HEADER    TRANSFERASE                             06-JUN-05   2BTR              
TITLE     STRUCTURE OF CDK2 COMPLEXED WITH PNU-198873                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.1.37;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE, TRANSFERASE, SERINE/THREONINE-PROTEIN 2 KINASE,       
KEYWDS   2 PHOSPHORYLATION, CELL DIVISION                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.VULPETTI,E.CASALE,F.ROLETTO,R.AMICI,M.VILLA,P.PEVARELLO             
REVDAT   4   03-APR-19 2BTR    1       SOURCE                                   
REVDAT   3   24-FEB-09 2BTR    1       VERSN                                    
REVDAT   2   09-MAR-06 2BTR    1       SOURCE JRNL                              
REVDAT   1   09-NOV-05 2BTR    0                                                
JRNL        AUTH   A.VULPETTI,E.CASALE,F.ROLETTO,R.AMICI,M.VILLA,P.PEVARELLO    
JRNL        TITL   STRUCTURE-BASED DRUG DESIGN TO THE DISCOVERY OF NEW          
JRNL        TITL 2 2-AMINOTHIAZOLE CDK2 INHIBITORS.                             
JRNL        REF    J.MOL.GRAPH.MODEL.            V.  24   341 2006              
JRNL        REFN                   ISSN 1093-3263                               
JRNL        PMID   16260160                                                     
JRNL        DOI    10.1016/J.JMGM.2005.09.012                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22169                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1606                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2215                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 67                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -1.53000                                             
REMARK   3    B33 (A**2) : 1.52000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.167         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.374         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2289 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2142 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3101 ; 1.521 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4985 ; 0.911 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   272 ; 6.338 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   350 ; 0.143 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2465 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   464 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   463 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2454 ; 0.242 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1342 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    65 ; 0.125 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    12 ; 0.131 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    58 ; 0.271 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.159 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1375 ; 1.104 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2231 ; 1.947 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   914 ; 2.593 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   870 ; 4.109 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2BTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JUN-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290024364.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.40                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 PERCENT PEG4000,50 MM AMMONIUM        
REMARK 280  ACETATE, 50 MM HEPES PH 7.4, PH 7.40                                
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       26.60750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.79400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.80750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.79400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.60750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.80750            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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 465     VAL A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ARG A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     PHE A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     VAL A   154                                                      
REMARK 465     PRO A   155                                                      
REMARK 465     VAL A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     THR A   158                                                      
REMARK 465     TYR A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  25      -86.22    -78.87                                   
REMARK 500    THR A  72      114.01   -176.71                                   
REMARK 500    GLU A  73       36.79     70.96                                   
REMARK 500    ASN A  74       12.59     57.19                                   
REMARK 500    ARG A 126      -22.31     83.11                                   
REMARK 500    ASP A 145       41.31     71.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U73 A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B38   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1BUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CDK2 KINASE COMPLEX WITHCELL CYCLE-   
REMARK 900 REGULATORY PROTEIN CKSHS1                                            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3- HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                         
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU2058  
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR NU6027  
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5- SULPHONATE BOUND                              
REMARK 900 RELATED ID: 1F5Q   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MURINE GAMMA HERPESVIRUS CYCLIN COMPLEXED TO    
REMARK 900 HUMAN CYCLIN DEPENDANT KINASE 2                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FQ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF KINASE ASSOCIATED PHOSPHATASE (KAP) INCOMPLEX   
REMARK 900 WITH PHOSPHO-CDK2                                                    
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH AN  
REMARK 900 OXINDOLE INHIBITOR                                                   
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLEINHIBITOR  
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)IN        
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4INHIBITOR     
REMARK 900 RELATED ID: 1GY3   RELATED DB: PDB                                   
REMARK 900 PCDK2/CYCLIN A IN COMPLEX WITH MGADP, NITRATE AND PEPTIDE SUBSTRATE  
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL- 2'-OXO)BUTOXYPURINE                              
REMARK 900 RELATED ID: 1H00   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H01   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H07   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H08   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 2, 4 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1H0V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[(R )-PYRROLIDINO-5'-YL]METHOXYPURINE            
REMARK 900 RELATED ID: 1H0W   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 2-AMINO-6-[ CYCLOHEX-3-ENYL]METHOXYPURINE                  
REMARK 900 RELATED ID: 1H1P   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU2058                                                     
REMARK 900 RELATED ID: 1H1Q   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6094                                                     
REMARK 900 RELATED ID: 1H1R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6086                                                     
REMARK 900 RELATED ID: 1H1S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH THE  
REMARK 900 INHIBITOR NU6102                                                     
REMARK 900 RELATED ID: 1H24   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH A 9 RESIDUE RECRUITMENT PEPTIDE FROM    
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H25   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 E2F                                                                  
REMARK 900 RELATED ID: 1H26   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P53                                                                  
REMARK 900 RELATED ID: 1H27   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P27                                                                  
REMARK 900 RELATED ID: 1H28   RELATED DB: PDB                                   
REMARK 900 CDK2/CYCLINA IN COMPLEX WITH AN 11-RESIDUE RECRUITMENT PEPTIDE FROM  
REMARK 900 P107                                                                 
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JST   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CYCLIN-DEPENDENT KINASE-2 BOUND TO CYCLIN A           
REMARK 900 RELATED ID: 1JSU   RELATED DB: PDB                                   
REMARK 900 P27(KIP1)/CYCLIN A/CDK2 COMPLEX                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) INCOMPLEX WITH 4-  
REMARK 900 [(6-AMINO-4- PYRIMIDINYL)AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 ( UNPHOSPHORYLATED) INCOMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO- 1,2-DIHYDRO-3H-INDOL-3-     
REMARK 900 YLIDENE)METHYL] AMINO}BENZENESULFONAMIDE                             
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4-[2-(7-   
REMARK 900 OXO-6,7-DIHYDRO -8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]  
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-DIOXIDO-1,  
REMARK 900 3-DIHYDRO-2- BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-(1,3- OXAZOL-5-YL)-  
REMARK 900 1,3-DIHYDRO-2H-INDOL-2- ONE                                          
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-1,2-      
REMARK 900 DIHYDRO-3H-INDOL-3 -YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL-2- YL)      
REMARK 900 BENZENESULFONAMIDE                                                   
REMARK 900 RELATED ID: 1KE9   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[4-({             
REMARK 900 [AMINO(IMINO)METHYL] AMINOSULFONYL)ANILINO]METHYLENE}-2-OXO-2,3-     
REMARK 900 DIHYDRO-1H-INDOLE                                                    
