HEADER    TRANSFERASE                             17-DEC-98   1B38              
TITLE     HUMAN CYCLIN-DEPENDENT KINASE 2                                       
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 1B38    1       REMARK LINK                              
REVDAT   4   24-FEB-09 1B38    1       VERSN                                    
REVDAT   3   01-APR-03 1B38    1       JRNL                                     
REVDAT   2   22-DEC-99 1B38    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   23-DEC-98 1B38    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.    2.00 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) : 2.00                           
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             : 19547                          
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 10%                      
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.250                           
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            : 206                                     
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) : 0.016 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.042 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.046 ; 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) : 0.144 ; 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 1B38 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_1000008203.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.5                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18076                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.260                              
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): 2.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 10 MG/ML IN 10MM HEPES/HCL    
REMARK 280  PH7.4, 15MM NACL WELL BUFFER CONTAINING 50MM AMMONIUM ACETATE,      
REMARK 280  12% PEG 3350, 100MM HEPES/HCL PH 7.4                                
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       26.66650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.09500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.56100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.09500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.66650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.56100            
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A    15     O    GLY A   153              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   431     O    HOH A   489     2564     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  22   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A  22   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ILE A  35   CA  -  C   -  O   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TYR A 168   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    GLU A 172   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    TYR A 179   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 199   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 199   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    GLU A 208   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 214   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 217   CD  -  NE  -  CZ  ANGL. DEV. =  27.8 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    MET A 233   CA  -  CB  -  CG  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TYR A 236   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    PRO A 238   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A 245   CD  -  NE  -  CZ  ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    SER A 264   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ASN A 272   OD1 -  CG  -  ND2 ANGL. DEV. =  15.2 DEGREES          
REMARK 500    HIS A 295   CA  -  CB  -  CG  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    ARG A 297   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    LYS A  24        9.33    -62.27                                   
REMARK 500    LEU A  25      -43.27   -143.99                                   
REMARK 500    GLU A  73       53.28     29.35                                   
REMARK 500    ARG A 126      -20.78     89.85                                   
REMARK 500    HIS A 161       -4.68     62.34                                   
REMARK 500    SER A 181     -169.37   -102.31                                   
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         11.09                                           
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 100.5                                              
REMARK 620 3 ATP A 381   O2G  96.2  91.5                                        
REMARK 620 4 ATP A 381   O2A 172.9  84.4  88.7                                  
REMARK 620 5 ATP A 381   O1B  89.1 169.6  83.5  86.3                            
REMARK 620 6 HOH A 412   O    86.0  92.9 174.6  88.6  91.6                      
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  1B38 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   *206(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  SER A  120  1                                  20    
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  PHE A  286  5                                   3    
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  2.12  
LINK         OD2 ASP A 145                MG    MG A 382     1555   1555  2.02  
LINK         O2G ATP A 381                MG    MG A 382     1555   1555  2.16  
LINK         O2A ATP A 381                MG    MG A 382     1555   1555  2.12  
LINK         O1B ATP A 381                MG    MG A 382     1555   1555  2.13  
LINK        MG    MG A 382                 O   HOH A 412     1555   1555  2.09  
SITE     1 AC1  4 ASN A 132  ASP A 145  ATP A 381  HOH A 412                    
SITE     1 AC2 25 ILE A  10  GLU A  12  GLY A  13  THR A  14                    
SITE     2 AC2 25 GLY A  16  VAL A  18  ALA A  31  LYS A  33                    
SITE     3 AC2 25 VAL A  64  PHE A  80  GLU A  81  PHE A  82                    
SITE     4 AC2 25 LEU A  83  ASP A  86  ASP A 127  LYS A 129                    
SITE     5 AC2 25 GLN A 131  ASN A 132  LEU A 134  ASP A 145                    
SITE     6 AC2 25  MG A 382  HOH A 412  HOH A 414  HOH A 580                    
SITE     7 AC2 25 HOH A 585                                                     
CRYST1   53.333   71.122   72.190  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      0.018750  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013852        0.00000                         
HETATM    1  C   ACE A   0     -13.948  32.824  -3.419  1.00 48.44           C  
HETATM    2  O   ACE A   0     -12.734  33.456  -3.978  1.00 46.48           O  
HETATM    3  CH3 ACE A   0     -15.034  33.432  -3.317  1.00 51.81           C  
ATOM      4  N   MET A   1     -13.811  31.565  -3.020  1.00 46.72           N  
ATOM      5  CA  MET A   1     -12.746  30.700  -3.438  1.00 46.67           C  
ATOM      6  C   MET A   1     -12.341  30.709  -4.893  1.00 46.10           C  
ATOM      7  O   MET A   1     -11.126  30.557  -5.194  1.00 46.62           O  
ATOM      8  CB  MET A   1     -13.145  29.275  -2.988  1.00 47.35           C  
ATOM      9  CG  MET A   1     -13.116  29.175  -1.475  1.00 47.41           C  
ATOM     10  SD  MET A   1     -11.596  29.920  -0.844  1.00 49.54           S  
ATOM     11  CE  MET A   1     -12.164  31.573  -0.421  1.00 47.90           C  
ATOM     12  N   GLU A   2     -13.142  31.008  -5.900  1.00 44.97           N  
ATOM     13  CA  GLU A   2     -12.723  31.063  -7.281  1.00 44.54           C  
ATOM     14  C   GLU A   2     -11.590  32.046  -7.540  1.00 43.71           C  
ATOM     15  O   GLU A   2     -11.019  31.995  -8.644  1.00 43.33           O  
ATOM     16  CB  GLU A   2     -13.894  31.513  -8.189  1.00 47.52           C  
ATOM     17  CG  GLU A   2     -14.632  32.722  -7.633  1.00 51.42           C  
ATOM     18  CD  GLU A   2     -15.885  32.361  -6.847  1.00 53.64           C  
ATOM     19  OE1 GLU A   2     -16.201  31.136  -6.782  1.00 54.63           O  
ATOM     20  OE2 GLU A   2     -16.544  33.298  -6.322  1.00 53.19           O  
ATOM     21  N   ASN A   3     -11.327  33.000  -6.654  1.00 39.87           N  
ATOM     22  CA  ASN A   3     -10.324  34.007  -6.750  1.00 38.41           C  
ATOM     23  C   ASN A   3      -8.940  33.511  -6.297  1.00 36.32           C  
ATOM     24  O   ASN A   3      -7.929  34.186  -6.539  1.00 35.68           O  
ATOM     25  CB  ASN A   3     -10.713  35.217  -5.883  1.00 39.37           C  
ATOM     26  CG  ASN A   3     -11.991  35.944  -6.231  1.00 40.18           C  
ATOM     27  OD1 ASN A   3     -13.032  35.727  -5.595  1.00 40.77           O  
ATOM     28  ND2 ASN A   3     -11.969  36.894  -7.163  1.00 38.41           N  
ATOM     29  N   PHE A   4      -8.831  32.336  -5.737  1.00 33.23           N  
ATOM     30  CA  PHE A   4      -7.669  31.689  -5.245  1.00 32.88           C  
ATOM     31  C   PHE A   4      -7.292  30.386  -5.944  1.00 35.95           C  
ATOM     32  O   PHE A   4      -8.098  29.465  -6.120  1.00 37.39           O  
ATOM     33  CB  PHE A   4      -7.850  31.294  -3.734  1.00 29.90           C  
ATOM     34  CG  PHE A   4      -8.012  32.561  -2.934  1.00 29.49           C  
ATOM     35  CD1 PHE A   4      -6.932  33.354  -2.634  1.00 28.14           C  
ATOM     36  CD2 PHE A   4      -9.278  32.976  -2.552  1.00 27.88           C  
ATOM     37  CE1 PHE A   4      -7.069  34.536  -1.931  1.00 29.47           C  
ATOM     38  CE2 PHE A   4      -9.440  34.177  -1.901  1.00 28.36           C  
ATOM     39  CZ  PHE A   4      -8.348  34.973  -1.583  1.00 29.82           C  
ATOM     40  N   GLN A   5      -5.992  30.226  -6.185  1.00 37.31           N  
ATOM     41  CA  GLN A   5      -5.493  28.963  -6.728  1.00 38.40           C  
ATOM     42  C   GLN A   5      -4.729  28.227  -5.629  1.00 35.74           C  
ATOM     43  O   GLN A   5      -3.699  28.750  -5.194  1.00 33.67           O  
ATOM     44  CB  GLN A   5      -4.528  29.199  -7.890  1.00 42.58           C  
ATOM     45  CG  GLN A   5      -4.228  27.979  -8.749  1.00 48.39           C  
ATOM     46  CD  GLN A   5      -5.130  27.988  -9.991  1.00 53.22           C  
ATOM     47  OE1 GLN A   5      -5.468  29.069 -10.520  1.00 55.03           O  
ATOM     48  NE2 GLN A   5      -5.526  26.811 -10.491  1.00 54.61           N  
ATOM     49  N   LYS A   6      -5.201  27.063  -5.225  1.00 35.83           N  
ATOM     50  CA  LYS A   6      -4.486  26.258  -4.245  1.00 38.34           C  
ATOM     51  C   LYS A   6      -3.124  25.815  -4.774  1.00 40.94           C  
ATOM     52  O   LYS A   6      -3.098  25.027  -5.741  1.00 41.23           O  
ATOM     53  CB  LYS A   6      -5.260  25.007  -3.849  1.00 39.58           C  
ATOM     54  CG  LYS A   6      -6.216  25.231  -2.668  1.00 42.29           C  
ATOM     55  CD  LYS A   6      -6.835  23.912  -2.223  1.00 43.62           C  
ATOM     56  CE  LYS A   6      -8.316  23.771  -2.516  1.00 45.48           C  
ATOM     57  NZ  LYS A   6      -9.067  24.823  -1.751  1.00 47.73           N  
ATOM     58  N   VAL A   7      -2.016  26.303  -4.221  1.00 40.35           N  
ATOM     59  CA  VAL A   7      -0.681  25.885  -4.652  1.00 39.06           C  
ATOM     60  C   VAL A   7      -0.303  24.550  -4.000  1.00 39.24           C  
ATOM     61  O   VAL A   7       0.386  23.696  -4.578  1.00 39.02           O  
ATOM     62  CB  VAL A   7       0.394  26.933  -4.246  1.00 38.76           C  
ATOM     63  CG1 VAL A   7       1.833  26.418  -4.435  1.00 36.56           C  
ATOM     64  CG2 VAL A   7       0.150  28.232  -5.002  1.00 36.88           C  
ATOM     65  N   GLU A   8      -0.563  24.419  -2.710  1.00 37.51           N  
ATOM     66  CA  GLU A   8      -0.224  23.211  -1.969  1.00 37.33           C  
ATOM     67  C   GLU A   8      -0.872  23.232  -0.581  1.00 36.54           C  
ATOM     68  O   GLU A   8      -1.221  24.268  -0.026  1.00 33.88           O  
ATOM     69  CB  GLU A   8       1.283  23.081  -1.792  1.00 39.66           C  
ATOM     70  CG  GLU A   8       1.849  24.028  -0.730  1.00 43.90           C  
ATOM     71  CD  GLU A   8       3.359  23.976  -0.664  1.00 47.30           C  
ATOM     72  OE1 GLU A   8       3.951  23.825  -1.753  1.00 47.83           O  
ATOM     73  OE2 GLU A   8       3.948  24.081   0.450  1.00 49.83           O  
ATOM     74  N   LYS A   9      -0.952  22.044  -0.004  1.00 36.59           N  
ATOM     75  CA  LYS A   9      -1.455  21.788   1.327  1.00 37.61           C  
ATOM     76  C   LYS A   9      -0.281  21.966   2.299  1.00 39.10           C  
ATOM     77  O   LYS A   9       0.779  21.316   2.135  1.00 38.76           O  
ATOM     78  CB  LYS A   9      -2.037  20.377   1.421  1.00 39.90           C  
ATOM     79  CG  LYS A   9      -2.884  20.215   2.674  1.00 42.05           C  
ATOM     80  CD  LYS A   9      -3.435  18.802   2.847  1.00 43.07           C  
ATOM     81  CE  LYS A   9      -3.751  18.562   4.314  1.00 45.10           C  
ATOM     82  NZ  LYS A   9      -4.700  17.419   4.501  1.00 46.23           N  
ATOM     83  N   ILE A  10      -0.421  22.951   3.188  1.00 35.75           N  
ATOM     84  CA  ILE A  10       0.668  23.242   4.119  1.00 34.73           C  
ATOM     85  C   ILE A  10       0.476  22.297   5.303  1.00 35.49           C  
ATOM     86  O   ILE A  10       1.491  21.808   5.809  1.00 39.89           O  
ATOM     87  CB  ILE A  10       0.725  24.668   4.679  1.00 31.45           C  
ATOM     88  CG1 ILE A  10       0.890  25.704   3.592  1.00 30.37           C  
ATOM     89  CG2 ILE A  10       1.828  24.821   5.747  1.00 31.18           C  
ATOM     90  CD1 ILE A  10       0.652  27.145   4.008  1.00 26.48           C  
ATOM     91  N   GLY A  11      -0.751  22.170   5.799  1.00 33.96           N  
ATOM     92  CA  GLY A  11      -0.925  21.271   6.958  1.00 34.23           C  
ATOM     93  C   GLY A  11      -2.385  21.347   7.361  1.00 34.49           C  
ATOM     94  O   GLY A  11      -3.180  21.956   6.638  1.00 35.66           O  
ATOM     95  N   GLU A  12      -2.717  20.795   8.506  1.00 34.89           N  
ATOM     96  CA  GLU A  12      -4.085  20.791   8.967  1.00 37.91           C  
ATOM     97  C   GLU A  12      -3.995  20.907  10.472  1.00 37.63           C  
ATOM     98  O   GLU A  12      -2.977  20.467  11.016  1.00 38.19           O  
ATOM     99  CB  GLU A  12      -4.809  19.538   8.498  1.00 40.15           C  
ATOM    100  CG  GLU A  12      -4.118  18.282   9.003  1.00 44.76           C  
ATOM    101  CD  GLU A  12      -4.221  17.068   8.083  1.00 47.91           C  
ATOM    102  OE1 GLU A  12      -4.646  17.186   6.898  1.00 49.29           O  
ATOM    103  OE2 GLU A  12      -3.851  15.981   8.612  1.00 48.37           O  
ATOM    104  N   GLY A  13      -5.008  21.510  11.078  1.00 36.80           N  
ATOM    105  CA  GLY A  13      -4.891  21.667  12.519  1.00 35.66           C  
ATOM    106  C   GLY A  13      -6.173  21.441  13.279  1.00 35.36           C  
ATOM    107  O   GLY A  13      -7.014  20.613  12.959  1.00 33.01           O  
ATOM    108  N   THR A  14      -6.304  22.289  14.303  1.00 35.48           N  
ATOM    109  CA  THR A  14      -7.432  22.208  15.197  1.00 37.81           C  
ATOM    110  C   THR A  14      -8.739  22.425  14.449  1.00 37.53           C  
ATOM    111  O   THR A  14      -9.638  21.608  14.539  1.00 38.24           O  
ATOM    112  CB  THR A  14      -7.327  23.237  16.354  1.00 39.03           C  
ATOM    113  OG1 THR A  14      -6.102  23.007  17.069  1.00 39.93           O  
ATOM    114  CG2 THR A  14      -8.491  23.078  17.333  1.00 39.40           C  
ATOM    115  N   TYR A  15      -8.793  23.533  13.718  1.00 37.27           N  
ATOM    116  CA  TYR A  15     -10.015  23.950  13.066  1.00 37.79           C  
ATOM    117  C   TYR A  15     -10.148  23.618  11.605  1.00 37.37           C  
ATOM    118  O   TYR A  15     -11.310  23.671  11.172  1.00 38.69           O  
ATOM    119  CB  TYR A  15     -10.188  25.473  13.244  1.00 39.72           C  
ATOM    120  CG  TYR A  15     -10.296  25.844  14.709  1.00 42.27           C  
ATOM    121  CD1 TYR A  15     -11.383  25.445  15.492  1.00 43.53           C  
ATOM    122  CD2 TYR A  15      -9.286  26.563  15.310  1.00 43.03           C  
ATOM    123  CE1 TYR A  15     -11.465  25.795  16.825  1.00 45.14           C  
ATOM    124  CE2 TYR A  15      -9.334  26.901  16.645  1.00 44.17           C  
ATOM    125  CZ  TYR A  15     -10.430  26.526  17.387  1.00 46.76           C  
ATOM    126  OH  TYR A  15     -10.467  26.907  18.731  1.00 49.05           O  
ATOM    127  N   GLY A  16      -9.067  23.301  10.897  1.00 34.10           N  
ATOM    128  CA  GLY A  16      -9.259  22.971   9.498  1.00 31.10           C  
ATOM    129  C   GLY A  16      -7.943  22.876   8.754  1.00 29.82           C  
ATOM    130  O   GLY A  16      -6.892  22.821   9.360  1.00 30.04           O  
ATOM    131  N   VAL A  17      -7.981  22.792   7.430  1.00 29.26           N  
ATOM    132  CA  VAL A  17      -6.773  22.588   6.647  1.00 28.08           C  
ATOM    133  C   VAL A  17      -6.213  23.909   6.145  1.00 26.94           C  
ATOM    134  O   VAL A  17      -7.007  24.810   5.897  1.00 28.40           O  
ATOM    135  CB  VAL A  17      -7.104  21.615   5.514  1.00 28.74           C  
ATOM    136  CG1 VAL A  17      -8.176  22.298   4.642  1.00 32.16           C  
ATOM    137  CG2 VAL A  17      -5.919  21.246   4.667  1.00 28.32           C  
ATOM    138  N   VAL A  18      -4.899  24.011   5.982  1.00 26.00           N  
ATOM    139  CA  VAL A  18      -4.297  25.277   5.540  1.00 25.12           C  
ATOM    140  C   VAL A  18      -3.596  25.000   4.212  1.00 25.52           C  
ATOM    141  O   VAL A  18      -2.776  24.066   4.064  1.00 21.89           O  
ATOM    142  CB  VAL A  18      -3.212  25.787   6.489  1.00 26.75           C  
ATOM    143  CG1 VAL A  18      -2.513  27.048   5.918  1.00 24.19           C  
ATOM    144  CG2 VAL A  18      -3.643  26.072   7.917  1.00 24.82           C  
ATOM    145  N   TYR A  19      -3.929  25.865   3.270  1.00 24.75           N  
ATOM    146  CA  TYR A  19      -3.286  25.789   1.970  1.00 24.34           C  
ATOM    147  C   TYR A  19      -2.464  27.044   1.639  1.00 20.40           C  
ATOM    148  O   TYR A  19      -2.871  28.168   1.909  1.00 19.90           O  
ATOM    149  CB  TYR A  19      -4.301  25.622   0.821  1.00 28.62           C  
ATOM    150  CG  TYR A  19      -5.169  24.363   0.911  1.00 33.48           C  
ATOM    151  CD1 TYR A  19      -6.323  24.396   1.662  1.00 36.28           C  
ATOM    152  CD2 TYR A  19      -4.862  23.199   0.250  1.00 34.25           C  
ATOM    153  CE1 TYR A  19      -7.149  23.277   1.749  1.00 40.97           C  
ATOM    154  CE2 TYR A  19      -5.665  22.085   0.324  1.00 38.26           C  
ATOM    155  CZ  TYR A  19      -6.800  22.118   1.090  1.00 40.21           C  
ATOM    156  OH  TYR A  19      -7.650  21.027   1.188  1.00 44.37           O  
ATOM    157  N   LYS A  20      -1.370  26.829   0.923  1.00 16.90           N  
ATOM    158  CA  LYS A  20      -0.665  27.916   0.292  1.00 19.11           C  
ATOM    159  C   LYS A  20      -1.506  28.246  -0.963  1.00 20.27           C  
ATOM    160  O   LYS A  20      -1.866  27.305  -1.665  1.00 20.01           O  
ATOM    161  CB  LYS A  20       0.755  27.537  -0.149  1.00 17.15           C  
ATOM    162  CG  LYS A  20       1.594  28.716  -0.543  1.00 19.20           C  
ATOM    163  CD  LYS A  20       3.062  28.362  -0.866  1.00 19.77           C  
ATOM    164  CE  LYS A  20       3.848  29.617  -1.267  1.00 21.01           C  
ATOM    165  NZ  LYS A  20       5.314  29.252  -1.534  1.00 20.71           N  
ATOM    166  N   ALA A  21      -1.884  29.493  -1.235  1.00 20.58           N  
ATOM    167  CA  ALA A  21      -2.749  29.718  -2.398  1.00 22.24           C  
ATOM    168  C   ALA A  21      -2.308  31.013  -3.057  1.00 23.36           C  
ATOM    169  O   ALA A  21      -1.614  31.745  -2.371  1.00 22.65           O  
ATOM    170  CB  ALA A  21      -4.224  29.833  -2.025  1.00 23.87           C  
ATOM    171  N   ARG A  22      -2.716  31.234  -4.296  1.00 27.00           N  
ATOM    172  CA  ARG A  22      -2.393  32.483  -4.980  1.00 30.03           C  
ATOM    173  C   ARG A  22      -3.677  33.240  -5.325  1.00 31.24           C  
ATOM    174  O   ARG A  22      -4.660  32.699  -5.836  1.00 31.90           O  
ATOM    175  CB  ARG A  22      -1.497  32.288  -6.218  1.00 30.72           C  
ATOM    176  CG  ARG A  22      -1.204  33.643  -6.879  1.00 35.96           C  
ATOM    177  CD  ARG A  22      -0.539  33.500  -8.273  1.00 38.44           C  
ATOM    178  NE  ARG A  22       0.519  32.502  -8.036  1.00 41.75           N  
ATOM    179  CZ  ARG A  22       1.686  32.894  -7.521  1.00 41.51           C  
ATOM    180  NH1 ARG A  22       1.847  34.206  -7.345  1.00 40.84           N  
ATOM    181  NH2 ARG A  22       2.545  31.904  -7.307  1.00 41.39           N  
ATOM    182  N   ASN A  23      -3.714  34.500  -4.970  1.00 33.57           N  
ATOM    183  CA  ASN A  23      -4.843  35.343  -5.345  1.00 41.19           C  
ATOM    184  C   ASN A  23      -4.821  35.540  -6.866  1.00 43.71           C  
ATOM    185  O   ASN A  23      -3.990  36.206  -7.454  1.00 42.91           O  
ATOM    186  CB  ASN A  23      -4.830  36.699  -4.637  1.00 42.95           C  
ATOM    187  CG  ASN A  23      -6.137  37.435  -4.984  1.00 45.38           C  
ATOM    188  OD1 ASN A  23      -6.405  37.628  -6.184  1.00 47.51           O  
ATOM    189  ND2 ASN A  23      -6.915  37.749  -3.958  1.00 43.78           N  
ATOM    190  N   LYS A  24      -5.776  34.939  -7.561  1.00 49.50           N  
ATOM    191  CA  LYS A  24      -5.989  34.991  -9.000  1.00 52.39           C  
ATOM    192  C   LYS A  24      -6.291  36.390  -9.542  1.00 53.90           C  
ATOM    193  O   LYS A  24      -6.680  36.434 -10.711  1.00 55.65           O  
ATOM    194  CB  LYS A  24      -7.179  34.140  -9.448  1.00 51.54           C  
ATOM    195  CG  LYS A  24      -7.014  32.674  -9.705  1.00 53.26           C  
ATOM    196  CD  LYS A  24      -8.338  32.000 -10.049  1.00 53.56           C  
ATOM    197  CE  LYS A  24      -8.333  30.546  -9.627  1.00 54.54           C  
ATOM    198  NZ  LYS A  24      -9.667  29.933  -9.392  1.00 54.63           N  
ATOM    199  N   LEU A  25      -6.181  37.487  -8.816  1.00 55.30           N  
ATOM    200  CA  LEU A  25      -6.446  38.830  -9.328  1.00 56.66           C  
ATOM    201  C   LEU A  25      -5.479  39.833  -8.706  1.00 57.78           C  
ATOM    202  O   LEU A  25      -4.889  40.667  -9.419  1.00 58.47           O  
ATOM    203  CB  LEU A  25      -7.919  39.159  -9.165  1.00 56.61           C  
ATOM    204  CG  LEU A  25      -8.503  40.494  -8.763  1.00 56.83           C  
ATOM    205  CD1 LEU A  25      -8.520  41.543  -9.863  1.00 55.43           C  
ATOM    206  CD2 LEU A  25      -9.930  40.273  -8.239  1.00 55.99           C  
ATOM    207  N   THR A  26      -5.240  39.736  -7.399  1.00 55.95           N  
ATOM    208  CA  THR A  26      -4.260  40.588  -6.734  1.00 55.20           C  
ATOM    209  C   THR A  26      -2.859  40.064  -7.011  1.00 52.36           C  
ATOM    210  O   THR A  26      -1.841  40.751  -6.878  1.00 52.97           O  
ATOM    211  CB  THR A  26      -4.595  40.714  -5.235  1.00 57.03           C  
ATOM    212  OG1 THR A  26      -5.359  41.907  -4.919  1.00 57.66           O  
ATOM    213  CG2 THR A  26      -3.443  40.831  -4.261  1.00 56.69           C  
ATOM    214  N   GLY A  27      -2.684  38.808  -7.382  1.00 50.18           N  
ATOM    215  CA  GLY A  27      -1.407  38.142  -7.587  1.00 45.33           C  
ATOM    216  C   GLY A  27      -0.774  37.660  -6.265  1.00 41.74           C  
ATOM    217  O   GLY A  27       0.103  36.790  -6.223  1.00 42.55           O  
ATOM    218  N   GLU A  28      -1.195  38.145  -5.121  1.00 36.94           N  
ATOM    219  CA  GLU A  28      -0.729  37.800  -3.795  1.00 34.28           C  
ATOM    220  C   GLU A  28      -0.707  36.317  -3.443  1.00 28.90           C  
ATOM    221  O   GLU A  28      -1.510  35.449  -3.790  1.00 27.45           O  
ATOM    222  CB  GLU A  28      -1.678  38.567  -2.868  1.00 35.91           C  
ATOM    223  CG  GLU A  28      -1.221  39.057  -1.537  1.00 38.98           C  
ATOM    224  CD  GLU A  28      -2.336  39.782  -0.789  1.00 41.59           C  
ATOM    225  OE1 GLU A  28      -3.488  39.731  -1.298  1.00 43.43           O  
ATOM    226  OE2 GLU A  28      -2.042  40.380   0.278  1.00 41.43           O  
ATOM    227  N   VAL A  29       0.371  35.896  -2.800  1.00 27.05           N  
ATOM    228  CA  VAL A  29       0.578  34.521  -2.310  1.00 24.55           C  
ATOM    229  C   VAL A  29       0.186  34.567  -0.833  1.00 23.90           C  
ATOM    230  O   VAL A  29       0.478  35.530  -0.122  1.00 23.60           O  
ATOM    231  CB  VAL A  29       1.937  33.938  -2.587  1.00 26.80           C  
ATOM    232  CG1 VAL A  29       2.205  32.751  -1.639  1.00 27.93           C  
ATOM    233  CG2 VAL A  29       1.978  33.376  -4.010  1.00 28.50           C  
ATOM    234  N   VAL A  30      -0.754  33.704  -0.463  1.00 22.31           N  
ATOM    235  CA  VAL A  30      -1.417  33.776   0.844  1.00 18.42           C  
ATOM    236  C   VAL A  30      -1.508  32.370   1.462  1.00 18.96           C  
ATOM    237  O   VAL A  30      -1.249  31.342   0.836  1.00 17.13           O  
ATOM    238  CB  VAL A  30      -2.823  34.353   0.739  1.00 17.71           C  
ATOM    239  CG1 VAL A  30      -2.943  35.665  -0.098  1.00 17.66           C  
ATOM    240  CG2 VAL A  30      -3.823  33.379   0.114  1.00 17.58           C  
ATOM    241  N   ALA A  31      -1.943  32.333   2.723  1.00 19.59           N  
ATOM    242  CA  ALA A  31      -2.211  31.055   3.383  1.00 19.35           C  
ATOM    243  C   ALA A  31      -3.726  31.064   3.609  1.00 20.98           C  
ATOM    244  O   ALA A  31      -4.354  31.922   4.206  1.00 21.41           O  
ATOM    245  CB  ALA A  31      -1.388  31.036   4.678  1.00 21.48           C  
ATOM    246  N   LEU A  32      -4.414  30.059   3.129  1.00 21.72           N  
ATOM    247  CA  LEU A  32      -5.860  29.974   3.126  1.00 21.46           C  
ATOM    248  C   LEU A  32      -6.333  28.923   4.120  1.00 21.10           C  
ATOM    249  O   LEU A  32      -5.900  27.805   3.856  1.00 19.44           O  
ATOM    250  CB  LEU A  32      -6.274  29.516   1.736  1.00 24.00           C  
ATOM    251  CG  LEU A  32      -7.099  30.418   0.828  1.00 30.07           C  
