A 256      22.565  35.383  29.628  1.00 31.97           O  
ATOM   2000  N   GLU A 257      21.911  34.117  34.383  1.00 23.02           N  
ATOM   2001  CA  GLU A 257      20.996  34.505  35.452  1.00 21.65           C  
ATOM   2002  C   GLU A 257      19.967  35.538  35.145  1.00 19.82           C  
ATOM   2003  O   GLU A 257      18.887  35.539  35.752  1.00 15.37           O  
ATOM   2004  CB  GLU A 257      21.790  34.919  36.715  1.00 26.66           C  
ATOM   2005  CG  GLU A 257      21.110  35.126  38.009  1.00 27.57           C  
ATOM   2006  CD  GLU A 257      20.022  34.265  38.547  1.00 32.56           C  
ATOM   2007  OE1 GLU A 257      19.793  33.040  38.471  1.00 33.72           O  
ATOM   2008  OE2 GLU A 257      19.161  34.973  39.148  1.00 36.94           O  
ATOM   2009  N   ASP A 258      20.166  36.485  34.247  1.00 18.50           N  
ATOM   2010  CA  ASP A 258      19.151  37.424  33.810  1.00 20.52           C  
ATOM   2011  C   ASP A 258      18.018  36.554  33.147  1.00 20.92           C  
ATOM   2012  O   ASP A 258      16.824  36.698  33.313  1.00 18.28           O  
ATOM   2013  CB  ASP A 258      19.645  38.412  32.765  1.00 19.37           C  
ATOM   2014  CG  ASP A 258      20.385  39.616  33.337  1.00 27.88           C  
ATOM   2015  OD1 ASP A 258      20.113  40.019  34.487  1.00 26.74           O  
ATOM   2016  OD2 ASP A 258      21.227  40.292  32.660  1.00 26.65           O  
ATOM   2017  N   GLY A 259      18.389  35.737  32.164  1.00 17.97           N  
ATOM   2018  CA  GLY A 259      17.516  34.792  31.455  1.00 17.15           C  
ATOM   2019  C   GLY A 259      16.778  33.902  32.437  1.00 20.30           C  
ATOM   2020  O   GLY A 259      15.525  33.751  32.291  1.00 20.76           O  
ATOM   2021  N   ARG A 260      17.433  33.275  33.428  1.00 18.59           N  
ATOM   2022  CA  ARG A 260      16.667  32.379  34.329  1.00 21.23           C  
ATOM   2023  C   ARG A 260      15.695  33.168  35.196  1.00 22.31           C  
ATOM   2024  O   ARG A 260      14.612  32.726  35.493  1.00 21.30           O  
ATOM   2025  CB  ARG A 260      17.591  31.467  35.156  1.00 22.74           C  
ATOM   2026  CG  ARG A 260      18.653  30.782  34.247  1.00 27.74           C  
ATOM   2027  CD  ARG A 260      19.451  29.789  35.101  1.00 32.48           C  
ATOM   2028  NE  ARG A 260      20.139  30.502  36.207  1.00 36.97           N  
ATOM   2029  CZ  ARG A 260      21.419  30.314  36.520  1.00 40.20           C  
ATOM   2030  NH1 ARG A 260      22.164  29.423  35.887  1.00 39.02           N  
ATOM   2031  NH2 ARG A 260      21.943  31.009  37.543  1.00 42.62           N  
ATOM   2032  N   SER A 261      16.100  34.309  35.719  1.00 22.91           N  
ATOM   2033  CA  SER A 261      15.315  35.262  36.497  1.00 22.97           C  
ATOM   2034  C   SER A 261      14.082  35.732  35.669  1.00 21.57           C  
ATOM   2035  O   SER A 261      12.942  35.626  36.084  1.00 17.86           O  
ATOM   2036  CB  SER A 261      16.192  36.460  36.826  1.00 19.67           C  
ATOM   2037  OG  SER A 261      15.337  37.536  37.218  1.00 25.12           O  
ATOM   2038  N   LEU A 262      14.251  36.154  34.440  1.00 15.87           N  
ATOM   2039  CA  LEU A 262      13.050  36.441  33.646  1.00 18.21           C  
ATOM   2040  C   LEU A 262      12.181  35.189  33.507  1.00 16.51           C  
ATOM   2041  O   LEU A 262      10.956  35.209  33.693  1.00 16.45           O  
ATOM   2042  CB  LEU A 262      13.419  36.867  32.207  1.00 16.96           C  
ATOM   2043  CG  LEU A 262      12.234  37.080  31.280  1.00 20.08           C  
ATOM   2044  CD1 LEU A 262      11.199  37.976  31.974  1.00 14.27           C  
ATOM   2045  CD2 LEU A 262      12.780  37.727  29.975  1.00 15.93           C  
ATOM   2046  N   LEU A 263      12.716  34.020  33.200  1.00 20.10           N  
ATOM   2047  CA  LEU A 263      11.962  32.805  32.971  1.00 20.55           C  
ATOM   2048  C   LEU A 263      11.186  32.434  34.229  1.00 20.91           C  
ATOM   2049  O   LEU A 263       9.998  32.018  34.272  1.00 17.07           O  
ATOM   2050  CB  LEU A 263      12.838  31.600  32.504  1.00 16.95           C  
ATOM   2051  CG  LEU A 263      12.048  30.283  32.535  1.00 20.49           C  
ATOM   2052  CD1 LEU A 263      10.988  30.240  31.373  1.00 21.25           C  
ATOM   2053  CD2 LEU A 263      12.813  28.963  32.401  1.00 15.05           C  
ATOM   2054  N   SER A 264      11.881  32.564  35.400  1.00 20.59           N  
ATOM   2055  CA  SER A 264      11.138  32.127  36.599  1.00 20.34           C  
ATOM   2056  C   SER A 264       9.970  33.055  36.859  1.00 16.82           C  
ATOM   2057  O   SER A 264       8.995  32.602  37.401  1.00 16.29           O  
ATOM   2058  CB  SER A 264      11.918  31.975  37.953  1.00 21.60           C  
ATOM   2059  OG  SER A 264      12.094  33.319  38.341  1.00 23.26           O  
ATOM   2060  N   GLN A 265       9.983  34.356  36.590  1.00 16.73           N  
ATOM   2061  CA  GLN A 265       8.869  35.232  36.830  1.00 17.22           C  
ATOM   2062  C   GLN A 265       7.785  34.958  35.751  1.00 18.27           C  
ATOM   2063  O   GLN A 265       6.577  35.152  36.027  1.00 18.91           O  
ATOM   2064  CB  GLN A 265       9.308  36.714  36.728  1.00 19.30           C  
ATOM   2065  CG  GLN A 265      10.152  37.205  37.844  1.00 25.96           C  
ATOM   2066  CD  GLN A 265      10.594  38.641  37.725  1.00 28.89           C  
ATOM   2067  OE1 GLN A 265      10.107  39.586  38.304  1.00 31.53           O  
ATOM   2068  NE2 GLN A 265      11.615  38.807  36.941  1.00 31.20           N  