REMARK 900 RELATED ID: 1OGU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 2- 
REMARK 900 ARYLAMINO-4- CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR  
REMARK 900 RELATED ID: 1OI9   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIQ   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIR   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIT   RELATED DB: PDB                                   
REMARK 900 IMIDAZOPYRIDINES: A POTENT AND SELECTIVE CLASS OF CYCLIN-DEPENDENT   
REMARK 900 KINASE INHIBITORS IDENTIFIED THROUGH STRUCTURE-BASED HYBRIDISATION   
REMARK 900 RELATED ID: 1OIU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OIY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/ CYCLIN A COMPLEXED WITH A 6- 
REMARK 900 CYCLOHEXYLMETHYLOXY-2-ANILINO-PURINE INHIBITOR                       
REMARK 900 RELATED ID: 1OKU   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ALA- ALA-ABU-ARG-ER-LEU-ILE-(P-  
REMARK 900 F-PHE)-NH2                                                           
REMARK 900 RELATED ID: 1OKV   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ILE-PHE-NH2         
REMARK 900 RELATED ID: 1OKW   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR AC-ARG- ARG-LEU-ASN-(M-CL-PHE)-NH2 
REMARK 900 RELATED ID: 1OL1   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-CIT- CIT-LEU-ILE-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1OL2   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1P2A   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN DEPENDENT KINASE 2 (CKD2) WITH               
REMARK 900 ATRISUBSTITUTED NAPHTHOSTYRIL INHIBITOR                              
REMARK 900 RELATED ID: 1P5E   RELATED DB: PDB                                   
REMARK 900 THE STRUCURE OF PHOSPHO-CDK2/CYCLIN A IN COMPLEX WITH THEINHIBITOR   
REMARK 900 4,5,6,7- TETRABROMOBENZOTRIAZOLE (TBS)                               
REMARK 900 RELATED ID: 1PF8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2COMPLEXED WITH   
REMARK 900 A NUCLEOSIDE INHIBITOR                                               
REMARK 900 RELATED ID: 1PKD   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF UCN-01 IN COMPLEX WITH PHOSPHO-CDK2/CYCLIN  
REMARK 900 A                                                                    
REMARK 900 RELATED ID: 1PW2   RELATED DB: PDB                                   
REMARK 900 APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2                     
REMARK 900 RELATED ID: 1PXI   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,5-  
REMARK 900 DICHLORO-THIOPHEN- 3-YL)-PYRIMIDIN-2-YLAMINE                         
REMARK 900 RELATED ID: 1PXJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-(2,4-  
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YLAMINE                          
REMARK 900 RELATED ID: 1PXK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)PYRIMIDIN-2-YL]-N'- HYDROXYIMINOFORMAMIDE   
REMARK 900 RELATED ID: 1PXL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2,4- 
REMARK 900 DIMETHYL-THIAZOL- 5-YL)-PYRIMIDIN-2-YL]-(4-TRIFLUOROMETHYL- PHENYL)- 
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXM   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 3-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YLAMINO]-PHENOL                
REMARK 900 RELATED ID: 1PXN   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR 4-[4-(4- 
REMARK 900 METHYL-2- METHYLAMINO-THIAZOL-5-YL)-PYRIMIDIN-2- YLAMINO]-PHENOL     
REMARK 900 RELATED ID: 1PXO   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR [4-(2-   
REMARK 900 AMINO-4-METHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-NITRO- PHENYL)-     
REMARK 900 AMINE                                                                
REMARK 900 RELATED ID: 1PXP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THEINHIBITOR N-[4-(2, 
REMARK 900 4-DIMETHYL- THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'- DIMETHYL-BENZENE-1, 
REMARK 900 4-DIAMINE                                                            
REMARK 900 RELATED ID: 1PYE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF CDK2 WITH INHIBITOR                             
REMARK 900 RELATED ID: 1QMZ   RELATED DB: PDB                                   
REMARK 900 PHOSPHORYLATED CDK2-CYCLYIN A-SUBSTRATE PEPTIDE COMPLEX              
REMARK 900 RELATED ID: 1R78   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEX WITH A 4-ALKYNYL OXINDOLE INHIBITOR                     
REMARK 900 RELATED ID: 1URC   RELATED DB: PDB                                   
REMARK 900 CYCLIN A BINDING GROOVE INHIBITOR H-ARG- ARG-LEU-ASN-(P-F-PHE)-NH2   
REMARK 900 RELATED ID: 1URW   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH AN IMIDAZO[1,2-B] PYRIDAZINE                    
REMARK 900 RELATED ID: 1V1K   RELATED DB: PDB                                   
REMARK 900 CDK2 IN COMPLEX WITH A DISUBSTITUTED 4, 6 -BIS ANILINO PYRIMIDINE    
REMARK 900 CDK4 INHIBITOR                                                       
REMARK 900 RELATED ID: 1VYW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2/CYCLIN A WITH PNU-292137                           
REMARK 900 RELATED ID: 1VYZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-181227                          
REMARK 900 RELATED ID: 1W0X   RELATED DB: PDB                                   
REMARK 900 CRYSTALS STRUCTURE OF HUMAN CDK2 IN COMPLEX WITH THE INHIBITOR       
REMARK 900 OLOMOUCINE.                                                          
REMARK 900 RELATED ID: 1W8C   RELATED DB: PDB                                   
REMARK 900 CO-CRYSTAL STRUCTURE OF 6-CYCLOHEXYLMETHOXY- 8-ISOPROPYL-9H-PURIN-2- 
REMARK 900 YLAMINE AND MONOMERIC CDK2                                           
REMARK 900 RELATED ID: 1W98   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURAL BASIS OF CDK2 ACTIVATION BY CYCLIN E                  
REMARK 900 RELATED ID: 1WCC   RELATED DB: PDB                                   
REMARK 900 SCREENING FOR FRAGMENT BINDING BY X-RAY CRYSTALLOGRAPHY              
REMARK 900 RELATED ID: 1Y8Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 1Y91   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 COMPLEXED WITH A PYRAZOLO[1,5-A]     
REMARK 900 PYRIMIDINE INHIBITOR                                                 
REMARK 900 RELATED ID: 2B52   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DPH-042562     
REMARK 900 RELATED ID: 2B53   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH DIN-234325     
REMARK 900 RELATED ID: 2B54   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CKD2) COMPLEXED WITH DIN-232305     
REMARK 900 RELATED ID: 2B55   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) COMPLEXED WITHINDENOPYRAXOLE  
REMARK 900 DIN-101312                                                           
REMARK 900 RELATED ID: 2BHE   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 5-BROMO- INDIRUBINE                                        
REMARK 900 RELATED ID: 2BHH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT PROTEIN KINASE 2 IN COMPLEX WITH THE          
REMARK 900 INHIBITOR 4- HYDROXYPIPERINDINESULFONYL-INDIRUBINE                   
REMARK 900 RELATED ID: 2BKZ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-404611                           
REMARK 900 RELATED ID: 2BPM   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-630529                           
REMARK 900 RELATED ID: 2BTS   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2 COMPLEXED WITH PNU-230032                          
REMARK 900 RELATED ID: 2C4G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CDK2-CYCLIN A WITH PHA-533514                           
REMARK 900 RELATED ID: 2C5N   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5O   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5P   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5T   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5X   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
REMARK 900 RELATED ID: 2C5Y   RELATED DB: PDB                                   
REMARK 900 DIFFERENTIAL BINDING OF INHIBITORS TO ACTIVE AND INACTIVE CDK2       
REMARK 900 PROVIDES INSIGHTS FOR DRUG DESIGN                                    
DBREF  2BTR A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    U73  A 300      18                                                       
HETNAM     U73 N-(5-ISOPROPYL-THIAZOL-2-YL)-2-PYRIDIN-3-YL-ACETAMIDE            
FORMUL   2  U73    C13 H15 N3 O S                                               
FORMUL   3  HOH   *67(H2 O)                                                     
HELIX    1   1 THR A   47  LYS A   56  1                                  10    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ALA A  170  LEU A  175  1                                   6    
HELIX    6   6 THR A  182  ARG A  199  1                                  18    
HELIX    7   7 SER A  207  GLY A  220  1                                  14    
HELIX    8   8 GLY A  229  MET A  233  5                                   5    
HELIX    9   9 ASP A  247  VAL A  252  1                                   6    
HELIX   10  10 ASP A  256  LEU A  267  1                                  12    
HELIX   11  11 SER A  276  ALA A  282  1                                   7    
HELIX   12  12 HIS A  283  GLN A  287  5                                   5    
SHEET    1  AA 5 PHE A   4  GLU A  12  0                                        
SHEET    2  AA 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  ILE A  10           
SHEET    3  AA 5 VAL A  29  ILE A  35 -1  O  VAL A  30   N  ALA A  21           
SHEET    4  AA 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 LEU A  66  THR A  72 -1  N  LEU A  67   O  VAL A  79           
SHEET    1  AB 3 GLN A  85  ASP A  86  0                                        
SHEET    2  AB 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3  AB 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0        -3.24                     
SITE     1 AC1  9 ILE A  10  VAL A  18  ALA A  31  GLU A  81                    
SITE     2 AC1  9 PHE A  82  LEU A  83  HIS A  84  LEU A 134                    
SITE     3 AC1  9 ASP A 145                                                     