ATOM    252  CD1 LEU A  32      -7.713  29.512  -0.225  1.00 28.69           C  
ATOM    253  CD2 LEU A  32      -8.238  31.132   1.563  1.00 31.51           C  
ATOM    254  N   LYS A  33      -7.042  29.320   5.179  1.00 20.72           N  
ATOM    255  CA  LYS A  33      -7.458  28.261   6.099  1.00 23.32           C  
ATOM    256  C   LYS A  33      -8.939  27.987   5.922  1.00 22.81           C  
ATOM    257  O   LYS A  33      -9.770  28.876   6.069  1.00 24.46           O  
ATOM    258  CB  LYS A  33      -7.106  28.605   7.545  1.00 25.91           C  
ATOM    259  CG  LYS A  33      -7.604  27.538   8.516  1.00 27.20           C  
ATOM    260  CD  LYS A  33      -7.181  27.777   9.952  1.00 30.97           C  
ATOM    261  CE  LYS A  33      -5.669  27.635  10.132  1.00 32.54           C  
ATOM    262  NZ  LYS A  33      -5.388  27.850  11.581  1.00 34.03           N  
ATOM    263  N   LYS A  34      -9.316  26.778   5.593  1.00 25.38           N  
ATOM    264  CA  LYS A  34     -10.737  26.419   5.472  1.00 29.97           C  
ATOM    265  C   LYS A  34     -11.208  25.870   6.816  1.00 30.00           C  
ATOM    266  O   LYS A  34     -10.583  24.918   7.288  1.00 32.82           O  
ATOM    267  CB  LYS A  34     -10.933  25.400   4.342  1.00 34.67           C  
ATOM    268  CG  LYS A  34     -12.452  25.038   4.268  1.00 39.00           C  
ATOM    269  CD  LYS A  34     -12.647  23.908   3.270  1.00 42.76           C  
ATOM    270  CE  LYS A  34     -13.824  23.014   3.683  1.00 45.11           C  
ATOM    271  NZ  LYS A  34     -13.487  21.584   3.382  1.00 46.60           N  
ATOM    272  N   ILE A  35     -12.172  26.445   7.503  1.00 29.12           N  
ATOM    273  CA  ILE A  35     -12.530  26.059   8.859  1.00 32.56           C  
ATOM    274  C   ILE A  35     -13.592  24.946   8.863  1.00 33.92           C  
ATOM    275  O   ILE A  35     -14.383  25.189   7.917  1.00 35.86           O  
ATOM    276  CB  ILE A  35     -13.085  27.284   9.598  1.00 31.94           C  
ATOM    277  CG1 ILE A  35     -12.044  28.397   9.717  1.00 30.19           C  
ATOM    278  CG2 ILE A  35     -13.672  26.893  10.949  1.00 33.24           C  
ATOM    279  CD1 ILE A  35     -10.746  28.067  10.406  1.00 29.12           C  
ATOM    280  N   VAL A  44     -21.912  29.172   9.354  1.00 49.29           N  
ATOM    281  CA  VAL A  44     -21.065  29.584  10.468  1.00 52.00           C  
ATOM    282  C   VAL A  44     -21.836  30.359  11.534  1.00 52.92           C  
ATOM    283  O   VAL A  44     -22.547  31.337  11.271  1.00 53.61           O  
ATOM    284  CB  VAL A  44     -19.883  30.464  10.019  1.00 52.57           C  
ATOM    285  CG1 VAL A  44     -19.304  31.363  11.096  1.00 54.08           C  
ATOM    286  CG2 VAL A  44     -18.762  29.612   9.454  1.00 52.79           C  
ATOM    287  N   PRO A  45     -21.577  29.979  12.780  1.00 53.52           N  
ATOM    288  CA  PRO A  45     -22.201  30.617  13.915  1.00 51.92           C  
ATOM    289  C   PRO A  45     -21.915  32.102  13.897  1.00 51.61           C  
ATOM    290  O   PRO A  45     -20.817  32.592  13.619  1.00 51.45           O  
ATOM    291  CB  PRO A  45     -21.622  29.910  15.132  1.00 53.98           C  
ATOM    292  CG  PRO A  45     -20.523  29.011  14.663  1.00 54.01           C  
ATOM    293  CD  PRO A  45     -20.700  28.836  13.177  1.00 53.83           C  
ATOM    294  N   SER A  46     -22.940  32.872  14.230  1.00 51.05           N  
ATOM    295  CA  SER A  46     -22.929  34.308  14.361  1.00 49.74           C  
ATOM    296  C   SER A  46     -21.808  34.914  15.183  1.00 48.23           C  
ATOM    297  O   SER A  46     -21.147  35.894  14.807  1.00 47.08           O  
ATOM    298  CB  SER A  46     -24.196  34.673  15.177  1.00 52.15           C  
ATOM    299  OG  SER A  46     -24.260  36.087  15.358  1.00 54.15           O  
ATOM    300  N   THR A  47     -21.694  34.404  16.427  1.00 46.44           N  
ATOM    301  CA  THR A  47     -20.700  34.970  17.349  1.00 44.81           C  
ATOM    302  C   THR A  47     -19.288  34.816  16.810  1.00 41.19           C  
ATOM    303  O   THR A  47     -18.506  35.771  16.946  1.00 40.17           O  
ATOM    304  CB  THR A  47     -20.909  34.433  18.768  1.00 47.95           C  
ATOM    305  OG1 THR A  47     -20.142  35.206  19.717  1.00 50.60           O  
ATOM    306  CG2 THR A  47     -20.480  32.971  18.850  1.00 49.25           C  
ATOM    307  N   ALA A  48     -18.959  33.741  16.119  1.00 37.44           N  
ATOM    308  CA  ALA A  48     -17.652  33.544  15.524  1.00 35.60           C  
ATOM    309  C   ALA A  48     -17.385  34.511  14.367  1.00 35.56           C  
ATOM    310  O   ALA A  48     -16.279  35.074  14.347  1.00 33.27           O  
ATOM    311  CB  ALA A  48     -17.483  32.126  15.012  1.00 36.61           C  
ATOM    312  N   ILE A  49     -18.389  34.760  13.504  1.00 34.11           N  
ATOM    313  CA  ILE A  49     -18.167  35.705  12.405  1.00 34.63           C  
ATOM    314  C   ILE A  49     -17.809  37.084  12.940  1.00 32.50           C  
ATOM    315  O   ILE A  49     -16.935  37.825  12.491  1.00 31.03           O  
ATOM    316  CB  ILE A  49     -19.382  35.824  11.458  1.00 34.93           C  
ATOM    317  CG1 ILE A  49     -19.599  34.604  10.563  1.00 34.56           C  
ATOM    318  CG2 ILE A  49     -19.224  37.019  10.491  1.00 36.70           C  
ATOM    319  CD1 ILE A  49     -18.504  34.344   9.541  1.00 33.98           C  
ATOM    320  N   ARG A  50     -18.533  37.466  13.970  1.00 32.44           N  
ATOM    321  CA  ARG A  50     -18.337  38.774  14.574  1.00 35.03           C  
ATOM    322  C   ARG A  50     -16.968  38.884  15.218  1.00 35.27           C  
ATOM    323  O   ARG A  50     -16.216  39.829  15.019  1.00 36.89           O  
ATOM    324  CB  ARG A  50     -19.465  38.981  15.568  1.00 36.06           C  
ATOM    325  CG  ARG A  50     -20.701  39.493  14.793  1.00 39.02           C  
ATOM    326  CD  ARG A  50     -21.705  40.140  15.732  1.00 38.25           C  
ATOM    327  NE  ARG A  50     -23.086  39.876  15.322  1.00 38.38           N  
ATOM    328  CZ  ARG A  50     -23.835  38.873  15.786  1.00 39.25           C  
ATOM    329  NH1 ARG A  50     -23.290  38.011  16.686  1.00 39.76           N  
ATOM    330  NH2 ARG A  50     -25.096  38.750  15.361  1.00 33.79           N  
ATOM    331  N   GLU A  51     -16.648  37.833  15.946  1.00 33.48           N  
ATOM    332  CA  GLU A  51     -15.366  37.749  16.635  1.00 35.18           C  
ATOM    333  C   GLU A  51     -14.227  37.709  15.631  1.00 32.40           C  
ATOM    334  O   GLU A  51     -13.210  38.357  15.865  1.00 30.34           O  
ATOM    335  CB  GLU A  51     -15.432  36.469  17.468  1.00 37.48           C  
ATOM    336  CG  GLU A  51     -14.374  36.310  18.541  1.00 43.58           C  
ATOM    337  CD  GLU A  51     -14.681  37.251  19.698  1.00 45.81           C  
ATOM    338  OE1 GLU A  51     -14.547  38.458  19.431  1.00 47.50           O  
ATOM    339  OE2 GLU A  51     -15.046  36.804  20.800  1.00 47.42           O  
ATOM    340  N   ILE A  52     -14.359  36.932  14.558  1.00 31.62           N  
ATOM    341  CA  ILE A  52     -13.255  36.841  13.592  1.00 34.70           C  
ATOM    342  C   ILE A  52     -13.103  38.207  12.936  1.00 34.60           C  
ATOM    343  O   ILE A  52     -11.984  38.725  12.881  1.00 32.69           O  
ATOM    344  CB  ILE A  52     -13.368  35.762  12.518  1.00 36.96           C  
ATOM    345  CG1 ILE A  52     -13.602  34.343  13.096  1.00 38.60           C  
ATOM    346  CG2 ILE A  52     -12.089  35.595  11.693  1.00 37.99           C  
ATOM    347  CD1 ILE A  52     -12.502  33.894  14.042  1.00 37.87           C  
ATOM    348  N   SER A  53     -14.230  38.894  12.696  1.00 35.25           N  
ATOM    349  CA  SER A  53     -14.167  40.205  12.030  1.00 36.59           C  
ATOM    350  C   SER A  53     -13.439  41.221  12.852  1.00 37.74           C  
ATOM    351  O   SER A  53     -12.678  41.988  12.272  1.00 41.02           O  
ATOM    352  CB  SER A  53     -15.580  40.637  11.575  1.00 36.43           C  
ATOM    353  OG  SER A  53     -16.012  39.587  10.691  1.00 36.11           O  
ATOM    354  N   LEU A  54     -13.508  41.200  14.187  1.00 38.87           N  
ATOM    355  CA  LEU A  54     -12.706  42.166  14.948  1.00 40.25           C  
ATOM    356  C   LEU A  54     -11.206  41.868  14.863  1.00 38.26           C  
ATOM    357  O   LEU A  54     -10.332  42.764  14.912  1.00 36.18           O  
ATOM    358  CB  LEU A  54     -13.326  42.250  16.345  1.00 42.81           C  
ATOM    359  CG  LEU A  54     -14.845  41.959  16.398  1.00 46.45           C  
ATOM    360  CD1 LEU A  54     -15.524  42.210  17.745  1.00 45.06           C  
ATOM    361  CD2 LEU A  54     -15.634  42.799  15.382  1.00 46.90           C  
ATOM    362  N   LEU A  55     -10.801  40.615  14.555  1.00 34.10           N  
ATOM    363  CA  LEU A  55      -9.391  40.279  14.453  1.00 29.57           C  
ATOM    364  C   LEU A  55      -8.722  40.987  13.279  1.00 28.15           C  
ATOM    365  O   LEU A  55      -7.529  41.267  13.398  1.00 26.57           O  
ATOM    366  CB  LEU A  55      -9.114  38.775  14.281  1.00 27.94           C  
ATOM    367  CG  LEU A  55      -9.675  37.932  15.382  1.00 29.42           C  
ATOM    368  CD1 LEU A  55      -9.255  36.469  15.209  1.00 29.62           C  
ATOM    369  CD2 LEU A  55      -9.207  38.503  16.715  1.00 28.92           C  
ATOM    370  N   LYS A  56      -9.486  41.285  12.260  1.00 26.31           N  
ATOM    371  CA  LYS A  56      -8.980  42.027  11.123  1.00 30.25           C  
ATOM    372  C   LYS A  56      -8.381  43.385  11.433  1.00 29.28           C  
ATOM    373  O   LYS A  56      -7.548  43.806  10.625  1.00 32.69           O  
ATOM    374  CB  LYS A  56     -10.052  42.251  10.041  1.00 30.30           C  
ATOM    375  CG  LYS A  56     -10.442  40.862   9.476  1.00 32.75           C  
ATOM    376  CD  LYS A  56     -11.223  41.044   8.186  1.00 34.69           C  
ATOM    377  CE  LYS A  56     -12.556  41.737   8.502  1.00 35.36           C  
ATOM    378  NZ  LYS A  56     -13.361  41.840   7.271  1.00 36.53           N  
ATOM    379  N   GLU A  57      -8.807  44.056  12.464  1.00 28.75           N  
ATOM    380  CA  GLU A  57      -8.263  45.338  12.858  1.00 30.08           C  
ATOM    381  C   GLU A  57      -7.150  45.212  13.892  1.00 28.09           C  
ATOM    382  O   GLU A  57      -6.423  46.156  14.186  1.00 26.09           O  
ATOM    383  CB  GLU A  57      -9.397  46.168  13.454  1.00 34.52           C  
ATOM    384  CG  GLU A  57     -10.688  46.140  12.651  1.00 39.74           C  
ATOM    385  CD  GLU A  57     -11.646  47.234  13.092  1.00 41.92           C  
ATOM    386  OE1 GLU A  57     -11.807  47.418  14.319  1.00 43.00           O  
ATOM    387  OE2 GLU A  57     -12.171  47.867  12.143  1.00 45.59           O  
ATOM    388  N   LEU A  58      -6.899  44.044  14.465  1.00 26.77           N  
ATOM    389  CA  LEU A  58      -5.792  43.884  15.410  1.00 24.45           C  
ATOM    390  C   LEU A  58      -4.521  43.616  14.606  1.00 22.82           C  
ATOM    391  O   LEU A  58      -4.025  42.475  14.496  1.00 22.76           O  
ATOM    392  CB  LEU A  58      -6.150  42.659  16.246  1.00 27.57           C  
ATOM    393  CG  LEU A  58      -5.300  42.190  17.406  1.00 30.17           C  
ATOM    394  CD1 LEU A  58      -5.585  43.099  18.583  1.00 29.19           C  
ATOM    395  CD2 LEU A  58      -5.586  40.734  17.798  1.00 31.51           C  
ATOM    396  N   ASN A  59      -3.927  44.642  14.069  1.00 18.59           N  
ATOM    397  CA  ASN A  59      -2.744  44.541  13.259  1.00 20.96           C  
ATOM    398  C   ASN A  59      -1.497  44.929  14.018  1.00 18.41           C  
ATOM    399  O   ASN A  59      -1.449  45.942  14.688  1.00 21.15           O  
ATOM    400  CB  ASN A  59      -2.863  45.475  12.041  1.00 21.91           C  
ATOM    401  CG  ASN A  59      -4.030  45.017  11.177  1.00 24.74           C  
ATOM    402  OD1 ASN A  59      -4.749  45.851  10.643  1.00 27.87           O  
ATOM    403  ND2 ASN A  59      -4.228  43.745  10.992  1.00 22.53           N  
ATOM    404  N   HIS A  60      -0.453  44.160  13.827  1.00 17.15           N  
ATOM    405  CA  HIS A  60       0.810  44.449  14.507  1.00 16.40           C  
ATOM    406  C   HIS A  60       1.809  43.652  13.721  1.00 16.15           C  
ATOM    407  O   HIS A  60       1.527  42.652  13.072  1.00 17.64           O  
ATOM    408  CB  HIS A  60       0.630  44.169  16.028  1.00 14.91           C  
ATOM    409  CG  HIS A  60       1.911  44.244  16.778  1.00 11.54           C  
ATOM    410  ND1 HIS A  60       2.305  45.284  17.650  1.00 16.10           N  
ATOM    411  CD2 HIS A  60       2.957  43.439  16.709  1.00 11.38           C  
ATOM    412  CE1 HIS A  60       3.519  45.106  18.064  1.00 13.38           C  
ATOM    413  NE2 HIS A  60       3.977  43.967  17.493  1.00 17.11           N  
ATOM    414  N   PRO A  61       3.046  44.147  13.603  1.00 17.71           N  
ATOM    415  CA  PRO A  61       4.060  43.473  12.795  1.00 19.09           C  
ATOM    416  C   PRO A  61       4.464  42.123  13.365  1.00 19.08           C  
ATOM    417  O   PRO A  61       5.099  41.346  12.666  1.00 16.67           O  
ATOM    418  CB  PRO A  61       5.258  44.415  12.808  1.00 19.56           C  
ATOM    419  CG  PRO A  61       4.978  45.408  13.847  1.00 20.34           C  
ATOM    420  CD  PRO A  61       3.467  45.483  14.061  1.00 15.93           C  
ATOM    421  N   ASN A  62       4.150  41.824  14.655  1.00 18.33           N  
ATOM    422  CA  ASN A  62       4.473  40.507  15.189  1.00 17.25           C  
ATOM    423  C   ASN A  62       3.219  39.677  15.307  1.00 16.46           C  
ATOM    424  O   ASN A  62       3.215  38.684  16.046  1.00 17.13           O  
ATOM    425  CB  ASN A  62       5.240  40.478  16.503  1.00 17.90           C  
ATOM    426  CG  ASN A  62       6.597  41.136  16.261  1.00 15.07           C  
ATOM    427  OD1 ASN A  62       6.688  42.249  16.686  1.00 17.28           O  
ATOM    428  ND2 ASN A  62       7.545  40.500  15.624  1.00 15.24           N  
ATOM    429  N   ILE A  63       2.180  40.074  14.547  1.00 17.73           N  
ATOM    430  CA  ILE A  63       0.945  39.275  14.475  1.00 17.81           C  
ATOM    431  C   ILE A  63       0.719  38.894  13.007  1.00 17.25           C  
ATOM    432  O   ILE A  63       0.743  39.835  12.228  1.00 16.38           O  
ATOM    433  CB  ILE A  63      -0.316  39.924  15.008  1.00 17.61           C  
ATOM    434  CG1 ILE A  63      -0.398  40.274  16.469  1.00 19.10           C  
ATOM    435  CG2 ILE A  63      -1.580  39.070  14.732  1.00 16.81           C  
ATOM    436  CD1 ILE A  63       0.273  39.291  17.386  1.00 24.32           C  
ATOM    437  N   VAL A  64       0.524  37.642  12.624  1.00 18.26           N  
ATOM    438  CA  VAL A  64       0.312  37.247  11.215  1.00 18.54           C  
ATOM    439  C   VAL A  64      -0.929  37.981  10.683  1.00 20.18           C  
ATOM    440  O   VAL A  64      -1.959  37.986  11.358  1.00 18.28           O  
ATOM    441  CB  VAL A  64       0.101  35.738  11.012  1.00 20.10           C  
ATOM    442  CG1 VAL A  64      -0.225  35.364   9.562  1.00 17.77           C  
ATOM    443  CG2 VAL A  64       1.362  34.959  11.344  1.00 16.32           C  
ATOM    444  N   LYS A  65      -0.794  38.718   9.574  1.00 18.83           N  
ATOM    445  CA  LYS A  65      -1.951  39.520   9.184  1.00 19.65           C  
ATOM    446  C   LYS A  65      -3.132  38.697   8.695  1.00 17.16           C  
ATOM    447  O   LYS A  65      -2.921  37.867   7.803  1.00 16.15           O  
ATOM    448  CB  LYS A  65      -1.581  40.517   8.048  1.00 23.65           C  
ATOM    449  CG  LYS A  65      -2.730  41.624   7.963  1.00 23.45           C  
ATOM    450  CD  LYS A  65      -2.095  42.623   6.991  1.00 29.08           C  
ATOM    451  CE  LYS A  65      -2.992  43.685   6.407  1.00 28.31           C  
ATOM    452  NZ  LYS A  65      -3.744  44.457   7.409  1.00 28.03           N  
ATOM    453  N   LEU A  66      -4.316  38.956   9.229  1.00 15.38           N  
ATOM    454  CA  LEU A  66      -5.547  38.388   8.730  1.00 17.76           C  
ATOM    455  C   LEU A  66      -6.001  39.291   7.535  1.00 19.20           C  
ATOM    456  O   LEU A  66      -6.448  40.417   7.706  1.00 17.28           O  
ATOM    457  CB  LEU A  66      -6.571  38.268   9.820  1.00 17.79           C  
ATOM    458  CG  LEU A  66      -8.018  37.858   9.437  1.00 20.42           C  
ATOM    459  CD1 LEU A  66      -8.053  36.461   8.829  1.00 20.07           C  
ATOM    460  CD2 LEU A  66      -8.919  37.870  10.671  1.00 21.27           C  
ATOM    461  N   LEU A  67      -5.744  38.889   6.280  1.00 20.96           N  
ATOM    462  CA  LEU A  67      -6.124  39.745   5.151  1.00 24.18           C  
ATOM    463  C   LEU A  67      -7.615  39.780   4.914  1.00 27.22           C  
ATOM    464  O   LEU A  67      -8.180  40.856   4.730  1.00 27.10           O  
ATOM    465  CB  LEU A  67      -5.401  39.429   3.845  1.00 22.63           C  
ATOM    466  CG  LEU A  67      -3.916  39.091   3.963  1.00 24.32           C  
ATOM    467  CD1 LEU A  67      -3.394  38.419   2.694  1.00 23.83           C  
ATOM    468  CD2 LEU A  67      -3.086  40.340   4.181  1.00 24.27           C  
ATOM    469  N   ASP A  68      -8.340  38.657   4.923  1.00 29.28           N  
ATOM    470  CA  ASP A  68      -9.766  38.691   4.623  1.00 29.19           C  
ATOM    471  C   ASP A  68     -10.458  37.447   5.181  1.00 27.99           C  
ATOM    472  O   ASP A  68      -9.785  36.464   5.476  1.00 24.54           O  
ATOM    473  CB  ASP A  68     -10.038  38.675   3.098  1.00 32.92           C  
ATOM    474  CG  ASP A  68     -10.179  40.109   2.595  1.00 37.05           C  
ATOM    475  OD1 ASP A  68     -11.161  40.762   2.962  1.00 36.78           O  
ATOM    476  OD2 ASP A  68      -9.244  40.565   1.903  1.00 38.29           O  
ATOM    477  N   VAL A  69     -11.759  37.570   5.310  1.00 27.73           N  
ATOM    478  CA  VAL A  69     -12.640  36.568   5.859  1.00 31.63           C  
ATOM    479  C   VAL A  69     -13.700  36.254   4.828  1.00 33.08           C  
ATOM    480  O   VAL A  69     -14.449  37.084   4.304  1.00 35.70           O  
ATOM    481  CB  VAL A  69     -13.223  37.048   7.200  1.00 32.43           C  
ATOM    482  CG1 VAL A  69     -14.265  36.139   7.823  1.00 32.97           C  
ATOM    483  CG2 VAL A  69     -12.087  37.214   8.208  1.00 33.28           C  
ATOM    484  N   ILE A  70     -13.737  35.007   4.382  1.00 32.32           N  
ATOM    485  CA  ILE A  70     -14.698  34.604   3.369  1.00 30.73           C  
ATOM    486  C   ILE A  70     -15.662  33.618   3.994  1.00 33.60           C  
ATOM    487  O   ILE A  70     -15.339  32.522   4.427  1.00 29.11           O  
ATOM    488  CB  ILE A  70     -13.994  34.107   2.111  1.00 30.02           C  
ATOM    489  CG1 ILE A  70     -13.177  35.293   1.525  1.00 27.99           C  
ATOM    490  CG2 ILE A  70     -14.947  33.608   1.035  1.00 28.50           C  
ATOM    491  CD1 ILE A  70     -11.999  34.965   0.683  1.00 27.32           C  
ATOM    492  N   HIS A  71     -16.917  34.098   4.062  1.00 38.06           N  
ATOM    493  CA  HIS A  71     -18.011  33.271   4.547  1.00 41.81           C  
ATOM    494  C   HIS A  71     -18.897  32.934   3.345  1.00 44.73           C  
ATOM    495  O   HIS A  71     -19.625  33.793   2.860  1.00 44.04           O  
ATOM    496  CB  HIS A  71     -18.820  33.979   5.645  1.00 41.57           C  
ATOM    497  CG  HIS A  71     -19.766  33.046   6.344  1.00 42.09           C  
ATOM    498  ND1 HIS A  71     -19.532  31.682   6.339  1.00 42.52           N  
ATOM    499  CD2 HIS A  71     -20.874  33.215   7.081  1.00 42.05           C  
ATOM    500  CE1 HIS A  71     -20.474  31.043   6.995  1.00 42.65           C  
ATOM    501  NE2 HIS A  71     -21.295  31.967   7.498  1.00 44.85           N  
ATOM    502  N   THR A  72     -18.880  31.678   2.916  1.00 47.84           N  
ATOM    503  CA  THR A  72     -19.711  31.227   1.827  1.00 51.17           C  
ATOM    504  C   THR A  72     -20.265  29.843   2.162  1.00 53.42           C  
ATOM    505  O   THR A  72     -19.702  29.041   2.878  1.00 53.53           O  
ATOM    506  CB  THR A  72     -19.045  31.127   0.452  1.00 51.42           C  
ATOM    507  OG1 THR A  72     -17.642  30.885   0.612  1.00 53.97           O  
ATOM    508  CG2 THR A  72     -19.180  32.359  -0.412  1.00 51.48           C  
ATOM    509  N   GLU A  73     -21.466  29.584   1.642  1.00 55.22           N  
ATOM    510  CA  GLU A  73     -22.198  28.353   1.720  1.00 56.75           C  
ATOM    511  C   GLU A  73     -21.919  27.537   2.960  1.00 58.10           C  
ATOM    512  O   GLU A  73     -21.511  26.357   2.902  1.00 58.58           O  
ATOM    513  CB  GLU A  73     -21.841  27.512   0.474  1.00 59.32           C  
ATOM    514  CG  GLU A  73     -21.459  28.331  -0.753  1.00 61.46           C  
ATOM    515  CD  GLU A  73     -21.218  27.465  -1.974  1.00 64.14           C  
ATOM    516  OE1 GLU A  73     -22.012  26.516  -2.188  1.00 64.37           O  
ATOM    517  OE2 GLU A  73     -20.228  27.743  -2.693  1.00 65.28           O  
ATOM    518  N   ASN A  74     -22.053  28.146   4.143  1.00 57.56           N  
ATOM    519  CA  ASN A  74     -21.851  27.420   5.387  1.00 58.10           C  
ATOM    520  C   ASN A  74     -20.415  27.148   5.774  1.00 54.77           C  
ATOM    521  O   ASN A  74     -20.154  26.499   6.793  1.00 54.14           O  
ATOM    522  CB  ASN A  74     -22.631  26.078   5.307  1.00 60.79           C  
ATOM    523  CG  ASN A  74     -24.021  26.341   5.883  1.00 63.44           C  
ATOM    524  OD1 ASN A  74     -24.947  26.681   5.147  1.00 63.52           O  
ATOM    525  ND2 ASN A  74     -24.076  26.206   7.211  1.00 64.05           N  
ATOM    526  N   LYS A  75     -19.496  27.639   4.956  1.00 51.52           N  
ATOM    527  CA  LYS A  75     -18.064  27.461   5.175  1.00 46.31           C  
ATOM    528  C   LYS A  75     -17.402  28.839   5.242  1.00 40.78           C  
ATOM    529  O   LYS A  75     -17.826  29.855   4.723  1.00 38.98           O  
ATOM    530  CB  LYS A  75     -17.400  26.515   4.220  1.00 47.08           C  
ATOM    531  CG  LYS A  75     -18.054  26.118   2.919  1.00 49.18           C  
ATOM    532  CD  LYS A  75     -17.409  24.791   2.465  1.00 50.07           C  
ATOM    533  CE  LYS A  75     -17.782  24.372   1.055  1.00 50.90           C  
ATOM    534  NZ  LYS A  75     -19.258  24.310   0.825  1.00 51.01           N  
ATOM    535  N   LEU A  76     -16.358  28.853   6.038  1.00 35.81           N  
ATOM    536  CA  LEU A  76     -15.609  29.998   6.435  1.00 30.49           C  
ATOM    537  C   LEU A  76     -14.176  29.832   5.956  1.00 28.67           C  
ATOM    538  O   LEU A  76     -13.587  28.800   6.273  1.00 27.83           O  
ATOM    539  CB  LEU A  76     -15.675  30.061   8.001  1.00 30.16           C  
ATOM    540  CG  LEU A  76     -15.165  31.370   8.605  1.00 30.45           C  
ATOM    541  CD1 LEU A  76     -15.915  32.558   7.997  1.00 29.60           C  
ATOM    542  CD2 LEU A  76     -15.192  31.422  10.127  1.00 26.74           C  
ATOM    543  N   TYR A  77     -13.612  30.825   5.293  1.00 26.29           N  
ATOM    544  CA  TYR A  77     -12.229  30.712   4.802  1.00 25.36           C  
ATOM    545  C   TYR A  77     -11.469  31.917   5.328  1.00 23.64           C  
ATOM    546  O   TYR A  77     -11.983  33.035   5.237  1.00 21.44           O  
ATOM    547  CB  TYR A  77     -12.071  30.678   3.278  1.00 26.72           C  
ATOM    548  CG  TYR A  77     -12.874  29.591   2.623  1.00 30.91           C  
ATOM    549  CD1 TYR A  77     -14.241  29.755   2.422  1.00 33.15           C  
ATOM    550  CD2 TYR A  77     -12.297  28.387   2.260  1.00 33.64           C  
ATOM    551  CE1 TYR A  77     -15.007  28.748   1.851  1.00 36.53           C  
ATOM    552  CE2 TYR A  77     -13.024  27.357   1.682  1.00 35.85           C  
ATOM    553  CZ  TYR A  77     -14.375  27.553   1.490  1.00 37.20           C  
ATOM    554  OH  TYR A  77     -15.121  26.566   0.887  1.00 41.34           O  
ATOM    555  N   LEU A  78     -10.375  31.646   6.037  1.00 20.85           N  
ATOM    556  CA  LEU A  78      -9.607  32.775   6.567  1.00 21.83           C  
ATOM    557  C   LEU A  78      -8.354  32.914   5.688  1.00 20.65           C  
ATOM    558  O   LEU A  78      -7.681  31.899   5.396  1.00 19.45           O  
ATOM    559  CB  LEU A  78      -9.170  32.617   8.028  1.00 23.20           C  
ATOM    560  CG  LEU A  78     -10.211  32.217   9.046  1.00 23.31           C  
ATOM    561  CD1 LEU A  78      -9.578  32.104  10.439  1.00 26.87           C  
ATOM    562  CD2 LEU A  78     -11.359  33.211   9.090  1.00 24.05           C  
ATOM    563  N   VAL A  79      -8.163  34.134   5.217  1.00 19.22           N  
ATOM    564  CA  VAL A  79      -7.023  34.428   4.345  1.00 19.51           C  
ATOM    565  C   VAL A  79      -5.965  35.193   5.132  1.00 21.43           C  
ATOM    566  O   VAL A  79      -6.232  36.294   5.641  1.00 20.59           O  
ATOM    567  CB  VAL A  79      -7.406  35.309   3.131  1.00 22.26           C  
ATOM    568  CG1 VAL A  79      -6.179  35.417   2.259  1.00 18.92           C  
ATOM    569  CG2 VAL A  79      -8.576  34.664   2.347  1.00 23.37           C  
ATOM    570  N   PHE A  80      -4.788  34.561   5.236  1.00 21.82           N  
ATOM    571  CA  PHE A  80      -3.714  35.096   6.019  1.00 20.91           C  
ATOM    572  C   PHE A  80      -2.490  35.446   5.168  1.00 19.58           C  
ATOM    573  O   PHE A  80      -2.267  34.759   4.200  1.00 20.13           O  
ATOM    574  CB  PHE A  80      -3.139  34.146   7.119  1.00 18.75           C  
ATOM    575  CG  PHE A  80      -4.069  33.906   8.282  1.00 21.49           C  
ATOM    576  CD1 PHE A  80      -4.256  34.877   9.262  1.00 21.49           C  
ATOM    577  CD2 PHE A  80      -4.722  32.709   8.435  1.00 22.31           C  
ATOM    578  CE1 PHE A  80      -5.108  34.657  10.305  1.00 22.76           C  
ATOM    579  CE2 PHE A  80      -5.613  32.439   9.454  1.00 24.17           C  
ATOM    580  CZ  PHE A  80      -5.791  33.450  10.415  1.00 24.32           C  
ATOM    581  N   GLU A  81      -1.688  36.355   5.743  1.00 19.81           N  
ATOM    582  CA  GLU A  81      -0.357  36.605   5.187  1.00 20.64           C  
ATOM    583  C   GLU A  81       0.400  35.291   5.223  1.00 18.19           C  
ATOM    584  O   GLU A  81       0.236  34.518   6.195  1.00 18.32           O  