ATOM   2069  N   MET A 266       8.119  34.432  34.575  1.00 15.86           N  
ATOM   2070  CA  MET A 266       7.094  34.036  33.588  1.00 16.95           C  
ATOM   2071  C   MET A 266       6.343  32.765  34.021  1.00 19.00           C  
ATOM   2072  O   MET A 266       5.220  32.425  33.623  1.00 18.73           O  
ATOM   2073  CB  MET A 266       7.762  33.750  32.178  1.00 13.42           C  
ATOM   2074  CG  MET A 266       8.301  35.098  31.540  1.00 13.60           C  
ATOM   2075  SD  MET A 266       9.162  34.825  29.916  1.00 15.85           S  
ATOM   2076  CE  MET A 266       7.722  34.860  28.795  1.00  7.97           C  
ATOM   2077  N   LEU A 267       7.017  31.899  34.795  1.00 18.47           N  
ATOM   2078  CA  LEU A 267       6.500  30.674  35.337  1.00 20.07           C  
ATOM   2079  C   LEU A 267       5.993  30.825  36.800  1.00 19.82           C  
ATOM   2080  O   LEU A 267       5.774  29.762  37.425  1.00 18.91           O  
ATOM   2081  CB  LEU A 267       7.367  29.429  35.150  1.00 12.37           C  
ATOM   2082  CG  LEU A 267       7.770  29.193  33.658  1.00 18.42           C  
ATOM   2083  CD1 LEU A 267       8.854  28.111  33.586  1.00 14.75           C  
ATOM   2084  CD2 LEU A 267       6.673  28.841  32.607  1.00 14.40           C  
ATOM   2085  N   HIS A 268       5.579  32.003  37.251  1.00 20.42           N  
ATOM   2086  CA  HIS A 268       5.047  32.084  38.620  1.00 23.49           C  
ATOM   2087  C   HIS A 268       3.740  31.301  38.628  1.00 21.99           C  
ATOM   2088  O   HIS A 268       2.938  31.365  37.681  1.00 14.64           O  
ATOM   2089  CB  HIS A 268       4.791  33.489  39.215  1.00 27.81           C  
ATOM   2090  CG  HIS A 268       6.047  34.040  39.820  1.00 32.63           C  
ATOM   2091  ND1 HIS A 268       6.383  35.390  39.800  1.00 34.72           N  
ATOM   2092  CD2 HIS A 268       7.134  33.382  40.370  1.00 33.14           C  
ATOM   2093  CE1 HIS A 268       7.588  35.567  40.346  1.00 30.68           C  
ATOM   2094  NE2 HIS A 268       8.057  34.383  40.637  1.00 32.23           N  
ATOM   2095  N   TYR A 269       3.472  30.590  39.712  1.00 20.67           N  
ATOM   2096  CA  TYR A 269       2.262  29.799  39.864  1.00 18.86           C  
ATOM   2097  C   TYR A 269       1.011  30.681  39.937  1.00 20.44           C  
ATOM   2098  O   TYR A 269       0.050  30.571  39.139  1.00 19.43           O  
ATOM   2099  CB  TYR A 269       2.248  28.871  41.068  1.00 14.14           C  
ATOM   2100  CG  TYR A 269       2.726  27.476  40.763  1.00 17.03           C  
ATOM   2101  CD1 TYR A 269       2.115  26.658  39.863  1.00 13.17           C  
ATOM   2102  CD2 TYR A 269       3.834  26.958  41.520  1.00 16.90           C  
ATOM   2103  CE1 TYR A 269       2.535  25.359  39.626  1.00 16.68           C  
ATOM   2104  CE2 TYR A 269       4.259  25.691  41.287  1.00 14.97           C  
ATOM   2105  CZ  TYR A 269       3.614  24.881  40.353  1.00 17.54           C  
ATOM   2106  OH  TYR A 269       4.082  23.574  40.111  1.00 16.87           O  
ATOM   2107  N   ASP A 270       1.182  31.788  40.599  1.00 20.47           N  
ATOM   2108  CA  ASP A 270       0.002  32.652  40.786  1.00 19.39           C  
ATOM   2109  C   ASP A 270      -0.034  33.648  39.662  1.00 21.32           C  
ATOM   2110  O   ASP A 270       0.943  34.410  39.501  1.00 24.84           O  
ATOM   2111  CB  ASP A 270       0.183  33.337  42.144  1.00 20.02           C  
ATOM   2112  CG  ASP A 270      -0.886  34.322  42.474  1.00 19.71           C  
ATOM   2113  OD1 ASP A 270      -1.792  34.587  41.692  1.00 18.15           O  
ATOM   2114  OD2 ASP A 270      -0.886  34.847  43.590  1.00 20.39           O  
ATOM   2115  N   PRO A 271      -1.108  33.644  38.870  1.00 17.25           N  
ATOM   2116  CA  PRO A 271      -1.253  34.497  37.735  1.00 21.25           C  
ATOM   2117  C   PRO A 271      -1.290  35.973  38.110  1.00 26.96           C  
ATOM   2118  O   PRO A 271      -0.963  36.810  37.249  1.00 27.42           O  
ATOM   2119  CB  PRO A 271      -2.544  34.038  37.048  1.00 21.78           C  
ATOM   2120  CG  PRO A 271      -3.231  33.081  38.008  1.00 19.79           C  
ATOM   2121  CD  PRO A 271      -2.182  32.628  38.988  1.00 16.67           C  
ATOM   2122  N   ASN A 272      -1.559  36.378  39.350  1.00 27.00           N  
ATOM   2123  CA  ASN A 272      -1.433  37.787  39.695  1.00 30.59           C  
ATOM   2124  C   ASN A 272       0.027  38.171  39.972  1.00 31.88           C  
ATOM   2125  O   ASN A 272       0.296  39.380  39.943  1.00 32.30           O  
ATOM   2126  CB  ASN A 272      -2.234  38.197  40.971  1.00 34.44           C  
ATOM   2127  CG  ASN A 272      -3.563  38.713  40.434  1.00 38.86           C  
ATOM   2128  OD1 ASN A 272      -4.389  37.810  40.197  1.00 41.35           O  
ATOM   2129  ND2 ASN A 272      -3.635  40.031  40.254  1.00 39.46           N  
ATOM   2130  N   LYS A 273       0.838  37.164  40.303  1.00 27.02           N  
ATOM   2131  CA  LYS A 273       2.245  37.492  40.491  1.00 30.97           C  
ATOM   2132  C   LYS A 273       3.047  37.273  39.180  1.00 28.42           C  
ATOM   2133  O   LYS A 273       4.197  37.684  39.094  1.00 27.05           O  
ATOM   2134  CB  LYS A 273       2.865  36.557  41.552  1.00 33.78           C  
ATOM   2135  CG  LYS A 273       2.378  36.572  42.968  1.00 39.64           C  
ATOM   2136  CD  LYS A 273       1.973  37.960  43.475  1.00 44.00           C  
ATOM   2137  CE  LYS A 273       0.532  38.027  43.950  1.00 47.49           C  
ATOM   2138  NZ  LYS A 273       0.202  39.438  44.341  1.00 50.17           N  