CRYST1   53.215   71.615   71.588  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      0.018792  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013964  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013969        0.00000                         
ATOM      1  N   MET A   1      25.019  56.635  24.604  1.00 50.61           N  
ATOM      2  CA  MET A   1      26.039  57.131  23.621  1.00 50.43           C  
ATOM      3  C   MET A   1      25.684  58.529  23.125  1.00 50.08           C  
ATOM      4  O   MET A   1      24.523  58.914  23.155  1.00 50.51           O  
ATOM      5  CB  MET A   1      26.140  56.180  22.425  1.00 50.38           C  
ATOM      6  CG  MET A   1      27.364  56.387  21.561  1.00 50.52           C  
ATOM      7  SD  MET A   1      27.019  56.967  19.876  1.00 53.37           S  
ATOM      8  CE  MET A   1      28.655  56.543  19.147  1.00 52.89           C  
ATOM      9  N   GLU A   2      26.692  59.272  22.663  1.00 49.49           N  
ATOM     10  CA  GLU A   2      26.534  60.651  22.190  1.00 48.61           C  
ATOM     11  C   GLU A   2      25.316  60.842  21.308  1.00 47.13           C  
ATOM     12  O   GLU A   2      24.647  61.869  21.404  1.00 46.77           O  
ATOM     13  CB  GLU A   2      27.742  61.125  21.357  1.00 49.15           C  
ATOM     14  CG  GLU A   2      29.123  60.959  21.974  1.00 51.50           C  
ATOM     15  CD  GLU A   2      29.822  59.666  21.572  1.00 53.34           C  
ATOM     16  OE1 GLU A   2      30.337  59.561  20.429  1.00 52.44           O  
ATOM     17  OE2 GLU A   2      29.861  58.753  22.432  1.00 56.84           O  
ATOM     18  N   ASN A   3      25.082  59.881  20.413  1.00 45.45           N  
ATOM     19  CA  ASN A   3      24.069  60.002  19.370  1.00 44.70           C  
ATOM     20  C   ASN A   3      22.651  59.659  19.848  1.00 43.93           C  
ATOM     21  O   ASN A   3      21.695  59.852  19.107  1.00 43.10           O  
ATOM     22  CB  ASN A   3      24.422  59.106  18.174  1.00 44.36           C  
ATOM     23  CG  ASN A   3      25.610  59.630  17.368  1.00 44.58           C  
ATOM     24  OD1 ASN A   3      25.520  60.664  16.689  1.00 45.01           O  
ATOM     25  ND2 ASN A   3      26.713  58.909  17.424  1.00 43.14           N  
ATOM     26  N   PHE A   4      22.533  59.137  21.070  1.00 43.48           N  
ATOM     27  CA  PHE A   4      21.247  58.722  21.637  1.00 43.02           C  
ATOM     28  C   PHE A   4      20.965  59.428  22.959  1.00 43.22           C  
ATOM     29  O   PHE A   4      21.880  59.687  23.752  1.00 43.61           O  
ATOM     30  CB  PHE A   4      21.230  57.191  21.828  1.00 42.90           C  
ATOM     31  CG  PHE A   4      21.407  56.424  20.553  1.00 42.16           C  
ATOM     32  CD1 PHE A   4      20.312  56.142  19.741  1.00 41.08           C  
ATOM     33  CD2 PHE A   4      22.669  55.993  20.145  1.00 41.97           C  
ATOM     34  CE1 PHE A   4      20.468  55.440  18.548  1.00 40.24           C  
ATOM     35  CE2 PHE A   4      22.838  55.302  18.948  1.00 41.54           C  
ATOM     36  CZ  PHE A   4      21.734  55.024  18.148  1.00 41.41           C  
ATOM     37  N   GLN A   5      19.697  59.772  23.171  1.00 43.27           N  
ATOM     38  CA  GLN A   5      19.201  60.316  24.428  1.00 43.62           C  
ATOM     39  C   GLN A   5      18.377  59.220  25.083  1.00 43.42           C  
ATOM     40  O   GLN A   5      17.408  58.750  24.483  1.00 42.52           O  
ATOM     41  CB  GLN A   5      18.319  61.547  24.159  1.00 44.02           C  
ATOM     42  CG  GLN A   5      17.265  61.859  25.235  1.00 46.02           C  
ATOM     43  CD  GLN A   5      16.049  62.681  24.737  1.00 49.42           C  
ATOM     44  OE1 GLN A   5      15.444  63.435  25.521  1.00 50.37           O  
ATOM     45  NE2 GLN A   5      15.685  62.529  23.459  1.00 51.17           N  
ATOM     46  N   LYS A   6      18.738  58.823  26.302  1.00 43.40           N  
ATOM     47  CA  LYS A   6      17.964  57.829  27.036  1.00 43.71           C  
ATOM     48  C   LYS A   6      16.624  58.440  27.401  1.00 44.14           C  
ATOM     49  O   LYS A   6      16.556  59.593  27.809  1.00 44.20           O  
ATOM     50  CB  LYS A   6      18.685  57.358  28.301  1.00 43.70           C  
ATOM     51  CG  LYS A   6      19.745  56.294  28.057  1.00 44.85           C  
ATOM     52  CD  LYS A   6      20.752  56.172  29.233  1.00 45.43           C  
ATOM     53  CE  LYS A   6      22.215  56.313  28.778  1.00 47.07           C  
ATOM     54  NZ  LYS A   6      23.195  55.914  29.865  1.00 46.98           N  
ATOM     55  N   VAL A   7      15.556  57.668  27.222  1.00 44.21           N  
ATOM     56  CA  VAL A   7      14.206  58.087  27.578  1.00 44.15           C  
ATOM     57  C   VAL A   7      13.759  57.392  28.871  1.00 44.33           C  
ATOM     58  O   VAL A   7      13.296  58.037  29.799  1.00 44.17           O  
ATOM     59  CB  VAL A   7      13.212  57.764  26.452  1.00 43.87           C  
ATOM     60  CG1 VAL A   7      11.786  58.079  26.888  1.00 44.38           C  
ATOM     61  CG2 VAL A   7      13.581  58.536  25.179  1.00 43.59           C  
ATOM     62  N   GLU A   8      13.868  56.073  28.913  1.00 44.36           N  
ATOM     63  CA  GLU A   8      13.587  55.320  30.144  1.00 44.51           C  
ATOM     64  C   GLU A   8      14.215  53.940  30.120  1.00 44.88           C  
ATOM     65  O   GLU A   8      14.521  53.407  29.056  1.00 43.10           O  
ATOM     66  CB  GLU A   8      12.082  55.181  30.359  1.00 44.82           C  
ATOM     67  CG  GLU A   8      11.348  54.510  29.200  1.00 45.25           C  
ATOM     68  CD  GLU A   8       9.857  54.741  29.228  1.00 46.81           C  
ATOM     69  OE1 GLU A   8       9.111  53.778  29.529  1.00 47.31           O  
ATOM     70  OE2 GLU A   8       9.442  55.892  28.930  1.00 50.82           O  
ATOM     71  N   LYS A   9      14.387  53.357  31.303  1.00 45.39           N  
ATOM     72  CA  LYS A   9      14.865  51.984  31.419  1.00 46.32           C  
ATOM     73  C   LYS A   9      13.720  51.009  31.216  1.00 46.70           C  
ATOM     74  O   LYS A   9      12.762  50.976  31.989  1.00 47.01           O  
ATOM     75  CB  LYS A   9      15.526  51.739  32.781  1.00 46.55           C  
ATOM     76  CG  LYS A   9      16.528  50.580  32.775  1.00 47.53           C  
ATOM     77  CD  LYS A   9      17.325  50.510  34.087  1.00 48.46           C  
ATOM     78  CE  LYS A   9      18.477  51.515  34.085  1.00 48.74           C  
ATOM     79  NZ  LYS A   9      18.648  52.227  35.376  1.00 48.99           N  
ATOM     80  N   ILE A  10      13.835  50.237  30.149  1.00 47.17           N  
ATOM     81  CA  ILE A  10      12.899  49.174  29.793  1.00 48.15           C  
ATOM     82  C   ILE A  10      13.019  47.991  30.725  1.00 49.04           C  
ATOM     83  O   ILE A  10      12.020  47.433  31.178  1.00 49.85           O  
ATOM     84  CB  ILE A  10      13.219  48.681  28.357  1.00 48.23           C  
ATOM     85  CG1 ILE A  10      12.763  49.716  27.331  1.00 47.72           C  
ATOM     86  CG2 ILE A  10      12.636  47.283  28.106  1.00 49.34           C  
ATOM     87  CD1 ILE A  10      12.902  49.282  25.904  1.00 46.06           C  
ATOM     88  N   GLY A  11      14.247  47.560  30.967  1.00 49.71           N  
ATOM     89  CA  GLY A  11      14.458  46.368  31.762  1.00 50.42           C  
ATOM     90  C   GLY A  11      15.904  45.993  31.974  1.00 51.12           C  
ATOM     91  O   GLY A  11      16.823  46.726  31.595  1.00 50.03           O  
ATOM     92  N   GLU A  12      16.093  44.827  32.584  1.00 52.34           N  
ATOM     93  CA  GLU A  12      17.407  44.389  33.027  1.00 53.54           C  
ATOM     94  C   GLU A  12      17.586  42.908  32.774  1.00 54.12           C  
ATOM     95  O   GLU A  12      16.692  42.096  33.037  1.00 54.54           O  
ATOM     96  CB  GLU A  12      17.586  44.669  34.512  1.00 53.97           C  
ATOM     97  CG  GLU A  12      17.835  46.132  34.852  1.00 55.22           C  
ATOM     98  CD  GLU A  12      17.859  46.375  36.350  1.00 57.07           C  
ATOM     99  OE1 GLU A  12      17.283  45.540  37.097  1.00 56.87           O  
ATOM    100  OE2 GLU A  12      18.454  47.396  36.773  1.00 58.33           O  
ATOM    101  N   GLY A  13      18.779  42.553  32.321  1.00 54.70           N  
ATOM    102  CA  GLY A  13      18.982  41.289  31.653  1.00 55.29           C  
ATOM    103  C   GLY A  13      20.097  40.427  32.195  1.00 55.80           C  
ATOM    104  O   GLY A  13      20.901  40.836  33.061  1.00 55.81           O  
ATOM    105  N   THR A  14      20.084  39.196  31.688  1.00 56.29           N  
ATOM    106  CA  THR A  14      21.189  38.259  31.791  1.00 56.62           C  
ATOM    107  C   THR A  14      22.513  39.013  31.583  1.00 56.26           C  
ATOM    108  O   THR A  14      23.304  39.169  32.529  1.00 56.29           O  
ATOM    109  CB  THR A  14      21.003  37.089  30.744  1.00 57.02           C  
ATOM    110  OG1 THR A  14      20.300  37.549  29.577  1.00 57.91           O  
ATOM    111  CG2 THR A  14      20.078  35.988  31.279  1.00 56.88           C  
ATOM    112  N   TYR A  15      22.719  39.539  30.374  1.00 55.64           N  
ATOM    113  CA  TYR A  15      23.983  40.213  30.053  1.00 54.80           C  
ATOM    114  C   TYR A  15      23.960  41.668  30.546  1.00 53.10           C  
ATOM    115  O   TYR A  15      24.787  42.045  31.394  1.00 53.72           O  
ATOM    116  CB  TYR A  15      24.342  40.157  28.550  1.00 55.51           C  
ATOM    117  CG  TYR A  15      23.542  39.199  27.683  1.00 57.03           C  
ATOM    118  CD1 TYR A  15      23.323  37.876  28.069  1.00 59.35           C  
ATOM    119  CD2 TYR A  15      23.023  39.618  26.463  1.00 59.11           C  
ATOM    120  CE1 TYR A  15      22.586  37.008  27.269  1.00 60.07           C  
ATOM    121  CE2 TYR A  15      22.295  38.755  25.652  1.00 60.16           C  
ATOM    122  CZ  TYR A  15      22.082  37.458  26.056  1.00 60.31           C  
ATOM    123  OH  TYR A  15      21.363  36.606  25.255  1.00 62.16           O  
ATOM    124  N   GLY A  16      22.998  42.461  30.050  1.00 50.31           N  
ATOM    125  CA  GLY A  16      22.998  43.895  30.278  1.00 47.97           C  