ATOM    585  CB  GLU A  81       0.215  37.595   6.267  1.00 21.29           C  
ATOM    586  CG  GLU A  81       1.706  37.674   6.252  1.00 23.21           C  
ATOM    587  CD  GLU A  81       2.303  38.579   7.325  1.00 24.11           C  
ATOM    588  OE1 GLU A  81       1.788  38.975   8.362  1.00 21.54           O  
ATOM    589  OE2 GLU A  81       3.455  38.921   7.080  1.00 25.47           O  
ATOM    590  N   PHE A  82       1.218  34.903   4.314  1.00 16.92           N  
ATOM    591  CA  PHE A  82       1.918  33.635   4.231  1.00 19.31           C  
ATOM    592  C   PHE A  82       3.341  33.775   4.742  1.00 21.16           C  
ATOM    593  O   PHE A  82       3.978  34.755   4.317  1.00 20.28           O  
ATOM    594  CB  PHE A  82       2.040  33.262   2.756  1.00 19.55           C  
ATOM    595  CG  PHE A  82       2.873  32.024   2.594  1.00 21.46           C  
ATOM    596  CD1 PHE A  82       2.299  30.751   2.751  1.00 19.83           C  
ATOM    597  CD2 PHE A  82       4.202  32.125   2.226  1.00 21.52           C  
ATOM    598  CE1 PHE A  82       3.060  29.628   2.601  1.00 19.17           C  
ATOM    599  CE2 PHE A  82       4.964  30.982   2.088  1.00 23.17           C  
ATOM    600  CZ  PHE A  82       4.381  29.740   2.251  1.00 20.70           C  
ATOM    601  N   LEU A  83       3.790  32.826   5.572  1.00 18.06           N  
ATOM    602  CA  LEU A  83       5.194  33.013   6.008  1.00 19.19           C  
ATOM    603  C   LEU A  83       5.770  31.648   5.606  1.00 20.37           C  
ATOM    604  O   LEU A  83       5.003  30.680   5.659  1.00 19.63           O  
ATOM    605  CB  LEU A  83       5.396  33.341   7.475  1.00 17.41           C  
ATOM    606  CG  LEU A  83       5.226  34.830   7.790  1.00 18.79           C  
ATOM    607  CD1 LEU A  83       3.807  35.034   8.320  1.00 18.62           C  
ATOM    608  CD2 LEU A  83       6.221  35.332   8.844  1.00 19.18           C  
ATOM    609  N   HIS A  84       7.058  31.635   5.389  1.00 20.53           N  
ATOM    610  CA  HIS A  84       7.585  30.405   4.867  1.00 23.40           C  
ATOM    611  C   HIS A  84       7.870  29.322   5.835  1.00 23.40           C  
ATOM    612  O   HIS A  84       8.200  28.278   5.280  1.00 25.36           O  
ATOM    613  CB  HIS A  84       8.820  30.682   3.998  1.00 23.69           C  
ATOM    614  CG  HIS A  84       8.528  31.280   2.645  1.00 23.85           C  
ATOM    615  ND1 HIS A  84       8.289  32.647   2.472  1.00 24.85           N  
ATOM    616  CD2 HIS A  84       8.517  30.709   1.421  1.00 26.06           C  
ATOM    617  CE1 HIS A  84       8.105  32.828   1.167  1.00 28.30           C  
ATOM    618  NE2 HIS A  84       8.255  31.699   0.472  1.00 24.89           N  
ATOM    619  N   GLN A  85       7.926  29.531   7.129  1.00 26.06           N  
ATOM    620  CA  GLN A  85       8.234  28.429   8.018  1.00 24.76           C  
ATOM    621  C   GLN A  85       7.665  28.710   9.392  1.00 23.34           C  
ATOM    622  O   GLN A  85       7.581  29.860   9.792  1.00 23.32           O  
ATOM    623  CB  GLN A  85       9.763  28.284   8.173  1.00 26.66           C  
ATOM    624  CG  GLN A  85       9.981  26.941   8.880  1.00 30.49           C  
ATOM    625  CD  GLN A  85      11.377  26.423   8.854  1.00 30.60           C  
ATOM    626  OE1 GLN A  85      11.487  25.322   8.284  1.00 36.14           O  
ATOM    627  NE2 GLN A  85      12.417  27.037   9.351  1.00 28.60           N  
ATOM    628  N   ASP A  86       7.415  27.650  10.128  1.00 22.05           N  
ATOM    629  CA  ASP A  86       6.914  27.743  11.483  1.00 22.24           C  
ATOM    630  C   ASP A  86       8.113  27.381  12.368  1.00 21.76           C  
ATOM    631  O   ASP A  86       9.107  26.818  11.865  1.00 18.58           O  
ATOM    632  CB  ASP A  86       5.707  26.907  11.798  1.00 24.30           C  
ATOM    633  CG  ASP A  86       5.950  25.409  11.838  1.00 27.41           C  
ATOM    634  OD1 ASP A  86       6.883  24.877  12.492  1.00 27.90           O  
ATOM    635  OD2 ASP A  86       5.111  24.783  11.158  1.00 30.03           O  
ATOM    636  N   LEU A  87       7.897  27.700  13.642  1.00 19.32           N  
ATOM    637  CA  LEU A  87       8.963  27.493  14.615  1.00 18.83           C  
ATOM    638  C   LEU A  87       9.173  26.018  14.927  1.00 18.61           C  
ATOM    639  O   LEU A  87      10.293  25.643  15.327  1.00 16.68           O  
ATOM    640  CB  LEU A  87       8.747  28.385  15.837  1.00 17.68           C  
ATOM    641  CG  LEU A  87       9.794  28.308  16.974  1.00 18.85           C  
ATOM    642  CD1 LEU A  87      11.063  28.997  16.529  1.00 20.49           C  
ATOM    643  CD2 LEU A  87       9.263  28.936  18.283  1.00 14.84           C  
ATOM    644  N   LYS A  88       8.194  25.145  14.783  1.00 18.56           N  
ATOM    645  CA  LYS A  88       8.495  23.747  15.103  1.00 22.47           C  
ATOM    646  C   LYS A  88       9.521  23.215  14.104  1.00 23.21           C  
ATOM    647  O   LYS A  88      10.523  22.548  14.400  1.00 22.27           O  
ATOM    648  CB  LYS A  88       7.246  22.878  15.103  1.00 24.35           C  
ATOM    649  CG  LYS A  88       7.535  21.428  15.401  1.00 28.59           C  
ATOM    650  CD  LYS A  88       8.178  21.220  16.761  1.00 34.91           C  
ATOM    651  CE  LYS A  88       8.006  19.721  17.157  1.00 39.17           C  
ATOM    652  NZ  LYS A  88       8.580  19.424  18.530  1.00 40.18           N  
ATOM    653  N   LYS A  89       9.196  23.459  12.829  1.00 23.66           N  
ATOM    654  CA  LYS A  89      10.114  23.085  11.756  1.00 24.43           C  
ATOM    655  C   LYS A  89      11.452  23.739  11.955  1.00 21.57           C  
ATOM    656  O   LYS A  89      12.471  23.088  11.707  1.00 23.33           O  
ATOM    657  CB  LYS A  89       9.512  23.495  10.389  1.00 28.26           C  
ATOM    658  CG  LYS A  89       8.436  22.518   9.935  1.00 31.54           C  
ATOM    659  CD  LYS A  89       7.954  22.818   8.504  1.00 33.16           C  
ATOM    660  CE  LYS A  89       6.446  22.463   8.436  1.00 34.06           C  
ATOM    661  NZ  LYS A  89       5.885  22.939   7.109  1.00 37.77           N  
ATOM    662  N   PHE A  90      11.561  24.997  12.383  1.00 20.36           N  
ATOM    663  CA  PHE A  90      12.893  25.628  12.578  1.00 21.71           C  
ATOM    664  C   PHE A  90      13.694  24.972  13.702  1.00 23.58           C  
ATOM    665  O   PHE A  90      14.940  24.751  13.690  1.00 22.38           O  
ATOM    666  CB  PHE A  90      12.667  27.154  12.763  1.00 18.76           C  
ATOM    667  CG  PHE A  90      13.929  27.937  12.817  1.00 19.55           C  
ATOM    668  CD1 PHE A  90      14.781  27.988  11.700  1.00 20.22           C  
ATOM    669  CD2 PHE A  90      14.302  28.627  13.938  1.00 19.03           C  
ATOM    670  CE1 PHE A  90      15.978  28.653  11.755  1.00 21.89           C  
ATOM    671  CE2 PHE A  90      15.464  29.346  13.981  1.00 21.46           C  
ATOM    672  CZ  PHE A  90      16.332  29.353  12.891  1.00 22.29           C  
ATOM    673  N   MET A  91      13.009  24.657  14.802  1.00 22.26           N  
ATOM    674  CA  MET A  91      13.601  23.935  15.920  1.00 25.35           C  
ATOM    675  C   MET A  91      14.121  22.527  15.503  1.00 26.58           C  
ATOM    676  O   MET A  91      15.235  22.177  15.880  1.00 24.08           O  
ATOM    677  CB  MET A  91      12.633  23.783  17.080  1.00 23.73           C  
ATOM    678  CG  MET A  91      12.547  25.169  17.795  1.00 23.72           C  
ATOM    679  SD  MET A  91      11.553  25.040  19.267  1.00 27.39           S  
ATOM    680  CE  MET A  91       9.953  24.543  18.829  1.00 21.17           C  
ATOM    681  N   ASP A  92      13.280  21.743  14.858  1.00 25.38           N  
ATOM    682  CA  ASP A  92      13.651  20.458  14.303  1.00 29.05           C  
ATOM    683  C   ASP A  92      14.845  20.670  13.375  1.00 30.26           C  
ATOM    684  O   ASP A  92      15.862  20.068  13.641  1.00 32.56           O  
ATOM    685  CB  ASP A  92      12.526  19.808  13.504  1.00 28.61           C  
ATOM    686  CG  ASP A  92      11.386  19.303  14.348  1.00 29.52           C  
ATOM    687  OD1 ASP A  92      11.533  19.110  15.573  1.00 30.08           O  
ATOM    688  OD2 ASP A  92      10.263  19.112  13.828  1.00 30.97           O  
ATOM    689  N   ALA A  93      14.891  21.583  12.418  1.00 31.67           N  
ATOM    690  CA  ALA A  93      16.063  21.848  11.613  1.00 32.29           C  
ATOM    691  C   ALA A  93      17.310  22.319  12.354  1.00 34.76           C  
ATOM    692  O   ALA A  93      18.389  22.246  11.748  1.00 35.36           O  
ATOM    693  CB  ALA A  93      15.821  22.964  10.594  1.00 30.49           C  
ATOM    694  N   SER A  94      17.219  22.948  13.522  1.00 33.63           N  
ATOM    695  CA  SER A  94      18.367  23.477  14.220  1.00 33.43           C  
ATOM    696  C   SER A  94      18.719  22.565  15.419  1.00 34.37           C  
ATOM    697  O   SER A  94      19.457  23.026  16.290  1.00 32.85           O  
ATOM    698  CB  SER A  94      18.108  24.829  14.909  1.00 33.15           C  
ATOM    699  OG  SER A  94      17.424  25.782  14.152  1.00 33.80           O  
ATOM    700  N   ALA A  95      18.149  21.368  15.455  1.00 35.05           N  
ATOM    701  CA  ALA A  95      18.361  20.482  16.575  1.00 39.20           C  
ATOM    702  C   ALA A  95      19.813  20.092  16.863  1.00 39.73           C  
ATOM    703  O   ALA A  95      20.284  20.002  18.000  1.00 39.12           O  
ATOM    704  CB  ALA A  95      17.533  19.230  16.331  1.00 38.31           C  
ATOM    705  N   LEU A  96      20.588  19.849  15.808  1.00 41.62           N  
ATOM    706  CA  LEU A  96      21.975  19.446  16.001  1.00 40.73           C  
ATOM    707  C   LEU A  96      22.753  20.548  16.676  1.00 37.48           C  
ATOM    708  O   LEU A  96      23.578  20.228  17.508  1.00 33.94           O  
ATOM    709  CB  LEU A  96      22.629  18.957  14.713  1.00 44.24           C  
ATOM    710  CG  LEU A  96      22.835  17.435  14.630  1.00 46.94           C  
ATOM    711  CD1 LEU A  96      21.557  16.676  14.988  1.00 48.53           C  
ATOM    712  CD2 LEU A  96      23.264  17.046  13.219  1.00 47.63           C  
ATOM    713  N   THR A  97      22.483  21.794  16.341  1.00 34.86           N  
ATOM    714  CA  THR A  97      23.193  22.928  16.876  1.00 35.83           C  
ATOM    715  C   THR A  97      22.440  23.773  17.876  1.00 33.99           C  
ATOM    716  O   THR A  97      23.056  24.482  18.675  1.00 33.69           O  
ATOM    717  CB  THR A  97      23.521  23.811  15.629  1.00 40.31           C  
ATOM    718  OG1 THR A  97      22.333  24.022  14.798  1.00 40.71           O  
ATOM    719  CG2 THR A  97      24.513  23.027  14.765  1.00 41.89           C  
ATOM    720  N   GLY A  98      21.120  23.768  17.883  1.00 32.54           N  
ATOM    721  CA  GLY A  98      20.365  24.682  18.748  1.00 31.21           C  
ATOM    722  C   GLY A  98      20.324  26.060  18.067  1.00 30.82           C  
ATOM    723  O   GLY A  98      21.194  26.443  17.273  1.00 31.42           O  
ATOM    724  N   ILE A  99      19.263  26.801  18.274  1.00 29.08           N  
ATOM    725  CA  ILE A  99      19.085  28.171  17.807  1.00 26.25           C  
ATOM    726  C   ILE A  99      20.061  28.997  18.630  1.00 24.32           C  
ATOM    727  O   ILE A  99      19.977  28.861  19.809  1.00 21.07           O  
ATOM    728  CB  ILE A  99      17.628  28.605  18.065  1.00 24.45           C  
ATOM    729  CG1 ILE A  99      16.685  27.657  17.318  1.00 27.70           C  
ATOM    730  CG2 ILE A  99      17.372  30.047  17.670  1.00 25.54           C  
ATOM    731  CD1 ILE A  99      15.202  27.958  17.569  1.00 27.20           C  
ATOM    732  N   PRO A 100      20.936  29.849  18.078  1.00 24.35           N  
ATOM    733  CA  PRO A 100      21.859  30.614  18.897  1.00 23.73           C  
ATOM    734  C   PRO A 100      21.044  31.483  19.832  1.00 26.72           C  
ATOM    735  O   PRO A 100      19.981  32.052  19.469  1.00 26.76           O  
ATOM    736  CB  PRO A 100      22.702  31.448  17.916  1.00 25.44           C  
ATOM    737  CG  PRO A 100      22.221  31.070  16.562  1.00 24.95           C  
ATOM    738  CD  PRO A 100      21.091  30.070  16.643  1.00 22.64           C  
ATOM    739  N   LEU A 101      21.586  31.737  21.040  1.00 25.65           N  
ATOM    740  CA  LEU A 101      20.921  32.546  22.026  1.00 23.81           C  
ATOM    741  C   LEU A 101      20.470  33.899  21.521  1.00 20.63           C  
ATOM    742  O   LEU A 101      19.392  34.310  21.907  1.00 19.71           O  
ATOM    743  CB  LEU A 101      21.752  32.707  23.342  1.00 25.76           C  
ATOM    744  CG  LEU A 101      20.861  33.347  24.460  1.00 28.98           C  
ATOM    745  CD1 LEU A 101      19.777  32.418  24.977  1.00 29.13           C  
ATOM    746  CD2 LEU A 101      21.642  33.902  25.615  1.00 31.34           C  
ATOM    747  N   PRO A 102      21.247  34.706  20.803  1.00 21.03           N  
ATOM    748  CA  PRO A 102      20.839  36.008  20.310  1.00 18.65           C  
ATOM    749  C   PRO A 102      19.596  35.913  19.430  1.00 17.30           C  
ATOM    750  O   PRO A 102      18.728  36.791  19.515  1.00 17.38           O  
ATOM    751  CB  PRO A 102      22.048  36.486  19.464  1.00 19.00           C  
ATOM    752  CG  PRO A 102      23.199  35.784  20.116  1.00 21.99           C  
ATOM    753  CD  PRO A 102      22.632  34.361  20.329  1.00 21.61           C  
ATOM    754  N   LEU A 103      19.423  34.858  18.640  1.00 15.65           N  
ATOM    755  CA  LEU A 103      18.171  34.711  17.852  1.00 16.79           C  
ATOM    756  C   LEU A 103      16.983  34.317  18.765  1.00 16.94           C  
ATOM    757  O   LEU A 103      15.821  34.757  18.579  1.00 15.65           O  
ATOM    758  CB  LEU A 103      18.400  33.669  16.772  1.00 16.52           C  
ATOM    759  CG  LEU A 103      17.333  33.417  15.732  1.00 17.18           C  
ATOM    760  CD1 LEU A 103      16.862  34.724  15.070  1.00 19.63           C  
ATOM    761  CD2 LEU A 103      17.741  32.386  14.689  1.00 17.01           C  
ATOM    762  N   ILE A 104      17.299  33.498  19.796  1.00 14.29           N  
ATOM    763  CA  ILE A 104      16.273  33.042  20.752  1.00 15.33           C  
ATOM    764  C   ILE A 104      15.717  34.285  21.418  1.00 15.41           C  
ATOM    765  O   ILE A 104      14.523  34.519  21.567  1.00 14.97           O  
ATOM    766  CB  ILE A 104      16.808  32.065  21.842  1.00 16.07           C  
ATOM    767  CG1 ILE A 104      17.192  30.704  21.183  1.00 16.24           C  
ATOM    768  CG2 ILE A 104      15.869  31.809  23.019  1.00 10.05           C  
ATOM    769  CD1 ILE A 104      17.907  29.792  22.210  1.00 16.58           C  
ATOM    770  N   LYS A 105      16.656  35.123  21.855  1.00 15.83           N  
ATOM    771  CA  LYS A 105      16.313  36.352  22.571  1.00 17.61           C  
ATOM    772  C   LYS A 105      15.495  37.309  21.734  1.00 15.49           C  
ATOM    773  O   LYS A 105      14.557  38.000  22.125  1.00 16.63           O  
ATOM    774  CB  LYS A 105      17.676  37.007  23.018  1.00 17.75           C  
ATOM    775  CG  LYS A 105      17.479  38.271  23.818  1.00 20.91           C  
ATOM    776  CD  LYS A 105      18.766  38.806  24.459  1.00 22.66           C  
ATOM    777  CE  LYS A 105      19.381  37.767  25.454  1.00 21.55           C  
ATOM    778  NZ  LYS A 105      20.467  38.518  26.188  1.00 20.21           N  
ATOM    779  N   SER A 106      15.913  37.526  20.485  1.00 16.54           N  
ATOM    780  CA  SER A 106      15.210  38.390  19.523  1.00 14.30           C  
ATOM    781  C   SER A 106      13.798  37.863  19.247  1.00 12.63           C  
ATOM    782  O   SER A 106      12.783  38.560  19.240  1.00 13.32           O  
ATOM    783  CB  SER A 106      16.048  38.278  18.215  1.00 16.35           C  
ATOM    784  OG  SER A 106      15.278  38.911  17.178  1.00 17.14           O  
ATOM    785  N   TYR A 107      13.661  36.557  19.155  1.00 12.28           N  
ATOM    786  CA  TYR A 107      12.337  35.976  18.910  1.00 16.49           C  
ATOM    787  C   TYR A 107      11.396  36.162  20.091  1.00 16.66           C  
ATOM    788  O   TYR A 107      10.250  36.584  19.943  1.00 16.74           O  
ATOM    789  CB  TYR A 107      12.373  34.483  18.553  1.00 14.19           C  
ATOM    790  CG  TYR A 107      12.826  34.173  17.131  1.00 15.82           C  
ATOM    791  CD1 TYR A 107      12.854  35.142  16.128  1.00 16.04           C  
ATOM    792  CD2 TYR A 107      13.165  32.842  16.825  1.00 15.50           C  
ATOM    793  CE1 TYR A 107      13.229  34.816  14.821  1.00 17.17           C  
ATOM    794  CE2 TYR A 107      13.535  32.545  15.515  1.00 17.47           C  
ATOM    795  CZ  TYR A 107      13.574  33.501  14.547  1.00 18.35           C  
ATOM    796  OH  TYR A 107      13.974  33.133  13.272  1.00 20.99           O  
ATOM    797  N   LEU A 108      11.972  35.909  21.286  1.00 16.30           N  
ATOM    798  CA  LEU A 108      11.209  36.030  22.493  1.00 14.95           C  
ATOM    799  C   LEU A 108      10.775  37.495  22.690  1.00 14.79           C  
ATOM    800  O   LEU A 108       9.643  37.788  23.081  1.00 12.04           O  
ATOM    801  CB  LEU A 108      12.050  35.590  23.708  1.00 14.25           C  
ATOM    802  CG  LEU A 108      11.332  35.676  25.072  1.00 13.90           C  
ATOM    803  CD1 LEU A 108      10.097  34.774  25.055  1.00 15.20           C  
ATOM    804  CD2 LEU A 108      12.298  35.293  26.194  1.00 13.44           C  
ATOM    805  N   PHE A 109      11.659  38.437  22.373  1.00 12.98           N  
ATOM    806  CA  PHE A 109      11.408  39.847  22.506  1.00 15.59           C  
ATOM    807  C   PHE A 109      10.255  40.328  21.614  1.00 15.52           C  
ATOM    808  O   PHE A 109       9.367  41.069  22.049  1.00 15.99           O  
ATOM    809  CB  PHE A 109      12.680  40.665  22.068  1.00 20.15           C  
ATOM    810  CG  PHE A 109      12.624  42.137  22.391  1.00 22.23           C  
ATOM    811  CD1 PHE A 109      12.584  42.565  23.702  1.00 24.03           C  
ATOM    812  CD2 PHE A 109      12.710  43.101  21.411  1.00 26.58           C  
ATOM    813  CE1 PHE A 109      12.548  43.893  24.062  1.00 25.29           C  
ATOM    814  CE2 PHE A 109      12.687  44.459  21.752  1.00 26.59           C  
ATOM    815  CZ  PHE A 109      12.595  44.846  23.064  1.00 24.61           C  
ATOM    816  N   GLN A 110      10.316  39.833  20.379  1.00 15.94           N  
ATOM    817  CA  GLN A 110       9.311  40.177  19.342  1.00 15.41           C  
ATOM    818  C   GLN A 110       7.940  39.576  19.657  1.00 13.25           C  
ATOM    819  O   GLN A 110       6.868  40.185  19.508  1.00 14.21           O  
ATOM    820  CB  GLN A 110       9.807  39.733  17.966  1.00 11.17           C  
ATOM    821  CG  GLN A 110      10.967  40.473  17.238  1.00 13.25           C  
ATOM    822  CD  GLN A 110      11.261  39.701  15.966  1.00 15.23           C  
ATOM    823  OE1 GLN A 110      10.441  39.665  15.027  1.00 15.93           O  
ATOM    824  NE2 GLN A 110      12.413  39.017  15.898  1.00 14.40           N  
ATOM    825  N   LEU A 111       7.966  38.315  20.113  1.00 11.97           N  
ATOM    826  CA  LEU A 111       6.681  37.663  20.534  1.00 11.52           C  
ATOM    827  C   LEU A 111       6.126  38.421  21.736  1.00 13.85           C  
ATOM    828  O   LEU A 111       4.926  38.655  21.853  1.00 12.64           O  
ATOM    829  CB  LEU A 111       7.015  36.197  20.832  1.00 12.04           C  
ATOM    830  CG  LEU A 111       7.309  35.447  19.473  1.00 15.75           C  
ATOM    831  CD1 LEU A 111       7.667  34.001  19.706  1.00 14.23           C  
ATOM    832  CD2 LEU A 111       6.169  35.574  18.484  1.00 15.92           C  
ATOM    833  N   LEU A 112       6.966  38.855  22.722  1.00 11.36           N  
ATOM    834  CA  LEU A 112       6.450  39.642  23.814  1.00 11.88           C  
ATOM    835  C   LEU A 112       5.840  40.954  23.318  1.00 14.82           C  
ATOM    836  O   LEU A 112       4.837  41.422  23.873  1.00 13.90           O  
ATOM    837  CB  LEU A 112       7.535  39.881  24.886  1.00 11.60           C  
ATOM    838  CG  LEU A 112       7.744  38.565  25.731  1.00 13.32           C  
ATOM    839  CD1 LEU A 112       9.058  38.809  26.458  1.00 14.17           C  
ATOM    840  CD2 LEU A 112       6.627  38.347  26.774  1.00 10.87           C  
ATOM    841  N   GLN A 113       6.463  41.609  22.317  1.00 13.62           N  
ATOM    842  CA  GLN A 113       5.851  42.828  21.796  1.00 15.43           C  
ATOM    843  C   GLN A 113       4.519  42.450  21.192  1.00 17.63           C  
ATOM    844  O   GLN A 113       3.575  43.214  21.400  1.00 20.10           O  
ATOM    845  CB  GLN A 113       6.701  43.391  20.635  1.00 15.94           C  
ATOM    846  CG  GLN A 113       8.010  43.933  21.176  1.00 22.58           C  
ATOM    847  CD  GLN A 113       9.037  44.304  20.141  1.00 25.99           C  
ATOM    848  OE1 GLN A 113       9.986  43.580  19.809  1.00 28.98           O  
ATOM    849  NE2 GLN A 113       8.867  45.518  19.677  1.00 25.39           N  
ATOM    850  N   GLY A 114       4.434  41.333  20.432  1.00 18.37           N  
ATOM    851  CA  GLY A 114       3.109  40.965  19.877  1.00 16.74           C  
ATOM    852  C   GLY A 114       2.087  40.810  21.027  1.00 18.37           C  
ATOM    853  O   GLY A 114       0.981  41.351  21.055  1.00 15.84           O  
ATOM    854  N   LEU A 115       2.447  40.050  22.054  1.00 16.79           N  
ATOM    855  CA  LEU A 115       1.572  39.769  23.181  1.00 18.02           C  
ATOM    856  C   LEU A 115       1.184  41.040  23.918  1.00 19.03           C  
ATOM    857  O   LEU A 115      -0.017  41.201  24.272  1.00 20.27           O  
ATOM    858  CB  LEU A 115       2.085  38.743  24.193  1.00 13.99           C  
ATOM    859  CG  LEU A 115       2.283  37.282  23.771  1.00 17.31           C  
ATOM    860  CD1 LEU A 115       2.713  36.409  24.950  1.00 15.60           C  
ATOM    861  CD2 LEU A 115       0.931  36.738  23.239  1.00 17.26           C  
ATOM    862  N   ALA A 116       2.105  41.955  24.165  1.00 17.05           N  
ATOM    863  CA  ALA A 116       1.687  43.183  24.862  1.00 16.62           C  
ATOM    864  C   ALA A 116       0.668  43.959  24.040  1.00 18.33           C  
ATOM    865  O   ALA A 116      -0.197  44.613  24.628  1.00 18.20           O  
ATOM    866  CB  ALA A 116       2.904  44.033  25.156  1.00 15.01           C  
ATOM    867  N   PHE A 117       0.761  43.927  22.710  1.00 20.54           N  
ATOM    868  CA  PHE A 117      -0.184  44.663  21.849  1.00 20.50           C  
ATOM    869  C   PHE A 117      -1.595  44.044  21.947  1.00 20.79           C  
ATOM    870  O   PHE A 117      -2.497  44.796  22.238  1.00 22.61           O  
ATOM    871  CB  PHE A 117       0.287  44.698  20.389  1.00 18.14           C  
ATOM    872  CG  PHE A 117      -0.793  45.187  19.453  1.00 17.61           C  
ATOM    873  CD1 PHE A 117      -0.940  46.547  19.226  1.00 20.75           C  
ATOM    874  CD2 PHE A 117      -1.679  44.291  18.870  1.00 20.19           C  
ATOM    875  CE1 PHE A 117      -1.927  47.033  18.371  1.00 21.32           C  
ATOM    876  CE2 PHE A 117      -2.691  44.800  18.008  1.00 22.70           C  
ATOM    877  CZ  PHE A 117      -2.825  46.146  17.787  1.00 21.08           C  
ATOM    878  N   CYS A 118      -1.774  42.745  21.794  1.00 20.28           N  
ATOM    879  CA  CYS A 118      -3.046  42.065  21.852  1.00 21.66           C  
ATOM    880  C   CYS A 118      -3.648  42.160  23.256  1.00 19.87           C  
ATOM    881  O   CYS A 118      -4.846  42.324  23.388  1.00 19.70           O  
ATOM    882  CB  CYS A 118      -2.891  40.531  21.518  1.00 23.57           C  
ATOM    883  SG  CYS A 118      -2.315  40.146  19.848  1.00 30.49           S  
ATOM    884  N   HIS A 119      -2.790  41.935  24.258  1.00 15.85           N  
ATOM    885  CA  HIS A 119      -3.147  41.996  25.638  1.00 20.49           C  
ATOM    886  C   HIS A 119      -3.598  43.407  26.051  1.00 22.56           C  
ATOM    887  O   HIS A 119      -4.621  43.498  26.777  1.00 22.98           O  
ATOM    888  CB  HIS A 119      -2.056  41.477  26.577  1.00 19.62           C  
ATOM    889  CG  HIS A 119      -1.738  40.017  26.480  1.00 18.26           C  
ATOM    890  ND1 HIS A 119      -0.671  39.444  27.130  1.00 19.72           N  
ATOM    891  CD2 HIS A 119      -2.329  38.991  25.829  1.00 19.40           C  
ATOM    892  CE1 HIS A 119      -0.635  38.143  26.898  1.00 18.77           C  
ATOM    893  NE2 HIS A 119      -1.650  37.830  26.117  1.00 18.67           N  
ATOM    894  N   SER A 120      -2.962  44.459  25.481  1.00 20.18           N  
ATOM    895  CA  SER A 120      -3.405  45.790  25.817  1.00 23.73           C  
ATOM    896  C   SER A 120      -4.781  46.041  25.190  1.00 26.19           C  
ATOM    897  O   SER A 120      -5.473  46.912  25.754  1.00 29.14           O  
ATOM    898  CB  SER A 120      -2.434  46.923  25.420  1.00 23.50           C  
ATOM    899  OG  SER A 120      -2.596  46.991  24.011  1.00 26.21           O  
ATOM    900  N   HIS A 121      -5.244  45.328  24.198  1.00 26.65           N  
ATOM    901  CA  HIS A 121      -6.586  45.386  23.629  1.00 29.02           C  
ATOM    902  C   HIS A 121      -7.479  44.250  24.187  1.00 29.88           C  
ATOM    903  O   HIS A 121      -8.420  43.792  23.544  1.00 28.02           O  
ATOM    904  CB  HIS A 121      -6.590  45.187  22.107  1.00 28.41           C  
ATOM    905  CG  HIS A 121      -5.943  46.326  21.379  1.00 33.13           C  
ATOM    906  ND1 HIS A 121      -4.569  46.427  21.207  1.00 34.93           N  
ATOM    907  CD2 HIS A 121      -6.460  47.413  20.750  1.00 32.51           C  
ATOM    908  CE1 HIS A 121      -4.281  47.537  20.555  1.00 34.96           C  
ATOM    909  NE2 HIS A 121      -5.416  48.143  20.272  1.00 33.54           N  
ATOM    910  N   ARG A 122      -7.057  43.634  25.277  1.00 31.22           N  
ATOM    911  CA  ARG A 122      -7.763  42.575  25.978  1.00 34.46           C  
ATOM    912  C   ARG A 122      -8.047  41.361  25.126  1.00 32.32           C  
ATOM    913  O   ARG A 122      -9.116  40.769  25.252  1.00 32.90           O  
ATOM    914  CB  ARG A 122      -9.033  43.091  26.705  1.00 36.79           C  
ATOM    915  CG  ARG A 122      -8.655  44.120  27.769  1.00 42.87           C  
ATOM    916  CD  ARG A 122      -7.950  43.412  28.935  1.00 49.86           C  
ATOM    917  NE  ARG A 122      -6.719  44.090  29.347  1.00 54.89           N  