ATOM   2139  N   ARG A 274       2.485  36.612  38.177  1.00 24.79           N  
ATOM   2140  CA  ARG A 274       3.225  36.334  36.927  1.00 22.21           C  
ATOM   2141  C   ARG A 274       3.591  37.635  36.216  1.00 20.64           C  
ATOM   2142  O   ARG A 274       2.715  38.511  36.173  1.00 19.60           O  
ATOM   2143  CB  ARG A 274       2.419  35.348  36.111  1.00 18.81           C  
ATOM   2144  CG  ARG A 274       3.133  34.482  35.120  1.00 21.55           C  
ATOM   2145  CD  ARG A 274       2.359  33.350  34.438  1.00 21.08           C  
ATOM   2146  NE  ARG A 274       1.762  32.368  35.376  1.00 20.38           N  
ATOM   2147  CZ  ARG A 274       0.577  31.827  35.182  1.00 19.69           C  
ATOM   2148  NH1 ARG A 274      -0.194  32.156  34.107  1.00 12.31           N  
ATOM   2149  NH2 ARG A 274       0.125  30.924  36.077  1.00 18.31           N  
ATOM   2150  N   ILE A 275       4.793  37.823  35.638  1.00 19.13           N  
ATOM   2151  CA  ILE A 275       5.107  39.153  35.069  1.00 14.27           C  
ATOM   2152  C   ILE A 275       4.186  39.415  33.897  1.00 16.02           C  
ATOM   2153  O   ILE A 275       3.725  38.440  33.283  1.00 13.72           O  
ATOM   2154  CB  ILE A 275       6.605  39.224  34.766  1.00 14.03           C  
ATOM   2155  CG1 ILE A 275       7.136  40.635  34.466  1.00 17.87           C  
ATOM   2156  CG2 ILE A 275       7.005  38.202  33.671  1.00 12.09           C  
ATOM   2157  CD1 ILE A 275       8.659  40.730  34.372  1.00 15.42           C  
ATOM   2158  N   SER A 276       3.839  40.655  33.632  1.00 14.03           N  
ATOM   2159  CA  SER A 276       3.107  41.061  32.494  1.00 17.56           C  
ATOM   2160  C   SER A 276       4.111  41.159  31.299  1.00 19.39           C  
ATOM   2161  O   SER A 276       5.323  41.289  31.423  1.00 18.22           O  
ATOM   2162  CB  SER A 276       2.432  42.417  32.680  1.00 15.88           C  
ATOM   2163  OG  SER A 276       3.483  43.408  32.834  1.00 18.93           O  
ATOM   2164  N   ALA A 277       3.572  41.169  30.071  1.00 18.82           N  
ATOM   2165  CA  ALA A 277       4.426  41.350  28.899  1.00 21.44           C  
ATOM   2166  C   ALA A 277       5.120  42.739  28.930  1.00 23.08           C  
ATOM   2167  O   ALA A 277       6.334  42.740  28.684  1.00 22.09           O  
ATOM   2168  CB  ALA A 277       3.560  41.235  27.633  1.00 20.96           C  
ATOM   2169  N   LYS A 278       4.397  43.802  29.319  1.00 23.37           N  
ATOM   2170  CA  LYS A 278       5.008  45.109  29.360  1.00 25.87           C  
ATOM   2171  C   LYS A 278       6.084  45.181  30.414  1.00 23.77           C  
ATOM   2172  O   LYS A 278       7.147  45.736  30.137  1.00 26.90           O  
ATOM   2173  CB  LYS A 278       4.099  46.299  29.640  1.00 32.11           C  
ATOM   2174  CG  LYS A 278       3.231  46.724  28.470  1.00 40.91           C  
ATOM   2175  CD  LYS A 278       2.310  47.919  28.735  1.00 44.60           C  
ATOM   2176  CE  LYS A 278       1.319  48.043  27.569  1.00 48.74           C  
ATOM   2177  NZ  LYS A 278       1.196  49.444  27.024  1.00 49.74           N  
ATOM   2178  N   ALA A 279       5.954  44.634  31.596  1.00 23.73           N  
ATOM   2179  CA  ALA A 279       7.084  44.675  32.555  1.00 23.76           C  
ATOM   2180  C   ALA A 279       8.199  43.781  31.990  1.00 23.13           C  
ATOM   2181  O   ALA A 279       9.350  44.194  32.128  1.00 26.69           O  
ATOM   2182  CB  ALA A 279       6.627  44.153  33.903  1.00 23.42           C  
ATOM   2183  N   ALA A 280       7.887  42.606  31.380  1.00 16.77           N  
ATOM   2184  CA  ALA A 280       8.961  41.780  30.924  1.00 17.52           C  
ATOM   2185  C   ALA A 280       9.909  42.430  29.912  1.00 19.75           C  
ATOM   2186  O   ALA A 280      11.157  42.300  29.982  1.00 20.54           O  
ATOM   2187  CB  ALA A 280       8.454  40.397  30.475  1.00 17.84           C  
ATOM   2188  N   LEU A 281       9.470  43.318  29.074  1.00 20.07           N  
ATOM   2189  CA  LEU A 281      10.170  44.083  28.064  1.00 24.52           C  
ATOM   2190  C   LEU A 281      11.214  45.006  28.712  1.00 27.28           C  
ATOM   2191  O   LEU A 281      12.226  45.214  28.081  1.00 23.51           O  
ATOM   2192  CB  LEU A 281       9.232  45.009  27.232  1.00 20.46           C  
ATOM   2193  CG  LEU A 281       8.321  44.243  26.273  1.00 24.22           C  
ATOM   2194  CD1 LEU A 281       7.360  45.178  25.487  1.00 26.79           C  
ATOM   2195  CD2 LEU A 281       9.130  43.517  25.177  1.00 21.31           C  
ATOM   2196  N   ALA A 282      10.968  45.428  29.954  1.00 28.62           N  
ATOM   2197  CA  ALA A 282      11.908  46.287  30.697  1.00 28.43           C  
ATOM   2198  C   ALA A 282      12.843  45.467  31.543  1.00 25.83           C  
ATOM   2199  O   ALA A 282      13.794  45.937  32.217  1.00 28.96           O  
ATOM   2200  CB  ALA A 282      11.085  47.295  31.549  1.00 28.79           C  
ATOM   2201  N   HIS A 283      12.748  44.128  31.540  1.00 24.38           N  
ATOM   2202  CA  HIS A 283      13.686  43.289  32.291  1.00 22.50           C  
ATOM   2203  C   HIS A 283      15.145  43.469  31.874  1.00 22.71           C  
ATOM   2204  O   HIS A 283      15.415  43.546  30.656  1.00 20.31           O  
ATOM   2205  CB  HIS A 283      13.293  41.830  32.084  1.00 21.10           C  
ATOM   2206  CG  HIS A 283      13.979  40.895  33.059  1.00 21.45           C  
ATOM   2207  ND1 HIS A 283      15.276  40.457  33.007  1.00 19.03           N  