ATOM    126  C   GLY A  16      21.664  44.581  30.484  1.00 45.50           C  
ATOM    127  O   GLY A  16      20.669  43.937  30.809  1.00 45.60           O  
ATOM    128  N   VAL A  17      21.665  45.904  30.326  1.00 42.06           N  
ATOM    129  CA  VAL A  17      20.504  46.731  30.611  1.00 39.52           C  
ATOM    130  C   VAL A  17      19.968  47.382  29.338  1.00 36.54           C  
ATOM    131  O   VAL A  17      20.722  47.700  28.442  1.00 34.56           O  
ATOM    132  CB  VAL A  17      20.798  47.799  31.687  1.00 40.10           C  
ATOM    133  CG1 VAL A  17      21.680  48.927  31.167  1.00 41.72           C  
ATOM    134  CG2 VAL A  17      19.513  48.373  32.210  1.00 41.64           C  
ATOM    135  N   VAL A  18      18.652  47.564  29.297  1.00 33.83           N  
ATOM    136  CA  VAL A  18      17.920  47.961  28.091  1.00 32.19           C  
ATOM    137  C   VAL A  18      17.218  49.283  28.304  1.00 30.26           C  
ATOM    138  O   VAL A  18      16.465  49.434  29.255  1.00 29.40           O  
ATOM    139  CB  VAL A  18      16.871  46.926  27.732  1.00 32.29           C  
ATOM    140  CG1 VAL A  18      16.189  47.303  26.406  1.00 32.27           C  
ATOM    141  CG2 VAL A  18      17.498  45.555  27.638  1.00 33.70           C  
ATOM    142  N   TYR A  19      17.460  50.230  27.402  1.00 28.39           N  
ATOM    143  CA  TYR A  19      16.857  51.538  27.456  1.00 28.61           C  
ATOM    144  C   TYR A  19      16.004  51.794  26.235  1.00 26.81           C  
ATOM    145  O   TYR A  19      16.402  51.479  25.126  1.00 27.27           O  
ATOM    146  CB  TYR A  19      17.924  52.608  27.480  1.00 29.14           C  
ATOM    147  CG  TYR A  19      18.659  52.715  28.805  1.00 35.01           C  
ATOM    148  CD1 TYR A  19      19.957  52.273  28.927  1.00 40.99           C  
ATOM    149  CD2 TYR A  19      18.047  53.269  29.915  1.00 38.95           C  
ATOM    150  CE1 TYR A  19      20.631  52.376  30.129  1.00 44.61           C  
ATOM    151  CE2 TYR A  19      18.705  53.371  31.115  1.00 42.75           C  
ATOM    152  CZ  TYR A  19      19.997  52.925  31.219  1.00 44.30           C  
ATOM    153  OH  TYR A  19      20.685  53.017  32.408  1.00 50.87           O  
ATOM    154  N   LYS A  20      14.863  52.424  26.426  1.00 24.94           N  
ATOM    155  CA  LYS A  20      14.218  53.146  25.340  1.00 24.78           C  
ATOM    156  C   LYS A  20      15.033  54.413  25.112  1.00 25.25           C  
ATOM    157  O   LYS A  20      15.405  55.101  26.058  1.00 24.98           O  
ATOM    158  CB  LYS A  20      12.757  53.490  25.678  1.00 24.72           C  
ATOM    159  CG  LYS A  20      11.970  54.103  24.475  1.00 24.19           C  
ATOM    160  CD  LYS A  20      10.501  54.361  24.860  1.00 21.75           C  
ATOM    161  CE  LYS A  20       9.714  54.831  23.657  1.00 21.57           C  
ATOM    162  NZ  LYS A  20       8.284  55.085  23.998  1.00 20.91           N  
ATOM    163  N   ALA A  21      15.290  54.739  23.858  1.00 25.32           N  
ATOM    164  CA  ALA A  21      16.187  55.830  23.524  1.00 26.29           C  
ATOM    165  C   ALA A  21      15.784  56.469  22.217  1.00 28.02           C  
ATOM    166  O   ALA A  21      15.108  55.843  21.391  1.00 25.87           O  
ATOM    167  CB  ALA A  21      17.608  55.323  23.437  1.00 26.50           C  
ATOM    168  N   ARG A  22      16.185  57.726  22.034  1.00 30.54           N  
ATOM    169  CA  ARG A  22      15.927  58.450  20.798  1.00 34.01           C  
ATOM    170  C   ARG A  22      17.244  58.822  20.113  1.00 36.24           C  
ATOM    171  O   ARG A  22      18.167  59.299  20.766  1.00 35.98           O  
ATOM    172  CB  ARG A  22      15.147  59.724  21.103  1.00 34.83           C  
ATOM    173  CG  ARG A  22      15.027  60.673  19.946  1.00 37.82           C  
ATOM    174  CD  ARG A  22      14.293  61.949  20.325  1.00 42.65           C  
ATOM    175  NE  ARG A  22      13.006  61.642  20.935  1.00 44.01           N  
ATOM    176  CZ  ARG A  22      11.942  61.212  20.260  1.00 46.24           C  
ATOM    177  NH1 ARG A  22      11.981  61.037  18.938  1.00 47.23           N  
ATOM    178  NH2 ARG A  22      10.822  60.969  20.910  1.00 48.18           N  
ATOM    179  N   ASN A  23      17.312  58.584  18.812  1.00 39.04           N  
ATOM    180  CA  ASN A  23      18.404  59.056  17.984  1.00 41.88           C  
ATOM    181  C   ASN A  23      18.233  60.556  17.735  1.00 44.36           C  
ATOM    182  O   ASN A  23      17.244  60.976  17.154  1.00 45.29           O  
ATOM    183  CB  ASN A  23      18.402  58.285  16.663  1.00 42.29           C  
ATOM    184  CG  ASN A  23      19.709  58.416  15.898  1.00 42.99           C  
ATOM    185  OD1 ASN A  23      20.476  59.327  16.142  1.00 45.33           O  
ATOM    186  ND2 ASN A  23      19.966  57.488  14.987  1.00 43.57           N  
ATOM    187  N   LYS A  24      19.187  61.371  18.182  1.00 47.30           N  
ATOM    188  CA  LYS A  24      19.142  62.819  17.898  1.00 48.83           C  
ATOM    189  C   LYS A  24      19.316  63.130  16.403  1.00 50.04           C  
ATOM    190  O   LYS A  24      18.980  64.234  15.946  1.00 50.54           O  
ATOM    191  CB  LYS A  24      20.207  63.559  18.681  1.00 49.24           C  
ATOM    192  CG  LYS A  24      20.167  63.329  20.172  1.00 50.01           C  
ATOM    193  CD  LYS A  24      21.577  63.380  20.780  1.00 50.84           C  
ATOM    194  CE  LYS A  24      21.607  64.153  22.109  1.00 51.96           C  
ATOM    195  NZ  LYS A  24      22.586  63.605  23.117  1.00 51.75           N  
ATOM    196  N   LEU A  25      19.857  62.161  15.660  1.00 50.92           N  
ATOM    197  CA  LEU A  25      19.958  62.233  14.194  1.00 51.49           C  
ATOM    198  C   LEU A  25      18.624  61.898  13.510  1.00 51.12           C  
ATOM    199  O   LEU A  25      17.832  62.797  13.209  1.00 52.56           O  
ATOM    200  CB  LEU A  25      21.049  61.283  13.674  1.00 51.73           C  
ATOM    201  CG  LEU A  25      22.521  61.528  14.064  1.00 53.45           C  
ATOM    202  CD1 LEU A  25      23.174  60.244  14.603  1.00 54.39           C  
ATOM    203  CD2 LEU A  25      23.313  62.058  12.871  1.00 53.29           C  
ATOM    204  N   THR A  26      18.376  60.610  13.278  1.00 50.07           N  
ATOM    205  CA  THR A  26      17.191  60.151  12.546  1.00 49.08           C  
ATOM    206  C   THR A  26      15.851  60.598  13.180  1.00 47.37           C  
ATOM    207  O   THR A  26      14.795  60.540  12.522  1.00 47.88           O  
ATOM    208  CB  THR A  26      17.221  58.590  12.396  1.00 49.29           C  
ATOM    209  OG1 THR A  26      17.484  57.978  13.661  1.00 49.73           O  
ATOM    210  CG2 THR A  26      18.391  58.113  11.545  1.00 49.64           C  
ATOM    211  N   GLY A  27      15.892  61.045  14.435  1.00 45.08           N  
ATOM    212  CA  GLY A  27      14.695  61.217  15.245  1.00 43.17           C  
ATOM    213  C   GLY A  27      14.133  59.892  15.765  1.00 40.87           C  
ATOM    214  O   GLY A  27      13.134  59.869  16.513  1.00 41.19           O  
ATOM    215  N   GLU A  28      14.816  58.798  15.430  1.00 37.59           N  
ATOM    216  CA  GLU A  28      14.322  57.436  15.616  1.00 35.08           C  
ATOM    217  C   GLU A  28      14.237  57.076  17.118  1.00 31.68           C  
ATOM    218  O   GLU A  28      15.126  57.406  17.905  1.00 29.27           O  
ATOM    219  CB  GLU A  28      15.247  56.459  14.875  1.00 35.57           C  
ATOM    220  CG  GLU A  28      14.654  55.160  14.327  1.00 39.66           C  
ATOM    221  CD  GLU A  28      15.716  54.277  13.642  1.00 43.10           C  
ATOM    222  OE1 GLU A  28      15.356  53.277  12.966  1.00 44.47           O  
ATOM    223  OE2 GLU A  28      16.934  54.572  13.775  1.00 46.91           O  
ATOM    224  N   VAL A  29      13.147  56.407  17.481  1.00 27.95           N  
ATOM    225  CA  VAL A  29      12.943  55.845  18.812  1.00 26.10           C  
ATOM    226  C   VAL A  29      13.390  54.383  18.696  1.00 23.57           C  
ATOM    227  O   VAL A  29      12.944  53.652  17.824  1.00 21.23           O  
ATOM    228  CB  VAL A  29      11.470  55.975  19.223  1.00 26.14           C  
ATOM    229  CG1 VAL A  29      11.149  55.094  20.410  1.00 27.60           C  
ATOM    230  CG2 VAL A  29      11.115  57.468  19.525  1.00 27.78           C  
ATOM    231  N   VAL A  30      14.340  53.974  19.537  1.00 22.64           N  
ATOM    232  CA  VAL A  30      14.944  52.667  19.466  1.00 20.74           C  
ATOM    233  C   VAL A  30      15.049  52.099  20.892  1.00 21.40           C  
ATOM    234  O   VAL A  30      14.797  52.815  21.865  1.00 18.65           O  
ATOM    235  CB  VAL A  30      16.355  52.756  18.895  1.00 22.36           C  
ATOM    236  CG1 VAL A  30      16.371  53.337  17.456  1.00 23.23           C  
ATOM    237  CG2 VAL A  30      17.255  53.563  19.805  1.00 20.62           C  
ATOM    238  N   ALA A  31      15.434  50.826  20.977  1.00 21.63           N  
ATOM    239  CA  ALA A  31      15.827  50.210  22.225  1.00 22.48           C  
ATOM    240  C   ALA A  31      17.325  50.004  22.155  1.00 24.27           C  
ATOM    241  O   ALA A  31      17.860  49.415  21.195  1.00 22.65           O  
ATOM    242  CB  ALA A  31      15.130  48.916  22.416  1.00 22.70           C  
ATOM    243  N   LEU A  32      18.008  50.483  23.178  1.00 24.97           N  
ATOM    244  CA  LEU A  32      19.436  50.246  23.326  1.00 27.25           C  
ATOM    245  C   LEU A  32      19.762  49.191  24.380  1.00 27.86           C  
ATOM    246  O   LEU A  32      19.334  49.298  25.523  1.00 28.06           O  
ATOM    247  CB  LEU A  32      20.083  51.552  23.715  1.00 28.18           C  
ATOM    248  CG  LEU A  32      21.211  52.059  22.854  1.00 33.49           C  
ATOM    249  CD1 LEU A  32      20.685  52.484  21.480  1.00 36.09           C  
ATOM    250  CD2 LEU A  32      21.836  53.187  23.610  1.00 34.45           C  
ATOM    251  N   LYS A  33      20.562  48.188  24.019  1.00 28.82           N  
ATOM    252  CA  LYS A  33      20.965  47.167  24.970  1.00 29.83           C  
ATOM    253  C   LYS A  33      22.449  47.330  25.223  1.00 31.28           C  