ATOM    918  CZ  ARG A 122      -6.614  45.183  30.102  1.00 56.82           C  
ATOM    919  NH1 ARG A 122      -7.714  45.750  30.586  1.00 57.47           N  
ATOM    920  NH2 ARG A 122      -5.415  45.701  30.386  1.00 57.73           N  
ATOM    921  N   VAL A 123      -7.134  41.023  24.206  1.00 29.48           N  
ATOM    922  CA  VAL A 123      -7.358  39.857  23.390  1.00 29.18           C  
ATOM    923  C   VAL A 123      -6.261  38.841  23.782  1.00 27.39           C  
ATOM    924  O   VAL A 123      -5.088  39.158  23.891  1.00 26.71           O  
ATOM    925  CB  VAL A 123      -7.405  40.138  21.895  1.00 29.77           C  
ATOM    926  CG1 VAL A 123      -7.462  38.826  21.116  1.00 30.23           C  
ATOM    927  CG2 VAL A 123      -8.616  40.988  21.532  1.00 32.03           C  
ATOM    928  N   LEU A 124      -6.673  37.594  23.954  1.00 25.77           N  
ATOM    929  CA  LEU A 124      -5.754  36.569  24.384  1.00 24.79           C  
ATOM    930  C   LEU A 124      -5.586  35.578  23.222  1.00 21.61           C  
ATOM    931  O   LEU A 124      -6.483  35.461  22.420  1.00 18.44           O  
ATOM    932  CB  LEU A 124      -6.195  35.730  25.552  1.00 26.13           C  
ATOM    933  CG  LEU A 124      -7.321  35.992  26.497  1.00 29.85           C  
ATOM    934  CD1 LEU A 124      -7.375  34.905  27.568  1.00 28.64           C  
ATOM    935  CD2 LEU A 124      -7.209  37.322  27.233  1.00 29.08           C  
ATOM    936  N   HIS A 125      -4.406  35.001  23.158  1.00 18.82           N  
ATOM    937  CA  HIS A 125      -4.269  33.943  22.120  1.00 20.08           C  
ATOM    938  C   HIS A 125      -4.966  32.667  22.611  1.00 19.65           C  
ATOM    939  O   HIS A 125      -5.818  32.121  21.868  1.00 18.20           O  
ATOM    940  CB  HIS A 125      -2.790  33.804  21.775  1.00 19.40           C  
ATOM    941  CG  HIS A 125      -2.649  32.792  20.658  1.00 20.81           C  
ATOM    942  ND1 HIS A 125      -2.105  33.103  19.394  1.00 23.61           N  
ATOM    943  CD2 HIS A 125      -3.041  31.554  20.562  1.00 18.62           C  
ATOM    944  CE1 HIS A 125      -2.195  32.040  18.645  1.00 21.19           C  
ATOM    945  NE2 HIS A 125      -2.759  31.082  19.328  1.00 22.09           N  
ATOM    946  N   ARG A 126      -4.585  32.090  23.733  1.00 18.50           N  
ATOM    947  CA  ARG A 126      -5.130  30.921  24.401  1.00 21.96           C  
ATOM    948  C   ARG A 126      -4.453  29.653  23.924  1.00 20.91           C  
ATOM    949  O   ARG A 126      -4.601  28.596  24.534  1.00 24.25           O  
ATOM    950  CB  ARG A 126      -6.625  30.685  24.120  1.00 28.17           C  
ATOM    951  CG  ARG A 126      -7.597  30.053  25.076  1.00 35.36           C  
ATOM    952  CD  ARG A 126      -8.208  28.705  24.769  1.00 38.73           C  
ATOM    953  NE  ARG A 126      -7.400  27.565  25.208  1.00 41.78           N  
ATOM    954  CZ  ARG A 126      -7.724  26.696  26.159  1.00 43.60           C  
ATOM    955  NH1 ARG A 126      -8.887  26.731  26.809  1.00 45.83           N  
ATOM    956  NH2 ARG A 126      -6.881  25.731  26.484  1.00 42.70           N  
ATOM    957  N   ASP A 127      -3.827  29.649  22.771  1.00 20.69           N  
ATOM    958  CA  ASP A 127      -3.242  28.406  22.273  1.00 21.61           C  
ATOM    959  C   ASP A 127      -1.881  28.598  21.635  1.00 21.22           C  
ATOM    960  O   ASP A 127      -1.650  28.223  20.484  1.00 23.14           O  
ATOM    961  CB  ASP A 127      -4.201  27.733  21.245  1.00 22.56           C  
ATOM    962  CG  ASP A 127      -3.803  26.254  21.258  1.00 24.42           C  
ATOM    963  OD1 ASP A 127      -3.033  25.843  22.187  1.00 20.41           O  
ATOM    964  OD2 ASP A 127      -4.220  25.603  20.273  1.00 26.44           O  
ATOM    965  N   LEU A 128      -0.992  29.335  22.344  1.00 19.86           N  
ATOM    966  CA  LEU A 128       0.333  29.489  21.757  1.00 20.30           C  
ATOM    967  C   LEU A 128       1.081  28.137  21.749  1.00 18.74           C  
ATOM    968  O   LEU A 128       1.013  27.465  22.783  1.00 17.00           O  
ATOM    969  CB  LEU A 128       1.232  30.438  22.506  1.00 20.96           C  
ATOM    970  CG  LEU A 128       0.960  31.916  22.558  1.00 24.54           C  
ATOM    971  CD1 LEU A 128       2.231  32.619  23.043  1.00 22.81           C  
ATOM    972  CD2 LEU A 128       0.632  32.423  21.147  1.00 27.09           C  
ATOM    973  N   LYS A 129       1.800  27.855  20.694  1.00 14.39           N  
ATOM    974  CA  LYS A 129       2.612  26.683  20.496  1.00 16.80           C  
ATOM    975  C   LYS A 129       3.533  26.911  19.286  1.00 17.31           C  
ATOM    976  O   LYS A 129       3.291  27.854  18.522  1.00 18.28           O  
ATOM    977  CB  LYS A 129       1.788  25.438  20.231  1.00 17.60           C  
ATOM    978  CG  LYS A 129       0.873  25.534  18.994  1.00 20.70           C  
ATOM    979  CD  LYS A 129      -0.429  24.832  19.343  1.00 19.89           C  
ATOM    980  CE  LYS A 129      -1.252  24.347  18.197  1.00 23.81           C  
ATOM    981  NZ  LYS A 129      -2.582  23.847  18.682  1.00 25.47           N  
ATOM    982  N   PRO A 130       4.598  26.157  19.105  1.00 19.04           N  
ATOM    983  CA  PRO A 130       5.554  26.422  18.019  1.00 18.42           C  
ATOM    984  C   PRO A 130       4.938  26.513  16.642  1.00 19.01           C  
ATOM    985  O   PRO A 130       5.381  27.308  15.806  1.00 18.46           O  
ATOM    986  CB  PRO A 130       6.573  25.275  18.165  1.00 21.56           C  
ATOM    987  CG  PRO A 130       6.564  24.986  19.690  1.00 18.18           C  
ATOM    988  CD  PRO A 130       5.067  25.057  19.994  1.00 16.40           C  
ATOM    989  N   GLN A 131       3.932  25.726  16.289  1.00 17.03           N  
ATOM    990  CA  GLN A 131       3.300  25.693  15.002  1.00 20.97           C  
ATOM    991  C   GLN A 131       2.585  27.025  14.735  1.00 20.82           C  
ATOM    992  O   GLN A 131       2.217  27.301  13.618  1.00 21.93           O  
ATOM    993  CB  GLN A 131       2.304  24.534  14.802  1.00 23.80           C  
ATOM    994  CG  GLN A 131       2.814  23.179  15.294  1.00 30.23           C  
ATOM    995  CD  GLN A 131       2.688  22.968  16.815  1.00 34.22           C  
ATOM    996  OE1 GLN A 131       3.391  23.438  17.704  1.00 31.91           O  
ATOM    997  NE2 GLN A 131       1.666  22.175  17.221  1.00 37.55           N  
ATOM    998  N   ASN A 132       2.274  27.792  15.758  1.00 17.98           N  
ATOM    999  CA  ASN A 132       1.568  29.042  15.710  1.00 19.38           C  
ATOM   1000  C   ASN A 132       2.553  30.218  15.752  1.00 14.93           C  
ATOM   1001  O   ASN A 132       2.163  31.289  16.122  1.00 14.49           O  
ATOM   1002  CB  ASN A 132       0.588  29.089  16.887  1.00 20.72           C  
ATOM   1003  CG  ASN A 132      -0.736  28.425  16.520  1.00 24.08           C  
ATOM   1004  OD1 ASN A 132      -0.902  28.182  15.329  1.00 24.40           O  
ATOM   1005  ND2 ASN A 132      -1.657  28.185  17.443  1.00 21.46           N  
ATOM   1006  N   LEU A 133       3.815  29.967  15.557  1.00 16.48           N  
ATOM   1007  CA  LEU A 133       4.842  31.028  15.616  1.00 18.68           C  
ATOM   1008  C   LEU A 133       5.535  30.966  14.234  1.00 18.81           C  
ATOM   1009  O   LEU A 133       6.007  29.876  13.927  1.00 18.58           O  
ATOM   1010  CB  LEU A 133       5.731  30.830  16.807  1.00 17.16           C  
ATOM   1011  CG  LEU A 133       5.133  30.939  18.212  1.00 15.34           C  
ATOM   1012  CD1 LEU A 133       6.222  30.710  19.246  1.00 12.05           C  
ATOM   1013  CD2 LEU A 133       4.515  32.360  18.242  1.00 14.10           C  
ATOM   1014  N   LEU A 134       5.294  31.948  13.387  1.00 13.71           N  
ATOM   1015  CA  LEU A 134       5.798  31.808  12.014  1.00 17.01           C  
ATOM   1016  C   LEU A 134       6.972  32.744  11.776  1.00 17.07           C  
ATOM   1017  O   LEU A 134       6.935  33.813  12.387  1.00 15.51           O  
ATOM   1018  CB  LEU A 134       4.641  32.096  11.023  1.00 17.99           C  
ATOM   1019  CG  LEU A 134       3.376  31.191  11.216  1.00 16.66           C  
ATOM   1020  CD1 LEU A 134       2.374  31.548  10.158  1.00 16.42           C  
ATOM   1021  CD2 LEU A 134       3.737  29.728  11.076  1.00 18.57           C  
ATOM   1022  N   ILE A 135       7.955  32.344  10.961  1.00 17.44           N  
ATOM   1023  CA  ILE A 135       9.167  33.171  10.860  1.00 19.86           C  
ATOM   1024  C   ILE A 135       9.400  33.470   9.354  1.00 19.25           C  
ATOM   1025  O   ILE A 135       8.891  32.730   8.551  1.00 14.30           O  
ATOM   1026  CB  ILE A 135      10.420  32.428  11.372  1.00 19.73           C  
ATOM   1027  CG1 ILE A 135      10.650  31.083  10.654  1.00 20.49           C  
ATOM   1028  CG2 ILE A 135      10.289  32.078  12.871  1.00 22.47           C  
ATOM   1029  CD1 ILE A 135      12.033  30.451  10.977  1.00 20.57           C  
ATOM   1030  N   ASN A 136      10.167  34.521   9.099  1.00 21.58           N  
ATOM   1031  CA  ASN A 136      10.572  34.807   7.703  1.00 22.31           C  
ATOM   1032  C   ASN A 136      12.096  34.891   7.629  1.00 24.85           C  
ATOM   1033  O   ASN A 136      12.812  34.810   8.660  1.00 23.87           O  
ATOM   1034  CB  ASN A 136       9.978  36.082   7.209  1.00 19.30           C  
ATOM   1035  CG  ASN A 136      10.351  37.347   7.944  1.00 18.19           C  
ATOM   1036  OD1 ASN A 136      11.401  37.387   8.599  1.00 20.19           O  
ATOM   1037  ND2 ASN A 136       9.487  38.312   7.818  1.00 15.73           N  
ATOM   1038  N   THR A 137      12.621  35.261   6.454  1.00 25.62           N  
ATOM   1039  CA  THR A 137      14.076  35.331   6.270  1.00 26.92           C  
ATOM   1040  C   THR A 137      14.747  36.538   6.879  1.00 27.42           C  
ATOM   1041  O   THR A 137      15.964  36.634   6.982  1.00 29.66           O  
ATOM   1042  CB  THR A 137      14.320  35.444   4.720  1.00 30.00           C  
ATOM   1043  OG1 THR A 137      13.508  36.561   4.213  1.00 30.93           O  
ATOM   1044  CG2 THR A 137      13.840  34.171   4.067  1.00 28.71           C  
ATOM   1045  N   GLU A 138      13.993  37.578   7.219  1.00 27.10           N  
ATOM   1046  CA  GLU A 138      14.501  38.791   7.775  1.00 26.41           C  
ATOM   1047  C   GLU A 138      14.817  38.685   9.281  1.00 26.38           C  
ATOM   1048  O   GLU A 138      15.082  39.756   9.852  1.00 27.12           O  
ATOM   1049  CB  GLU A 138      13.438  39.864   7.688  1.00 30.25           C  
ATOM   1050  CG  GLU A 138      12.702  40.263   6.430  1.00 35.29           C  
ATOM   1051  CD  GLU A 138      13.637  40.501   5.265  1.00 38.76           C  
ATOM   1052  OE1 GLU A 138      14.750  41.017   5.481  1.00 38.11           O  
ATOM   1053  OE2 GLU A 138      13.170  40.136   4.145  1.00 43.24           O  
ATOM   1054  N   GLY A 139      14.460  37.641   9.997  1.00 21.58           N  
ATOM   1055  CA  GLY A 139      14.611  37.605  11.440  1.00 20.05           C  
ATOM   1056  C   GLY A 139      13.299  37.925  12.191  1.00 18.52           C  
ATOM   1057  O   GLY A 139      13.309  38.102  13.408  1.00 17.27           O  
ATOM   1058  N   ALA A 140      12.189  38.128  11.511  1.00 18.30           N  
ATOM   1059  CA  ALA A 140      10.942  38.452  12.227  1.00 19.30           C  
ATOM   1060  C   ALA A 140      10.251  37.150  12.686  1.00 20.06           C  
ATOM   1061  O   ALA A 140      10.427  36.092  12.096  1.00 19.17           O  
ATOM   1062  CB  ALA A 140      10.104  39.243  11.226  1.00 14.46           C  
ATOM   1063  N   ILE A 141       9.364  37.196  13.694  1.00 21.03           N  
ATOM   1064  CA  ILE A 141       8.565  36.038  14.126  1.00 16.92           C  
ATOM   1065  C   ILE A 141       7.228  36.654  14.546  1.00 16.69           C  
ATOM   1066  O   ILE A 141       7.142  37.809  14.972  1.00 15.84           O  
ATOM   1067  CB  ILE A 141       9.222  35.192  15.220  1.00 15.34           C  
ATOM   1068  CG1 ILE A 141       8.439  33.923  15.562  1.00 16.73           C  
ATOM   1069  CG2 ILE A 141       9.515  36.012  16.494  1.00 13.65           C  
ATOM   1070  CD1 ILE A 141       9.262  32.902  16.441  1.00 12.39           C  
ATOM   1071  N   LYS A 142       6.148  35.971  14.191  1.00 15.63           N  
ATOM   1072  CA  LYS A 142       4.813  36.461  14.387  1.00 16.13           C  
ATOM   1073  C   LYS A 142       3.931  35.390  15.021  1.00 14.49           C  
ATOM   1074  O   LYS A 142       4.127  34.177  14.754  1.00 15.45           O  
ATOM   1075  CB  LYS A 142       4.216  36.832  12.977  1.00 13.52           C  
ATOM   1076  CG  LYS A 142       5.170  37.780  12.212  1.00 15.13           C  
ATOM   1077  CD  LYS A 142       4.541  38.293  10.905  1.00 17.32           C  
ATOM   1078  CE  LYS A 142       5.570  39.052   9.997  1.00 17.33           C  
ATOM   1079  NZ  LYS A 142       4.694  40.094   9.289  1.00 16.52           N  
ATOM   1080  N   LEU A 143       2.915  35.815  15.730  1.00 12.50           N  
ATOM   1081  CA  LEU A 143       1.957  34.864  16.308  1.00 14.43           C  
ATOM   1082  C   LEU A 143       0.836  34.528  15.335  1.00 14.83           C  
ATOM   1083  O   LEU A 143       0.260  35.525  14.813  1.00 15.53           O  
ATOM   1084  CB  LEU A 143       1.306  35.639  17.466  1.00 15.13           C  
ATOM   1085  CG  LEU A 143       2.324  35.986  18.557  1.00 20.20           C  
ATOM   1086  CD1 LEU A 143       1.849  37.298  19.215  1.00 21.45           C  
ATOM   1087  CD2 LEU A 143       2.315  34.803  19.518  1.00 13.22           C  
ATOM   1088  N   ALA A 144       0.579  33.298  14.961  1.00 13.23           N  
ATOM   1089  CA  ALA A 144      -0.466  32.924  14.014  1.00 15.09           C  
ATOM   1090  C   ALA A 144      -1.746  32.515  14.725  1.00 15.05           C  
ATOM   1091  O   ALA A 144      -1.657  32.010  15.873  1.00 13.85           O  
ATOM   1092  CB  ALA A 144       0.033  31.691  13.223  1.00 14.94           C  
ATOM   1093  N   ASP A 145      -2.912  32.585  14.117  1.00 18.24           N  
ATOM   1094  CA  ASP A 145      -4.177  32.109  14.785  1.00 19.10           C  
ATOM   1095  C   ASP A 145      -4.522  32.821  16.048  1.00 19.26           C  
ATOM   1096  O   ASP A 145      -5.251  32.276  16.887  1.00 22.47           O  
ATOM   1097  CB  ASP A 145      -4.182  30.570  15.027  1.00 18.36           C  
ATOM   1098  CG  ASP A 145      -4.012  29.921  13.636  1.00 23.38           C  
ATOM   1099  OD1 ASP A 145      -4.491  30.493  12.630  1.00 23.53           O  
ATOM   1100  OD2 ASP A 145      -3.386  28.856  13.448  1.00 23.63           O  
ATOM   1101  N   PHE A 146      -4.084  34.082  16.242  1.00 19.90           N  
ATOM   1102  CA  PHE A 146      -4.440  34.802  17.401  1.00 22.66           C  
ATOM   1103  C   PHE A 146      -5.969  34.873  17.457  1.00 23.82           C  
ATOM   1104  O   PHE A 146      -6.554  35.362  16.508  1.00 20.03           O  
ATOM   1105  CB  PHE A 146      -3.995  36.301  17.365  1.00 26.52           C  
ATOM   1106  CG  PHE A 146      -3.467  36.678  18.720  1.00 30.48           C  
ATOM   1107  CD1 PHE A 146      -4.253  37.083  19.755  1.00 31.79           C  
ATOM   1108  CD2 PHE A 146      -2.085  36.584  18.928  1.00 33.37           C  
ATOM   1109  CE1 PHE A 146      -3.682  37.398  20.964  1.00 33.80           C  
ATOM   1110  CE2 PHE A 146      -1.508  36.890  20.136  1.00 35.26           C  
ATOM   1111  CZ  PHE A 146      -2.339  37.280  21.180  1.00 35.81           C  
ATOM   1112  N   GLY A 147      -6.624  34.593  18.581  1.00 25.31           N  
ATOM   1113  CA  GLY A 147      -8.040  34.905  18.687  1.00 23.97           C  
ATOM   1114  C   GLY A 147      -8.975  33.853  18.160  1.00 25.38           C  
ATOM   1115  O   GLY A 147     -10.161  33.937  18.476  1.00 25.54           O  
ATOM   1116  N   LEU A 148      -8.526  32.886  17.402  1.00 26.31           N  
ATOM   1117  CA  LEU A 148      -9.357  31.798  16.910  1.00 29.14           C  
ATOM   1118  C   LEU A 148      -9.935  30.848  17.939  1.00 30.80           C  
ATOM   1119  O   LEU A 148     -11.031  30.260  17.743  1.00 32.00           O  
ATOM   1120  CB  LEU A 148      -8.534  31.038  15.839  1.00 30.39           C  
ATOM   1121  CG  LEU A 148      -8.138  31.845  14.590  1.00 29.78           C  
ATOM   1122  CD1 LEU A 148      -7.789  30.909  13.459  1.00 30.38           C  
ATOM   1123  CD2 LEU A 148      -9.251  32.787  14.131  1.00 29.21           C  
ATOM   1124  N   ALA A 149      -9.284  30.551  19.057  1.00 31.99           N  
ATOM   1125  CA  ALA A 149      -9.755  29.614  20.080  1.00 33.08           C  
ATOM   1126  C   ALA A 149     -11.014  30.154  20.765  1.00 35.38           C  
ATOM   1127  O   ALA A 149     -11.997  29.468  21.086  1.00 34.81           O  
ATOM   1128  CB  ALA A 149      -8.627  29.449  21.098  1.00 35.34           C  
ATOM   1129  N   ARG A 150     -11.017  31.465  21.003  1.00 33.76           N  
ATOM   1130  CA  ARG A 150     -12.188  32.101  21.582  1.00 36.31           C  
ATOM   1131  C   ARG A 150     -13.310  32.200  20.540  1.00 37.87           C  
ATOM   1132  O   ARG A 150     -14.496  32.113  20.853  1.00 36.94           O  
ATOM   1133  CB  ARG A 150     -11.885  33.548  21.995  1.00 35.30           C  
ATOM   1134  CG  ARG A 150     -13.156  34.289  22.385  1.00 36.54           C  
ATOM   1135  CD  ARG A 150     -12.815  35.529  23.204  1.00 39.70           C  
ATOM   1136  NE  ARG A 150     -14.052  35.967  23.825  1.00 43.39           N  
ATOM   1137  CZ  ARG A 150     -14.255  37.098  24.489  1.00 44.85           C  
ATOM   1138  NH1 ARG A 150     -13.220  37.943  24.604  1.00 45.27           N  
ATOM   1139  NH2 ARG A 150     -15.480  37.324  24.976  1.00 42.72           N  
ATOM   1140  N   ALA A 151     -12.913  32.485  19.299  1.00 38.72           N  
ATOM   1141  CA  ALA A 151     -13.939  32.625  18.276  1.00 42.63           C  
ATOM   1142  C   ALA A 151     -14.632  31.309  17.970  1.00 45.65           C  
ATOM   1143  O   ALA A 151     -15.805  31.382  17.581  1.00 47.77           O  
ATOM   1144  CB  ALA A 151     -13.372  33.161  16.986  1.00 42.35           C  
ATOM   1145  N   PHE A 152     -13.971  30.170  18.049  1.00 48.52           N  
ATOM   1146  CA  PHE A 152     -14.544  28.907  17.641  1.00 50.83           C  
ATOM   1147  C   PHE A 152     -14.657  27.774  18.643  1.00 55.53           C  
ATOM   1148  O   PHE A 152     -15.397  26.838  18.281  1.00 57.47           O  
ATOM   1149  CB  PHE A 152     -13.702  28.391  16.478  1.00 47.98           C  
ATOM   1150  CG  PHE A 152     -13.526  29.162  15.218  1.00 46.57           C  
ATOM   1151  CD1 PHE A 152     -14.589  29.608  14.456  1.00 46.64           C  
ATOM   1152  CD2 PHE A 152     -12.251  29.406  14.732  1.00 45.84           C  
ATOM   1153  CE1 PHE A 152     -14.356  30.296  13.276  1.00 47.04           C  
ATOM   1154  CE2 PHE A 152     -11.986  30.080  13.568  1.00 44.22           C  
ATOM   1155  CZ  PHE A 152     -13.066  30.540  12.826  1.00 46.56           C  
ATOM   1156  N   GLY A 153     -13.979  27.730  19.780  1.00 58.85           N  
ATOM   1157  CA  GLY A 153     -14.044  26.630  20.745  1.00 61.90           C  
ATOM   1158  C   GLY A 153     -12.760  25.831  20.738  1.00 64.87           C  
ATOM   1159  O   GLY A 153     -12.174  25.898  19.647  1.00 66.39           O  
ATOM   1160  N   VAL A 154     -12.199  25.139  21.726  1.00 66.90           N  
ATOM   1161  CA  VAL A 154     -10.936  24.395  21.539  1.00 67.42           C  
ATOM   1162  C   VAL A 154     -11.102  22.894  21.830  1.00 67.14           C  
ATOM   1163  O   VAL A 154     -10.923  22.417  22.952  1.00 67.49           O  
ATOM   1164  CB  VAL A 154      -9.739  24.888  22.362  1.00 67.59           C  
ATOM   1165  CG1 VAL A 154      -8.499  24.041  22.067  1.00 67.18           C  
ATOM   1166  CG2 VAL A 154      -9.404  26.346  22.121  1.00 67.67           C  
ATOM   1167  N   PRO A 155     -11.388  22.112  20.791  1.00 66.72           N  
ATOM   1168  CA  PRO A 155     -11.677  20.693  20.904  1.00 66.54           C  
ATOM   1169  C   PRO A 155     -10.570  19.772  21.373  1.00 65.81           C  
ATOM   1170  O   PRO A 155      -9.418  20.076  21.061  1.00 64.57           O  
ATOM   1171  CB  PRO A 155     -12.161  20.296  19.507  1.00 67.23           C  
ATOM   1172  CG  PRO A 155     -11.705  21.382  18.597  1.00 67.30           C  
ATOM   1173  CD  PRO A 155     -11.625  22.632  19.418  1.00 66.79           C  
ATOM   1174  N   VAL A 156     -10.880  18.650  22.047  1.00 65.07           N  
ATOM   1175  CA  VAL A 156      -9.840  17.730  22.511  1.00 65.02           C  
ATOM   1176  C   VAL A 156      -9.117  17.063  21.341  1.00 65.77           C  
ATOM   1177  O   VAL A 156      -7.920  16.762  21.414  1.00 64.13           O  
ATOM   1178  CB  VAL A 156     -10.273  16.631  23.477  1.00 65.12           C  
ATOM   1179  CG1 VAL A 156      -9.050  16.037  24.176  1.00 65.22           C  
ATOM   1180  CG2 VAL A 156     -11.278  17.109  24.510  1.00 65.30           C  
ATOM   1181  N   ARG A 157      -9.832  16.870  20.223  1.00 66.56           N  
ATOM   1182  CA  ARG A 157      -9.165  16.394  19.011  1.00 66.76           C  
ATOM   1183  C   ARG A 157      -9.330  17.436  17.897  1.00 67.64           C  
ATOM   1184  O   ARG A 157     -10.277  18.230  17.922  1.00 68.14           O  
ATOM   1185  CB  ARG A 157      -9.652  15.038  18.557  1.00 65.61           C  
ATOM   1186  CG  ARG A 157      -9.390  13.951  19.582  1.00 65.68           C  
ATOM   1187  CD  ARG A 157      -7.915  13.724  19.894  1.00 65.90           C  
ATOM   1188  NE  ARG A 157      -7.823  12.668  20.911  1.00 66.27           N  
ATOM   1189  CZ  ARG A 157      -7.999  11.387  20.583  1.00 66.75           C  
ATOM   1190  NH1 ARG A 157      -8.219  11.073  19.315  1.00 67.02           N  
ATOM   1191  NH2 ARG A 157      -7.945  10.448  21.506  1.00 66.80           N  
ATOM   1192  N   THR A 158      -8.372  17.429  16.979  1.00 66.61           N  
ATOM   1193  CA  THR A 158      -8.413  18.297  15.811  1.00 66.64           C  
ATOM   1194  C   THR A 158      -9.537  17.827  14.892  1.00 66.17           C  
ATOM   1195  O   THR A 158     -10.121  16.756  15.069  1.00 66.83           O  
ATOM   1196  CB  THR A 158      -7.128  18.229  14.959  1.00 66.51           C  
ATOM   1197  OG1 THR A 158      -7.021  16.883  14.448  1.00 66.61           O  
ATOM   1198  CG2 THR A 158      -5.858  18.529  15.736  1.00 65.57           C  
ATOM   1199  N   TYR A 159      -9.788  18.576  13.821  1.00 65.92           N  
ATOM   1200  CA  TYR A 159     -10.829  18.254  12.842  1.00 64.89           C  
ATOM   1201  C   TYR A 159     -10.413  16.949  12.177  1.00 63.89           C  
ATOM   1202  O   TYR A 159     -11.222  16.080  11.845  1.00 63.96           O  
ATOM   1203  CB  TYR A 159     -11.055  19.440  11.877  1.00 66.09           C  
ATOM   1204  CG  TYR A 159     -10.161  19.265  10.659  1.00 66.68           C  
ATOM   1205  CD1 TYR A 159      -8.790  19.404  10.842  1.00 66.61           C  
ATOM   1206  CD2 TYR A 159     -10.653  18.909   9.418  1.00 66.56           C  
ATOM   1207  CE1 TYR A 159      -7.929  19.194   9.799  1.00 67.67           C  
ATOM   1208  CE2 TYR A 159      -9.782  18.715   8.361  1.00 67.82           C  
ATOM   1209  CZ  TYR A 159      -8.428  18.855   8.558  1.00 68.49           C  
ATOM   1210  OH  TYR A 159      -7.513  18.666   7.541  1.00 69.96           O  
ATOM   1211  N   THR A 160      -9.093  16.747  12.084  1.00 62.22           N  
ATOM   1212  CA  THR A 160      -8.453  15.542  11.636  1.00 61.63           C  
ATOM   1213  C   THR A 160      -8.345  14.526  12.754  1.00 61.10           C  
ATOM   1214  O   THR A 160      -7.654  13.476  12.662  1.00 62.07           O  
ATOM   1215  CB  THR A 160      -7.028  15.701  11.067  1.00 61.88           C  
ATOM   1216  OG1 THR A 160      -6.216  16.642  11.769  1.00 62.25           O  
ATOM   1217  CG2 THR A 160      -7.092  16.017   9.577  1.00 62.48           C  
ATOM   1218  N   HIS A 161      -9.054  14.643  13.879  1.00 59.11           N  
ATOM   1219  CA  HIS A 161      -9.060  13.767  15.043  1.00 57.44           C  
ATOM   1220  C   HIS A 161      -7.681  13.712  15.725  1.00 56.46           C  
ATOM   1221  O   HIS A 161      -7.544  13.173  16.844  1.00 55.71           O  
ATOM   1222  CB  HIS A 161      -9.637  12.359  14.816  1.00 58.39           C  
ATOM   1223  CG  HIS A 161     -10.518  12.224  13.593  1.00 58.92           C  
ATOM   1224  ND1 HIS A 161     -11.794  12.728  13.500  1.00 59.37           N  
ATOM   1225  CD2 HIS A 161     -10.201  11.721  12.362  1.00 58.24           C  
ATOM   1226  CE1 HIS A 161     -12.239  12.506  12.272  1.00 59.79           C  
ATOM   1227  NE2 HIS A 161     -11.292  11.905  11.550  1.00 59.77           N  
ATOM   1228  N   GLU A 162      -6.650  14.353  15.162  1.00 52.78           N  
ATOM   1229  CA  GLU A 162      -5.337  14.456  15.752  1.00 51.39           C  
ATOM   1230  C   GLU A 162      -5.477  15.138  17.125  1.00 45.81           C  
ATOM   1231  O   GLU A 162      -6.359  15.939  17.376  1.00 44.50           O  
ATOM   1232  CB  GLU A 162      -4.360  15.198  14.846  1.00 53.67           C  
ATOM   1233  CG  GLU A 162      -3.388  16.139  15.526  1.00 57.32           C  
ATOM   1234  CD  GLU A 162      -2.512  16.912  14.552  1.00 60.52           C  
ATOM   1235  OE1 GLU A 162      -3.082  17.716  13.766  1.00 61.79           O  
ATOM   1236  OE2 GLU A 162      -1.273  16.685  14.608  1.00 60.27           O  
ATOM   1237  N   VAL A 163      -4.559  14.841  18.010  1.00 42.72           N  
ATOM   1238  CA  VAL A 163      -4.618  15.280  19.399  1.00 38.53           C  
ATOM   1239  C   VAL A 163      -4.224  16.720  19.667  1.00 35.49           C  
ATOM   1240  O   VAL A 163      -3.266  17.312  19.156  1.00 34.25           O  
ATOM   1241  CB  VAL A 163      -3.747  14.301  20.235  1.00 37.03           C  
ATOM   1242  CG1 VAL A 163      -3.542  14.800  21.657  1.00 35.41           C  
ATOM   1243  CG2 VAL A 163      -4.384  12.919  20.165  1.00 37.01           C  
ATOM   1244  N   VAL A 164      -4.989  17.251  20.624  1.00 34.04           N  
ATOM   1245  CA  VAL A 164      -4.631  18.617  21.056  1.00 34.94           C  
ATOM   1246  C   VAL A 164      -3.382  18.597  21.939  1.00 30.62           C  
ATOM   1247  O   VAL A 164      -3.196  17.752  22.808  1.00 29.06           O  
ATOM   1248  CB  VAL A 164      -5.822  19.352  21.656  1.00 37.79           C  
ATOM   1249  CG1 VAL A 164      -5.428  20.721  22.207  1.00 37.41           C  
ATOM   1250  CG2 VAL A 164      -6.788  19.533  20.481  1.00 38.65           C  