ATOM   2208  CD2 HIS A 283      13.422  40.326  34.190  1.00 19.43           C  
ATOM   2209  CE1 HIS A 283      15.517  39.660  34.045  1.00 20.13           C  
ATOM   2210  NE2 HIS A 283      14.418  39.561  34.788  1.00 19.86           N  
ATOM   2211  N   PRO A 284      16.144  43.416  32.790  1.00 22.22           N  
ATOM   2212  CA  PRO A 284      17.534  43.554  32.405  1.00 22.54           C  
ATOM   2213  C   PRO A 284      18.033  42.546  31.387  1.00 25.39           C  
ATOM   2214  O   PRO A 284      18.940  42.985  30.635  1.00 24.47           O  
ATOM   2215  CB  PRO A 284      18.399  43.601  33.685  1.00 21.14           C  
ATOM   2216  CG  PRO A 284      17.390  43.750  34.806  1.00 20.33           C  
ATOM   2217  CD  PRO A 284      15.990  43.376  34.252  1.00 19.04           C  
ATOM   2218  N   PHE A 285      17.526  41.323  31.198  1.00 26.47           N  
ATOM   2219  CA  PHE A 285      17.932  40.410  30.141  1.00 26.36           C  
ATOM   2220  C   PHE A 285      17.934  41.064  28.746  1.00 26.29           C  
ATOM   2221  O   PHE A 285      18.712  40.611  27.905  1.00 24.96           O  
ATOM   2222  CB  PHE A 285      17.026  39.167  29.971  1.00 24.38           C  
ATOM   2223  CG  PHE A 285      17.246  38.005  29.049  1.00 21.49           C  
ATOM   2224  CD1 PHE A 285      18.406  37.253  29.039  1.00 20.02           C  
ATOM   2225  CD2 PHE A 285      16.220  37.620  28.170  1.00 18.24           C  
ATOM   2226  CE1 PHE A 285      18.582  36.166  28.140  1.00 19.69           C  
ATOM   2227  CE2 PHE A 285      16.391  36.507  27.351  1.00 17.07           C  
ATOM   2228  CZ  PHE A 285      17.549  35.750  27.304  1.00 15.41           C  
ATOM   2229  N   PHE A 286      17.000  41.943  28.440  1.00 21.77           N  
ATOM   2230  CA  PHE A 286      16.891  42.583  27.152  1.00 24.67           C  
ATOM   2231  C   PHE A 286      17.775  43.797  26.933  1.00 27.99           C  
ATOM   2232  O   PHE A 286      17.716  44.507  25.935  1.00 27.64           O  
ATOM   2233  CB  PHE A 286      15.413  43.042  26.911  1.00 21.82           C  
ATOM   2234  CG  PHE A 286      14.567  41.789  26.815  1.00 21.79           C  
ATOM   2235  CD1 PHE A 286      14.877  40.734  25.916  1.00 20.43           C  
ATOM   2236  CD2 PHE A 286      13.492  41.672  27.700  1.00 22.00           C  
ATOM   2237  CE1 PHE A 286      14.057  39.597  25.910  1.00 21.76           C  
ATOM   2238  CE2 PHE A 286      12.688  40.544  27.654  1.00 22.49           C  
ATOM   2239  CZ  PHE A 286      12.967  39.493  26.783  1.00 20.86           C  
ATOM   2240  N   GLN A 287      18.588  44.130  27.925  1.00 30.54           N  
ATOM   2241  CA  GLN A 287      19.499  45.263  27.856  1.00 33.58           C  
ATOM   2242  C   GLN A 287      20.365  45.174  26.613  1.00 28.71           C  
ATOM   2243  O   GLN A 287      20.645  46.217  26.033  1.00 26.44           O  
ATOM   2244  CB  GLN A 287      20.486  45.237  29.066  1.00 36.79           C  
ATOM   2245  CG  GLN A 287      21.247  46.561  29.148  1.00 45.64           C  
ATOM   2246  CD  GLN A 287      20.266  47.719  29.335  1.00 50.68           C  
ATOM   2247  OE1 GLN A 287      19.107  47.453  29.726  1.00 53.40           O  
ATOM   2248  NE2 GLN A 287      20.723  48.968  29.084  1.00 51.31           N  
ATOM   2249  N   ASP A 288      20.875  43.959  26.305  1.00 27.93           N  
ATOM   2250  CA  ASP A 288      21.680  44.000  25.052  1.00 31.10           C  
ATOM   2251  C   ASP A 288      20.966  43.392  23.867  1.00 30.31           C  
ATOM   2252  O   ASP A 288      21.629  42.771  23.017  1.00 28.44           O  
ATOM   2253  CB  ASP A 288      22.973  43.306  25.352  1.00 33.58           C  
ATOM   2254  CG  ASP A 288      22.762  41.873  25.757  1.00 36.65           C  
ATOM   2255  OD1 ASP A 288      21.619  41.375  25.881  1.00 38.05           O  
ATOM   2256  OD2 ASP A 288      23.847  41.340  25.974  1.00 36.65           O  
ATOM   2257  N   VAL A 289      19.629  43.565  23.818  1.00 28.85           N  
ATOM   2258  CA  VAL A 289      18.905  42.911  22.717  1.00 24.76           C  
ATOM   2259  C   VAL A 289      19.276  43.492  21.353  1.00 25.26           C  
ATOM   2260  O   VAL A 289      19.380  44.685  21.089  1.00 27.19           O  
ATOM   2261  CB  VAL A 289      17.384  42.993  22.977  1.00 22.94           C  
ATOM   2262  CG1 VAL A 289      16.872  44.422  22.790  1.00 18.53           C  
ATOM   2263  CG2 VAL A 289      16.660  42.050  22.010  1.00 24.59           C  
ATOM   2264  N   THR A 290      19.482  42.638  20.351  1.00 23.08           N  
ATOM   2265  CA  THR A 290      19.720  43.020  18.964  1.00 21.76           C  
ATOM   2266  C   THR A 290      18.643  42.350  18.104  1.00 22.87           C  
ATOM   2267  O   THR A 290      17.789  41.611  18.584  1.00 19.93           O  
ATOM   2268  CB  THR A 290      21.152  42.612  18.558  1.00 20.36           C  
ATOM   2269  OG1 THR A 290      21.336  41.121  18.624  1.00 19.25           O  
ATOM   2270  CG2 THR A 290      22.162  43.177  19.562  1.00 19.18           C  
ATOM   2271  N   LYS A 291      18.719  42.480  16.788  1.00 23.41           N  
ATOM   2272  CA  LYS A 291      17.983  41.708  15.829  1.00 26.54           C  
ATOM   2273  C   LYS A 291      18.848  40.989  14.765  1.00 24.25           C  
ATOM   2274  O   LYS A 291      18.971  41.455  13.611  1.00 24.33           O  
ATOM   2275  CB  LYS A 291      16.913  42.644  15.197  1.00 27.54           C  
ATOM   2276  CG  LYS A 291      15.830  41.833  14.479  1.00 30.53           C  
ATOM   2277  CD  LYS A 291      15.126  42.816  13.525  1.00 35.97           C  