ATOM    254  O   LYS A  33      23.246  47.196  24.296  1.00 30.36           O  
ATOM    255  CB  LYS A  33      20.686  45.766  24.459  1.00 29.74           C  
ATOM    256  CG  LYS A  33      21.042  44.647  25.461  1.00 31.40           C  
ATOM    257  CD  LYS A  33      20.555  43.265  25.012  1.00 32.99           C  
ATOM    258  CE  LYS A  33      20.849  42.204  26.053  1.00 36.11           C  
ATOM    259  NZ  LYS A  33      20.096  42.337  27.344  1.00 38.93           N  
ATOM    260  N   LYS A  34      22.816  47.614  26.467  1.00 32.93           N  
ATOM    261  CA  LYS A  34      24.235  47.734  26.802  1.00 35.55           C  
ATOM    262  C   LYS A  34      24.755  46.505  27.580  1.00 36.36           C  
ATOM    263  O   LYS A  34      24.202  46.124  28.610  1.00 36.21           O  
ATOM    264  CB  LYS A  34      24.505  49.084  27.482  1.00 36.25           C  
ATOM    265  CG  LYS A  34      24.609  49.117  29.005  1.00 40.14           C  
ATOM    266  CD  LYS A  34      25.948  49.724  29.494  1.00 42.31           C  
ATOM    267  CE  LYS A  34      25.735  50.849  30.512  1.00 43.99           C  
ATOM    268  NZ  LYS A  34      24.839  50.436  31.645  1.00 45.57           N  
ATOM    269  N   ILE A  35      25.824  45.891  27.075  1.00 37.31           N  
ATOM    270  CA  ILE A  35      26.378  44.664  27.665  1.00 38.55           C  
ATOM    271  C   ILE A  35      27.748  44.961  28.247  1.00 39.20           C  
ATOM    272  O   ILE A  35      28.558  45.632  27.607  1.00 39.21           O  
ATOM    273  CB  ILE A  35      26.497  43.578  26.600  1.00 39.08           C  
ATOM    274  CG1 ILE A  35      25.130  43.286  25.961  1.00 40.19           C  
ATOM    275  CG2 ILE A  35      27.142  42.303  27.203  1.00 39.18           C  
ATOM    276  CD1 ILE A  35      25.232  42.713  24.569  1.00 41.51           C  
ATOM    277  N   THR A  47      34.978  36.764  19.960  1.00 51.34           N  
ATOM    278  CA  THR A  47      34.358  36.610  18.645  1.00 50.94           C  
ATOM    279  C   THR A  47      32.866  37.009  18.638  1.00 50.69           C  
ATOM    280  O   THR A  47      32.119  36.640  17.727  1.00 49.96           O  
ATOM    281  CB  THR A  47      34.467  35.143  18.200  1.00 51.22           C  
ATOM    282  OG1 THR A  47      33.975  34.291  19.244  1.00 50.28           O  
ATOM    283  CG2 THR A  47      35.926  34.708  18.013  1.00 51.25           C  
ATOM    284  N   ALA A  48      32.423  37.740  19.657  1.00 50.53           N  
ATOM    285  CA  ALA A  48      31.049  38.246  19.686  1.00 50.41           C  
ATOM    286  C   ALA A  48      30.804  39.203  18.521  1.00 50.44           C  
ATOM    287  O   ALA A  48      29.746  39.194  17.906  1.00 49.66           O  
ATOM    288  CB  ALA A  48      30.761  38.946  20.999  1.00 50.61           C  
ATOM    289  N   ILE A  49      31.798  40.020  18.205  1.00 50.60           N  
ATOM    290  CA  ILE A  49      31.639  40.998  17.138  1.00 50.65           C  
ATOM    291  C   ILE A  49      31.181  40.348  15.830  1.00 50.59           C  
ATOM    292  O   ILE A  49      30.247  40.827  15.201  1.00 49.71           O  
ATOM    293  CB  ILE A  49      32.940  41.813  16.946  1.00 50.80           C  
ATOM    294  CG1 ILE A  49      33.286  42.566  18.239  1.00 50.84           C  
ATOM    295  CG2 ILE A  49      32.810  42.794  15.756  1.00 50.72           C  
ATOM    296  CD1 ILE A  49      32.132  43.392  18.820  1.00 51.53           C  
ATOM    297  N   ARG A  50      31.817  39.252  15.431  1.00 51.15           N  
ATOM    298  CA  ARG A  50      31.472  38.620  14.155  1.00 51.69           C  
ATOM    299  C   ARG A  50      30.081  37.966  14.222  1.00 51.53           C  
ATOM    300  O   ARG A  50      29.330  38.024  13.247  1.00 50.94           O  
ATOM    301  CB  ARG A  50      32.559  37.616  13.704  1.00 52.42           C  
ATOM    302  CG  ARG A  50      33.693  38.241  12.841  1.00 54.24           C  
ATOM    303  CD  ARG A  50      35.067  38.409  13.539  1.00 57.18           C  
ATOM    304  NE  ARG A  50      35.800  37.151  13.663  1.00 60.81           N  
ATOM    305  CZ  ARG A  50      37.110  37.032  13.922  1.00 63.68           C  
ATOM    306  NH1 ARG A  50      37.903  38.104  14.080  1.00 64.15           N  
ATOM    307  NH2 ARG A  50      37.640  35.813  14.015  1.00 64.70           N  
ATOM    308  N   GLU A  51      29.746  37.366  15.368  1.00 51.11           N  
ATOM    309  CA  GLU A  51      28.448  36.709  15.546  1.00 51.48           C  
ATOM    310  C   GLU A  51      27.315  37.725  15.488  1.00 50.65           C  
ATOM    311  O   GLU A  51      26.266  37.465  14.903  1.00 50.27           O  
ATOM    312  CB  GLU A  51      28.368  35.997  16.890  1.00 51.82           C  
ATOM    313  CG  GLU A  51      28.663  34.514  16.863  1.00 54.91           C  
ATOM    314  CD  GLU A  51      28.464  33.882  18.230  1.00 58.03           C  
ATOM    315  OE1 GLU A  51      29.037  34.418  19.209  1.00 60.11           O  
ATOM    316  OE2 GLU A  51      27.733  32.862  18.328  1.00 60.29           O  
ATOM    317  N   ILE A  52      27.531  38.874  16.123  1.00 49.85           N  
ATOM    318  CA  ILE A  52      26.533  39.929  16.190  1.00 49.17           C  
ATOM    319  C   ILE A  52      26.350  40.586  14.839  1.00 48.84           C  
ATOM    320  O   ILE A  52      25.230  40.866  14.432  1.00 48.50           O  
ATOM    321  CB  ILE A  52      26.937  40.981  17.243  1.00 49.67           C  
ATOM    322  CG1 ILE A  52      26.910  40.369  18.648  1.00 49.79           C  
ATOM    323  CG2 ILE A  52      26.017  42.185  17.180  1.00 50.13           C  
ATOM    324  CD1 ILE A  52      25.632  39.652  19.008  1.00 50.54           C  
ATOM    325  N   SER A  53      27.452  40.834  14.145  1.00 47.96           N  
ATOM    326  CA  SER A  53      27.397  41.352  12.786  1.00 47.65           C  
ATOM    327  C   SER A  53      26.519  40.448  11.898  1.00 46.76           C  
ATOM    328  O   SER A  53      25.762  40.938  11.059  1.00 47.51           O  
ATOM    329  CB  SER A  53      28.815  41.458  12.205  1.00 47.70           C  
ATOM    330  OG  SER A  53      29.566  42.480  12.849  1.00 49.08           O  
ATOM    331  N   LEU A  54      26.625  39.133  12.097  1.00 45.12           N  
ATOM    332  CA  LEU A  54      25.863  38.148  11.332  1.00 43.79           C  
ATOM    333  C   LEU A  54      24.371  38.264  11.641  1.00 41.65           C  
ATOM    334  O   LEU A  54      23.535  38.026  10.787  1.00 40.20           O  
ATOM    335  CB  LEU A  54      26.346  36.738  11.674  1.00 44.45           C  
ATOM    336  CG  LEU A  54      25.812  35.571  10.838  1.00 46.56           C  
ATOM    337  CD1 LEU A  54      26.337  35.619   9.386  1.00 48.07           C  
ATOM    338  CD2 LEU A  54      26.195  34.242  11.502  1.00 48.57           C  
ATOM    339  N   LEU A  55      24.054  38.629  12.877  1.00 39.21           N  
ATOM    340  CA  LEU A  55      22.662  38.859  13.267  1.00 38.23           C  
ATOM    341  C   LEU A  55      22.042  40.083  12.579  1.00 36.68           C  
ATOM    342  O   LEU A  55      20.837  40.100  12.310  1.00 35.48           O  
ATOM    343  CB  LEU A  55      22.548  38.981  14.787  1.00 37.69           C  
ATOM    344  CG  LEU A  55      22.799  37.648  15.458  1.00 40.42           C  
ATOM    345  CD1 LEU A  55      22.992  37.841  16.950  1.00 41.99           C  
ATOM    346  CD2 LEU A  55      21.651  36.654  15.147  1.00 41.14           C  
ATOM    347  N   LYS A  56      22.860  41.089  12.282  1.00 35.54           N  
ATOM    348  CA  LYS A  56      22.379  42.256  11.560  1.00 35.15           C  
ATOM    349  C   LYS A  56      21.797  41.910  10.202  1.00 34.24           C  
ATOM    350  O   LYS A  56      21.037  42.702   9.669  1.00 34.34           O  
ATOM    351  CB  LYS A  56      23.465  43.307  11.356  1.00 35.30           C  
ATOM    352  CG  LYS A  56      24.076  43.852  12.651  1.00 36.99           C  
ATOM    353  CD  LYS A  56      25.379  44.616  12.367  1.00 39.62           C  
ATOM    354  CE  LYS A  56      25.137  46.086  12.079  1.00 41.46           C  
ATOM    355  NZ  LYS A  56      26.391  46.773  11.574  1.00 41.62           N  
ATOM    356  N   GLU A  57      22.189  40.781   9.616  1.00 33.16           N  
ATOM    357  CA  GLU A  57      21.667  40.403   8.303  1.00 33.19           C  
ATOM    358  C   GLU A  57      20.488  39.425   8.392  1.00 31.92           C  
ATOM    359  O   GLU A  57      19.853  39.124   7.391  1.00 32.23           O  
ATOM    360  CB  GLU A  57      22.771  39.828   7.428  1.00 34.23           C  
ATOM    361  CG  GLU A  57      23.897  40.804   7.131  1.00 36.47           C  
ATOM    362  CD  GLU A  57      25.070  40.152   6.430  1.00 42.55           C  
ATOM    363  OE1 GLU A  57      24.940  38.992   5.965  1.00 46.76           O  
ATOM    364  OE2 GLU A  57      26.142  40.806   6.345  1.00 50.30           O  
ATOM    365  N   LEU A  58      20.190  38.952   9.592  1.00 30.13           N  
ATOM    366  CA  LEU A  58      19.091  38.046   9.826  1.00 29.36           C  
ATOM    367  C   LEU A  58      17.796  38.844   9.947  1.00 28.77           C  
ATOM    368  O   LEU A  58      17.274  39.032  11.038  1.00 27.68           O  
ATOM    369  CB  LEU A  58      19.386  37.224  11.096  1.00 30.04           C  
ATOM    370  CG  LEU A  58      18.456  36.079  11.499  1.00 31.69           C  
ATOM    371  CD1 LEU A  58      18.704  34.870  10.642  1.00 32.51           C  
ATOM    372  CD2 LEU A  58      18.574  35.713  12.981  1.00 33.40           C  
ATOM    373  N   ASN A  59      17.278  39.318   8.811  1.00 25.73           N  
ATOM    374  CA  ASN A  59      16.117  40.178   8.789  1.00 25.00           C  
ATOM    375  C   ASN A  59      14.823  39.481   8.370  1.00 24.00           C  
ATOM    376  O   ASN A  59      14.705  38.864   7.298  1.00 22.76           O  
ATOM    377  CB  ASN A  59      16.389  41.411   7.888  1.00 25.51           C  
ATOM    378  CG  ASN A  59      17.574  42.239   8.389  1.00 27.98           C  
ATOM    379  OD1 ASN A  59      18.472  42.618   7.598  1.00 33.20           O  
ATOM    380  ND2 ASN A  59      17.621  42.493   9.699  1.00 19.61           N  