ATOM   1251  N   THR A 165      -2.425  19.444  21.585  1.00 26.54           N  
ATOM   1252  CA  THR A 165      -1.237  19.547  22.395  1.00 25.67           C  
ATOM   1253  C   THR A 165      -1.586  20.272  23.728  1.00 24.15           C  
ATOM   1254  O   THR A 165      -2.098  21.389  23.782  1.00 19.05           O  
ATOM   1255  CB  THR A 165      -0.053  20.259  21.795  1.00 26.16           C  
ATOM   1256  OG1 THR A 165       1.068  19.930  22.661  1.00 27.49           O  
ATOM   1257  CG2 THR A 165      -0.172  21.755  21.799  1.00 29.03           C  
ATOM   1258  N   LEU A 166      -1.166  19.614  24.823  1.00 22.34           N  
ATOM   1259  CA  LEU A 166      -1.331  20.217  26.153  1.00 19.93           C  
ATOM   1260  C   LEU A 166      -0.070  20.815  26.683  1.00 17.22           C  
ATOM   1261  O   LEU A 166       0.026  21.391  27.771  1.00 14.79           O  
ATOM   1262  CB  LEU A 166      -1.609  19.014  27.091  1.00 20.48           C  
ATOM   1263  CG  LEU A 166      -2.917  18.280  26.640  1.00 20.76           C  
ATOM   1264  CD1 LEU A 166      -3.042  16.986  27.459  1.00 19.26           C  
ATOM   1265  CD2 LEU A 166      -4.061  19.260  26.774  1.00 19.09           C  
ATOM   1266  N   TRP A 167       1.005  20.590  25.924  1.00 17.65           N  
ATOM   1267  CA  TRP A 167       2.374  20.936  26.366  1.00 16.19           C  
ATOM   1268  C   TRP A 167       2.583  22.350  26.850  1.00 14.44           C  
ATOM   1269  O   TRP A 167       3.411  22.567  27.766  1.00 15.31           O  
ATOM   1270  CB  TRP A 167       3.324  20.586  25.221  1.00 16.64           C  
ATOM   1271  CG  TRP A 167       3.524  19.167  24.850  1.00 15.40           C  
ATOM   1272  CD1 TRP A 167       2.768  18.093  25.269  1.00 16.39           C  
ATOM   1273  CD2 TRP A 167       4.439  18.639  23.871  1.00 17.06           C  
ATOM   1274  NE1 TRP A 167       3.239  16.933  24.715  1.00 16.72           N  
ATOM   1275  CE2 TRP A 167       4.249  17.246  23.820  1.00 16.52           C  
ATOM   1276  CE3 TRP A 167       5.412  19.207  23.041  1.00 17.67           C  
ATOM   1277  CZ2 TRP A 167       4.990  16.428  22.986  1.00 17.47           C  
ATOM   1278  CZ3 TRP A 167       6.160  18.365  22.229  1.00 18.13           C  
ATOM   1279  CH2 TRP A 167       5.919  16.971  22.164  1.00 16.94           C  
ATOM   1280  N   TYR A 168       1.855  23.317  26.312  1.00 11.69           N  
ATOM   1281  CA  TYR A 168       1.995  24.728  26.594  1.00 12.52           C  
ATOM   1282  C   TYR A 168       0.817  25.277  27.415  1.00 13.29           C  
ATOM   1283  O   TYR A 168       0.675  26.493  27.616  1.00 13.52           O  
ATOM   1284  CB  TYR A 168       2.075  25.552  25.227  1.00  9.74           C  
ATOM   1285  CG  TYR A 168       3.208  24.877  24.375  1.00 11.57           C  
ATOM   1286  CD1 TYR A 168       4.546  25.140  24.598  1.00  8.36           C  
ATOM   1287  CD2 TYR A 168       2.806  23.930  23.435  1.00 11.05           C  
ATOM   1288  CE1 TYR A 168       5.545  24.439  23.896  1.00  9.84           C  
ATOM   1289  CE2 TYR A 168       3.811  23.218  22.706  1.00 11.15           C  
ATOM   1290  CZ  TYR A 168       5.144  23.482  23.001  1.00  9.35           C  
ATOM   1291  OH  TYR A 168       6.073  22.824  22.234  1.00 11.39           O  
ATOM   1292  N   ARG A 169      -0.067  24.447  27.921  1.00 13.64           N  
ATOM   1293  CA  ARG A 169      -1.227  24.972  28.676  1.00 15.57           C  
ATOM   1294  C   ARG A 169      -0.884  25.354  30.123  1.00 14.51           C  
ATOM   1295  O   ARG A 169      -0.261  24.582  30.919  1.00 14.17           O  
ATOM   1296  CB  ARG A 169      -2.309  23.879  28.558  1.00 17.74           C  
ATOM   1297  CG  ARG A 169      -3.652  24.212  29.174  1.00 22.53           C  
ATOM   1298  CD  ARG A 169      -4.736  23.213  28.776  1.00 25.84           C  
ATOM   1299  NE  ARG A 169      -5.049  23.055  27.356  1.00 25.78           N  
ATOM   1300  CZ  ARG A 169      -6.036  22.160  27.047  1.00 29.16           C  
ATOM   1301  NH1 ARG A 169      -6.657  21.526  28.058  1.00 22.38           N  
ATOM   1302  NH2 ARG A 169      -6.346  21.940  25.747  1.00 27.19           N  
ATOM   1303  N   ALA A 170      -1.345  26.544  30.517  1.00  9.56           N  
ATOM   1304  CA  ALA A 170      -1.089  27.093  31.802  1.00 13.54           C  
ATOM   1305  C   ALA A 170      -1.851  26.211  32.848  1.00 16.49           C  
ATOM   1306  O   ALA A 170      -2.895  25.636  32.552  1.00 14.35           O  
ATOM   1307  CB  ALA A 170      -1.611  28.502  31.885  1.00 11.33           C  
ATOM   1308  N   PRO A 171      -1.313  26.164  34.054  1.00 14.77           N  
ATOM   1309  CA  PRO A 171      -1.864  25.322  35.080  1.00 13.84           C  
ATOM   1310  C   PRO A 171      -3.213  25.778  35.542  1.00 14.57           C  
ATOM   1311  O   PRO A 171      -3.986  24.890  35.959  1.00 18.33           O  
ATOM   1312  CB  PRO A 171      -0.785  25.363  36.197  1.00 14.56           C  
ATOM   1313  CG  PRO A 171      -0.136  26.713  35.946  1.00 15.68           C  
ATOM   1314  CD  PRO A 171      -0.023  26.833  34.430  1.00 13.41           C  
ATOM   1315  N   GLU A 172      -3.581  27.040  35.542  1.00 15.51           N  
ATOM   1316  CA  GLU A 172      -4.907  27.491  35.958  1.00 17.11           C  
ATOM   1317  C   GLU A 172      -5.925  26.894  34.985  1.00 17.88           C  
ATOM   1318  O   GLU A 172      -7.064  26.585  35.436  1.00 18.97           O  
ATOM   1319  CB  GLU A 172      -5.048  29.031  36.051  1.00 18.76           C  
ATOM   1320  CG  GLU A 172      -4.805  29.795  34.722  1.00 16.26           C  
ATOM   1321  CD  GLU A 172      -3.330  30.192  34.578  1.00 14.90           C  
ATOM   1322  OE1 GLU A 172      -2.389  29.531  35.063  1.00 12.00           O  
ATOM   1323  OE2 GLU A 172      -3.017  31.285  34.058  1.00 17.56           O  
ATOM   1324  N   ILE A 173      -5.614  26.745  33.713  1.00 15.02           N  
ATOM   1325  CA  ILE A 173      -6.566  26.163  32.754  1.00 15.88           C  
ATOM   1326  C   ILE A 173      -6.754  24.669  33.149  1.00 19.94           C  
ATOM   1327  O   ILE A 173      -7.887  24.167  33.316  1.00 17.85           O  
ATOM   1328  CB  ILE A 173      -6.150  26.240  31.254  1.00 16.04           C  
ATOM   1329  CG1 ILE A 173      -5.902  27.705  30.841  1.00 16.65           C  
ATOM   1330  CG2 ILE A 173      -7.181  25.599  30.273  1.00 15.07           C  
ATOM   1331  CD1 ILE A 173      -5.323  27.841  29.456  1.00 16.58           C  
ATOM   1332  N   LEU A 174      -5.622  23.994  33.335  1.00 16.59           N  
ATOM   1333  CA  LEU A 174      -5.654  22.572  33.720  1.00 17.50           C  
ATOM   1334  C   LEU A 174      -6.379  22.402  35.050  1.00 18.59           C  
ATOM   1335  O   LEU A 174      -7.128  21.451  35.205  1.00 19.19           O  
ATOM   1336  CB  LEU A 174      -4.272  21.971  33.819  1.00 16.42           C  
ATOM   1337  CG  LEU A 174      -3.410  21.919  32.513  1.00 16.34           C  
ATOM   1338  CD1 LEU A 174      -1.956  21.814  32.899  1.00 16.53           C  
ATOM   1339  CD2 LEU A 174      -3.819  20.667  31.699  1.00 19.61           C  
ATOM   1340  N   LEU A 175      -6.282  23.324  36.005  1.00 16.28           N  
ATOM   1341  CA  LEU A 175      -7.002  23.181  37.241  1.00 18.84           C  
ATOM   1342  C   LEU A 175      -8.470  23.613  37.123  1.00 22.09           C  
ATOM   1343  O   LEU A 175      -9.127  23.580  38.172  1.00 20.55           O  
ATOM   1344  CB  LEU A 175      -6.222  23.923  38.309  1.00 15.59           C  
ATOM   1345  CG  LEU A 175      -4.917  23.175  38.655  1.00 17.05           C  
ATOM   1346  CD1 LEU A 175      -4.012  24.020  39.528  1.00 16.64           C  
ATOM   1347  CD2 LEU A 175      -5.176  21.841  39.345  1.00 18.03           C  
ATOM   1348  N   GLY A 176      -8.953  23.922  35.907  1.00 23.25           N  
ATOM   1349  CA  GLY A 176     -10.367  24.210  35.703  1.00 25.36           C  
ATOM   1350  C   GLY A 176     -10.850  25.620  35.898  1.00 25.76           C  
ATOM   1351  O   GLY A 176     -12.052  25.846  36.018  1.00 26.74           O  
ATOM   1352  N   CYS A 177      -9.979  26.611  35.920  1.00 24.70           N  
ATOM   1353  CA  CYS A 177     -10.371  28.013  35.990  1.00 25.55           C  
ATOM   1354  C   CYS A 177     -11.041  28.332  34.630  1.00 25.05           C  
ATOM   1355  O   CYS A 177     -10.550  28.056  33.542  1.00 20.19           O  
ATOM   1356  CB  CYS A 177      -9.177  28.910  36.284  1.00 27.02           C  
ATOM   1357  SG  CYS A 177      -9.435  30.682  36.548  1.00 27.92           S  
ATOM   1358  N   LYS A 178     -12.253  28.898  34.788  1.00 27.07           N  
ATOM   1359  CA  LYS A 178     -13.088  29.222  33.637  1.00 27.78           C  
ATOM   1360  C   LYS A 178     -12.731  30.527  32.958  1.00 24.93           C  
ATOM   1361  O   LYS A 178     -12.903  30.722  31.778  1.00 25.62           O  
ATOM   1362  CB  LYS A 178     -14.514  29.482  34.202  1.00 31.02           C  
ATOM   1363  CG  LYS A 178     -15.549  28.445  33.900  1.00 33.12           C  
ATOM   1364  CD  LYS A 178     -14.943  27.048  34.127  1.00 35.80           C  
ATOM   1365  CE  LYS A 178     -14.773  26.326  32.790  1.00 34.94           C  
ATOM   1366  NZ  LYS A 178     -15.241  24.905  32.952  1.00 36.07           N  
ATOM   1367  N   TYR A 179     -12.326  31.473  33.751  1.00 24.12           N  
ATOM   1368  CA  TYR A 179     -12.013  32.835  33.336  1.00 25.28           C  
ATOM   1369  C   TYR A 179     -10.561  33.209  33.388  1.00 23.32           C  
ATOM   1370  O   TYR A 179     -10.247  34.247  33.981  1.00 23.18           O  
ATOM   1371  CB  TYR A 179     -12.704  33.751  34.396  1.00 28.88           C  
ATOM   1372  CG  TYR A 179     -14.169  33.489  34.448  1.00 33.75           C  
ATOM   1373  CD1 TYR A 179     -14.962  33.617  33.317  1.00 33.59           C  
ATOM   1374  CD2 TYR A 179     -14.694  33.021  35.652  1.00 36.05           C  
ATOM   1375  CE1 TYR A 179     -16.310  33.348  33.394  1.00 37.45           C  
ATOM   1376  CE2 TYR A 179     -16.058  32.724  35.723  1.00 39.03           C  
ATOM   1377  CZ  TYR A 179     -16.840  32.920  34.603  1.00 39.04           C  
ATOM   1378  OH  TYR A 179     -18.166  32.632  34.714  1.00 41.41           O  
ATOM   1379  N   TYR A 180      -9.659  32.401  32.954  1.00 24.72           N  
ATOM   1380  CA  TYR A 180      -8.235  32.753  33.056  1.00 26.85           C  
ATOM   1381  C   TYR A 180      -7.958  33.955  32.143  1.00 29.36           C  
ATOM   1382  O   TYR A 180      -8.683  34.353  31.226  1.00 28.63           O  
ATOM   1383  CB  TYR A 180      -7.484  31.479  32.664  1.00 27.85           C  
ATOM   1384  CG  TYR A 180      -8.014  31.009  31.294  1.00 29.52           C  
ATOM   1385  CD1 TYR A 180      -7.589  31.629  30.148  1.00 30.39           C  
ATOM   1386  CD2 TYR A 180      -8.918  29.985  31.179  1.00 28.83           C  
ATOM   1387  CE1 TYR A 180      -8.048  31.228  28.921  1.00 32.00           C  
ATOM   1388  CE2 TYR A 180      -9.401  29.584  29.956  1.00 31.16           C  
ATOM   1389  CZ  TYR A 180      -8.951  30.220  28.831  1.00 33.28           C  
ATOM   1390  OH  TYR A 180      -9.432  29.872  27.571  1.00 37.84           O  
ATOM   1391  N   SER A 181      -6.814  34.591  32.377  1.00 27.94           N  
ATOM   1392  CA  SER A 181      -6.338  35.823  31.798  1.00 23.73           C  
ATOM   1393  C   SER A 181      -5.287  35.685  30.701  1.00 22.28           C  
ATOM   1394  O   SER A 181      -4.763  34.664  30.234  1.00 21.30           O  
ATOM   1395  CB  SER A 181      -5.689  36.585  32.986  1.00 24.27           C  
ATOM   1396  OG  SER A 181      -4.432  36.059  33.427  1.00 19.66           O  
ATOM   1397  N   THR A 182      -4.723  36.854  30.364  1.00 19.66           N  
ATOM   1398  CA  THR A 182      -3.655  37.054  29.411  1.00 19.92           C  
ATOM   1399  C   THR A 182      -2.412  36.388  29.990  1.00 14.99           C  
ATOM   1400  O   THR A 182      -1.551  35.926  29.212  1.00 18.01           O  
ATOM   1401  CB  THR A 182      -3.323  38.567  29.171  1.00 18.15           C  
ATOM   1402  OG1 THR A 182      -3.083  39.045  30.481  1.00 20.88           O  
ATOM   1403  CG2 THR A 182      -4.504  39.290  28.593  1.00 21.02           C  
ATOM   1404  N   ALA A 183      -2.390  36.045  31.260  1.00 14.35           N  
ATOM   1405  CA  ALA A 183      -1.271  35.292  31.837  1.00 15.47           C  
ATOM   1406  C   ALA A 183      -1.133  33.908  31.211  1.00 14.49           C  
ATOM   1407  O   ALA A 183      -0.026  33.376  31.238  1.00 12.40           O  
ATOM   1408  CB  ALA A 183      -1.362  35.149  33.358  1.00 14.83           C  
ATOM   1409  N   VAL A 184      -2.181  33.365  30.569  1.00 12.76           N  
ATOM   1410  CA  VAL A 184      -1.993  32.032  30.001  1.00 12.80           C  
ATOM   1411  C   VAL A 184      -1.057  32.038  28.790  1.00 11.67           C  
ATOM   1412  O   VAL A 184      -0.322  31.065  28.661  1.00  8.71           O  
ATOM   1413  CB  VAL A 184      -3.327  31.302  29.671  1.00 11.35           C  
ATOM   1414  CG1 VAL A 184      -4.211  31.371  30.908  1.00 12.67           C  
ATOM   1415  CG2 VAL A 184      -3.968  31.940  28.455  1.00 12.98           C  
ATOM   1416  N   ASP A 185      -1.017  33.147  28.049  1.00 11.40           N  
ATOM   1417  CA  ASP A 185      -0.127  33.247  26.888  1.00 13.01           C  
ATOM   1418  C   ASP A 185       1.333  33.469  27.323  1.00 12.57           C  
ATOM   1419  O   ASP A 185       2.287  33.029  26.687  1.00 11.36           O  
ATOM   1420  CB  ASP A 185      -0.484  34.444  25.967  1.00 11.03           C  
ATOM   1421  CG  ASP A 185      -1.841  34.287  25.313  1.00 15.11           C  
ATOM   1422  OD1 ASP A 185      -2.206  33.093  25.199  1.00 14.60           O  
ATOM   1423  OD2 ASP A 185      -2.407  35.369  24.919  1.00 16.35           O  
ATOM   1424  N   ILE A 186       1.531  34.048  28.513  1.00 12.27           N  
ATOM   1425  CA  ILE A 186       2.865  34.244  29.036  1.00 12.69           C  
ATOM   1426  C   ILE A 186       3.444  32.885  29.510  1.00 12.01           C  
ATOM   1427  O   ILE A 186       4.579  32.566  29.245  1.00 12.58           O  
ATOM   1428  CB  ILE A 186       2.794  35.230  30.206  1.00 13.58           C  
ATOM   1429  CG1 ILE A 186       2.476  36.645  29.647  1.00 18.58           C  
ATOM   1430  CG2 ILE A 186       4.172  35.173  30.900  1.00 13.56           C  
ATOM   1431  CD1 ILE A 186       3.667  37.250  28.861  1.00 18.02           C  
ATOM   1432  N   TRP A 187       2.607  32.049  30.134  1.00 12.34           N  
ATOM   1433  CA  TRP A 187       3.005  30.723  30.528  1.00 10.44           C  
ATOM   1434  C   TRP A 187       3.442  29.970  29.270  1.00  8.27           C  
ATOM   1435  O   TRP A 187       4.523  29.367  29.233  1.00 11.89           O  
ATOM   1436  CB  TRP A 187       1.808  29.977  31.131  1.00 12.59           C  
ATOM   1437  CG  TRP A 187       2.209  28.530  31.424  1.00 11.99           C  
ATOM   1438  CD1 TRP A 187       2.147  27.470  30.588  1.00 10.73           C  
ATOM   1439  CD2 TRP A 187       2.686  28.089  32.693  1.00  9.40           C  
ATOM   1440  NE1 TRP A 187       2.615  26.317  31.304  1.00 12.75           N  
ATOM   1441  CE2 TRP A 187       2.909  26.713  32.592  1.00 10.81           C  
ATOM   1442  CE3 TRP A 187       2.881  28.743  33.919  1.00 11.56           C  
ATOM   1443  CZ2 TRP A 187       3.343  25.925  33.681  1.00 11.89           C  
ATOM   1444  CZ3 TRP A 187       3.395  27.995  34.997  1.00 12.78           C  
ATOM   1445  CH2 TRP A 187       3.606  26.605  34.829  1.00 11.89           C  
ATOM   1446  N   SER A 188       2.575  29.884  28.295  1.00 10.52           N  
ATOM   1447  CA  SER A 188       2.919  29.230  27.010  1.00  9.62           C  
ATOM   1448  C   SER A 188       4.225  29.711  26.454  1.00 10.84           C  
ATOM   1449  O   SER A 188       5.059  28.882  26.057  1.00 12.24           O  
ATOM   1450  CB  SER A 188       1.845  29.525  25.923  1.00 10.58           C  
ATOM   1451  OG  SER A 188       0.544  29.002  26.407  1.00 10.97           O  
ATOM   1452  N   LEU A 189       4.430  31.030  26.241  1.00 10.71           N  
ATOM   1453  CA  LEU A 189       5.629  31.545  25.659  1.00 11.50           C  
ATOM   1454  C   LEU A 189       6.826  31.150  26.537  1.00 13.74           C  
ATOM   1455  O   LEU A 189       7.881  30.824  25.996  1.00 14.08           O  
ATOM   1456  CB  LEU A 189       5.519  33.067  25.545  1.00 11.38           C  
ATOM   1457  CG  LEU A 189       6.664  33.795  24.810  1.00 12.25           C  
ATOM   1458  CD1 LEU A 189       6.865  33.166  23.441  1.00 12.41           C  
ATOM   1459  CD2 LEU A 189       6.255  35.270  24.610  1.00 13.42           C  
ATOM   1460  N   GLY A 190       6.648  31.089  27.860  1.00 15.16           N  
ATOM   1461  CA  GLY A 190       7.729  30.708  28.792  1.00 14.25           C  
ATOM   1462  C   GLY A 190       8.183  29.258  28.451  1.00 13.50           C  
ATOM   1463  O   GLY A 190       9.368  28.907  28.386  1.00 12.65           O  
ATOM   1464  N   CYS A 191       7.174  28.410  28.235  1.00 11.47           N  
ATOM   1465  CA  CYS A 191       7.407  27.026  27.910  1.00 13.83           C  
ATOM   1466  C   CYS A 191       8.136  26.915  26.538  1.00 15.45           C  
ATOM   1467  O   CYS A 191       9.035  26.044  26.343  1.00 12.05           O  
ATOM   1468  CB  CYS A 191       6.177  26.119  27.828  1.00 12.24           C  
ATOM   1469  SG  CYS A 191       5.223  25.958  29.360  1.00 11.30           S  
ATOM   1470  N   ILE A 192       7.691  27.812  25.644  1.00 11.52           N  
ATOM   1471  CA  ILE A 192       8.377  27.719  24.322  1.00 10.91           C  
ATOM   1472  C   ILE A 192       9.805  28.251  24.411  1.00  9.81           C  
ATOM   1473  O   ILE A 192      10.711  27.739  23.758  1.00 10.63           O  
ATOM   1474  CB  ILE A 192       7.525  28.527  23.307  1.00 10.67           C  
ATOM   1475  CG1 ILE A 192       6.231  27.811  23.031  1.00  9.64           C  
ATOM   1476  CG2 ILE A 192       8.430  28.802  22.079  1.00 11.15           C  
ATOM   1477  CD1 ILE A 192       5.075  28.483  22.282  1.00 13.58           C  
ATOM   1478  N   PHE A 193      10.069  29.244  25.264  1.00  8.85           N  
ATOM   1479  CA  PHE A 193      11.379  29.819  25.510  1.00 10.05           C  
ATOM   1480  C   PHE A 193      12.284  28.698  26.036  1.00 11.29           C  
ATOM   1481  O   PHE A 193      13.382  28.529  25.537  1.00 10.32           O  
ATOM   1482  CB  PHE A 193      11.282  30.993  26.471  1.00 12.51           C  
ATOM   1483  CG  PHE A 193      12.522  31.632  27.025  1.00 15.23           C  
ATOM   1484  CD1 PHE A 193      13.750  31.592  26.326  1.00 13.72           C  
ATOM   1485  CD2 PHE A 193      12.472  32.320  28.213  1.00 14.01           C  
ATOM   1486  CE1 PHE A 193      14.834  32.225  26.823  1.00 14.07           C  
ATOM   1487  CE2 PHE A 193      13.595  32.975  28.694  1.00 15.38           C  
ATOM   1488  CZ  PHE A 193      14.805  32.898  28.043  1.00 13.61           C  
ATOM   1489  N   ALA A 194      11.881  27.951  27.058  1.00 14.08           N  
ATOM   1490  CA  ALA A 194      12.667  26.849  27.625  1.00 14.14           C  
ATOM   1491  C   ALA A 194      12.988  25.798  26.561  1.00 14.42           C  
ATOM   1492  O   ALA A 194      14.098  25.282  26.462  1.00 14.29           O  
ATOM   1493  CB  ALA A 194      11.864  26.199  28.792  1.00 11.50           C  
ATOM   1494  N   GLU A 195      12.042  25.446  25.678  1.00 14.00           N  
ATOM   1495  CA  GLU A 195      12.233  24.522  24.576  1.00 14.04           C  
ATOM   1496  C   GLU A 195      13.203  24.981  23.493  1.00 15.94           C  
ATOM   1497  O   GLU A 195      14.034  24.190  23.045  1.00 16.09           O  
ATOM   1498  CB  GLU A 195      10.917  24.163  23.928  1.00 17.95           C  
ATOM   1499  CG  GLU A 195      10.945  22.992  22.939  1.00 17.25           C  
ATOM   1500  CD  GLU A 195       9.564  22.704  22.407  1.00 18.40           C  
ATOM   1501  OE1 GLU A 195       8.465  23.020  22.926  1.00 18.02           O  
ATOM   1502  OE2 GLU A 195       9.524  22.078  21.365  1.00 18.51           O  
ATOM   1503  N   MET A 196      13.260  26.255  23.103  1.00 14.36           N  
ATOM   1504  CA  MET A 196      14.268  26.759  22.235  1.00 15.29           C  
ATOM   1505  C   MET A 196      15.631  26.581  22.897  1.00 16.63           C  
ATOM   1506  O   MET A 196      16.603  26.204  22.281  1.00 14.50           O  
ATOM   1507  CB  MET A 196      14.039  28.308  22.073  1.00 13.92           C  
ATOM   1508  CG  MET A 196      12.825  28.553  21.095  1.00 13.74           C  
ATOM   1509  SD  MET A 196      12.853  30.184  20.291  1.00 15.66           S  
ATOM   1510  CE  MET A 196      12.083  31.065  21.702  1.00 15.80           C  
ATOM   1511  N   VAL A 197      15.778  26.958  24.175  1.00 17.21           N  
ATOM   1512  CA  VAL A 197      17.111  26.890  24.781  1.00 16.75           C  
ATOM   1513  C   VAL A 197      17.614  25.462  24.944  1.00 18.36           C  
ATOM   1514  O   VAL A 197      18.785  25.289  24.682  1.00 19.40           O  
ATOM   1515  CB  VAL A 197      17.055  27.546  26.176  1.00 18.34           C  
ATOM   1516  CG1 VAL A 197      18.284  27.263  27.050  1.00 14.11           C  
ATOM   1517  CG2 VAL A 197      16.826  29.051  25.975  1.00 15.75           C  
ATOM   1518  N   THR A 198      16.771  24.530  25.374  1.00 17.46           N  
ATOM   1519  CA  THR A 198      17.275  23.183  25.657  1.00 16.80           C  
ATOM   1520  C   THR A 198      17.091  22.208  24.555  1.00 16.92           C  
ATOM   1521  O   THR A 198      17.729  21.134  24.613  1.00 17.17           O  
ATOM   1522  CB  THR A 198      16.623  22.540  26.915  1.00 17.48           C  
ATOM   1523  OG1 THR A 198      15.247  22.302  26.577  1.00 16.63           O  
ATOM   1524  CG2 THR A 198      16.657  23.468  28.138  1.00 16.75           C  
ATOM   1525  N   ARG A 199      16.207  22.479  23.568  1.00 19.00           N  
ATOM   1526  CA  ARG A 199      15.994  21.619  22.402  1.00 20.66           C  
ATOM   1527  C   ARG A 199      15.201  20.360  22.775  1.00 23.90           C  
ATOM   1528  O   ARG A 199      15.129  19.331  22.076  1.00 21.61           O  
ATOM   1529  CB  ARG A 199      17.217  21.186  21.576  1.00 21.89           C  
ATOM   1530  CG  ARG A 199      18.249  22.335  21.440  1.00 24.62           C  
ATOM   1531  CD  ARG A 199      19.476  21.834  20.661  1.00 24.17           C  
ATOM   1532  NE  ARG A 199      20.607  22.473  21.272  1.00 24.48           N  
ATOM   1533  CZ  ARG A 199      21.831  21.977  21.058  1.00 27.42           C  
ATOM   1534  NH1 ARG A 199      22.028  20.887  20.320  1.00 27.15           N  
ATOM   1535  NH2 ARG A 199      22.751  22.680  21.676  1.00 27.76           N  
ATOM   1536  N   ARG A 200      14.433  20.557  23.856  1.00 23.52           N  
ATOM   1537  CA  ARG A 200      13.492  19.576  24.327  1.00 22.22           C  
ATOM   1538  C   ARG A 200      12.300  20.306  24.938  1.00 19.74           C  
ATOM   1539  O   ARG A 200      12.367  21.377  25.554  1.00 16.76           O  
ATOM   1540  CB  ARG A 200      14.316  18.625  25.179  1.00 27.11           C  
ATOM   1541  CG  ARG A 200      13.531  17.820  26.161  1.00 34.39           C  
ATOM   1542  CD  ARG A 200      13.755  16.329  26.145  1.00 39.62           C  
ATOM   1543  NE  ARG A 200      15.060  15.757  25.819  1.00 44.41           N  
ATOM   1544  CZ  ARG A 200      15.452  14.656  26.524  1.00 47.09           C  
ATOM   1545  NH1 ARG A 200      14.705  14.139  27.503  1.00 45.14           N  
ATOM   1546  NH2 ARG A 200      16.638  14.094  26.297  1.00 47.48           N  
ATOM   1547  N   ALA A 201      11.096  19.827  24.689  1.00 18.00           N  
ATOM   1548  CA  ALA A 201       9.890  20.454  25.241  1.00 18.18           C  
ATOM   1549  C   ALA A 201      10.064  20.482  26.754  1.00 16.78           C  
ATOM   1550  O   ALA A 201      10.621  19.525  27.295  1.00 17.16           O  
ATOM   1551  CB  ALA A 201       8.583  19.758  24.861  1.00 19.24           C  
ATOM   1552  N   LEU A 202       9.497  21.469  27.417  1.00 15.75           N  
ATOM   1553  CA  LEU A 202       9.684  21.523  28.898  1.00 15.60           C  
ATOM   1554  C   LEU A 202       8.792  20.501  29.563  1.00 14.77           C  
ATOM   1555  O   LEU A 202       9.204  19.760  30.458  1.00 15.43           O  
ATOM   1556  CB  LEU A 202       9.325  22.957  29.356  1.00 11.96           C  
ATOM   1557  CG  LEU A 202       9.416  23.290  30.837  1.00 14.38           C  
ATOM   1558  CD1 LEU A 202      10.874  23.046  31.376  1.00 11.64           C  
ATOM   1559  CD2 LEU A 202       9.063  24.791  31.075  1.00 11.75           C  
ATOM   1560  N   PHE A 203       7.491  20.541  29.288  1.00 13.34           N  
ATOM   1561  CA  PHE A 203       6.460  19.681  29.871  1.00 15.56           C  
ATOM   1562  C   PHE A 203       5.632  18.884  28.836  1.00 15.62           C  
ATOM   1563  O   PHE A 203       4.567  19.289  28.402  1.00 14.15           O  
ATOM   1564  CB  PHE A 203       5.507  20.647  30.599  1.00 13.65           C  
ATOM   1565  CG  PHE A 203       6.133  21.526  31.669  1.00 14.63           C  
ATOM   1566  CD1 PHE A 203       6.978  20.982  32.643  1.00 16.24           C  
ATOM   1567  CD2 PHE A 203       5.852  22.858  31.713  1.00 13.77           C  
ATOM   1568  CE1 PHE A 203       7.531  21.792  33.631  1.00 15.88           C  
ATOM   1569  CE2 PHE A 203       6.330  23.657  32.725  1.00 16.56           C  
ATOM   1570  CZ  PHE A 203       7.202  23.116  33.678  1.00 17.62           C  
ATOM   1571  N   PRO A 204       6.200  17.864  28.206  1.00 17.15           N  
ATOM   1572  CA  PRO A 204       5.511  17.170  27.148  1.00 18.13           C  
ATOM   1573  C   PRO A 204       4.366  16.319  27.656  1.00 17.90           C  
ATOM   1574  O   PRO A 204       4.456  15.137  27.403  1.00 19.20           O  
ATOM   1575  CB  PRO A 204       6.614  16.299  26.514  1.00 19.59           C  
ATOM   1576  CG  PRO A 204       7.750  16.178  27.467  1.00 18.26           C  
ATOM   1577  CD  PRO A 204       7.572  17.337  28.478  1.00 17.81           C  
ATOM   1578  N   GLY A 205       3.269  16.761  28.255  1.00 14.41           N  
ATOM   1579  CA  GLY A 205       2.220  15.908  28.785  1.00 13.47           C  
ATOM   1580  C   GLY A 205       1.459  15.168  27.713  1.00 14.38           C  
ATOM   1581  O   GLY A 205       1.304  15.651  26.597  1.00 12.95           O  
ATOM   1582  N   ASP A 206       1.046  13.932  28.018  1.00 15.14           N  
ATOM   1583  CA  ASP A 206       0.278  13.215  27.039  1.00 16.77           C  