ATOM   2278  CE  LYS A 291      13.865  42.204  12.911  1.00 36.58           C  
ATOM   2279  NZ  LYS A 291      12.940  43.291  12.467  1.00 38.48           N  
ATOM   2280  N   PRO A 292      19.238  39.730  14.996  1.00 22.26           N  
ATOM   2281  CA  PRO A 292      20.007  38.955  14.089  1.00 22.49           C  
ATOM   2282  C   PRO A 292      19.084  38.357  13.016  1.00 25.16           C  
ATOM   2283  O   PRO A 292      17.857  38.315  13.216  1.00 27.27           O  
ATOM   2284  CB  PRO A 292      20.653  37.832  14.920  1.00 22.34           C  
ATOM   2285  CG  PRO A 292      20.311  38.134  16.369  1.00 18.74           C  
ATOM   2286  CD  PRO A 292      19.103  39.003  16.295  1.00 21.59           C  
ATOM   2287  N   VAL A 293      19.638  37.973  11.900  1.00 27.13           N  
ATOM   2288  CA  VAL A 293      18.954  37.223  10.855  1.00 29.85           C  
ATOM   2289  C   VAL A 293      19.202  35.751  11.066  1.00 31.83           C  
ATOM   2290  O   VAL A 293      20.349  35.359  11.414  1.00 33.02           O  
ATOM   2291  CB  VAL A 293      19.480  37.624   9.450  1.00 31.93           C  
ATOM   2292  CG1 VAL A 293      19.983  39.050   9.318  1.00 32.41           C  
ATOM   2293  CG2 VAL A 293      20.498  36.750   8.784  1.00 31.83           C  
ATOM   2294  N   PRO A 294      18.176  34.897  10.956  1.00 33.82           N  
ATOM   2295  CA  PRO A 294      18.329  33.453  11.005  1.00 32.98           C  
ATOM   2296  C   PRO A 294      18.901  32.874   9.710  1.00 36.27           C  
ATOM   2297  O   PRO A 294      19.001  33.500   8.669  1.00 30.13           O  
ATOM   2298  CB  PRO A 294      16.889  32.983  11.124  1.00 31.69           C  
ATOM   2299  CG  PRO A 294      16.113  33.994  10.356  1.00 31.54           C  
ATOM   2300  CD  PRO A 294      16.817  35.266  10.553  1.00 32.59           C  
ATOM   2301  N   HIS A 295      19.277  31.601   9.775  1.00 42.17           N  
ATOM   2302  CA  HIS A 295      19.810  30.812   8.667  1.00 46.39           C  
ATOM   2303  C   HIS A 295      18.648  29.969   8.163  1.00 44.38           C  
ATOM   2304  O   HIS A 295      18.248  29.007   8.808  1.00 43.22           O  
ATOM   2305  CB  HIS A 295      20.962  29.958   9.245  1.00 53.30           C  
ATOM   2306  CG  HIS A 295      20.606  28.594   9.778  1.00 59.96           C  
ATOM   2307  ND1 HIS A 295      19.980  28.404  11.000  1.00 62.16           N  
ATOM   2308  CD2 HIS A 295      20.683  27.343   9.227  1.00 62.10           C  
ATOM   2309  CE1 HIS A 295      19.729  27.114  11.208  1.00 63.21           C  
ATOM   2310  NE2 HIS A 295      20.156  26.449  10.147  1.00 64.23           N  
ATOM   2311  N   LEU A 296      17.977  30.265   7.082  1.00 44.83           N  
ATOM   2312  CA  LEU A 296      16.763  29.600   6.648  1.00 48.33           C  
ATOM   2313  C   LEU A 296      16.714  28.998   5.252  1.00 51.54           C  
ATOM   2314  O   LEU A 296      16.935  29.767   4.288  1.00 51.81           O  
ATOM   2315  CB  LEU A 296      15.715  30.694   6.541  1.00 47.48           C  
ATOM   2316  CG  LEU A 296      14.927  31.241   7.687  1.00 49.26           C  
ATOM   2317  CD1 LEU A 296      13.511  31.425   7.098  1.00 49.68           C  
ATOM   2318  CD2 LEU A 296      14.941  30.393   8.955  1.00 48.20           C  
ATOM   2319  N   ARG A 297      16.285  27.738   5.142  1.00 54.37           N  
ATOM   2320  CA  ARG A 297      16.180  27.116   3.818  1.00 56.68           C  
ATOM   2321  C   ARG A 297      14.720  26.947   3.436  1.00 56.54           C  
ATOM   2322  O   ARG A 297      13.998  26.109   3.997  1.00 59.13           O  
ATOM   2323  CB  ARG A 297      16.913  25.778   3.723  1.00 59.31           C  
ATOM   2324  CG  ARG A 297      17.644  25.587   2.389  1.00 62.27           C  
ATOM   2325  CD  ARG A 297      18.941  24.823   2.569  1.00 65.68           C  
ATOM   2326  NE  ARG A 297      19.444  24.021   1.468  1.00 67.75           N  
ATOM   2327  CZ  ARG A 297      19.763  22.724   1.498  1.00 69.32           C  
ATOM   2328  NH1 ARG A 297      19.645  21.984   2.595  1.00 69.27           N  
ATOM   2329  NH2 ARG A 297      20.241  22.080   0.421  1.00 69.96           N  
ATOM   2330  N   LEU A 298      14.302  27.706   2.426  1.00 53.63           N  
ATOM   2331  CA  LEU A 298      12.916  27.721   1.997  1.00 50.66           C  
ATOM   2332  C   LEU A 298      12.596  26.726   0.902  1.00 52.96           C  
ATOM   2333  O   LEU A 298      11.447  26.227   0.795  1.00 50.06           O  
ATOM   2334  CB  LEU A 298      12.630  29.174   1.574  1.00 49.26           C  
ATOM   2335  CG  LEU A 298      12.758  30.172   2.750  1.00 48.71           C  
ATOM   2336  CD1 LEU A 298      12.464  31.588   2.323  1.00 49.06           C  
ATOM   2337  CD2 LEU A 298      11.876  29.779   3.923  1.00 47.06           C  
ATOM   2338  OXT LEU A 298      13.553  26.443   0.124  1.00 54.77           O  
TER    2339      LEU A 298                                                      
HETATM 2340 MG    MG A 382      -2.091  27.625  14.051  0.60 36.30          MG  
HETATM 2341  PG  ATP A 381      -3.806  25.217  15.796  1.00 49.04           P  
HETATM 2342  O1G ATP A 381      -4.147  25.277  17.223  1.00 49.00           O  
HETATM 2343  O2G ATP A 381      -3.514  26.569  15.259  1.00 50.27           O  
HETATM 2344  O3G ATP A 381      -4.998  24.742  15.025  1.00 51.63           O  
HETATM 2345  PB  ATP A 381      -1.436  24.535  14.401  1.00 45.09           P  
HETATM 2346  O1B ATP A 381      -0.793  25.836  14.439  1.00 44.57           O  
HETATM 2347  O2B ATP A 381      -0.434  23.440  14.436  1.00 44.91           O  