ATOM    381  N   HIS A  60      13.820  39.587   9.228  1.00 21.96           N  
ATOM    382  CA  HIS A  60      12.530  38.980   8.988  1.00 22.16           C  
ATOM    383  C   HIS A  60      11.453  39.797   9.697  1.00 22.34           C  
ATOM    384  O   HIS A  60      11.724  40.347  10.766  1.00 21.98           O  
ATOM    385  CB  HIS A  60      12.566  37.528   9.530  1.00 22.30           C  
ATOM    386  CG  HIS A  60      11.370  36.708   9.175  1.00 21.73           C  
ATOM    387  ND1 HIS A  60      10.185  36.773   9.875  1.00 21.26           N  
ATOM    388  CD2 HIS A  60      11.171  35.809   8.178  1.00 22.57           C  
ATOM    389  CE1 HIS A  60       9.305  35.958   9.319  1.00 24.46           C  
ATOM    390  NE2 HIS A  60       9.881  35.346   8.296  1.00 21.24           N  
ATOM    391  N   PRO A  61      10.243  39.855   9.147  1.00 21.90           N  
ATOM    392  CA  PRO A  61       9.172  40.642   9.774  1.00 22.34           C  
ATOM    393  C   PRO A  61       8.852  40.187  11.209  1.00 21.55           C  
ATOM    394  O   PRO A  61       8.349  40.971  11.987  1.00 20.57           O  
ATOM    395  CB  PRO A  61       7.946  40.387   8.910  1.00 23.25           C  
ATOM    396  CG  PRO A  61       8.430  39.763   7.627  1.00 25.07           C  
ATOM    397  CD  PRO A  61       9.819  39.243   7.879  1.00 23.17           C  
ATOM    398  N   ASN A  62       9.180  38.956  11.534  1.00 20.35           N  
ATOM    399  CA  ASN A  62       8.944  38.465  12.879  1.00 21.03           C  
ATOM    400  C   ASN A  62      10.186  38.318  13.715  1.00 20.70           C  
ATOM    401  O   ASN A  62      10.183  37.568  14.692  1.00 21.07           O  
ATOM    402  CB  ASN A  62       8.159  37.160  12.771  1.00 20.13           C  
ATOM    403  CG  ASN A  62       6.835  37.347  12.088  1.00 19.34           C  
ATOM    404  OD1 ASN A  62       6.637  36.869  10.992  1.00 22.02           O  
ATOM    405  ND2 ASN A  62       5.888  37.955  12.774  1.00 19.95           N  
ATOM    406  N   ILE A  63      11.241  39.061  13.373  1.00 20.56           N  
ATOM    407  CA  ILE A  63      12.406  39.171  14.219  1.00 21.08           C  
ATOM    408  C   ILE A  63      12.669  40.638  14.452  1.00 20.88           C  
ATOM    409  O   ILE A  63      12.713  41.451  13.479  1.00 19.18           O  
ATOM    410  CB  ILE A  63      13.622  38.452  13.542  1.00 20.74           C  
ATOM    411  CG1 ILE A  63      13.366  36.962  13.492  1.00 23.56           C  
ATOM    412  CG2 ILE A  63      14.943  38.752  14.226  1.00 24.20           C  
ATOM    413  CD1 ILE A  63      14.338  36.257  12.620  1.00 22.86           C  
ATOM    414  N   VAL A  64      12.838  41.024  15.712  1.00 19.47           N  
ATOM    415  CA  VAL A  64      13.109  42.411  16.039  1.00 19.56           C  
ATOM    416  C   VAL A  64      14.415  42.832  15.346  1.00 20.53           C  
ATOM    417  O   VAL A  64      15.464  42.229  15.557  1.00 17.78           O  
ATOM    418  CB  VAL A  64      13.224  42.658  17.588  1.00 18.76           C  
ATOM    419  CG1 VAL A  64      13.507  44.084  17.861  1.00 20.00           C  
ATOM    420  CG2 VAL A  64      11.951  42.288  18.242  1.00 22.06           C  
ATOM    421  N   LYS A  65      14.339  43.873  14.519  1.00 21.83           N  
ATOM    422  CA  LYS A  65      15.467  44.270  13.697  1.00 23.58           C  
ATOM    423  C   LYS A  65      16.631  44.794  14.548  1.00 24.53           C  
ATOM    424  O   LYS A  65      16.451  45.673  15.374  1.00 24.25           O  
ATOM    425  CB  LYS A  65      15.046  45.350  12.704  1.00 24.37           C  
ATOM    426  CG  LYS A  65      16.188  45.844  11.727  1.00 27.31           C  
ATOM    427  CD  LYS A  65      15.521  46.752  10.625  1.00 29.00           C  
ATOM    428  CE  LYS A  65      16.441  47.201   9.466  1.00 29.58           C  
ATOM    429  NZ  LYS A  65      17.343  46.109   9.054  1.00 31.53           N  
ATOM    430  N   LEU A  66      17.809  44.223  14.359  1.00 25.30           N  
ATOM    431  CA  LEU A  66      19.030  44.767  14.917  1.00 26.75           C  
ATOM    432  C   LEU A  66      19.520  45.863  13.982  1.00 28.67           C  
ATOM    433  O   LEU A  66      19.927  45.588  12.847  1.00 27.86           O  
ATOM    434  CB  LEU A  66      20.075  43.682  15.077  1.00 27.84           C  
ATOM    435  CG  LEU A  66      21.364  44.072  15.816  1.00 29.76           C  
ATOM    436  CD1 LEU A  66      21.071  44.391  17.274  1.00 31.88           C  
ATOM    437  CD2 LEU A  66      22.336  42.945  15.765  1.00 30.30           C  
ATOM    438  N   LEU A  67      19.426  47.103  14.453  1.00 29.36           N  
ATOM    439  CA  LEU A  67      19.688  48.276  13.637  1.00 31.63           C  
ATOM    440  C   LEU A  67      21.189  48.525  13.511  1.00 33.96           C  
ATOM    441  O   LEU A  67      21.693  48.768  12.423  1.00 34.02           O  
ATOM    442  CB  LEU A  67      18.979  49.505  14.201  1.00 31.21           C  
ATOM    443  CG  LEU A  67      17.452  49.523  14.244  1.00 29.60           C  
ATOM    444  CD1 LEU A  67      16.991  50.781  14.867  1.00 27.33           C  
ATOM    445  CD2 LEU A  67      16.800  49.359  12.881  1.00 33.12           C  
ATOM    446  N   ASP A  68      21.905  48.397  14.613  1.00 36.20           N  
ATOM    447  CA  ASP A  68      23.313  48.735  14.626  1.00 38.39           C  
ATOM    448  C   ASP A  68      24.003  48.106  15.825  1.00 39.42           C  
ATOM    449  O   ASP A  68      23.359  47.715  16.818  1.00 37.75           O  
ATOM    450  CB  ASP A  68      23.468  50.268  14.656  1.00 39.27           C  
ATOM    451  CG  ASP A  68      23.444  50.906  13.264  1.00 42.72           C  
ATOM    452  OD1 ASP A  68      24.459  50.780  12.532  1.00 46.60           O  
ATOM    453  OD2 ASP A  68      22.461  51.552  12.816  1.00 46.63           O  
ATOM    454  N   VAL A  69      25.322  47.996  15.703  1.00 41.06           N  
ATOM    455  CA  VAL A  69      26.199  47.463  16.729  1.00 42.69           C  
ATOM    456  C   VAL A  69      27.268  48.521  16.945  1.00 44.05           C  
ATOM    457  O   VAL A  69      27.910  48.949  15.997  1.00 44.46           O  
ATOM    458  CB  VAL A  69      26.876  46.168  16.268  1.00 43.05           C  
ATOM    459  CG1 VAL A  69      27.654  45.520  17.395  1.00 43.14           C  
ATOM    460  CG2 VAL A  69      25.856  45.212  15.727  1.00 44.17           C  
ATOM    461  N   ILE A  70      27.440  48.941  18.193  1.00 45.52           N  
ATOM    462  CA  ILE A  70      28.430  49.940  18.561  1.00 46.69           C  
ATOM    463  C   ILE A  70      29.385  49.343  19.614  1.00 48.08           C  
ATOM    464  O   ILE A  70      29.007  49.151  20.770  1.00 47.56           O  
ATOM    465  CB  ILE A  70      27.708  51.222  19.060  1.00 46.64           C  
ATOM    466  CG1 ILE A  70      26.943  51.884  17.901  1.00 46.53           C  
ATOM    467  CG2 ILE A  70      28.697  52.221  19.666  1.00 47.52           C  
ATOM    468  CD1 ILE A  70      25.791  52.813  18.319  1.00 46.13           C  
ATOM    469  N   HIS A  71      30.615  49.019  19.199  1.00 49.68           N  
ATOM    470  CA  HIS A  71      31.674  48.624  20.138  1.00 50.74           C  
ATOM    471  C   HIS A  71      32.495  49.884  20.436  1.00 52.10           C  
ATOM    472  O   HIS A  71      32.849  50.634  19.521  1.00 52.16           O  
ATOM    473  CB  HIS A  71      32.546  47.511  19.550  1.00 50.86           C  
ATOM    474  CG  HIS A  71      33.468  46.869  20.540  1.00 50.56           C  
ATOM    475  ND1 HIS A  71      34.447  45.973  20.167  1.00 50.75           N  
ATOM    476  CD2 HIS A  71      33.575  47.002  21.885  1.00 50.72           C  
ATOM    477  CE1 HIS A  71      35.110  45.576  21.239  1.00 51.77           C  
ATOM    478  NE2 HIS A  71      34.602  46.187  22.294  1.00 51.08           N  
ATOM    479  N   THR A  72      32.767  50.132  21.714  1.00 53.06           N  
ATOM    480  CA  THR A  72      33.295  51.417  22.149  1.00 53.86           C  
ATOM    481  C   THR A  72      33.573  51.349  23.648  1.00 53.99           C  
ATOM    482  O   THR A  72      32.635  51.193  24.431  1.00 54.16           O  
ATOM    483  CB  THR A  72      32.263  52.541  21.798  1.00 54.21           C  
ATOM    484  OG1 THR A  72      32.551  53.082  20.492  1.00 55.03           O  
ATOM    485  CG2 THR A  72      32.361  53.745  22.730  1.00 54.67           C  
ATOM    486  N   GLU A  73      34.857  51.435  24.028  1.00 54.03           N  
ATOM    487  CA  GLU A  73      35.272  51.514  25.438  1.00 54.34           C  
ATOM    488  C   GLU A  73      35.067  50.177  26.194  1.00 53.89           C  
ATOM    489  O   GLU A  73      34.694  50.176  27.368  1.00 54.97           O  
ATOM    490  CB  GLU A  73      34.515  52.675  26.126  1.00 54.57           C  
ATOM    491  CG  GLU A  73      34.917  53.035  27.558  1.00 56.65           C  
ATOM    492  CD  GLU A  73      36.141  53.917  27.664  1.00 58.94           C  
ATOM    493  OE1 GLU A  73      36.454  54.647  26.694  1.00 60.38           O  
ATOM    494  OE2 GLU A  73      36.784  53.885  28.747  1.00 60.53           O  
ATOM    495  N   ASN A  74      35.297  49.046  25.527  1.00 53.03           N  
ATOM    496  CA  ASN A  74      35.014  47.711  26.103  1.00 52.08           C  
ATOM    497  C   ASN A  74      33.534  47.504  26.551  1.00 50.98           C  
ATOM    498  O   ASN A  74      33.198  46.530  27.256  1.00 51.18           O  
ATOM    499  CB  ASN A  74      36.008  47.377  27.251  1.00 52.54           C  
ATOM    500  CG  ASN A  74      37.440  47.085  26.745  1.00 53.02           C  
ATOM    501  OD1 ASN A  74      37.654  46.204  25.895  1.00 54.87           O  
ATOM    502  ND2 ASN A  74      38.421  47.803  27.291  1.00 52.81           N  
ATOM    503  N   LYS A  75      32.663  48.426  26.132  1.00 48.90           N  
ATOM    504  CA  LYS A  75      31.217  48.263  26.216  1.00 47.28           C  
ATOM    505  C   LYS A  75      30.683  47.929  24.816  1.00 45.05           C  
ATOM    506  O   LYS A  75      31.258  48.320  23.795  1.00 44.71           O  
ATOM    507  CB  LYS A  75      30.566  49.542  26.738  1.00 47.46           C  
ATOM    508  CG  LYS A  75      31.124  50.045  28.063  1.00 48.70           C  