ATOM   1584  C   ASP A 206      -1.147  12.976  27.548  1.00 19.77           C  
ATOM   1585  O   ASP A 206      -1.891  12.230  26.922  1.00 21.99           O  
ATOM   1586  CB  ASP A 206       1.102  12.015  26.565  1.00 21.03           C  
ATOM   1587  CG  ASP A 206       1.247  10.996  27.693  1.00 20.55           C  
ATOM   1588  OD1 ASP A 206       0.805  11.236  28.827  1.00 20.50           O  
ATOM   1589  OD2 ASP A 206       1.775   9.911  27.425  1.00 22.25           O  
ATOM   1590  N   SER A 207      -1.594  13.696  28.568  1.00 16.51           N  
ATOM   1591  CA  SER A 207      -2.947  13.693  29.084  1.00 18.07           C  
ATOM   1592  C   SER A 207      -3.015  14.815  30.136  1.00 17.53           C  
ATOM   1593  O   SER A 207      -1.934  15.367  30.500  1.00 18.98           O  
ATOM   1594  CB  SER A 207      -3.365  12.389  29.790  1.00 17.14           C  
ATOM   1595  OG  SER A 207      -2.550  12.350  30.978  1.00 16.07           O  
ATOM   1596  N   GLU A 208      -4.201  15.242  30.513  1.00 15.29           N  
ATOM   1597  CA  GLU A 208      -4.237  16.409  31.420  1.00 20.03           C  
ATOM   1598  C   GLU A 208      -3.510  16.231  32.731  1.00 19.40           C  
ATOM   1599  O   GLU A 208      -2.801  17.128  33.252  1.00 18.72           O  
ATOM   1600  CB  GLU A 208      -5.677  16.863  31.688  1.00 21.42           C  
ATOM   1601  CG  GLU A 208      -6.208  17.591  30.409  1.00 25.68           C  
ATOM   1602  CD  GLU A 208      -7.549  18.255  30.695  1.00 27.67           C  
ATOM   1603  OE1 GLU A 208      -7.917  18.813  31.743  1.00 30.76           O  
ATOM   1604  OE2 GLU A 208      -8.349  18.277  29.761  1.00 33.79           O  
ATOM   1605  N   ILE A 209      -3.671  15.022  33.274  1.00 17.05           N  
ATOM   1606  CA  ILE A 209      -3.042  14.709  34.563  1.00 17.54           C  
ATOM   1607  C   ILE A 209      -1.555  14.556  34.361  1.00 17.05           C  
ATOM   1608  O   ILE A 209      -0.788  15.103  35.188  1.00 19.65           O  
ATOM   1609  CB  ILE A 209      -3.700  13.531  35.322  1.00 16.00           C  
ATOM   1610  CG1 ILE A 209      -3.321  13.651  36.807  1.00 15.80           C  
ATOM   1611  CG2 ILE A 209      -3.166  12.203  34.733  1.00 17.54           C  
ATOM   1612  CD1 ILE A 209      -3.977  14.845  37.518  1.00 14.54           C  
ATOM   1613  N   ASP A 210      -1.148  13.918  33.264  1.00 15.18           N  
ATOM   1614  CA  ASP A 210       0.268  13.856  32.942  1.00 15.41           C  
ATOM   1615  C   ASP A 210       0.870  15.278  32.794  1.00 14.21           C  
ATOM   1616  O   ASP A 210       1.987  15.595  33.257  1.00 13.99           O  
ATOM   1617  CB  ASP A 210       0.541  13.007  31.684  1.00 11.94           C  
ATOM   1618  CG  ASP A 210       2.031  12.806  31.479  1.00 16.22           C  
ATOM   1619  OD1 ASP A 210       2.700  12.208  32.366  1.00 15.59           O  
ATOM   1620  OD2 ASP A 210       2.653  13.246  30.486  1.00 16.43           O  
ATOM   1621  N   GLN A 211       0.195  16.140  32.046  1.00 14.70           N  
ATOM   1622  CA  GLN A 211       0.682  17.519  31.874  1.00 14.26           C  
ATOM   1623  C   GLN A 211       0.856  18.249  33.182  1.00 13.61           C  
ATOM   1624  O   GLN A 211       1.854  18.848  33.581  1.00 11.73           O  
ATOM   1625  CB  GLN A 211      -0.375  18.250  31.034  1.00 13.35           C  
ATOM   1626  CG  GLN A 211       0.110  19.702  30.727  1.00 14.83           C  
ATOM   1627  CD  GLN A 211       1.309  19.624  29.809  1.00 16.99           C  
ATOM   1628  OE1 GLN A 211       1.401  18.719  28.958  1.00 14.66           O  
ATOM   1629  NE2 GLN A 211       2.213  20.590  30.037  1.00 12.75           N  
ATOM   1630  N   LEU A 212      -0.191  18.206  33.999  1.00 17.90           N  
ATOM   1631  CA  LEU A 212      -0.201  18.831  35.337  1.00 18.93           C  
ATOM   1632  C   LEU A 212       0.919  18.239  36.195  1.00 20.50           C  
ATOM   1633  O   LEU A 212       1.638  19.046  36.863  1.00 18.59           O  
ATOM   1634  CB  LEU A 212      -1.560  18.591  36.006  1.00 19.65           C  
ATOM   1635  CG  LEU A 212      -1.912  19.482  37.199  1.00 24.65           C  
ATOM   1636  CD1 LEU A 212      -2.116  20.904  36.707  1.00 19.94           C  
ATOM   1637  CD2 LEU A 212      -3.095  18.888  37.996  1.00 23.32           C  
ATOM   1638  N   PHE A 213       0.969  16.881  36.201  1.00 17.71           N  
ATOM   1639  CA  PHE A 213       2.003  16.289  37.067  1.00 17.61           C  
ATOM   1640  C   PHE A 213       3.427  16.536  36.561  1.00 15.78           C  
ATOM   1641  O   PHE A 213       4.320  16.642  37.383  1.00 14.55           O  
ATOM   1642  CB  PHE A 213       1.725  14.788  37.307  1.00 17.85           C  
ATOM   1643  CG  PHE A 213       0.600  14.564  38.316  1.00 18.95           C  
ATOM   1644  CD1 PHE A 213      -0.117  15.568  38.883  1.00 19.55           C  
ATOM   1645  CD2 PHE A 213       0.201  13.254  38.574  1.00 21.13           C  
ATOM   1646  CE1 PHE A 213      -1.153  15.327  39.783  1.00 21.70           C  
ATOM   1647  CE2 PHE A 213      -0.815  12.997  39.496  1.00 18.10           C  
ATOM   1648  CZ  PHE A 213      -1.519  14.026  40.067  1.00 18.74           C  
ATOM   1649  N   ARG A 214       3.670  16.735  35.285  1.00 14.63           N  
ATOM   1650  CA  ARG A 214       4.978  17.190  34.781  1.00 13.84           C  
ATOM   1651  C   ARG A 214       5.285  18.609  35.250  1.00 15.01           C  
ATOM   1652  O   ARG A 214       6.410  18.838  35.761  1.00 12.31           O  
ATOM   1653  CB  ARG A 214       5.010  17.129  33.264  1.00 15.84           C  
ATOM   1654  CG  ARG A 214       5.321  15.712  32.779  1.00 16.12           C  
ATOM   1655  CD  ARG A 214       5.136  15.795  31.203  1.00 15.07           C  
ATOM   1656  NE  ARG A 214       5.407  14.435  30.698  1.00 15.69           N  
ATOM   1657  CZ  ARG A 214       6.633  13.979  30.599  1.00 18.30           C  
ATOM   1658  NH1 ARG A 214       7.736  14.591  30.953  1.00 19.46           N  
ATOM   1659  NH2 ARG A 214       6.760  12.742  30.105  1.00 20.40           N  
ATOM   1660  N   ILE A 215       4.253  19.465  35.275  1.00 12.28           N  
ATOM   1661  CA  ILE A 215       4.526  20.792  35.866  1.00 13.50           C  
ATOM   1662  C   ILE A 215       4.939  20.710  37.342  1.00 16.25           C  
ATOM   1663  O   ILE A 215       5.930  21.296  37.819  1.00 13.17           O  
ATOM   1664  CB  ILE A 215       3.264  21.631  35.647  1.00 11.40           C  
ATOM   1665  CG1 ILE A 215       2.920  21.759  34.132  1.00 11.38           C  
ATOM   1666  CG2 ILE A 215       3.369  22.994  36.281  1.00  7.47           C  
ATOM   1667  CD1 ILE A 215       1.567  22.481  33.986  1.00 10.60           C  
ATOM   1668  N   PHE A 216       4.111  19.991  38.133  1.00 14.85           N  
ATOM   1669  CA  PHE A 216       4.353  19.842  39.561  1.00 19.46           C  
ATOM   1670  C   PHE A 216       5.738  19.256  39.902  1.00 18.40           C  
ATOM   1671  O   PHE A 216       6.445  19.804  40.764  1.00 14.73           O  
ATOM   1672  CB  PHE A 216       3.269  19.015  40.256  1.00 17.64           C  
ATOM   1673  CG  PHE A 216       1.867  19.518  40.235  1.00 17.22           C  
ATOM   1674  CD1 PHE A 216       1.540  20.771  39.698  1.00 16.32           C  
ATOM   1675  CD2 PHE A 216       0.825  18.722  40.683  1.00 16.62           C  
ATOM   1676  CE1 PHE A 216       0.237  21.210  39.663  1.00 18.82           C  
ATOM   1677  CE2 PHE A 216      -0.488  19.177  40.670  1.00 16.43           C  
ATOM   1678  CZ  PHE A 216      -0.807  20.433  40.161  1.00 20.05           C  
ATOM   1679  N   ARG A 217       6.163  18.244  39.155  1.00 18.64           N  
ATOM   1680  CA  ARG A 217       7.479  17.667  39.323  1.00 19.85           C  
ATOM   1681  C   ARG A 217       8.610  18.622  38.992  1.00 19.08           C  
ATOM   1682  O   ARG A 217       9.635  18.403  39.616  1.00 19.84           O  
ATOM   1683  CB  ARG A 217       7.622  16.342  38.558  1.00 22.06           C  
ATOM   1684  CG  ARG A 217       6.725  15.295  39.241  1.00 27.59           C  
ATOM   1685  CD  ARG A 217       6.995  13.900  38.744  1.00 31.44           C  
ATOM   1686  NE  ARG A 217       6.939  13.648  37.341  1.00 34.03           N  
ATOM   1687  CZ  ARG A 217       6.281  13.369  36.261  1.00 38.47           C  
ATOM   1688  NH1 ARG A 217       4.966  13.148  36.160  1.00 37.75           N  
ATOM   1689  NH2 ARG A 217       6.989  13.220  35.095  1.00 40.00           N  
ATOM   1690  N   THR A 218       8.478  19.637  38.132  1.00 15.96           N  
ATOM   1691  CA  THR A 218       9.596  20.554  37.950  1.00 17.73           C  
ATOM   1692  C   THR A 218       9.496  21.763  38.879  1.00 17.67           C  
ATOM   1693  O   THR A 218      10.427  22.228  39.501  1.00 20.60           O  
ATOM   1694  CB  THR A 218       9.555  21.044  36.478  1.00 19.18           C  
ATOM   1695  OG1 THR A 218       9.751  19.835  35.697  1.00 18.24           O  
ATOM   1696  CG2 THR A 218      10.592  22.072  36.145  1.00 17.39           C  
ATOM   1697  N   LEU A 219       8.337  22.340  39.075  1.00 16.85           N  
ATOM   1698  CA  LEU A 219       8.065  23.596  39.719  1.00 16.99           C  
ATOM   1699  C   LEU A 219       7.526  23.386  41.128  1.00 16.58           C  
ATOM   1700  O   LEU A 219       7.440  24.358  41.802  1.00 13.23           O  
ATOM   1701  CB  LEU A 219       7.104  24.377  38.832  1.00 17.99           C  
ATOM   1702  CG  LEU A 219       7.579  24.791  37.412  1.00 19.81           C  
ATOM   1703  CD1 LEU A 219       6.504  25.700  36.805  1.00 19.48           C  
ATOM   1704  CD2 LEU A 219       8.882  25.592  37.436  1.00 18.68           C  
ATOM   1705  N   GLY A 220       7.278  22.164  41.531  1.00 17.26           N  
ATOM   1706  CA  GLY A 220       6.785  21.879  42.866  1.00 19.72           C  
ATOM   1707  C   GLY A 220       5.255  21.891  42.848  1.00 18.90           C  
ATOM   1708  O   GLY A 220       4.605  22.601  42.059  1.00 14.56           O  
ATOM   1709  N   THR A 221       4.703  20.989  43.654  1.00 20.18           N  
ATOM   1710  CA  THR A 221       3.209  20.997  43.716  1.00 18.63           C  
ATOM   1711  C   THR A 221       2.815  22.333  44.317  1.00 18.18           C  
ATOM   1712  O   THR A 221       3.275  22.690  45.384  1.00 20.59           O  
ATOM   1713  CB  THR A 221       2.665  19.840  44.548  1.00 19.32           C  
ATOM   1714  OG1 THR A 221       3.151  18.604  43.970  1.00 19.64           O  
ATOM   1715  CG2 THR A 221       1.123  19.845  44.586  1.00 15.20           C  
ATOM   1716  N   PRO A 222       1.983  23.140  43.676  1.00 18.51           N  
ATOM   1717  CA  PRO A 222       1.582  24.425  44.215  1.00 18.99           C  
ATOM   1718  C   PRO A 222       0.718  24.221  45.468  1.00 20.99           C  
ATOM   1719  O   PRO A 222       0.038  23.190  45.605  1.00 18.14           O  
ATOM   1720  CB  PRO A 222       0.745  25.002  43.048  1.00 19.39           C  
ATOM   1721  CG  PRO A 222       0.092  23.797  42.498  1.00 16.58           C  
ATOM   1722  CD  PRO A 222       1.258  22.802  42.407  1.00 16.63           C  
ATOM   1723  N   ASP A 223       0.727  25.143  46.400  1.00 21.51           N  
ATOM   1724  CA  ASP A 223      -0.102  25.143  47.593  1.00 22.61           C  
ATOM   1725  C   ASP A 223      -0.557  26.573  47.848  1.00 20.80           C  
ATOM   1726  O   ASP A 223      -0.245  27.477  47.070  1.00 16.06           O  
ATOM   1727  CB  ASP A 223       0.618  24.591  48.825  1.00 26.78           C  
ATOM   1728  CG  ASP A 223       1.923  25.344  49.070  1.00 30.55           C  
ATOM   1729  OD1 ASP A 223       2.173  26.470  48.585  1.00 29.02           O  
ATOM   1730  OD2 ASP A 223       2.770  24.733  49.759  1.00 33.69           O  
ATOM   1731  N   GLU A 224      -1.246  26.826  48.969  1.00 18.84           N  
ATOM   1732  CA  GLU A 224      -1.740  28.141  49.320  1.00 17.68           C  
ATOM   1733  C   GLU A 224      -0.641  29.144  49.554  1.00 19.69           C  
ATOM   1734  O   GLU A 224      -0.874  30.335  49.315  1.00 21.35           O  
ATOM   1735  CB  GLU A 224      -2.757  28.011  50.491  1.00 22.39           C  
ATOM   1736  CG  GLU A 224      -4.033  27.212  50.111  1.00 22.38           C  
ATOM   1737  CD  GLU A 224      -4.940  27.996  49.221  1.00 21.05           C  
ATOM   1738  OE1 GLU A 224      -4.829  29.236  49.223  1.00 20.95           O  
ATOM   1739  OE2 GLU A 224      -5.838  27.457  48.488  1.00 24.43           O  
ATOM   1740  N   VAL A 225       0.587  28.781  49.915  1.00 22.36           N  
ATOM   1741  CA  VAL A 225       1.706  29.682  50.032  1.00 23.45           C  
ATOM   1742  C   VAL A 225       2.080  30.258  48.651  1.00 23.61           C  
ATOM   1743  O   VAL A 225       2.245  31.476  48.544  1.00 22.53           O  
ATOM   1744  CB  VAL A 225       3.002  29.027  50.577  1.00 24.86           C  
ATOM   1745  CG1 VAL A 225       4.125  30.101  50.543  1.00 25.69           C  
ATOM   1746  CG2 VAL A 225       2.867  28.497  51.991  1.00 25.01           C  
ATOM   1747  N   VAL A 226       2.340  29.402  47.655  1.00 22.00           N  
ATOM   1748  CA  VAL A 226       2.785  30.006  46.382  1.00 24.38           C  
ATOM   1749  C   VAL A 226       1.634  30.487  45.519  1.00 22.03           C  
ATOM   1750  O   VAL A 226       1.766  31.421  44.736  1.00 21.64           O  
ATOM   1751  CB  VAL A 226       3.752  29.146  45.565  1.00 25.61           C  
ATOM   1752  CG1 VAL A 226       3.122  27.879  44.978  1.00 25.70           C  
ATOM   1753  CG2 VAL A 226       4.264  29.974  44.405  1.00 28.79           C  
ATOM   1754  N   TRP A 227       0.430  29.939  45.726  1.00 19.61           N  
ATOM   1755  CA  TRP A 227      -0.714  30.312  44.913  1.00 18.84           C  
ATOM   1756  C   TRP A 227      -1.989  30.337  45.740  1.00 20.74           C  
ATOM   1757  O   TRP A 227      -2.744  29.370  45.841  1.00 20.92           O  
ATOM   1758  CB  TRP A 227      -0.852  29.292  43.763  1.00 17.80           C  
ATOM   1759  CG  TRP A 227      -1.855  29.605  42.673  1.00 15.89           C  
ATOM   1760  CD1 TRP A 227      -2.775  30.624  42.599  1.00 14.25           C  
ATOM   1761  CD2 TRP A 227      -2.041  28.797  41.505  1.00 13.88           C  
ATOM   1762  NE1 TRP A 227      -3.540  30.471  41.442  1.00 13.27           N  
ATOM   1763  CE2 TRP A 227      -3.110  29.363  40.785  1.00 16.62           C  
ATOM   1764  CE3 TRP A 227      -1.424  27.621  41.044  1.00 15.96           C  
ATOM   1765  CZ2 TRP A 227      -3.529  28.866  39.540  1.00 18.37           C  
ATOM   1766  CZ3 TRP A 227      -1.862  27.080  39.839  1.00 20.44           C  
ATOM   1767  CH2 TRP A 227      -2.885  27.706  39.086  1.00 18.84           C  
ATOM   1768  N   PRO A 228      -2.254  31.480  46.355  1.00 20.77           N  
ATOM   1769  CA  PRO A 228      -3.446  31.656  47.192  1.00 21.41           C  
ATOM   1770  C   PRO A 228      -4.679  31.300  46.388  1.00 19.87           C  
ATOM   1771  O   PRO A 228      -4.772  31.837  45.305  1.00 21.86           O  
ATOM   1772  CB  PRO A 228      -3.459  33.136  47.572  1.00 18.85           C  
ATOM   1773  CG  PRO A 228      -1.992  33.448  47.570  1.00 22.23           C  
ATOM   1774  CD  PRO A 228      -1.423  32.696  46.379  1.00 21.42           C  
ATOM   1775  N   GLY A 229      -5.511  30.369  46.861  1.00 20.26           N  
ATOM   1776  CA  GLY A 229      -6.739  30.035  46.100  1.00 16.91           C  
ATOM   1777  C   GLY A 229      -6.557  28.737  45.352  1.00 18.43           C  
ATOM   1778  O   GLY A 229      -7.557  28.157  44.968  1.00 22.00           O  
ATOM   1779  N   VAL A 230      -5.359  28.232  45.114  1.00 17.28           N  
ATOM   1780  CA  VAL A 230      -5.162  27.014  44.350  1.00 18.22           C  
ATOM   1781  C   VAL A 230      -5.938  25.818  44.828  1.00 18.07           C  
ATOM   1782  O   VAL A 230      -6.684  25.193  44.074  1.00 18.32           O  
ATOM   1783  CB  VAL A 230      -3.663  26.713  44.202  1.00 18.69           C  
ATOM   1784  CG1 VAL A 230      -3.050  26.224  45.506  1.00 15.98           C  
ATOM   1785  CG2 VAL A 230      -3.471  25.731  43.044  1.00 18.71           C  
ATOM   1786  N   THR A 231      -5.983  25.501  46.115  1.00 23.39           N  
ATOM   1787  CA  THR A 231      -6.679  24.326  46.669  1.00 23.83           C  
ATOM   1788  C   THR A 231      -8.183  24.427  46.541  1.00 25.15           C  
ATOM   1789  O   THR A 231      -8.970  23.495  46.738  1.00 24.86           O  
ATOM   1790  CB  THR A 231      -6.292  24.131  48.160  1.00 23.73           C  
ATOM   1791  OG1 THR A 231      -6.884  25.158  48.987  1.00 26.29           O  
ATOM   1792  CG2 THR A 231      -4.796  24.036  48.354  1.00 21.99           C  
ATOM   1793  N   SER A 232      -8.709  25.608  46.171  1.00 25.51           N  
ATOM   1794  CA  SER A 232     -10.175  25.635  45.969  1.00 27.21           C  
ATOM   1795  C   SER A 232     -10.493  25.663  44.483  1.00 26.74           C  
ATOM   1796  O   SER A 232     -11.636  25.874  44.053  1.00 25.14           O  
ATOM   1797  CB  SER A 232     -10.704  26.724  46.902  1.00 28.62           C  
ATOM   1798  OG  SER A 232     -10.843  27.925  46.140  1.00 35.30           O  
ATOM   1799  N   MET A 233      -9.507  25.426  43.572  1.00 23.95           N  
ATOM   1800  CA  MET A 233      -9.931  25.398  42.136  1.00 23.08           C  
ATOM   1801  C   MET A 233     -10.709  24.127  41.826  1.00 22.31           C  
ATOM   1802  O   MET A 233     -10.486  23.102  42.463  1.00 19.17           O  
ATOM   1803  CB  MET A 233      -8.652  25.449  41.338  1.00 27.39           C  
ATOM   1804  CG  MET A 233      -8.139  26.889  41.738  1.00 32.41           C  
ATOM   1805  SD  MET A 233      -6.795  27.205  40.604  1.00 36.66           S  
ATOM   1806  CE  MET A 233      -7.844  27.669  39.243  1.00 32.05           C  
ATOM   1807  N   PRO A 234     -11.525  24.186  40.788  1.00 19.70           N  
ATOM   1808  CA  PRO A 234     -12.368  23.086  40.424  1.00 20.52           C  
ATOM   1809  C   PRO A 234     -11.745  21.721  40.332  1.00 21.62           C  
ATOM   1810  O   PRO A 234     -12.307  20.781  40.832  1.00 19.65           O  
ATOM   1811  CB  PRO A 234     -12.822  23.545  39.026  1.00 21.60           C  
ATOM   1812  CG  PRO A 234     -13.062  25.010  39.245  1.00 21.77           C  
ATOM   1813  CD  PRO A 234     -11.719  25.373  39.916  1.00 19.99           C  
ATOM   1814  N   ASP A 235     -10.584  21.575  39.648  1.00 20.16           N  
ATOM   1815  CA  ASP A 235      -9.999  20.269  39.417  1.00 18.73           C  
ATOM   1816  C   ASP A 235      -8.808  20.029  40.332  1.00 18.85           C  
ATOM   1817  O   ASP A 235      -8.056  19.088  40.196  1.00 21.60           O  
ATOM   1818  CB  ASP A 235      -9.611  20.110  37.938  1.00 20.13           C  
ATOM   1819  CG  ASP A 235     -10.844  20.277  37.083  1.00 22.91           C  
ATOM   1820  OD1 ASP A 235     -11.926  19.857  37.506  1.00 26.54           O  
ATOM   1821  OD2 ASP A 235     -10.849  20.965  36.066  1.00 23.51           O  
ATOM   1822  N   TYR A 236      -8.755  20.793  41.434  1.00 20.54           N  
ATOM   1823  CA  TYR A 236      -7.708  20.631  42.386  1.00 19.50           C  
ATOM   1824  C   TYR A 236      -8.039  19.426  43.259  1.00 20.97           C  
ATOM   1825  O   TYR A 236      -9.191  19.395  43.670  1.00 20.38           O  
ATOM   1826  CB  TYR A 236      -7.576  21.893  43.255  1.00 21.20           C  
ATOM   1827  CG  TYR A 236      -6.409  21.609  44.202  1.00 23.59           C  
ATOM   1828  CD1 TYR A 236      -5.058  21.800  43.918  1.00 24.45           C  
ATOM   1829  CD2 TYR A 236      -6.764  21.124  45.430  1.00 25.17           C  
ATOM   1830  CE1 TYR A 236      -4.115  21.489  44.899  1.00 25.52           C  
ATOM   1831  CE2 TYR A 236      -5.840  20.819  46.397  1.00 28.45           C  
ATOM   1832  CZ  TYR A 236      -4.501  21.002  46.106  1.00 27.83           C  
ATOM   1833  OH  TYR A 236      -3.688  20.637  47.157  1.00 30.87           O  
ATOM   1834  N   LYS A 237      -7.081  18.554  43.557  1.00 20.07           N  
ATOM   1835  CA  LYS A 237      -7.422  17.468  44.497  1.00 24.43           C  
ATOM   1836  C   LYS A 237      -6.319  17.410  45.557  1.00 23.63           C  
ATOM   1837  O   LYS A 237      -5.152  17.398  45.211  1.00 22.86           O  
ATOM   1838  CB  LYS A 237      -7.593  16.150  43.749  1.00 23.88           C  
ATOM   1839  CG  LYS A 237      -8.431  16.065  42.492  1.00 25.62           C  
ATOM   1840  CD  LYS A 237      -9.838  15.549  42.703  1.00 29.97           C  
ATOM   1841  CE  LYS A 237     -10.814  15.933  41.567  1.00 29.94           C  
ATOM   1842  NZ  LYS A 237     -10.023  15.642  40.325  1.00 33.12           N  
ATOM   1843  N   PRO A 238      -6.669  17.352  46.858  1.00 23.39           N  
ATOM   1844  CA  PRO A 238      -5.840  17.183  48.005  1.00 21.65           C  
ATOM   1845  C   PRO A 238      -4.981  15.917  47.957  1.00 23.22           C  
ATOM   1846  O   PRO A 238      -3.830  15.870  48.444  1.00 22.31           O  
ATOM   1847  CB  PRO A 238      -6.814  17.083  49.189  1.00 22.77           C  
ATOM   1848  CG  PRO A 238      -8.055  17.803  48.710  1.00 23.21           C  
ATOM   1849  CD  PRO A 238      -8.123  17.426  47.258  1.00 24.04           C  
ATOM   1850  N   SER A 239      -5.425  14.930  47.149  1.00 18.99           N  
ATOM   1851  CA  SER A 239      -4.591  13.753  46.942  1.00 20.85           C  
ATOM   1852  C   SER A 239      -3.497  14.026  45.919  1.00 20.21           C  
ATOM   1853  O   SER A 239      -2.791  13.054  45.600  1.00 17.60           O  
ATOM   1854  CB  SER A 239      -5.465  12.535  46.523  1.00 18.41           C  
ATOM   1855  OG  SER A 239      -6.316  12.991  45.430  1.00 17.49           O  
ATOM   1856  N   PHE A 240      -3.331  15.178  45.272  1.00 20.15           N  
ATOM   1857  CA  PHE A 240      -2.174  15.281  44.307  1.00 19.22           C  
ATOM   1858  C   PHE A 240      -0.877  14.988  45.058  1.00 21.06           C  
ATOM   1859  O   PHE A 240      -0.669  15.547  46.130  1.00 18.89           O  
ATOM   1860  CB  PHE A 240      -2.001  16.732  43.841  1.00 19.18           C  
ATOM   1861  CG  PHE A 240      -3.007  17.289  42.882  1.00 17.21           C  
ATOM   1862  CD1 PHE A 240      -3.744  16.423  42.048  1.00 17.63           C  
ATOM   1863  CD2 PHE A 240      -3.194  18.646  42.768  1.00 17.58           C  
ATOM   1864  CE1 PHE A 240      -4.647  16.907  41.118  1.00 16.63           C  
ATOM   1865  CE2 PHE A 240      -4.117  19.147  41.853  1.00 17.20           C  
ATOM   1866  CZ  PHE A 240      -4.848  18.299  41.047  1.00 16.33           C  
ATOM   1867  N   PRO A 241       0.070  14.247  44.510  1.00 20.37           N  
ATOM   1868  CA  PRO A 241       1.329  14.058  45.207  1.00 22.07           C  
ATOM   1869  C   PRO A 241       1.947  15.440  45.471  1.00 25.39           C  
ATOM   1870  O   PRO A 241       1.724  16.533  44.897  1.00 23.32           O  
ATOM   1871  CB  PRO A 241       2.112  13.216  44.231  1.00 21.73           C  
ATOM   1872  CG  PRO A 241       1.043  12.436  43.455  1.00 19.95           C  
ATOM   1873  CD  PRO A 241      -0.053  13.479  43.241  1.00 19.90           C  
ATOM   1874  N   LYS A 242       2.842  15.445  46.449  1.00 26.17           N  
ATOM   1875  CA  LYS A 242       3.622  16.607  46.847  1.00 29.43           C  
ATOM   1876  C   LYS A 242       5.076  16.488  46.400  1.00 29.05           C  
ATOM   1877  O   LYS A 242       5.897  15.805  47.022  1.00 30.75           O  
ATOM   1878  CB  LYS A 242       3.508  16.853  48.365  1.00 31.61           C  
ATOM   1879  CG  LYS A 242       2.084  17.419  48.585  1.00 34.87           C  
ATOM   1880  CD  LYS A 242       1.843  17.824  50.048  1.00 38.12           C  
ATOM   1881  CE  LYS A 242       0.352  18.227  50.132  1.00 38.52           C  
ATOM   1882  NZ  LYS A 242      -0.462  17.095  50.645  1.00 37.52           N  
ATOM   1883  N   TRP A 243       5.406  17.150  45.295  1.00 24.45           N  
ATOM   1884  CA  TRP A 243       6.762  17.129  44.769  1.00 24.20           C  
ATOM   1885  C   TRP A 243       7.480  18.429  45.085  1.00 23.48           C  
ATOM   1886  O   TRP A 243       6.855  19.484  45.177  1.00 21.68           O  
ATOM   1887  CB  TRP A 243       6.728  16.943  43.254  1.00 24.93           C  
ATOM   1888  CG  TRP A 243       6.352  15.594  42.746  1.00 24.68           C  
ATOM   1889  CD1 TRP A 243       7.151  14.485  42.816  1.00 27.23           C  
ATOM   1890  CD2 TRP A 243       5.151  15.174  42.096  1.00 23.55           C  
ATOM   1891  NE1 TRP A 243       6.511  13.393  42.263  1.00 25.96           N  
ATOM   1892  CE2 TRP A 243       5.292  13.798  41.797  1.00 25.38           C  
ATOM   1893  CE3 TRP A 243       3.983  15.811  41.728  1.00 21.89           C  
ATOM   1894  CZ2 TRP A 243       4.318  13.057  41.131  1.00 23.67           C  
ATOM   1895  CZ3 TRP A 243       2.983  15.070  41.124  1.00 22.20           C  
ATOM   1896  CH2 TRP A 243       3.171  13.741  40.797  1.00 22.87           C  
ATOM   1897  N   ALA A 244       8.799  18.347  45.290  1.00 25.42           N  
ATOM   1898  CA  ALA A 244       9.601  19.519  45.610  1.00 23.50           C  
ATOM   1899  C   ALA A 244       9.871  20.376  44.388  1.00 23.39           C  
ATOM   1900  O   ALA A 244       9.999  19.786  43.327  1.00 22.22           O  
ATOM   1901  CB  ALA A 244      11.028  19.042  46.062  1.00 24.28           C  
ATOM   1902  N   ARG A 245      10.132  21.671  44.522  1.00 22.50           N  
ATOM   1903  CA  ARG A 245      10.463  22.454  43.340  1.00 27.36           C  
ATOM   1904  C   ARG A 245      11.898  22.120  42.960  1.00 32.08           C  
ATOM   1905  O   ARG A 245      12.701  21.781  43.830  1.00 32.19           O  
ATOM   1906  CB  ARG A 245      10.244  23.936  43.595  1.00 25.79           C  
ATOM   1907  CG  ARG A 245      10.689  24.935  42.558  1.00 26.20           C  
ATOM   1908  CD  ARG A 245      10.246  26.355  43.035  1.00 23.71           C  
ATOM   1909  NE  ARG A 245      10.431  27.256  41.955  1.00 28.02           N  
ATOM   1910  CZ  ARG A 245       9.602  27.678  40.963  1.00 30.07           C  
ATOM   1911  NH1 ARG A 245       8.333  27.255  40.895  1.00 27.74           N  
ATOM   1912  NH2 ARG A 245      10.062  28.556  40.061  1.00 26.18           N  
ATOM   1913  N   GLN A 246      12.223  22.268  41.667  1.00 33.79           N  
ATOM   1914  CA  GLN A 246      13.571  22.065  41.174  1.00 34.38           C  
ATOM   1915  C   GLN A 246      14.197  23.422  40.842  1.00 33.31           C  
ATOM   1916  O   GLN A 246      13.462  24.352  40.454  1.00 30.77           O  