HETATM 2348  O3B ATP A 381      -2.579  24.269  15.473  1.00 46.88           O  
HETATM 2349  PA  ATP A 381      -2.802  25.365  11.864  1.00 46.91           P  
HETATM 2350  O1A ATP A 381      -3.884  24.619  11.123  1.00 45.20           O  
HETATM 2351  O2A ATP A 381      -3.419  26.609  12.377  1.00 44.42           O  
HETATM 2352  O3A ATP A 381      -2.263  24.357  13.015  1.00 46.05           O  
HETATM 2353  O5' ATP A 381      -1.554  25.630  10.942  1.00 45.44           O  
HETATM 2354  C5' ATP A 381      -1.296  24.510  10.035  1.00 46.44           C  
HETATM 2355  C4' ATP A 381       0.148  24.648   9.554  1.00 47.66           C  
HETATM 2356  O4' ATP A 381       0.247  25.795   8.690  1.00 46.10           O  
HETATM 2357  C3' ATP A 381       1.082  24.890  10.750  1.00 48.40           C  
HETATM 2358  O3' ATP A 381       2.358  24.311  10.322  1.00 51.24           O  
HETATM 2359  C2' ATP A 381       1.202  26.458  10.680  1.00 49.04           C  
HETATM 2360  O2' ATP A 381       2.449  26.818  11.324  1.00 49.93           O  
HETATM 2361  C1' ATP A 381       1.196  26.716   9.144  1.00 46.04           C  
HETATM 2362  N9  ATP A 381       0.588  27.996   8.742  1.00 44.38           N  
HETATM 2363  C8  ATP A 381      -0.427  28.592   9.427  1.00 43.54           C  
HETATM 2364  N7  ATP A 381      -0.608  29.839   9.246  1.00 41.55           N  
HETATM 2365  C5  ATP A 381       0.298  30.160   8.350  1.00 38.59           C  
HETATM 2366  C6  ATP A 381       0.559  31.388   7.783  1.00 36.10           C  
HETATM 2367  N6  ATP A 381      -0.055  32.538   8.020  1.00 32.35           N  
HETATM 2368  N1  ATP A 381       1.582  31.433   6.899  1.00 33.04           N  
HETATM 2369  C2  ATP A 381       2.291  30.294   6.618  1.00 36.11           C  
HETATM 2370  N3  ATP A 381       2.110  29.077   7.112  1.00 38.46           N  
HETATM 2371  C4  ATP A 381       1.076  29.074   7.991  1.00 41.60           C  
HETATM 2372  O   HOH A 383       5.705  30.787  41.914  1.00 18.41           O  
HETATM 2373  O   HOH A 384       2.520  23.915  30.697  1.00 20.51           O  
HETATM 2374  O   HOH A 385      -4.797  33.659  34.087  1.00 15.56           O  
HETATM 2375  O   HOH A 386      -1.292  30.596  25.205  1.00 14.83           O  
HETATM 2376  O   HOH A 387      -1.703  28.892  28.682  1.00 16.88           O  
HETATM 2377  O   HOH A 388       6.335  22.249  27.846  1.00 16.52           O  
HETATM 2378  O   HOH A 389      15.971  38.547  14.803  1.00 22.10           O  
HETATM 2379  O   HOH A 390       0.887  40.843  29.498  1.00 18.29           O  
HETATM 2380  O   HOH A 391       3.396  32.032  42.608  1.00 26.45           O  
HETATM 2381  O   HOH A 392       1.199  38.047  33.179  1.00 14.72           O  
HETATM 2382  O   HOH A 393       0.887  37.273   2.332  1.00 23.42           O  
HETATM 2383  O   HOH A 394       2.200  41.582  10.638  1.00 32.65           O  
HETATM 2384  O   HOH A 395       8.465  23.697  26.130  1.00 16.22           O  
HETATM 2385  O   HOH A 396      13.101  35.367  11.767  1.00 22.94           O  
HETATM 2386  O   HOH A 397       4.191  42.595  35.864  1.00 27.64           O  
HETATM 2387  O   HOH A 398       6.447  27.588   0.634  1.00 27.54           O  
HETATM 2388  O   HOH A 399       4.764  31.594  -6.056  1.00 26.66           O  
HETATM 2389  O   HOH A 400       5.255  26.724   4.980  1.00 46.14           O  
HETATM 2390  O   HOH A 401       8.483  17.346  32.093  1.00 31.65           O  
HETATM 2391  O   HOH A 402      21.942  40.113  22.207  1.00 26.53           O  
HETATM 2392  O   HOH A 403      17.982  31.137  38.774  1.00 44.39           O  
HETATM 2393  O   HOH A 404       4.050  33.556  48.262  1.00 27.55           O  
HETATM 2394  O   HOH A 405      -5.837  48.321  28.606  1.00 44.34           O  
HETATM 2395  O   HOH A 406       0.097  45.077  27.753  1.00 28.48           O  
HETATM 2396  O   HOH A 407       8.759  17.799  35.110  1.00 28.57           O  
HETATM 2397  O   HOH A 408       6.509  28.603  39.777  1.00 30.64           O  
HETATM 2398  O   HOH A 409      -1.701  24.812  51.140  1.00 31.41           O  
HETATM 2399  O   HOH A 410      21.226  23.125  39.412  1.00 26.20           O  
HETATM 2400  O   HOH A 411      19.836  39.748  20.616  1.00 23.48           O  
HETATM 2401  O   HOH A 412      -2.189  27.383  26.496  1.00 20.83           O  
HETATM 2402  O   HOH A 413      -7.089  39.541  31.258  1.00 33.63           O  
HETATM 2403  O   HOH A 414       1.464  43.746  29.419  1.00 20.71           O  
HETATM 2404  O   HOH A 415      -8.500  28.600  48.766  1.00 30.60           O  
HETATM 2405  O   HOH A 416      -0.371  39.776  31.833  1.00 27.58           O  
HETATM 2406  O   HOH A 417       0.215  39.828   1.989  1.00 37.10           O  
HETATM 2407  O   HOH A 418       2.989  44.966  35.587  1.00 42.04           O  
HETATM 2408  O   HOH A 419       4.812  22.268  10.947  1.00 60.10           O  
HETATM 2409  O   HOH A 420      -6.191  33.930  36.781  1.00 35.01           O  
HETATM 2410  O   HOH A 421      -0.181  38.778  35.507  1.00 26.65           O  
HETATM 2411  O   HOH A 422      -0.699  11.008  24.203  1.00 46.74           O  
HETATM 2412  O   HOH A 423      -1.159  42.606  12.440  1.00 27.84           O  
HETATM 2413  O   HOH A 424       2.909  29.179  -6.892  1.00 43.96           O  
HETATM 2414  O   HOH A 425      -7.138  25.860  -6.756  1.00 49.86           O  
HETATM 2415  O   HOH A 426      -0.689  23.524  24.925  1.00 25.01           O  
HETATM 2416  O   HOH A 427       1.972  37.943  -1.330  1.00 26.42           O  