ATOM    509  CD  LYS A  75      30.006  50.562  28.985  1.00 50.38           C  
ATOM    510  CE  LYS A  75      30.553  51.195  30.276  1.00 50.21           C  
ATOM    511  NZ  LYS A  75      29.743  50.804  31.474  1.00 51.17           N  
ATOM    512  N   LEU A  76      29.585  47.187  24.771  1.00 42.32           N  
ATOM    513  CA  LEU A  76      28.924  46.897  23.505  1.00 40.13           C  
ATOM    514  C   LEU A  76      27.465  47.327  23.581  1.00 37.83           C  
ATOM    515  O   LEU A  76      26.766  46.956  24.516  1.00 37.93           O  
ATOM    516  CB  LEU A  76      29.024  45.407  23.198  1.00 40.23           C  
ATOM    517  CG  LEU A  76      28.645  44.968  21.790  1.00 40.81           C  
ATOM    518  CD1 LEU A  76      29.560  45.569  20.745  1.00 42.17           C  
ATOM    519  CD2 LEU A  76      28.671  43.467  21.714  1.00 41.20           C  
ATOM    520  N   TYR A  77      27.014  48.098  22.593  1.00 35.28           N  
ATOM    521  CA  TYR A  77      25.631  48.591  22.525  1.00 33.28           C  
ATOM    522  C   TYR A  77      24.960  48.031  21.298  1.00 31.43           C  
ATOM    523  O   TYR A  77      25.474  48.164  20.185  1.00 32.28           O  
ATOM    524  CB  TYR A  77      25.593  50.100  22.395  1.00 32.94           C  
ATOM    525  CG  TYR A  77      26.266  50.818  23.530  1.00 36.21           C  
ATOM    526  CD1 TYR A  77      27.616  51.130  23.472  1.00 39.08           C  
ATOM    527  CD2 TYR A  77      25.565  51.166  24.658  1.00 38.57           C  
ATOM    528  CE1 TYR A  77      28.248  51.799  24.531  1.00 42.55           C  
ATOM    529  CE2 TYR A  77      26.186  51.844  25.722  1.00 39.80           C  
ATOM    530  CZ  TYR A  77      27.513  52.149  25.644  1.00 41.46           C  
ATOM    531  OH  TYR A  77      28.110  52.815  26.687  1.00 46.81           O  
ATOM    532  N   LEU A  78      23.813  47.414  21.474  1.00 28.98           N  
ATOM    533  CA  LEU A  78      23.048  46.931  20.350  1.00 28.11           C  
ATOM    534  C   LEU A  78      21.846  47.838  20.176  1.00 26.36           C  
ATOM    535  O   LEU A  78      21.182  48.157  21.140  1.00 25.84           O  
ATOM    536  CB  LEU A  78      22.598  45.513  20.630  1.00 28.43           C  
ATOM    537  CG  LEU A  78      23.692  44.474  20.904  1.00 30.26           C  
ATOM    538  CD1 LEU A  78      23.191  43.173  20.384  1.00 31.26           C  
ATOM    539  CD2 LEU A  78      25.015  44.788  20.293  1.00 30.29           C  
ATOM    540  N   VAL A  79      21.577  48.267  18.955  1.00 25.20           N  
ATOM    541  CA  VAL A  79      20.519  49.223  18.719  1.00 24.66           C  
ATOM    542  C   VAL A  79      19.482  48.407  18.016  1.00 24.67           C  
ATOM    543  O   VAL A  79      19.761  47.890  16.934  1.00 24.49           O  
ATOM    544  CB  VAL A  79      20.961  50.403  17.836  1.00 23.75           C  
ATOM    545  CG1 VAL A  79      19.819  51.383  17.652  1.00 23.70           C  
ATOM    546  CG2 VAL A  79      22.195  51.084  18.448  1.00 27.13           C  
ATOM    547  N   PHE A  80      18.298  48.304  18.628  1.00 22.87           N  
ATOM    548  CA  PHE A  80      17.200  47.519  18.100  1.00 22.23           C  
ATOM    549  C   PHE A  80      16.027  48.377  17.706  1.00 21.02           C  
ATOM    550  O   PHE A  80      15.807  49.424  18.261  1.00 21.39           O  
ATOM    551  CB  PHE A  80      16.698  46.550  19.163  1.00 22.08           C  
ATOM    552  CG  PHE A  80      17.614  45.432  19.453  1.00 23.34           C  
ATOM    553  CD1 PHE A  80      18.384  45.433  20.607  1.00 24.26           C  
ATOM    554  CD2 PHE A  80      17.682  44.345  18.588  1.00 26.57           C  
ATOM    555  CE1 PHE A  80      19.221  44.387  20.882  1.00 26.78           C  
ATOM    556  CE2 PHE A  80      18.511  43.296  18.862  1.00 29.81           C  
ATOM    557  CZ  PHE A  80      19.280  43.307  20.013  1.00 29.45           C  
ATOM    558  N   GLU A  81      15.197  47.853  16.813  1.00 20.77           N  
ATOM    559  CA  GLU A  81      13.853  48.356  16.622  1.00 21.29           C  
ATOM    560  C   GLU A  81      13.151  48.342  17.973  1.00 20.94           C  
ATOM    561  O   GLU A  81      13.325  47.398  18.724  1.00 21.94           O  
ATOM    562  CB  GLU A  81      13.153  47.390  15.627  1.00 22.10           C  
ATOM    563  CG  GLU A  81      11.651  47.485  15.525  1.00 24.62           C  
ATOM    564  CD  GLU A  81      11.060  46.359  14.654  1.00 24.87           C  
ATOM    565  OE1 GLU A  81      11.746  45.383  14.308  1.00 23.42           O  
ATOM    566  OE2 GLU A  81       9.872  46.450  14.325  1.00 29.52           O  
ATOM    567  N   PHE A  82      12.377  49.365  18.283  1.00 19.73           N  
ATOM    568  CA  PHE A  82      11.596  49.413  19.521  1.00 19.71           C  
ATOM    569  C   PHE A  82      10.184  48.933  19.276  1.00 19.58           C  
ATOM    570  O   PHE A  82       9.519  49.372  18.323  1.00 18.24           O  
ATOM    571  CB  PHE A  82      11.582  50.826  20.043  1.00 19.55           C  
ATOM    572  CG  PHE A  82      10.739  51.040  21.231  1.00 20.10           C  
ATOM    573  CD1 PHE A  82      11.251  50.793  22.503  1.00 21.04           C  
ATOM    574  CD2 PHE A  82       9.441  51.475  21.106  1.00 18.60           C  
ATOM    575  CE1 PHE A  82      10.483  51.004  23.613  1.00 21.16           C  
ATOM    576  CE2 PHE A  82       8.657  51.684  22.227  1.00 21.88           C  
ATOM    577  CZ  PHE A  82       9.173  51.442  23.475  1.00 23.01           C  
ATOM    578  N   LEU A  83       9.721  48.081  20.174  1.00 20.23           N  
ATOM    579  CA  LEU A  83       8.323  47.722  20.267  1.00 19.99           C  
ATOM    580  C   LEU A  83       7.770  48.063  21.658  1.00 19.66           C  
ATOM    581  O   LEU A  83       8.481  48.012  22.646  1.00 21.49           O  
ATOM    582  CB  LEU A  83       8.126  46.251  19.950  1.00 19.95           C  
ATOM    583  CG  LEU A  83       8.180  45.928  18.431  1.00 23.08           C  
ATOM    584  CD1 LEU A  83       9.595  45.598  18.015  1.00 24.85           C  
ATOM    585  CD2 LEU A  83       7.274  44.778  18.063  1.00 22.62           C  
ATOM    586  N   HIS A  84       6.477  48.334  21.713  1.00 19.64           N  
ATOM    587  CA  HIS A  84       5.902  48.962  22.885  1.00 19.93           C  
ATOM    588  C   HIS A  84       5.555  47.983  23.982  1.00 20.31           C  
ATOM    589  O   HIS A  84       5.365  48.384  25.115  1.00 20.41           O  
ATOM    590  CB  HIS A  84       4.683  49.762  22.485  1.00 21.06           C  
ATOM    591  CG  HIS A  84       5.002  51.084  21.864  1.00 22.33           C  
ATOM    592  ND1 HIS A  84       5.287  51.223  20.518  1.00 23.81           N  
ATOM    593  CD2 HIS A  84       5.048  52.331  22.393  1.00 21.25           C  
ATOM    594  CE1 HIS A  84       5.511  52.498  20.250  1.00 22.98           C  
ATOM    595  NE2 HIS A  84       5.381  53.190  21.370  1.00 23.87           N  
ATOM    596  N   GLN A  85       5.478  46.692  23.670  1.00 19.37           N  
ATOM    597  CA  GLN A  85       5.059  45.763  24.711  1.00 20.78           C  
ATOM    598  C   GLN A  85       5.582  44.377  24.467  1.00 20.16           C  
ATOM    599  O   GLN A  85       5.809  43.938  23.304  1.00 19.12           O  
ATOM    600  CB  GLN A  85       3.531  45.754  24.828  1.00 21.27           C  
ATOM    601  CG  GLN A  85       3.062  45.167  26.161  1.00 26.04           C  
ATOM    602  CD  GLN A  85       1.635  45.543  26.481  1.00 28.67           C  
ATOM    603  OE1 GLN A  85       0.764  44.688  26.441  1.00 31.21           O  
ATOM    604  NE2 GLN A  85       1.384  46.837  26.758  1.00 29.15           N  
ATOM    605  N   ASP A  86       5.794  43.662  25.564  1.00 20.49           N  
ATOM    606  CA  ASP A  86       6.235  42.280  25.472  1.00 20.07           C  
ATOM    607  C   ASP A  86       5.107  41.334  25.855  1.00 20.78           C  
ATOM    608  O   ASP A  86       4.067  41.765  26.421  1.00 19.95           O  
ATOM    609  CB  ASP A  86       7.527  42.033  26.250  1.00 20.63           C  
ATOM    610  CG  ASP A  86       7.361  42.067  27.767  1.00 23.19           C  
ATOM    611  OD1 ASP A  86       6.449  41.447  28.319  1.00 26.38           O  
ATOM    612  OD2 ASP A  86       8.185  42.645  28.463  1.00 25.97           O  
ATOM    613  N   LEU A  87       5.256  40.055  25.505  1.00 21.16           N  
ATOM    614  CA  LEU A  87       4.159  39.119  25.677  1.00 21.15           C  
ATOM    615  C   LEU A  87       3.918  38.828  27.159  1.00 22.82           C  
ATOM    616  O   LEU A  87       2.790  38.513  27.530  1.00 24.29           O  
ATOM    617  CB  LEU A  87       4.377  37.833  24.876  1.00 22.37           C  
ATOM    618  CG  LEU A  87       3.237  36.801  24.874  1.00 21.56           C  
ATOM    619  CD1 LEU A  87       2.054  37.310  24.030  1.00 22.28           C  
ATOM    620  CD2 LEU A  87       3.716  35.479  24.324  1.00 22.40           C  
ATOM    621  N   LYS A  88       4.958  38.889  27.964  1.00 23.66           N  
ATOM    622  CA  LYS A  88       4.808  38.656  29.390  1.00 26.14           C  
ATOM    623  C   LYS A  88       3.807  39.692  29.895  1.00 26.64           C  
ATOM    624  O   LYS A  88       2.743  39.330  30.384  1.00 26.88           O  
ATOM    625  CB  LYS A  88       6.138  38.722  30.132  1.00 26.05           C  
ATOM    626  CG  LYS A  88       6.011  38.219  31.560  1.00 28.56           C  
ATOM    627  CD  LYS A  88       6.599  39.132  32.579  1.00 34.47           C  
ATOM    628  CE  LYS A  88       6.309  38.600  34.042  1.00 35.35           C  
ATOM    629  NZ  LYS A  88       7.080  39.368  35.062  1.00 40.43           N  
ATOM    630  N   LYS A  89       4.063  40.975  29.643  1.00 27.46           N  
ATOM    631  CA  LYS A  89       3.138  42.043  30.090  1.00 28.18           C  
ATOM    632  C   LYS A  89       1.741  41.908  29.506  1.00 28.09           C  
ATOM    633  O   LYS A  89       0.764  42.101  30.211  1.00 28.72           O  
ATOM    634  CB  LYS A  89       3.723  43.443  29.784  1.00 28.74           C  
ATOM    635  CG  LYS A  89       2.722  44.607  29.972  1.00 32.59           C  
ATOM    636  CD  LYS A  89       3.373  45.898  30.428  1.00 37.19           C  