ATOM   1917  CB  GLN A 246      13.622  21.169  39.935  1.00 37.04           C  
ATOM   1918  CG  GLN A 246      12.885  19.833  40.062  1.00 43.61           C  
ATOM   1919  CD  GLN A 246      13.719  18.899  40.920  1.00 47.03           C  
ATOM   1920  OE1 GLN A 246      14.907  18.774  40.563  1.00 50.35           O  
ATOM   1921  NE2 GLN A 246      13.223  18.297  41.997  1.00 47.20           N  
ATOM   1922  N   ASP A 247      15.551  23.462  40.838  1.00 30.96           N  
ATOM   1923  CA  ASP A 247      16.257  24.666  40.482  1.00 30.34           C  
ATOM   1924  C   ASP A 247      16.244  24.903  38.991  1.00 28.29           C  
ATOM   1925  O   ASP A 247      16.776  24.040  38.289  1.00 28.96           O  
ATOM   1926  CB  ASP A 247      17.791  24.559  40.725  1.00 35.15           C  
ATOM   1927  CG  ASP A 247      18.312  24.610  42.118  1.00 39.99           C  
ATOM   1928  OD1 ASP A 247      17.629  25.208  43.002  1.00 41.24           O  
ATOM   1929  OD2 ASP A 247      19.433  24.062  42.332  1.00 42.54           O  
ATOM   1930  N   PHE A 248      15.970  26.050  38.449  1.00 26.92           N  
ATOM   1931  CA  PHE A 248      16.069  26.405  37.035  1.00 25.64           C  
ATOM   1932  C   PHE A 248      17.453  26.227  36.464  1.00 24.35           C  
ATOM   1933  O   PHE A 248      17.642  26.058  35.260  1.00 24.55           O  
ATOM   1934  CB  PHE A 248      15.714  27.922  36.855  1.00 26.18           C  
ATOM   1935  CG  PHE A 248      14.225  28.076  36.786  1.00 29.15           C  
ATOM   1936  CD1 PHE A 248      13.423  27.550  37.759  1.00 32.65           C  
ATOM   1937  CD2 PHE A 248      13.615  28.656  35.706  1.00 33.37           C  
ATOM   1938  CE1 PHE A 248      12.042  27.664  37.681  1.00 34.57           C  
ATOM   1939  CE2 PHE A 248      12.242  28.782  35.624  1.00 36.72           C  
ATOM   1940  CZ  PHE A 248      11.438  28.288  36.642  1.00 33.59           C  
ATOM   1941  N   SER A 249      18.469  26.171  37.355  1.00 21.76           N  
ATOM   1942  CA  SER A 249      19.809  25.919  36.858  1.00 23.32           C  
ATOM   1943  C   SER A 249      19.845  24.498  36.273  1.00 21.67           C  
ATOM   1944  O   SER A 249      20.526  24.236  35.243  1.00 19.02           O  
ATOM   1945  CB  SER A 249      20.828  26.237  37.998  1.00 22.99           C  
ATOM   1946  OG  SER A 249      20.642  25.149  38.945  1.00 20.88           O  
ATOM   1947  N   LYS A 250      19.056  23.615  36.854  1.00 19.24           N  
ATOM   1948  CA  LYS A 250      18.923  22.267  36.350  1.00 24.42           C  
ATOM   1949  C   LYS A 250      17.921  22.109  35.203  1.00 26.69           C  
ATOM   1950  O   LYS A 250      18.069  21.286  34.310  1.00 27.06           O  
ATOM   1951  CB  LYS A 250      18.424  21.330  37.496  1.00 28.13           C  
ATOM   1952  CG  LYS A 250      18.346  19.931  36.911  1.00 32.66           C  
ATOM   1953  CD  LYS A 250      18.188  18.763  37.852  1.00 36.42           C  
ATOM   1954  CE  LYS A 250      19.260  17.767  37.318  1.00 39.09           C  
ATOM   1955  NZ  LYS A 250      18.792  16.376  37.620  1.00 42.95           N  
ATOM   1956  N   VAL A 251      16.860  22.917  35.181  1.00 28.49           N  
ATOM   1957  CA  VAL A 251      15.827  22.854  34.149  1.00 28.70           C  
ATOM   1958  C   VAL A 251      16.205  23.429  32.800  1.00 28.30           C  
ATOM   1959  O   VAL A 251      15.915  22.838  31.740  1.00 28.95           O  
ATOM   1960  CB  VAL A 251      14.527  23.548  34.631  1.00 28.35           C  
ATOM   1961  CG1 VAL A 251      13.456  23.268  33.554  1.00 31.01           C  
ATOM   1962  CG2 VAL A 251      14.103  23.045  35.992  1.00 28.80           C  
ATOM   1963  N   VAL A 252      16.909  24.585  32.736  1.00 26.62           N  
ATOM   1964  CA  VAL A 252      17.322  25.135  31.436  1.00 25.15           C  
ATOM   1965  C   VAL A 252      18.792  25.499  31.450  1.00 27.11           C  
ATOM   1966  O   VAL A 252      19.176  26.637  31.120  1.00 29.05           O  
ATOM   1967  CB  VAL A 252      16.409  26.344  31.078  1.00 23.38           C  
ATOM   1968  CG1 VAL A 252      14.940  25.906  30.903  1.00 21.85           C  
ATOM   1969  CG2 VAL A 252      16.427  27.491  32.086  1.00 19.43           C  
ATOM   1970  N   PRO A 253      19.720  24.557  31.705  1.00 27.47           N  
ATOM   1971  CA  PRO A 253      21.105  24.780  32.063  1.00 29.09           C  
ATOM   1972  C   PRO A 253      21.935  25.804  31.393  1.00 33.49           C  
ATOM   1973  O   PRO A 253      22.568  26.735  31.941  1.00 38.57           O  
ATOM   1974  CB  PRO A 253      21.819  23.429  31.931  1.00 26.74           C  
ATOM   1975  CG  PRO A 253      20.715  22.444  31.776  1.00 24.14           C  
ATOM   1976  CD  PRO A 253      19.445  23.172  32.112  1.00 24.55           C  
ATOM   1977  N   PRO A 254      21.931  25.703  30.062  1.00 33.66           N  
ATOM   1978  CA  PRO A 254      22.786  26.678  29.367  1.00 33.32           C  
ATOM   1979  C   PRO A 254      22.363  28.076  29.740  1.00 31.81           C  
ATOM   1980  O   PRO A 254      23.257  28.911  29.944  1.00 33.32           O  
ATOM   1981  CB  PRO A 254      22.695  26.223  27.936  1.00 33.01           C  
ATOM   1982  CG  PRO A 254      21.604  25.221  27.850  1.00 33.64           C  
ATOM   1983  CD  PRO A 254      21.203  24.740  29.224  1.00 29.94           C  
ATOM   1984  N   LEU A 255      21.103  28.419  29.960  1.00 29.00           N  
ATOM   1985  CA  LEU A 255      20.667  29.815  30.166  1.00 26.07           C  
ATOM   1986  C   LEU A 255      21.322  30.612  31.272  1.00 25.87           C  
ATOM   1987  O   LEU A 255      21.483  30.155  32.411  1.00 24.36           O  
ATOM   1988  CB  LEU A 255      19.136  29.803  30.191  1.00 25.66           C  
ATOM   1989  CG  LEU A 255      18.321  31.056  29.917  1.00 23.96           C  
ATOM   1990  CD1 LEU A 255      18.629  31.656  28.563  1.00 21.59           C  
ATOM   1991  CD2 LEU A 255      16.839  30.853  30.178  1.00 20.62           C  
ATOM   1992  N   ASP A 256      21.686  31.890  31.004  1.00 21.86           N  
ATOM   1993  CA  ASP A 256      22.297  32.704  32.036  1.00 23.16           C  
ATOM   1994  C   ASP A 256      21.293  33.163  33.108  1.00 21.30           C  
ATOM   1995  O   ASP A 256      20.079  32.968  33.027  1.00 18.81           O  
ATOM   1996  CB  ASP A 256      23.063  33.874  31.434  1.00 23.75           C  
ATOM   1997  CG  ASP A 256      22.136  34.802  30.671  1.00 26.44           C  
ATOM   1998  OD1 ASP A 256      21.210  35.445  31.191  1.00 23.72           O  
ATOM   1999  OD2 ASP A 256      22.346  34.826  29.440  1.00 30.22           O  
ATOM   2000  N   GLU A 257      21.749  33.797  34.190  1.00 19.08           N  
ATOM   2001  CA  GLU A 257      20.868  34.189  35.275  1.00 20.01           C  
ATOM   2002  C   GLU A 257      19.811  35.205  34.870  1.00 18.11           C  
ATOM   2003  O   GLU A 257      18.674  35.092  35.382  1.00 16.51           O  
ATOM   2004  CB  GLU A 257      21.690  34.603  36.525  1.00 24.04           C  
ATOM   2005  CG  GLU A 257      20.853  35.218  37.626  1.00 26.02           C  
ATOM   2006  CD  GLU A 257      19.899  34.226  38.283  1.00 29.87           C  
ATOM   2007  OE1 GLU A 257      20.032  33.005  38.222  1.00 28.27           O  
ATOM   2008  OE2 GLU A 257      18.927  34.691  38.935  1.00 33.20           O  
ATOM   2009  N   ASP A 258      20.067  36.065  33.882  1.00 16.75           N  
ATOM   2010  CA  ASP A 258      18.959  36.967  33.448  1.00 17.80           C  
ATOM   2011  C   ASP A 258      17.796  36.167  32.807  1.00 16.51           C  
ATOM   2012  O   ASP A 258      16.596  36.317  33.056  1.00 12.74           O  
ATOM   2013  CB  ASP A 258      19.393  38.020  32.428  1.00 14.57           C  
ATOM   2014  CG  ASP A 258      20.233  39.095  33.086  1.00 18.56           C  
ATOM   2015  OD1 ASP A 258      19.934  39.554  34.219  1.00 20.11           O  
ATOM   2016  OD2 ASP A 258      21.224  39.564  32.517  1.00 19.00           O  
ATOM   2017  N   GLY A 259      18.136  35.276  31.900  1.00 16.06           N  
ATOM   2018  CA  GLY A 259      17.238  34.383  31.212  1.00 16.73           C  
ATOM   2019  C   GLY A 259      16.446  33.569  32.278  1.00 19.57           C  
ATOM   2020  O   GLY A 259      15.202  33.474  32.254  1.00 19.02           O  
ATOM   2021  N   ARG A 260      17.161  32.965  33.222  1.00 19.02           N  
ATOM   2022  CA  ARG A 260      16.529  32.117  34.224  1.00 20.34           C  
ATOM   2023  C   ARG A 260      15.569  32.895  35.114  1.00 18.92           C  
ATOM   2024  O   ARG A 260      14.427  32.474  35.266  1.00 19.14           O  
ATOM   2025  CB  ARG A 260      17.546  31.365  35.101  1.00 21.20           C  
ATOM   2026  CG  ARG A 260      18.417  30.433  34.287  1.00 26.59           C  
ATOM   2027  CD  ARG A 260      19.258  29.532  35.197  1.00 27.61           C  
ATOM   2028  NE  ARG A 260      19.992  30.330  36.177  1.00 31.03           N  
ATOM   2029  CZ  ARG A 260      21.293  30.256  36.311  1.00 34.38           C  
ATOM   2030  NH1 ARG A 260      21.968  29.469  35.500  1.00 37.08           N  
ATOM   2031  NH2 ARG A 260      21.962  30.971  37.219  1.00 39.33           N  
ATOM   2032  N   SER A 261      15.947  34.113  35.505  1.00 20.01           N  
ATOM   2033  CA  SER A 261      15.051  34.977  36.275  1.00 19.94           C  
ATOM   2034  C   SER A 261      13.796  35.353  35.497  1.00 20.31           C  
ATOM   2035  O   SER A 261      12.658  35.193  35.952  1.00 21.74           O  
ATOM   2036  CB  SER A 261      15.855  36.242  36.544  1.00 21.43           C  
ATOM   2037  OG  SER A 261      14.956  37.260  36.926  1.00 24.11           O  
ATOM   2038  N   LEU A 262      13.987  35.754  34.241  1.00 18.62           N  
ATOM   2039  CA  LEU A 262      12.844  36.038  33.386  1.00 16.69           C  
ATOM   2040  C   LEU A 262      11.965  34.788  33.232  1.00 15.61           C  
ATOM   2041  O   LEU A 262      10.749  34.861  33.385  1.00 13.50           O  
ATOM   2042  CB  LEU A 262      13.274  36.519  31.987  1.00 15.55           C  
ATOM   2043  CG  LEU A 262      12.150  36.742  30.992  1.00 16.49           C  
ATOM   2044  CD1 LEU A 262      10.972  37.568  31.482  1.00 14.29           C  
ATOM   2045  CD2 LEU A 262      12.712  37.325  29.697  1.00 17.95           C  
ATOM   2046  N   LEU A 263      12.537  33.629  32.872  1.00 17.11           N  
ATOM   2047  CA  LEU A 263      11.700  32.429  32.698  1.00 16.30           C  
ATOM   2048  C   LEU A 263      10.919  32.059  33.957  1.00 15.80           C  
ATOM   2049  O   LEU A 263       9.730  31.702  33.896  1.00 13.16           O  
ATOM   2050  CB  LEU A 263      12.598  31.225  32.255  1.00 15.08           C  
ATOM   2051  CG  LEU A 263      11.818  29.901  32.174  1.00 15.99           C  
ATOM   2052  CD1 LEU A 263      10.912  29.898  30.931  1.00 17.88           C  
ATOM   2053  CD2 LEU A 263      12.744  28.681  32.020  1.00 15.97           C  
ATOM   2054  N   SER A 264      11.509  32.167  35.173  1.00 15.58           N  
ATOM   2055  CA  SER A 264      10.759  31.773  36.372  1.00 17.58           C  
ATOM   2056  C   SER A 264       9.613  32.709  36.617  1.00 16.29           C  
ATOM   2057  O   SER A 264       8.630  32.342  37.266  1.00 16.03           O  
ATOM   2058  CB  SER A 264      11.451  31.689  37.793  1.00 19.68           C  
ATOM   2059  OG  SER A 264      12.373  32.726  37.840  1.00 26.84           O  
ATOM   2060  N   GLN A 265       9.763  33.973  36.208  1.00 16.44           N  
ATOM   2061  CA  GLN A 265       8.637  34.905  36.436  1.00 15.44           C  
ATOM   2062  C   GLN A 265       7.544  34.661  35.410  1.00 16.00           C  
ATOM   2063  O   GLN A 265       6.361  34.982  35.642  1.00 14.46           O  
ATOM   2064  CB  GLN A 265       9.144  36.361  36.315  1.00 17.85           C  
ATOM   2065  CG  GLN A 265      10.098  36.666  37.470  1.00 19.70           C  
ATOM   2066  CD  GLN A 265      10.446  38.157  37.458  1.00 24.04           C  
ATOM   2067  OE1 GLN A 265       9.899  38.968  38.165  1.00 28.15           O  
ATOM   2068  NE2 GLN A 265      11.386  38.581  36.664  1.00 24.65           N  
ATOM   2069  N   MET A 266       7.919  34.143  34.230  1.00 12.51           N  
ATOM   2070  CA  MET A 266       6.921  33.826  33.195  1.00 13.89           C  
ATOM   2071  C   MET A 266       6.178  32.534  33.536  1.00 14.63           C  
ATOM   2072  O   MET A 266       5.083  32.237  33.060  1.00 13.54           O  
ATOM   2073  CB  MET A 266       7.610  33.594  31.819  1.00 11.05           C  
ATOM   2074  CG  MET A 266       8.170  34.886  31.197  1.00 11.42           C  
ATOM   2075  SD  MET A 266       9.048  34.488  29.634  1.00 12.99           S  
ATOM   2076  CE  MET A 266       7.606  34.474  28.530  1.00  8.09           C  
ATOM   2077  N   LEU A 267       6.874  31.685  34.339  1.00 17.47           N  
ATOM   2078  CA  LEU A 267       6.252  30.472  34.879  1.00 16.19           C  
ATOM   2079  C   LEU A 267       5.725  30.582  36.306  1.00 17.41           C  
ATOM   2080  O   LEU A 267       5.514  29.506  36.934  1.00 15.33           O  
ATOM   2081  CB  LEU A 267       7.197  29.264  34.765  1.00 10.36           C  
ATOM   2082  CG  LEU A 267       7.654  28.996  33.325  1.00 10.96           C  
ATOM   2083  CD1 LEU A 267       8.559  27.728  33.346  1.00  8.19           C  
ATOM   2084  CD2 LEU A 267       6.478  28.776  32.354  1.00  9.13           C  
ATOM   2085  N   HIS A 268       5.394  31.793  36.781  1.00 18.77           N  
ATOM   2086  CA  HIS A 268       4.814  31.881  38.156  1.00 19.67           C  
ATOM   2087  C   HIS A 268       3.510  31.132  38.223  1.00 16.24           C  
ATOM   2088  O   HIS A 268       2.751  31.111  37.232  1.00 16.60           O  
ATOM   2089  CB  HIS A 268       4.605  33.316  38.699  1.00 24.35           C  
ATOM   2090  CG  HIS A 268       5.850  33.892  39.319  1.00 29.86           C  
ATOM   2091  ND1 HIS A 268       6.259  35.210  39.205  1.00 32.13           N  
ATOM   2092  CD2 HIS A 268       6.821  33.276  40.054  1.00 33.21           C  
ATOM   2093  CE1 HIS A 268       7.436  35.400  39.835  1.00 31.61           C  
ATOM   2094  NE2 HIS A 268       7.797  34.237  40.368  1.00 34.89           N  
ATOM   2095  N   TYR A 269       3.294  30.387  39.305  1.00 16.22           N  
ATOM   2096  CA  TYR A 269       2.040  29.605  39.424  1.00 14.71           C  
ATOM   2097  C   TYR A 269       0.857  30.547  39.487  1.00 17.28           C  
ATOM   2098  O   TYR A 269      -0.120  30.397  38.812  1.00 16.23           O  
ATOM   2099  CB  TYR A 269       2.027  28.674  40.624  1.00 10.39           C  
ATOM   2100  CG  TYR A 269       2.548  27.290  40.440  1.00 13.33           C  
ATOM   2101  CD1 TYR A 269       1.924  26.472  39.483  1.00 13.94           C  
ATOM   2102  CD2 TYR A 269       3.632  26.775  41.158  1.00 12.43           C  
ATOM   2103  CE1 TYR A 269       2.384  25.164  39.261  1.00 13.14           C  
ATOM   2104  CE2 TYR A 269       4.103  25.505  40.948  1.00 13.10           C  
ATOM   2105  CZ  TYR A 269       3.450  24.708  39.989  1.00 15.20           C  
ATOM   2106  OH  TYR A 269       3.891  23.395  39.721  1.00 15.91           O  
ATOM   2107  N   ASP A 270       0.904  31.579  40.360  1.00 21.12           N  
ATOM   2108  CA  ASP A 270      -0.247  32.465  40.521  1.00 20.52           C  
ATOM   2109  C   ASP A 270      -0.351  33.378  39.312  1.00 20.48           C  
ATOM   2110  O   ASP A 270       0.615  34.159  39.158  1.00 23.07           O  
ATOM   2111  CB  ASP A 270       0.084  33.350  41.737  1.00 18.18           C  
ATOM   2112  CG  ASP A 270      -1.146  34.215  42.059  1.00 20.77           C  
ATOM   2113  OD1 ASP A 270      -2.103  34.379  41.272  1.00 19.48           O  
ATOM   2114  OD2 ASP A 270      -1.136  34.655  43.188  1.00 21.75           O  
ATOM   2115  N   PRO A 271      -1.391  33.328  38.514  1.00 20.50           N  
ATOM   2116  CA  PRO A 271      -1.520  34.090  37.290  1.00 23.63           C  
ATOM   2117  C   PRO A 271      -1.480  35.588  37.510  1.00 25.97           C  
ATOM   2118  O   PRO A 271      -0.949  36.363  36.726  1.00 27.63           O  
ATOM   2119  CB  PRO A 271      -2.865  33.750  36.676  1.00 22.67           C  
ATOM   2120  CG  PRO A 271      -3.226  32.482  37.360  1.00 23.37           C  
ATOM   2121  CD  PRO A 271      -2.521  32.379  38.633  1.00 20.93           C  
ATOM   2122  N   ASN A 272      -1.920  36.021  38.690  1.00 28.72           N  
ATOM   2123  CA  ASN A 272      -1.846  37.413  39.051  1.00 28.14           C  
ATOM   2124  C   ASN A 272      -0.426  37.871  39.280  1.00 28.29           C  
ATOM   2125  O   ASN A 272      -0.291  39.095  39.328  1.00 28.74           O  
ATOM   2126  CB  ASN A 272      -2.561  37.608  40.391  1.00 30.67           C  
ATOM   2127  CG  ASN A 272      -3.948  38.012  39.910  1.00 35.36           C  
ATOM   2128  OD1 ASN A 272      -4.668  37.011  39.816  1.00 37.69           O  
ATOM   2129  ND2 ASN A 272      -4.055  39.336  39.659  1.00 34.33           N  
ATOM   2130  N   LYS A 273       0.448  36.922  39.653  1.00 25.13           N  
ATOM   2131  CA  LYS A 273       1.834  37.331  39.849  1.00 26.14           C  
ATOM   2132  C   LYS A 273       2.720  37.046  38.625  1.00 22.56           C  
ATOM   2133  O   LYS A 273       3.809  37.569  38.575  1.00 21.65           O  
ATOM   2134  CB  LYS A 273       2.406  36.634  41.095  1.00 29.38           C  
ATOM   2135  CG  LYS A 273       2.073  37.297  42.445  1.00 33.07           C  
ATOM   2136  CD  LYS A 273       0.837  38.110  42.480  1.00 34.70           C  
ATOM   2137  CE  LYS A 273       0.617  39.243  43.450  1.00 38.21           C  
ATOM   2138  NZ  LYS A 273       0.231  38.672  44.788  1.00 38.69           N  
ATOM   2139  N   ARG A 274       2.374  36.162  37.714  1.00 18.04           N  
ATOM   2140  CA  ARG A 274       3.207  35.891  36.516  1.00 17.33           C  
ATOM   2141  C   ARG A 274       3.575  37.243  35.871  1.00 15.12           C  
ATOM   2142  O   ARG A 274       2.672  38.069  35.812  1.00 16.68           O  
ATOM   2143  CB  ARG A 274       2.318  35.099  35.543  1.00 16.63           C  
ATOM   2144  CG  ARG A 274       3.021  34.138  34.585  1.00 15.55           C  
ATOM   2145  CD  ARG A 274       2.091  33.058  33.996  1.00 14.33           C  
ATOM   2146  NE  ARG A 274       1.648  32.056  34.978  1.00 13.53           N  
ATOM   2147  CZ  ARG A 274       0.430  31.510  34.800  1.00 15.82           C  
ATOM   2148  NH1 ARG A 274      -0.315  31.811  33.737  1.00 10.56           N  
ATOM   2149  NH2 ARG A 274      -0.096  30.611  35.679  1.00 16.13           N  
ATOM   2150  N   ILE A 275       4.741  37.461  35.292  1.00 13.91           N  
ATOM   2151  CA  ILE A 275       5.035  38.783  34.706  1.00 14.24           C  
ATOM   2152  C   ILE A 275       4.115  39.038  33.523  1.00 14.98           C  
ATOM   2153  O   ILE A 275       3.673  38.106  32.830  1.00 12.93           O  
ATOM   2154  CB  ILE A 275       6.538  38.775  34.365  1.00 15.38           C  
ATOM   2155  CG1 ILE A 275       7.130  40.112  33.911  1.00 14.25           C  
ATOM   2156  CG2 ILE A 275       6.834  37.719  33.253  1.00 13.84           C  
ATOM   2157  CD1 ILE A 275       8.650  40.218  34.082  1.00 16.47           C  
ATOM   2158  N   SER A 276       3.737  40.306  33.291  1.00 14.22           N  
ATOM   2159  CA  SER A 276       2.958  40.582  32.089  1.00 14.45           C  
ATOM   2160  C   SER A 276       3.932  40.720  30.917  1.00 13.75           C  
ATOM   2161  O   SER A 276       5.155  40.836  31.056  1.00 12.48           O  
ATOM   2162  CB  SER A 276       2.201  41.917  32.331  1.00 15.38           C  
ATOM   2163  OG  SER A 276       3.252  42.880  32.413  1.00 16.62           O  
ATOM   2164  N   ALA A 277       3.469  40.719  29.678  1.00 12.99           N  
ATOM   2165  CA  ALA A 277       4.331  40.902  28.523  1.00 14.39           C  
ATOM   2166  C   ALA A 277       5.034  42.280  28.562  1.00 16.90           C  
ATOM   2167  O   ALA A 277       6.244  42.317  28.267  1.00 15.55           O  
ATOM   2168  CB  ALA A 277       3.493  40.847  27.233  1.00 13.94           C  
ATOM   2169  N   LYS A 278       4.294  43.340  28.922  1.00 18.67           N  
ATOM   2170  CA  LYS A 278       4.917  44.648  29.006  1.00 21.14           C  
ATOM   2171  C   LYS A 278       6.027  44.675  30.062  1.00 20.88           C  
ATOM   2172  O   LYS A 278       7.090  45.243  29.784  1.00 18.38           O  
ATOM   2173  CB  LYS A 278       4.022  45.842  29.274  1.00 25.88           C  
ATOM   2174  CG  LYS A 278       2.659  45.853  28.662  1.00 32.99           C  
ATOM   2175  CD  LYS A 278       2.231  47.078  27.904  1.00 37.32           C  
ATOM   2176  CE  LYS A 278       2.767  47.068  26.468  1.00 39.14           C  
ATOM   2177  NZ  LYS A 278       2.258  48.231  25.668  1.00 40.81           N  
ATOM   2178  N   ALA A 279       5.851  44.179  31.287  1.00 18.72           N  
ATOM   2179  CA  ALA A 279       7.020  44.204  32.185  1.00 19.73           C  
ATOM   2180  C   ALA A 279       8.139  43.300  31.686  1.00 19.53           C  
ATOM   2181  O   ALA A 279       9.337  43.595  31.793  1.00 23.51           O  
ATOM   2182  CB  ALA A 279       6.575  43.835  33.594  1.00 18.20           C  
ATOM   2183  N   ALA A 280       7.808  42.154  31.078  1.00 17.16           N  
ATOM   2184  CA  ALA A 280       8.853  41.257  30.592  1.00 16.33           C  
ATOM   2185  C   ALA A 280       9.706  41.991  29.546  1.00 16.06           C  
ATOM   2186  O   ALA A 280      10.901  41.741  29.538  1.00 13.99           O  
ATOM   2187  CB  ALA A 280       8.317  39.956  29.954  1.00 13.22           C  
ATOM   2188  N   LEU A 281       9.134  42.880  28.707  1.00 16.71           N  
ATOM   2189  CA  LEU A 281       9.973  43.564  27.729  1.00 18.62           C  
ATOM   2190  C   LEU A 281      10.991  44.468  28.456  1.00 20.68           C  
ATOM   2191  O   LEU A 281      12.034  44.706  27.889  1.00 19.42           O  
ATOM   2192  CB  LEU A 281       9.148  44.442  26.746  1.00 16.40           C  
ATOM   2193  CG  LEU A 281       8.285  43.612  25.784  1.00 19.18           C  
ATOM   2194  CD1 LEU A 281       7.196  44.364  25.018  1.00 17.18           C  
ATOM   2195  CD2 LEU A 281       9.203  42.922  24.761  1.00 15.63           C  
ATOM   2196  N   ALA A 282      10.748  44.876  29.713  1.00 21.80           N  
ATOM   2197  CA  ALA A 282      11.719  45.714  30.411  1.00 22.70           C  
ATOM   2198  C   ALA A 282      12.687  44.854  31.169  1.00 21.35           C  
ATOM   2199  O   ALA A 282      13.597  45.400  31.799  1.00 20.67           O  
ATOM   2200  CB  ALA A 282      11.031  46.728  31.396  1.00 21.19           C  
ATOM   2201  N   HIS A 283      12.615  43.517  31.160  1.00 21.64           N  
ATOM   2202  CA  HIS A 283      13.542  42.737  31.974  1.00 17.37           C  
ATOM   2203  C   HIS A 283      14.977  42.965  31.539  1.00 18.67           C  
ATOM   2204  O   HIS A 283      15.273  42.923  30.360  1.00 16.70           O  
ATOM   2205  CB  HIS A 283      13.252  41.228  31.819  1.00 20.51           C  
ATOM   2206  CG  HIS A 283      13.840  40.368  32.903  1.00 20.24           C  
ATOM   2207  ND1 HIS A 283      15.131  39.859  32.768  1.00 18.22           N  
ATOM   2208  CD2 HIS A 283      13.320  39.929  34.091  1.00 18.05           C  
ATOM   2209  CE1 HIS A 283      15.397  39.110  33.839  1.00 20.11           C  
ATOM   2210  NE2 HIS A 283      14.334  39.148  34.662  1.00 21.72           N  
ATOM   2211  N   PRO A 284      15.966  42.933  32.461  1.00 19.34           N  
ATOM   2212  CA  PRO A 284      17.378  42.977  32.099  1.00 19.22           C  
ATOM   2213  C   PRO A 284      17.822  41.971  31.066  1.00 20.77           C  
ATOM   2214  O   PRO A 284      18.795  42.319  30.371  1.00 18.47           O  
ATOM   2215  CB  PRO A 284      18.182  42.871  33.415  1.00 18.10           C  
ATOM   2216  CG  PRO A 284      17.167  43.391  34.415  1.00 20.42           C  
ATOM   2217  CD  PRO A 284      15.776  42.912  33.930  1.00 17.19           C  
ATOM   2218  N   PHE A 285      17.177  40.809  30.875  1.00 20.10           N  
ATOM   2219  CA  PHE A 285      17.533  39.859  29.835  1.00 19.80           C  
ATOM   2220  C   PHE A 285      17.589  40.528  28.463  1.00 19.86           C  
ATOM   2221  O   PHE A 285      18.415  40.063  27.720  1.00 21.18           O  
ATOM   2222  CB  PHE A 285      16.506  38.710  29.613  1.00 16.46           C  
ATOM   2223  CG  PHE A 285      16.869  37.540  28.748  1.00 16.14           C  
ATOM   2224  CD1 PHE A 285      18.090  36.873  28.879  1.00 14.77           C  
ATOM   2225  CD2 PHE A 285      15.962  37.034  27.830  1.00 15.17           C  
ATOM   2226  CE1 PHE A 285      18.392  35.760  28.092  1.00 15.50           C  
ATOM   2227  CE2 PHE A 285      16.270  35.956  27.037  1.00 13.96           C  
ATOM   2228  CZ  PHE A 285      17.468  35.268  27.200  1.00 13.99           C  
ATOM   2229  N   PHE A 286      16.719  41.488  28.155  1.00 20.24           N  
ATOM   2230  CA  PHE A 286      16.723  42.094  26.821  1.00 23.08           C  
ATOM   2231  C   PHE A 286      17.651  43.282  26.622  1.00 25.07           C  
ATOM   2232  O   PHE A 286      17.655  43.943  25.579  1.00 25.43           O  
ATOM   2233  CB  PHE A 286      15.280  42.532  26.419  1.00 20.89           C  
ATOM   2234  CG  PHE A 286      14.427  41.269  26.336  1.00 19.81           C  
ATOM   2235  CD1 PHE A 286      14.679  40.315  25.371  1.00 16.98           C  
ATOM   2236  CD2 PHE A 286      13.419  41.063  27.279  1.00 20.08           C  
ATOM   2237  CE1 PHE A 286      13.921  39.149  25.314  1.00 15.76           C  
ATOM   2238  CE2 PHE A 286      12.632  39.905  27.230  1.00 18.37           C  
ATOM   2239  CZ  PHE A 286      12.912  38.963  26.242  1.00 18.30           C  
ATOM   2240  N   GLN A 287      18.569  43.486  27.557  1.00 26.94           N  
ATOM   2241  CA  GLN A 287      19.473  44.634  27.487  1.00 29.27           C  
ATOM   2242  C   GLN A 287      20.322  44.562  26.222  1.00 24.86           C  
ATOM   2243  O   GLN A 287      20.487  45.644  25.696  1.00 24.01           O  
ATOM   2244  CB  GLN A 287      20.371  44.763  28.725  1.00 31.33           C  
ATOM   2245  CG  GLN A 287      20.873  46.186  28.900  1.00 37.94           C  
ATOM   2246  CD  GLN A 287      19.832  47.082  29.552  1.00 43.41           C  
ATOM   2247  OE1 GLN A 287      18.980  46.564  30.322  1.00 44.46           O  
ATOM   2248  NE2 GLN A 287      19.962  48.397  29.245  1.00 43.47           N  
ATOM   2249  N   ASP A 288      20.801  43.411  25.810  1.00 23.27           N  