HETATM 2417  O   HOH A 428      -0.583  18.520  48.051  1.00 52.67           O  
HETATM 2418  O   HOH A 429     -11.811  18.805  42.557  1.00 46.75           O  
HETATM 2419  O   HOH A 430      16.648  33.812  39.415  1.00 32.71           O  
HETATM 2420  O   HOH A 431       5.265  28.042  -3.480  1.00 37.17           O  
HETATM 2421  O   HOH A 432     -14.037  24.477  35.698  1.00 30.15           O  
HETATM 2422  O   HOH A 433       0.181   8.781  25.508  1.00 25.50           O  
HETATM 2423  O   HOH A 434       6.557  26.252  44.065  1.00 28.56           O  
HETATM 2424  O   HOH A 435     -12.693  39.465  22.490  1.00 55.13           O  
HETATM 2425  O   HOH A 436      20.073  30.885  12.609  1.00 41.68           O  
HETATM 2426  O   HOH A 437      -8.410  33.569  22.085  1.00 29.71           O  
HETATM 2427  O   HOH A 438      10.753  42.065  37.034  1.00 32.15           O  
HETATM 2428  O   HOH A 439      -6.528  31.631  19.684  1.00 32.65           O  
HETATM 2429  O   HOH A 440      22.082  37.919  29.458  1.00 38.18           O  
HETATM 2430  O   HOH A 441     -12.602  15.650  39.269  1.00 53.99           O  
HETATM 2431  O   HOH A 442      22.215  27.164  41.787  1.00 46.30           O  
HETATM 2432  O   HOH A 443      -0.807  26.242  24.403  1.00 28.91           O  
HETATM 2433  O   HOH A 444       5.202  25.308  46.054  1.00 47.90           O  
HETATM 2434  O   HOH A 445     -10.074  25.879  32.590  1.00 34.28           O  
HETATM 2435  O   HOH A 446      -3.813  37.923  35.867  1.00 52.43           O  
HETATM 2436  O   HOH A 447      -6.239  24.910  12.854  1.00 55.73           O  
HETATM 2437  O   HOH A 448      -4.131  25.762  25.320  1.00 49.16           O  
HETATM 2438  O   HOH A 449       9.736  25.903   5.382  1.00 44.20           O  
HETATM 2439  O   HOH A 450      23.917  39.778  17.868  1.00 30.15           O  
HETATM 2440  O   HOH A 451      -2.842  33.365  11.564  1.00 32.39           O  
HETATM 2441  O   HOH A 452     -24.735  31.251  10.117  1.00 46.68           O  
HETATM 2442  O   HOH A 453      -4.695  27.528  18.504  1.00 42.33           O  
HETATM 2443  O   HOH A 454      -7.139  17.128  38.533  1.00 34.67           O  
HETATM 2444  O   HOH A 455      17.259  21.113  41.748  1.00 41.11           O  
HETATM 2445  O   HOH A 456      -7.658  21.459  31.263  1.00 47.72           O  
HETATM 2446  O   HOH A 457      17.493  14.538  38.312  1.00 43.38           O  
HETATM 2447  O   HOH A 458      -0.252  17.688  24.500  1.00 43.10           O  
HETATM 2448  O   HOH A 459      -5.529  32.835  41.053  1.00 28.96           O  
HETATM 2449  O   HOH A 460      14.025  45.289  10.404  1.00 41.09           O  
HETATM 2450  O   HOH A 461      -9.576  24.750  28.032  1.00 61.69           O  
HETATM 2451  O   HOH A 462       0.617  17.587  21.958  1.00 54.69           O  
HETATM 2452  O   HOH A 463       8.971  30.142  39.091  1.00 38.60           O  
HETATM 2453  O   HOH A 464      -2.283  45.032  29.403  1.00 41.19           O  
HETATM 2454  O   HOH A 465     -13.231  42.071   1.936  1.00 41.99           O  
HETATM 2455  O   HOH A 466       6.341  47.157  19.505  1.00 53.03           O  
HETATM 2456  O   HOH A 467      -0.269  41.119  35.996  1.00 51.06           O  
HETATM 2457  O   HOH A 468       9.816  23.662  47.494  1.00 41.99           O  
HETATM 2458  O   HOH A 469      18.956  27.885  39.692  1.00 39.53           O  
HETATM 2459  O   HOH A 470      11.605  17.534  29.448  1.00 39.78           O  
HETATM 2460  O   HOH A 471      -6.583  21.492  29.033  1.00 46.46           O  
HETATM 2461  O   HOH A 472     -13.562  21.817  35.957  1.00 42.16           O  
HETATM 2462  O   HOH A 473       2.015  11.543  35.414  1.00 42.00           O  
HETATM 2463  O   HOH A 474      21.209  25.260  43.325  1.00 56.02           O  
HETATM 2464  O   HOH A 475      10.970  35.205   4.401  1.00 36.88           O  
HETATM 2465  O   HOH A 476      24.212  39.975  21.337  1.00 41.31           O  
HETATM 2466  O   HOH A 477      16.445  42.658   9.616  1.00 58.63           O  
HETATM 2467  O   HOH A 478       9.251  26.513   2.121  1.00 53.11           O  
HETATM 2468  O   HOH A 479      -0.827  41.377  33.633  1.00 42.98           O  
HETATM 2469  O   HOH A 480       8.241  34.577   4.909  1.00 45.88           O  
HETATM 2470  O   HOH A 481      24.612  31.003  21.437  1.00 40.00           O  
HETATM 2471  O   HOH A 482      -9.613  29.765  44.006  1.00 53.14           O  
HETATM 2472  O   HOH A 483      10.531  17.224  42.452  1.00 52.64           O  
HETATM 2473  O   HOH A 484      24.208  37.368  16.507  1.00 34.56           O  
HETATM 2474  O   HOH A 485       8.590  38.407  41.270  1.00 41.31           O  
HETATM 2475  O   HOH A 486      -4.638  48.868  15.968  1.00 43.21           O  
HETATM 2476  O   HOH A 487      23.463  44.686  28.269  1.00 48.01           O  
HETATM 2477  O   HOH A 488      20.633  21.898  43.008  1.00 45.32           O  
HETATM 2478  O   HOH A 489      -2.748  36.004  13.984  1.00 49.56           O  
HETATM 2479  O   HOH A 490      -5.706  38.764  -0.744  1.00 54.76           O  
HETATM 2480  O   HOH A 491       2.288  34.701  45.410  1.00 47.62           O  
HETATM 2481  O   HOH A 492       8.020  34.550   7.184  1.00101.20           O  
HETATM 2482  O   HOH A 493      21.677  33.852  13.875  1.00 58.01           O  
HETATM 2483  O   HOH A 494      -1.281   9.761  31.507  1.00 52.01           O  
HETATM 2484  O   HOH A 495      -3.616   9.616  26.841  1.00 39.65           O  
HETATM 2485  O   HOH A 496       9.055  44.319  17.219  1.00 52.55           O  
HETATM 2486  O   HOH A 497      22.752  35.237  16.326  1.00 28.02           O  
HETATM 2487  O   HOH A 498     -26.200  36.871  17.298  1.00 49.05           O  
HETATM 2488  O   HOH A 499      26.020  38.074  22.762  1.00 41.43           O  
HETATM 2489  O   HOH A 500       6.160  39.546  41.289  1.00 77.69           O  
HETATM 2490  O   HOH A 501      -2.422  47.892  29.229  1.00 73.34           O  
HETATM 2491  O   HOH A 502      25.566  34.231  16.984  1.00 51.91           O  
HETATM 2492  O   HOH A 503      -6.360  50.502  17.370  1.00 63.67           O  
HETATM 2493  O   HOH A 504      10.808  39.089   4.903  1.00 53.61           O  
HETATM 2494  O   HOH A 505       6.921  25.338  -0.619  1.00 46.99           O  
HETATM 2495  O   HOH A 506       1.837  48.354  24.546  1.00 63.23           O  
HETATM 2496  O   HOH A 507      12.185  45.366  17.671  1.00 65.16           O  
HETATM 2497  O   HOH A 508       8.318  19.127  19.575  1.00 60.21           O  
HETATM 2498  O   HOH A 509      24.682  34.405  28.376  1.00 42.77           O  
HETATM 2499  O   HOH A 510     -10.358  37.810  25.619  1.00 69.76           O  
HETATM 2500  O   HOH A 511       1.425  40.053  -0.309  1.00 55.31           O  
HETATM 2501  O   HOH A 512       0.274  22.053  12.460  1.00 67.94           O  
HETATM 2502  O   HOH A 513     -11.816  40.959  24.479  1.00 62.85           O  
HETATM 2503  O   HOH A 514      -7.182  45.898   8.419  1.00 49.71           O  
HETATM 2504  O   HOH A 515      11.696  16.356  27.289  1.00 51.47           O  
HETATM 2505  O   HOH A 516      21.615  47.288  22.113  1.00 72.94           O  
HETATM 2506  O   HOH A 517      24.615  30.420  39.170  1.00 66.52           O  
HETATM 2507  O   HOH A 518      -4.342  38.282  13.639  1.00 42.53           O  
HETATM 2508  O   HOH A 519      21.395  42.182  28.661  1.00 50.77           O  
HETATM 2509  O   HOH A 520       3.657  22.622  -4.071  1.00 57.84           O  
HETATM 2510  O   HOH A 521     -11.217  34.132  29.954  1.00 54.48           O  
HETATM 2511  O   HOH A 522      -7.116  39.715   1.189  1.00 64.10           O  
HETATM 2512  O   HOH A 523     -10.544  44.302  22.374  1.00 59.44           O  
HETATM 2513  O   HOH A 524      12.172  43.500  15.098  1.00 60.03           O  
HETATM 2514  O   HOH A 525      16.168  47.114  25.428  1.00 56.12           O  
HETATM 2515  O   HOH A 526      11.698  19.727  33.101  1.00 57.72           O  
HETATM 2516  O   HOH A 527      -0.542  28.254  12.604  1.00 31.61           O  
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1                                                                
CONECT 1004 2340                                                                
CONECT 1100 2340                                                                
CONECT 2340 1004 1100 2343 2346                                                 
CONECT 2340 2351 2516                                                           
CONECT 2341 2342 2343 2344 2348                                                 
CONECT 2342 2341                                                                
CONECT 2343 2340 2341                                                           
CONECT 2344 2341                                                                
CONECT 2345 2346 2347 2348 2352                                                 
CONECT 2346 2340 2345                                                           
CONECT 2347 2345                                                                
CONECT 2348 2341 2345                                                           
CONECT 2349 2350 2351 2352 2353                                                 
CONECT 2350 2349                                                                
CONECT 2351 2340 2349                                                           
CONECT 2352 2345 2349                                                           
CONECT 2353 2349 2354                                                           
CONECT 2354 2353 2355                                                           
CONECT 2355 2354 2356 2357                                                      
CONECT 2356 2355 2361                                                           
CONECT 2357 2355 2358 2359                                                      
CONECT 2358 2357                                                                
CONECT 2359 2357 2360 2361                                                      
CONECT 2360 2359                                                                
CONECT 2361 2356 2359 2362                                                      
CONECT 2362 2361 2363 2371                                                      
CONECT 2363 2362 2364                                                           
CONECT 2364 2363 2365                                                           
CONECT 2365 2364 2366 2371                                                      
CONECT 2366 2365 2367 2368                                                      
CONECT 2367 2366                                                                
CONECT 2368 2366 2369                                                           
CONECT 2369 2368 2370                                                           
CONECT 2370 2369 2371                                                           
CONECT 2371 2362 2365 2370                                                      
CONECT 2516 2340                                                                
MASTER      331    0    3   13    7    0    7    6 2515    1   40   23          
END                                                                             