ATOM   2250  CA  ASP A 288      21.652  43.395  24.607  1.00 24.58           C  
ATOM   2251  C   ASP A 288      20.913  42.769  23.437  1.00 22.71           C  
ATOM   2252  O   ASP A 288      21.509  42.006  22.666  1.00 23.74           O  
ATOM   2253  CB  ASP A 288      22.921  42.585  24.920  1.00 22.14           C  
ATOM   2254  CG  ASP A 288      22.598  41.204  25.378  1.00 26.58           C  
ATOM   2255  OD1 ASP A 288      21.415  40.750  25.402  1.00 28.19           O  
ATOM   2256  OD2 ASP A 288      23.555  40.488  25.738  1.00 28.98           O  
ATOM   2257  N   VAL A 289      19.597  42.927  23.391  1.00 22.67           N  
ATOM   2258  CA  VAL A 289      18.827  42.245  22.358  1.00 21.35           C  
ATOM   2259  C   VAL A 289      19.110  42.882  20.987  1.00 22.31           C  
ATOM   2260  O   VAL A 289      19.300  44.082  20.844  1.00 21.49           O  
ATOM   2261  CB  VAL A 289      17.321  42.252  22.665  1.00 19.53           C  
ATOM   2262  CG1 VAL A 289      16.838  43.693  22.588  1.00 20.84           C  
ATOM   2263  CG2 VAL A 289      16.580  41.403  21.644  1.00 21.03           C  
ATOM   2264  N   THR A 290      19.204  42.039  19.959  1.00 19.46           N  
ATOM   2265  CA  THR A 290      19.516  42.481  18.608  1.00 22.06           C  
ATOM   2266  C   THR A 290      18.570  41.720  17.688  1.00 24.00           C  
ATOM   2267  O   THR A 290      17.672  40.975  18.177  1.00 22.13           O  
ATOM   2268  CB  THR A 290      20.994  42.132  18.307  1.00 23.09           C  
ATOM   2269  OG1 THR A 290      21.128  40.690  18.324  1.00 22.61           O  
ATOM   2270  CG2 THR A 290      22.003  42.712  19.311  1.00 19.48           C  
ATOM   2271  N   LYS A 291      18.748  41.739  16.395  1.00 22.25           N  
ATOM   2272  CA  LYS A 291      17.838  41.028  15.488  1.00 25.67           C  
ATOM   2273  C   LYS A 291      18.634  40.317  14.399  1.00 23.53           C  
ATOM   2274  O   LYS A 291      18.830  40.900  13.342  1.00 22.93           O  
ATOM   2275  CB  LYS A 291      16.894  42.082  14.919  1.00 29.43           C  
ATOM   2276  CG  LYS A 291      15.825  41.578  13.968  1.00 34.28           C  
ATOM   2277  CD  LYS A 291      15.067  42.765  13.373  1.00 37.06           C  
ATOM   2278  CE  LYS A 291      13.846  42.296  12.582  1.00 40.61           C  
ATOM   2279  NZ  LYS A 291      12.562  42.505  13.314  1.00 43.05           N  
ATOM   2280  N   PRO A 292      19.187  39.158  14.695  1.00 19.37           N  
ATOM   2281  CA  PRO A 292      19.941  38.384  13.772  1.00 21.95           C  
ATOM   2282  C   PRO A 292      18.975  37.801  12.711  1.00 23.99           C  
ATOM   2283  O   PRO A 292      17.754  37.795  12.882  1.00 24.07           O  
ATOM   2284  CB  PRO A 292      20.628  37.300  14.587  1.00 19.10           C  
ATOM   2285  CG  PRO A 292      20.337  37.652  16.034  1.00 22.30           C  
ATOM   2286  CD  PRO A 292      19.009  38.394  15.980  1.00 21.73           C  
ATOM   2287  N   VAL A 293      19.529  37.323  11.612  1.00 26.48           N  
ATOM   2288  CA  VAL A 293      18.703  36.707  10.576  1.00 28.93           C  
ATOM   2289  C   VAL A 293      19.020  35.221  10.697  1.00 31.18           C  
ATOM   2290  O   VAL A 293      20.159  34.817  10.969  1.00 33.88           O  
ATOM   2291  CB  VAL A 293      18.953  37.276   9.178  1.00 31.65           C  
ATOM   2292  CG1 VAL A 293      18.802  38.819   9.180  1.00 32.04           C  
ATOM   2293  CG2 VAL A 293      20.284  36.841   8.607  1.00 29.84           C  
ATOM   2294  N   PRO A 294      17.986  34.394  10.648  1.00 30.86           N  
ATOM   2295  CA  PRO A 294      18.159  32.967  10.735  1.00 31.06           C  
ATOM   2296  C   PRO A 294      18.740  32.364   9.464  1.00 35.62           C  
ATOM   2297  O   PRO A 294      18.618  32.904   8.366  1.00 32.02           O  
ATOM   2298  CB  PRO A 294      16.739  32.516  10.980  1.00 28.86           C  
ATOM   2299  CG  PRO A 294      15.877  33.510  10.298  1.00 29.42           C  
ATOM   2300  CD  PRO A 294      16.613  34.791  10.257  1.00 28.36           C  
ATOM   2301  N   HIS A 295      19.351  31.195   9.659  1.00 41.76           N  
ATOM   2302  CA  HIS A 295      19.852  30.402   8.530  1.00 46.46           C  
ATOM   2303  C   HIS A 295      18.577  29.740   8.028  1.00 45.29           C  
ATOM   2304  O   HIS A 295      18.118  28.886   8.808  1.00 43.21           O  
ATOM   2305  CB  HIS A 295      20.880  29.383   8.996  1.00 52.27           C  
ATOM   2306  CG  HIS A 295      20.595  28.079   9.656  1.00 54.91           C  
ATOM   2307  ND1 HIS A 295      20.189  27.955  10.975  1.00 56.43           N  
ATOM   2308  CD2 HIS A 295      20.662  26.803   9.173  1.00 56.21           C  
ATOM   2309  CE1 HIS A 295      20.002  26.669  11.279  1.00 56.93           C  
ATOM   2310  NE2 HIS A 295      20.297  25.944  10.211  1.00 57.72           N  
ATOM   2311  N   LEU A 296      17.964  30.241   6.963  1.00 46.24           N  
ATOM   2312  CA  LEU A 296      16.727  29.648   6.475  1.00 49.22           C  
ATOM   2313  C   LEU A 296      16.825  29.207   4.997  1.00 52.76           C  
ATOM   2314  O   LEU A 296      17.033  29.995   4.067  1.00 52.31           O  
ATOM   2315  CB  LEU A 296      15.489  30.514   6.489  1.00 49.27           C  
ATOM   2316  CG  LEU A 296      14.782  30.932   7.750  1.00 50.49           C  
ATOM   2317  CD1 LEU A 296      13.377  31.400   7.379  1.00 50.82           C  
ATOM   2318  CD2 LEU A 296      14.768  29.788   8.752  1.00 51.59           C  
ATOM   2319  N   ARG A 297      16.519  27.924   4.827  1.00 54.29           N  
ATOM   2320  CA  ARG A 297      16.552  27.299   3.503  1.00 56.43           C  
ATOM   2321  C   ARG A 297      15.122  26.920   3.115  1.00 56.97           C  
ATOM   2322  O   ARG A 297      14.462  26.024   3.658  1.00 57.04           O  
ATOM   2323  CB  ARG A 297      17.514  26.161   3.692  1.00 58.63           C  
ATOM   2324  CG  ARG A 297      18.400  25.658   2.572  1.00 61.74           C  
ATOM   2325  CD  ARG A 297      19.045  24.367   3.105  1.00 63.96           C  
ATOM   2326  NE  ARG A 297      19.287  23.378   2.071  1.00 65.07           N  
ATOM   2327  CZ  ARG A 297      19.575  22.100   2.285  1.00 65.76           C  
ATOM   2328  NH1 ARG A 297      19.654  21.588   3.509  1.00 65.99           N  
ATOM   2329  NH2 ARG A 297      19.787  21.342   1.212  1.00 66.63           N  
ATOM   2330  N   LEU A 298      14.572  27.696   2.181  1.00 55.61           N  
ATOM   2331  CA  LEU A 298      13.210  27.531   1.704  1.00 54.78           C  
ATOM   2332  C   LEU A 298      13.084  26.590   0.519  1.00 55.06           C  
ATOM   2333  O   LEU A 298      12.030  25.932   0.370  1.00 55.85           O  
ATOM   2334  CB  LEU A 298      12.684  28.913   1.313  1.00 54.32           C  
ATOM   2335  CG  LEU A 298      12.784  29.992   2.400  1.00 54.25           C  
ATOM   2336  CD1 LEU A 298      12.321  31.311   1.807  1.00 54.16           C  
ATOM   2337  CD2 LEU A 298      11.978  29.632   3.648  1.00 52.89           C  
ATOM   2338  OXT LEU A 298      14.003  26.489  -0.315  1.00 54.84           O  
TER    2339      LEU A 298                                                      
HETATM 2340 MG    MG A 382      -2.100  27.334  13.797  0.60 15.46          MG  
HETATM 2341  PG  ATP A 381      -3.904  24.971  15.435  1.00 34.03           P  
HETATM 2342  O1G ATP A 381      -4.443  24.771  16.773  1.00 31.74           O  
HETATM 2343  O2G ATP A 381      -3.510  26.367  15.111  1.00 31.67           O  
HETATM 2344  O3G ATP A 381      -5.021  24.580  14.486  1.00 34.15           O  
HETATM 2345  PB  ATP A 381      -1.539  24.124  14.051  1.00 26.96           P  
HETATM 2346  O1B ATP A 381      -1.019  25.507  14.007  1.00 24.99           O  
HETATM 2347  O2B ATP A 381      -0.564  23.045  14.136  1.00 26.27           O  
HETATM 2348  O3B ATP A 381      -2.713  23.985  15.119  1.00 30.69           O  
HETATM 2349  PA  ATP A 381      -2.808  25.087  11.645  1.00 28.45           P  
HETATM 2350  O1A ATP A 381      -3.918  24.413  10.871  1.00 29.15           O  
HETATM 2351  O2A ATP A 381      -3.073  26.408  12.152  1.00 25.70           O  
HETATM 2352  O3A ATP A 381      -2.494  23.945  12.771  1.00 28.02           O  
HETATM 2353  O5' ATP A 381      -1.528  25.116  10.700  1.00 29.13           O  
HETATM 2354  C5' ATP A 381      -1.323  24.047   9.756  1.00 30.43           C  
HETATM 2355  C4' ATP A 381       0.147  24.224   9.353  1.00 31.53           C  
HETATM 2356  O4' ATP A 381       0.267  25.324   8.443  1.00 30.60           O  
HETATM 2357  C3' ATP A 381       1.002  24.581  10.574  1.00 33.70           C  
HETATM 2358  O3' ATP A 381       2.298  23.979  10.395  1.00 32.98           O  
HETATM 2359  C2' ATP A 381       1.157  26.137  10.454  1.00 32.71           C  
HETATM 2360  O2' ATP A 381       2.524  26.414  10.854  1.00 35.33           O  
HETATM 2361  C1' ATP A 381       1.104  26.330   8.923  1.00 30.76           C  
HETATM 2362  N9  ATP A 381       0.481  27.594   8.542  1.00 27.75           N  
HETATM 2363  C8  ATP A 381      -0.528  28.141   9.258  1.00 25.73           C  
HETATM 2364  N7  ATP A 381      -0.708  29.377   9.057  1.00 26.50           N  
HETATM 2365  C5  ATP A 381       0.200  29.740   8.175  1.00 24.80           C  
HETATM 2366  C6  ATP A 381       0.435  30.983   7.580  1.00 23.93           C  
HETATM 2367  N6  ATP A 381      -0.195  32.128   7.775  1.00 18.86           N  
HETATM 2368  N1  ATP A 381       1.453  31.003   6.691  1.00 21.44           N  
HETATM 2369  C2  ATP A 381       2.120  29.859   6.398  1.00 21.19           C  
HETATM 2370  N3  ATP A 381       1.978  28.672   6.931  1.00 22.74           N  
HETATM 2371  C4  ATP A 381       0.963  28.657   7.804  1.00 24.84           C  
HETATM 2372  O   HOH A 383       8.200  23.512  25.827  1.00 10.86           O  
HETATM 2373  O   HOH A 384       2.353  23.588  30.169  1.00 15.04           O  
HETATM 2374  O   HOH A 385      -1.496  30.281  24.957  1.00 14.66           O  
HETATM 2375  O   HOH A 386       5.537  30.307  41.432  1.00 24.22           O  
HETATM 2376  O   HOH A 387      -1.965  28.596  28.278  1.00 18.19           O  
HETATM 2377  O   HOH A 388       0.780  40.460  29.118  1.00 14.84           O  
HETATM 2378  O   HOH A 389       0.942  37.621  32.867  1.00 14.70           O  
HETATM 2379  O   HOH A 390      -0.420  38.420  35.272  1.00 21.27           O  
HETATM 2380  O   HOH A 391      20.932  22.644  39.516  1.00 24.12           O  
HETATM 2381  O   HOH A 392      -2.756  27.229  25.927  1.00 17.23           O  
HETATM 2382  O   HOH A 393      -4.966  33.288  33.651  1.00 16.82           O  
HETATM 2383  O   HOH A 394       8.274  17.438  31.928  1.00 16.40           O  
HETATM 2384  O   HOH A 395      15.797  38.193  14.615  1.00 16.36           O  
HETATM 2385  O   HOH A 396       1.088  36.752   2.086  1.00 21.99           O  
HETATM 2386  O   HOH A 397       3.993  42.174  35.556  1.00 17.88           O  
HETATM 2387  O   HOH A 398      -0.532  39.347  31.605  1.00 19.84           O  
HETATM 2388  O   HOH A 399      -4.256  24.897  25.697  1.00 24.41           O  
HETATM 2389  O   HOH A 400      -0.709  23.363  24.717  1.00 11.11           O  
HETATM 2390  O   HOH A 401       6.093  22.318  27.526  1.00 14.61           O  
HETATM 2391  O   HOH A 402       3.154  31.904  42.350  1.00 19.62           O  
HETATM 2392  O   HOH A 403      -1.073  26.009  23.814  1.00 18.68           O  
HETATM 2393  O   HOH A 404       2.208  40.946  10.232  1.00 24.75           O  
HETATM 2394  O   HOH A 405       8.570  17.614  34.880  1.00 21.71           O  
HETATM 2395  O   HOH A 406      -5.095  39.996  13.479  1.00 19.84           O  
HETATM 2396  O   HOH A 407      19.680  39.288  20.422  1.00 19.41           O  
HETATM 2397  O   HOH A 408       6.434  25.825  43.915  1.00 20.39           O  
HETATM 2398  O   HOH A 409       6.258  28.519  39.420  1.00 25.43           O  
HETATM 2399  O   HOH A 410      -2.672  33.018  11.236  1.00 30.20           O  
HETATM 2400  O   HOH A 411      17.362  25.257  19.836  1.00 28.84           O  
HETATM 2401  O   HOH A 412      -0.677  28.092  12.465  1.00 22.99           O  
HETATM 2402  O   HOH A 413       1.373  43.262  29.185  1.00 19.68           O  
HETATM 2403  O   HOH A 414      -6.614  24.690  12.152  1.00 33.23           O  
HETATM 2404  O   HOH A 415       0.076  44.894  27.276  1.00 30.59           O  
HETATM 2405  O   HOH A 416      -6.763  38.881  31.281  1.00 38.92           O  
HETATM 2406  O   HOH A 417      -1.199  41.882  11.948  1.00 16.87           O  
HETATM 2407  O   HOH A 418       0.231   8.364  25.753  1.00 20.60           O  
HETATM 2408  O   HOH A 419      11.677  20.678  20.410  1.00 35.22           O  
HETATM 2409  O   HOH A 420      -0.220  16.964  24.610  1.00 20.59           O  
HETATM 2410  O   HOH A 421       2.114  37.805  -1.498  1.00 26.13           O  
HETATM 2411  O   HOH A 422      -7.528  21.493  30.645  1.00 24.50           O  
HETATM 2412  O   HOH A 423       8.822  43.983  17.295  1.00 41.60           O  
HETATM 2413  O   HOH A 424       1.149  16.561  22.179  1.00 26.27           O  
HETATM 2414  O   HOH A 425      21.779  39.226  22.059  1.00 26.91           O  
HETATM 2415  O   HOH A 426      -2.483  35.668  14.259  1.00 29.42           O  
HETATM 2416  O   HOH A 427       1.175  45.868  11.675  1.00 23.11           O  
HETATM 2417  O   HOH A 428      -6.370  31.281  19.476  1.00 26.98           O  
HETATM 2418  O   HOH A 429      -6.677  33.340  36.015  1.00 32.58           O  
HETATM 2419  O   HOH A 430       6.497  27.548   0.225  1.00 22.54           O  
HETATM 2420  O   HOH A 431       5.054  31.830  -6.130  1.00 24.89           O  
HETATM 2421  O   HOH A 432      -4.156  37.532  35.543  1.00 34.07           O  
HETATM 2422  O   HOH A 433      22.394  26.493  40.932  1.00 39.71           O  
HETATM 2423  O   HOH A 434      -3.946  41.010  11.393  1.00 21.64           O  
HETATM 2424  O   HOH A 435       3.980  34.145  41.366  1.00 52.81           O  
HETATM 2425  O   HOH A 436      13.231  43.118  16.097  1.00 41.16           O  
HETATM 2426  O   HOH A 437       4.230  11.856  28.849  1.00 26.24           O  
HETATM 2427  O   HOH A 438      14.423  41.789  17.788  1.00 24.17           O  
HETATM 2428  O   HOH A 439      18.335  36.759  40.862  1.00 28.70           O  
HETATM 2429  O   HOH A 440      -7.475  17.323  38.278  1.00 33.52           O  
HETATM 2430  O   HOH A 441       0.368  48.233  12.876  1.00 24.61           O  
HETATM 2431  O   HOH A 442       1.889  14.083  23.355  1.00 24.92           O  
HETATM 2432  O   HOH A 443      12.808  34.865  11.518  1.00 22.72           O  
HETATM 2433  O   HOH A 444      19.106  27.709  14.062  1.00 32.92           O  
HETATM 2434  O   HOH A 445      16.893  21.018  41.760  1.00 35.68           O  
HETATM 2435  O   HOH A 446      16.179  29.267   0.533  1.00 41.79           O  
HETATM 2436  O   HOH A 447      20.035  30.093  12.631  1.00 29.33           O  
HETATM 2437  O   HOH A 448     -10.213  25.535  32.650  1.00 25.61           O  
HETATM 2438  O   HOH A 449      -2.136  45.591  29.223  1.00 48.81           O  
HETATM 2439  O   HOH A 450      -5.278  23.535  23.843  1.00 44.51           O  
HETATM 2440  O   HOH A 451     -26.244  36.135  16.973  1.00 37.65           O  
HETATM 2441  O   HOH A 452       9.991  15.991  45.094  1.00 37.26           O  
HETATM 2442  O   HOH A 453      10.970  17.415  22.786  1.00 25.05           O  
HETATM 2443  O   HOH A 454      -5.563  32.014  40.958  1.00 29.19           O  
HETATM 2444  O   HOH A 455      -2.845  39.830  41.866  1.00 37.97           O  
HETATM 2445  O   HOH A 456       3.870  13.380  25.219  1.00 27.17           O  
HETATM 2446  O   HOH A 457      16.046  46.363  25.371  1.00 40.22           O  
HETATM 2447  O   HOH A 458      18.887  28.088  39.533  1.00 38.51           O  
HETATM 2448  O   HOH A 459       0.209  48.091  15.512  1.00 22.97           O  
HETATM 2449  O   HOH A 460       9.781  13.324  33.719  1.00 44.81           O  
HETATM 2450  O   HOH A 461       3.967  33.565  47.950  1.00 49.97           O  
HETATM 2451  O   HOH A 462     -14.364  24.354  35.396  1.00 36.38           O  
HETATM 2452  O   HOH A 463      -0.780  41.187  33.625  1.00 39.69           O  
HETATM 2453  O   HOH A 464      -8.377  28.535  48.605  1.00 36.73           O  
HETATM 2454  O   HOH A 465       1.996  43.479   8.936  1.00 31.78           O  
HETATM 2455  O   HOH A 466      -1.178  18.256  47.593  1.00 46.20           O  
HETATM 2456  O   HOH A 467      -0.528   9.732  30.607  1.00 27.87           O  
HETATM 2457  O   HOH A 468       3.112  44.241  34.805  1.00 41.82           O  
HETATM 2458  O   HOH A 469       3.312  26.044  -8.199  1.00 39.51           O  
HETATM 2459  O   HOH A 470      11.019  35.163   4.366  1.00 35.56           O  
HETATM 2460  O   HOH A 471       3.307  28.577  -7.332  1.00 37.95           O  
HETATM 2461  O   HOH A 472       8.296  31.183  41.678  1.00 51.96           O  
HETATM 2462  O   HOH A 473      -7.556  29.338  51.793  1.00 45.39           O  
HETATM 2463  O   HOH A 474      -4.849  34.427  41.032  1.00 32.45           O  
HETATM 2464  O   HOH A 475     -11.791  41.810  24.636  1.00 40.37           O  
HETATM 2465  O   HOH A 476     -11.836  18.706  42.310  1.00 38.96           O  
HETATM 2466  O   HOH A 477       9.570  29.320  43.514  1.00 52.79           O  
HETATM 2467  O   HOH A 478      10.673  17.550  42.084  1.00 43.52           O  
HETATM 2468  O   HOH A 479       7.670  47.853  28.972  1.00 38.41           O  
HETATM 2469  O   HOH A 480      -6.006  42.728   8.623  1.00 31.24           O  
HETATM 2470  O   HOH A 481       7.420  10.092  28.374  1.00 54.63           O  
HETATM 2471  O   HOH A 482      16.254  33.867  39.046  1.00 37.09           O  
HETATM 2472  O   HOH A 483     -13.290  41.873   1.453  1.00 41.93           O  
HETATM 2473  O   HOH A 484       6.625  28.505  43.175  1.00 39.24           O  
HETATM 2474  O   HOH A 485      23.599  39.274  17.884  1.00 25.15           O  
HETATM 2475  O   HOH A 486      -9.899  37.159  24.573  1.00 37.81           O  
HETATM 2476  O   HOH A 487      -1.793  24.421  50.757  1.00 29.75           O  
HETATM 2477  O   HOH A 488      -7.397  39.360   0.711  1.00 31.51           O  
HETATM 2478  O   HOH A 489      21.964  37.380  29.094  1.00 53.59           O  
HETATM 2479  O   HOH A 490      -5.370  48.046  27.903  1.00 47.60           O  
HETATM 2480  O   HOH A 491      -9.410  21.267  34.158  1.00 36.87           O  
HETATM 2481  O   HOH A 492       2.618  40.731  37.123  1.00 41.25           O  
HETATM 2482  O   HOH A 493     -17.420  32.643  18.984  1.00 50.50           O  
HETATM 2483  O   HOH A 494      -9.752  33.474  28.942  1.00 88.46           O  
HETATM 2484  O   HOH A 495      20.398  25.177  22.503  1.00 54.55           O  
HETATM 2485  O   HOH A 496      -2.621  14.757  24.788  1.00 34.84           O  
HETATM 2486  O   HOH A 497      -6.086  35.414  13.695  1.00 37.20           O  
HETATM 2487  O   HOH A 498     -14.595  38.409  -6.480  1.00 43.24           O  
HETATM 2488  O   HOH A 499     -10.511  34.262  26.190  1.00 37.23           O  
HETATM 2489  O   HOH A 500      23.967  37.219  16.436  1.00 31.43           O  
HETATM 2490  O   HOH A 501      -4.192  37.460  12.657  1.00 26.16           O  
HETATM 2491  O   HOH A 502      15.884  23.232  18.363  1.00 31.07           O  
HETATM 2492  O   HOH A 503       1.139  29.866  -8.036  1.00 48.31           O  
HETATM 2493  O   HOH A 504      -0.686  21.494  47.644  1.00 36.13           O  
HETATM 2494  O   HOH A 505     -23.347  32.267  16.854  1.00 40.14           O  
HETATM 2495  O   HOH A 506     -14.823  40.060  24.881  1.00 51.68           O  
HETATM 2496  O   HOH A 507      12.202  45.562  14.165  1.00 50.13           O  
HETATM 2497  O   HOH A 508      14.358  16.952  44.383  1.00 50.21           O  
HETATM 2498  O   HOH A 509       5.600  20.452  47.497  1.00 48.91           O  
HETATM 2499  O   HOH A 510      -4.130  20.264  49.713  1.00 34.50           O  
HETATM 2500  O   HOH A 511      -3.596  34.342  44.722  1.00 43.71           O  
HETATM 2501  O   HOH A 512      22.165  36.955  23.478  1.00 34.36           O  
HETATM 2502  O   HOH A 513      10.835  16.726  26.905  1.00 40.85           O  
HETATM 2503  O   HOH A 514      19.922  21.731  42.372  1.00 43.00           O  
HETATM 2504  O   HOH A 515       0.215  19.597   9.518  1.00 58.28           O  
HETATM 2505  O   HOH A 516      19.232  21.010   9.465  1.00 53.81           O  
HETATM 2506  O   HOH A 517      -1.310  42.598  -5.072  1.00 41.33           O  
HETATM 2507  O   HOH A 518     -23.532  34.329  10.625  1.00 46.63           O  
HETATM 2508  O   HOH A 519      -5.523  38.169  -0.898  1.00 46.37           O  
HETATM 2509  O   HOH A 520      -5.368  41.236   0.472  1.00 33.79           O  
HETATM 2510  O   HOH A 521     -15.905  35.532  -7.509  1.00 49.98           O  
HETATM 2511  O   HOH A 522     -12.669  40.361   4.924  1.00 33.62           O  
HETATM 2512  O   HOH A 523       2.050  41.620  39.456  1.00 38.62           O  
HETATM 2513  O   HOH A 524      15.825  27.800  -1.713  1.00 32.36           O  
HETATM 2514  O   HOH A 525     -13.257  39.711  -8.925  1.00 57.46           O  
HETATM 2515  O   HOH A 526     -10.777  11.615  18.640  1.00 53.31           O  
HETATM 2516  O   HOH A 527       7.722  21.391  19.744  1.00 40.46           O  
HETATM 2517  O   HOH A 528     -13.264  21.914  35.221  1.00 40.03           O  
HETATM 2518  O   HOH A 529      22.747  34.782  16.269  1.00 30.52           O  
HETATM 2519  O   HOH A 530     -18.207  25.134   9.239  1.00 43.69           O  
HETATM 2520  O   HOH A 531       5.018  21.934  11.289  1.00 46.29           O  
HETATM 2521  O   HOH A 532      -6.210  35.181  43.252  1.00 47.46           O  
HETATM 2522  O   HOH A 533      17.909  31.590  38.869  1.00 46.89           O  
HETATM 2523  O   HOH A 534      11.842  44.727  17.375  1.00 51.93           O  
HETATM 2524  O   HOH A 535       5.316  21.613  19.815  1.00 40.31           O  
HETATM 2525  O   HOH A 536      12.875  46.329  19.102  1.00 53.64           O  
HETATM 2526  O   HOH A 537      25.078  31.126  30.565  1.00 53.06           O  
HETATM 2527  O   HOH A 538      16.623  14.758  23.639  1.00 53.68           O  
HETATM 2528  O   HOH A 539      -5.455  11.307  16.503  1.00 49.47           O  
HETATM 2529  O   HOH A 540      15.413  45.684  19.369  1.00 50.56           O  
HETATM 2530  O   HOH A 541     -10.563  49.772   9.945  1.00 48.34           O  
HETATM 2531  O   HOH A 542     -16.351  27.652  -1.560  1.00 52.44           O  
HETATM 2532  O   HOH A 543      -3.469  47.747  14.614  1.00 50.03           O  
HETATM 2533  O   HOH A 544      22.524  25.854  34.620  1.00 39.07           O  
HETATM 2534  O   HOH A 545       2.460  21.244  47.970  1.00 48.51           O  
HETATM 2535  O   HOH A 546      -5.248  43.561   2.189  1.00 74.62           O  
HETATM 2536  O   HOH A 547     -15.138  20.869  40.932  1.00 45.11           O  
HETATM 2537  O   HOH A 548      -3.557  22.404  -6.394  1.00 58.10           O  
HETATM 2538  O   HOH A 549      21.087  28.578   6.068  1.00 71.90           O  
HETATM 2539  O   HOH A 550      13.353  21.368  28.164  1.00 40.69           O  
HETATM 2540  O   HOH A 551     -11.516  19.781  16.245  1.00 47.91           O  
HETATM 2541  O   HOH A 552       8.542  30.192  38.845  1.00 38.66           O  
HETATM 2542  O   HOH A 553       1.390  33.413  50.537  1.00 42.25           O  
HETATM 2543  O   HOH A 554      25.985  40.913  24.871  1.00 53.67           O  
HETATM 2544  O   HOH A 555       7.512  41.818  11.772  1.00 36.74           O  
HETATM 2545  O   HOH A 556      14.068  47.022  15.974  1.00 54.45           O  
HETATM 2546  O   HOH A 557      17.404  34.406   6.661  1.00 53.13           O  
HETATM 2547  O   HOH A 558     -24.072  30.816   0.863  1.00 49.78           O  
HETATM 2548  O   HOH A 559      -8.650  33.767  43.119  1.00 48.44           O  
HETATM 2549  O   HOH A 560      11.552  18.143  31.529  1.00 67.28           O  
HETATM 2550  O   HOH A 561     -16.672  23.318   9.762  1.00 52.80           O  
HETATM 2551  O   HOH A 562       8.158  27.720   2.314  1.00 54.80           O  
HETATM 2552  O   HOH A 563      16.494  17.385  14.314  1.00 72.72           O  
HETATM 2553  O   HOH A 564      14.998  42.694   9.153  1.00 45.35           O  
HETATM 2554  O   HOH A 565       5.076  24.602  45.784  1.00 55.00           O  
HETATM 2555  O   HOH A 566       1.647  35.775  49.087  1.00 53.47           O  
HETATM 2556  O   HOH A 567      23.947  37.806  25.978  1.00 52.92           O  
HETATM 2557  O   HOH A 568      10.582  12.534  30.477  1.00 59.14           O  
HETATM 2558  O   HOH A 569       7.091  39.625  37.811  1.00 45.60           O  
HETATM 2559  O   HOH A 570       5.388  26.602   4.804  1.00 51.92           O  
HETATM 2560  O   HOH A 571       6.372  25.719  48.473  1.00 57.87           O  
HETATM 2561  O   HOH A 572      22.905  30.686  27.873  1.00 68.45           O  
HETATM 2562  O   HOH A 573     -10.940  26.502  28.730  1.00 48.52           O  
HETATM 2563  O   HOH A 574      -9.518  29.489  44.123  1.00 42.14           O  
HETATM 2564  O   HOH A 575     -18.217  35.041  -0.761  1.00 50.82           O  
HETATM 2565  O   HOH A 576       5.174  27.934  -3.777  1.00 48.56           O  
HETATM 2566  O   HOH A 577      -6.238  23.108  20.596  1.00 46.64           O  
HETATM 2567  O   HOH A 578     -12.886  21.860   9.562  1.00 52.27           O  
HETATM 2568  O   HOH A 579      16.493  47.066  22.011  1.00 55.32           O  
HETATM 2569  O   HOH A 580      -1.194  21.685  16.705  1.00 62.22           O  
HETATM 2570  O   HOH A 581      21.378  33.944  13.612  1.00 54.27           O  
HETATM 2571  O   HOH A 582      22.621  17.422  18.098  1.00 71.44           O  
HETATM 2572  O   HOH A 583     -11.161  16.824  37.928  1.00 59.44           O  
HETATM 2573  O   HOH A 584      -6.782  33.076  39.164  1.00 55.63           O  
HETATM 2574  O   HOH A 585      -0.627  20.941  12.210  1.00 54.68           O  
HETATM 2575  O   HOH A 586     -17.341  38.944  19.651  1.00 55.97           O  
HETATM 2576  O   HOH A 587      -6.452  28.936  17.606  1.00 67.64           O  
HETATM 2577  O   HOH A 588      -5.616  11.440  12.999  1.00 51.50           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 2401                                                           
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 2401 2340                                                                
MASTER      346    0    3   13    7    0    8    6 2576    1   40   23          
END                                                                             