ATOM    637  CE  LYS A  89       2.382  47.060  30.427  1.00 40.42           C  
ATOM    638  NZ  LYS A  89       3.029  48.382  30.790  1.00 41.95           N  
ATOM    639  N   PHE A  90       1.636  41.511  28.242  1.00 27.46           N  
ATOM    640  CA  PHE A  90       0.355  41.363  27.580  1.00 27.72           C  
ATOM    641  C   PHE A  90      -0.451  40.184  28.140  1.00 27.95           C  
ATOM    642  O   PHE A  90      -1.672  40.262  28.241  1.00 28.17           O  
ATOM    643  CB  PHE A  90       0.541  41.191  26.080  1.00 26.83           C  
ATOM    644  CG  PHE A  90      -0.735  41.076  25.320  1.00 27.42           C  
ATOM    645  CD1 PHE A  90      -1.663  42.099  25.328  1.00 32.02           C  
ATOM    646  CD2 PHE A  90      -1.029  39.927  24.605  1.00 28.90           C  
ATOM    647  CE1 PHE A  90      -2.851  41.990  24.617  1.00 33.30           C  
ATOM    648  CE2 PHE A  90      -2.195  39.808  23.902  1.00 30.06           C  
ATOM    649  CZ  PHE A  90      -3.121  40.845  23.887  1.00 31.37           C  
ATOM    650  N   MET A  91       0.247  39.107  28.487  1.00 29.28           N  
ATOM    651  CA  MET A  91      -0.370  37.970  29.182  1.00 29.68           C  
ATOM    652  C   MET A  91      -0.833  38.315  30.596  1.00 30.99           C  
ATOM    653  O   MET A  91      -1.929  37.915  31.017  1.00 30.41           O  
ATOM    654  CB  MET A  91       0.609  36.815  29.245  1.00 29.79           C  
ATOM    655  CG  MET A  91       0.621  36.032  27.905  1.00 29.99           C  
ATOM    656  SD  MET A  91       1.162  34.399  28.186  1.00 33.08           S  
ATOM    657  CE  MET A  91       2.750  34.805  28.590  1.00 20.61           C  
ATOM    658  N   ASP A  92       0.005  39.040  31.318  1.00 32.68           N  
ATOM    659  CA  ASP A  92      -0.331  39.492  32.673  1.00 33.90           C  
ATOM    660  C   ASP A  92      -1.600  40.370  32.649  1.00 34.75           C  
ATOM    661  O   ASP A  92      -2.490  40.175  33.473  1.00 34.99           O  
ATOM    662  CB  ASP A  92       0.828  40.262  33.318  1.00 33.95           C  
ATOM    663  CG  ASP A  92       1.974  39.374  33.773  1.00 36.76           C  
ATOM    664  OD1 ASP A  92       1.818  38.140  33.960  1.00 39.06           O  
ATOM    665  OD2 ASP A  92       3.109  39.848  33.976  1.00 40.77           O  
ATOM    666  N   ALA A  93      -1.666  41.319  31.711  1.00 36.13           N  
ATOM    667  CA  ALA A  93      -2.834  42.192  31.458  1.00 37.15           C  
ATOM    668  C   ALA A  93      -4.095  41.530  30.862  1.00 37.84           C  
ATOM    669  O   ALA A  93      -5.180  42.112  30.925  1.00 38.26           O  
ATOM    670  CB  ALA A  93      -2.431  43.345  30.544  1.00 37.85           C  
ATOM    671  N   SER A  94      -3.948  40.364  30.242  1.00 37.74           N  
ATOM    672  CA  SER A  94      -5.056  39.647  29.619  1.00 37.78           C  
ATOM    673  C   SER A  94      -5.520  38.472  30.495  1.00 38.23           C  
ATOM    674  O   SER A  94      -6.268  37.623  30.031  1.00 38.59           O  
ATOM    675  CB  SER A  94      -4.610  39.082  28.263  1.00 37.63           C  
ATOM    676  OG  SER A  94      -4.256  40.106  27.335  1.00 37.89           O  
ATOM    677  N   ALA A  95      -5.048  38.392  31.731  1.00 38.77           N  
ATOM    678  CA  ALA A  95      -5.145  37.138  32.495  1.00 39.58           C  
ATOM    679  C   ALA A  95      -6.544  36.837  33.061  1.00 39.88           C  
ATOM    680  O   ALA A  95      -6.852  35.688  33.363  1.00 39.58           O  
ATOM    681  CB  ALA A  95      -4.120  37.120  33.602  1.00 39.65           C  
ATOM    682  N   LEU A  96      -7.377  37.863  33.222  1.00 40.71           N  
ATOM    683  CA  LEU A  96      -8.722  37.664  33.764  1.00 40.42           C  
ATOM    684  C   LEU A  96      -9.616  37.136  32.666  1.00 39.57           C  
ATOM    685  O   LEU A  96     -10.562  36.369  32.909  1.00 38.53           O  
ATOM    686  CB  LEU A  96      -9.274  38.976  34.349  1.00 40.87           C  
ATOM    687  CG  LEU A  96      -8.533  39.537  35.581  1.00 41.92           C  
ATOM    688  CD1 LEU A  96      -9.441  40.484  36.367  1.00 42.69           C  
ATOM    689  CD2 LEU A  96      -7.952  38.438  36.512  1.00 42.03           C  
ATOM    690  N   THR A  97      -9.276  37.514  31.445  1.00 38.36           N  
ATOM    691  CA  THR A  97     -10.067  37.215  30.270  1.00 38.23           C  
ATOM    692  C   THR A  97      -9.461  36.103  29.378  1.00 36.94           C  
ATOM    693  O   THR A  97     -10.181  35.322  28.754  1.00 38.05           O  
ATOM    694  CB  THR A  97     -10.222  38.514  29.426  1.00 39.01           C  
ATOM    695  OG1 THR A  97     -10.610  38.182  28.088  1.00 42.31           O  
ATOM    696  CG2 THR A  97      -8.864  39.268  29.244  1.00 38.31           C  
ATOM    697  N   GLY A  98      -8.140  36.039  29.348  1.00 34.91           N  
ATOM    698  CA  GLY A  98      -7.408  35.166  28.452  1.00 34.05           C  
ATOM    699  C   GLY A  98      -7.262  35.818  27.084  1.00 32.83           C  
ATOM    700  O   GLY A  98      -8.175  36.491  26.572  1.00 32.93           O  
ATOM    701  N   ILE A  99      -6.114  35.614  26.481  1.00 29.68           N  
ATOM    702  CA  ILE A  99      -5.926  36.007  25.099  1.00 28.54           C  
ATOM    703  C   ILE A  99      -6.872  35.229  24.209  1.00 27.20           C  
ATOM    704  O   ILE A  99      -6.883  34.002  24.255  1.00 25.72           O  
ATOM    705  CB  ILE A  99      -4.489  35.732  24.662  1.00 28.23           C  
ATOM    706  CG1 ILE A  99      -3.542  36.534  25.548  1.00 28.97           C  
ATOM    707  CG2 ILE A  99      -4.305  36.094  23.164  1.00 26.54           C  
ATOM    708  CD1 ILE A  99      -2.087  36.490  25.077  1.00 32.30           C  
ATOM    709  N   PRO A 100      -7.638  35.910  23.358  1.00 26.21           N  
ATOM    710  CA  PRO A 100      -8.578  35.200  22.486  1.00 25.87           C  
ATOM    711  C   PRO A 100      -7.862  34.152  21.635  1.00 25.82           C  
ATOM    712  O   PRO A 100      -6.774  34.454  21.154  1.00 25.56           O  
ATOM    713  CB  PRO A 100      -9.199  36.303  21.612  1.00 26.30           C  
ATOM    714  CG  PRO A 100      -8.849  37.616  22.283  1.00 27.41           C  
ATOM    715  CD  PRO A 100      -7.658  37.374  23.161  1.00 26.79           C  
ATOM    716  N   LEU A 101      -8.472  33.001  21.384  1.00 25.27           N  
ATOM    717  CA  LEU A 101      -7.763  31.931  20.675  1.00 25.84           C  
ATOM    718  C   LEU A 101      -7.263  32.357  19.257  1.00 24.91           C  
ATOM    719  O   LEU A 101      -6.172  31.964  18.849  1.00 23.42           O  
ATOM    720  CB  LEU A 101      -8.595  30.640  20.618  1.00 25.69           C  
ATOM    721  CG  LEU A 101      -8.009  29.516  19.737  1.00 30.41           C  
ATOM    722  CD1 LEU A 101      -6.840  28.807  20.485  1.00 31.67           C  
ATOM    723  CD2 LEU A 101      -9.062  28.515  19.318  1.00 34.30           C  
ATOM    724  N   PRO A 102      -8.030  33.128  18.481  1.00 23.62           N  
ATOM    725  CA  PRO A 102      -7.522  33.490  17.147  1.00 22.81           C  
ATOM    726  C   PRO A 102      -6.222  34.315  17.233  1.00 21.31           C  
ATOM    727  O   PRO A 102      -5.345  34.135  16.385  1.00 21.13           O  
ATOM    728  CB  PRO A 102      -8.675  34.286  16.512  1.00 23.41           C  
ATOM    729  CG  PRO A 102      -9.897  33.954  17.379  1.00 24.38           C  
ATOM    730  CD  PRO A 102      -9.396  33.635  18.725  1.00 24.48           C  
ATOM    731  N   LEU A 103      -6.082  35.163  18.245  1.00 19.56           N  
ATOM    732  CA  LEU A 103      -4.838  35.900  18.470  1.00 20.82           C  
ATOM    733  C   LEU A 103      -3.687  34.983  18.930  1.00 20.15           C  
ATOM    734  O   LEU A 103      -2.573  35.148  18.499  1.00 19.92           O  
ATOM    735  CB  LEU A 103      -5.063  37.032  19.458  1.00 19.67           C  
ATOM    736  CG  LEU A 103      -3.964  38.042  19.684  1.00 21.59           C  
ATOM    737  CD1 LEU A 103      -3.464  38.636  18.398  1.00 24.80           C  
ATOM    738  CD2 LEU A 103      -4.385  39.117  20.679  1.00 22.75           C  
ATOM    739  N   ILE A 104      -3.962  34.060  19.839  1.00 19.57           N  
ATOM    740  CA  ILE A 104      -2.965  33.051  20.227  1.00 19.19           C  
ATOM    741  C   ILE A 104      -2.479  32.342  18.975  1.00 18.30           C  
ATOM    742  O   ILE A 104      -1.299  32.200  18.756  1.00 18.44           O  
ATOM    743  CB  ILE A 104      -3.577  32.026  21.193  1.00 19.70           C  
ATOM    744  CG1 ILE A 104      -3.946  32.706  22.512  1.00 20.42           C  
ATOM    745  CG2 ILE A 104      -2.590  30.878  21.429  1.00 19.82           C  
ATOM    746  CD1 ILE A 104      -4.533  31.792  23.552  1.00 23.01           C  
ATOM    747  N   LYS A 105      -3.416  31.920  18.142  1.00 18.64           N  
ATOM    748  CA  LYS A 105      -3.077  31.173  16.948  1.00 18.02           C  
ATOM    749  C   LYS A 105      -2.244  32.031  15.981  1.00 18.38           C  
ATOM    750  O   LYS A 105      -1.291  31.552  15.382  1.00 16.75           O  
ATOM    751  CB  LYS A 105      -4.347  30.658  16.275  1.00 19.12           C  
ATOM    752  CG  LYS A 105      -4.139  29.836  14.975  1.00 19.08           C  
ATOM    753  CD  LYS A 105      -5.451  29.258  14.459  1.00 21.78           C  
ATOM    754  CE  LYS A 105      -6.108  28.265  15.440  1.00 22.84           C  
ATOM    755  NZ  LYS A 105      -7.377  27.602  14.901  1.00 24.35           N  
ATOM    756  N   SER A 106      -2.640  33.293  15.827  1.00 19.13           N  
ATOM    757  CA  SER A 106      -1.902  34.233  14.993  1.00 19.56           C  
ATOM    758  C   SER A 106      -0.476  34.446  15.505  1.00 19.03           C  
ATOM    759  O   SER A 106       0.469  34.375  14.746  1.00 18.77           O  
ATOM    760  CB  SER A 106      -2.609  35.570  14.928  1.00 20.74           C  
ATOM    761  OG  SER A 106      -1.804  36.501  14.209  1.00 19.93           O  
ATOM    762  N   TYR A 107      -0.331  34.628  16.807  1.00 17.59           N  
ATOM    763  CA  TYR A 107       0.988  34.804  17.409  1.00 16.99           C  
ATOM    764  C   TYR A 107       1.862  33.564  17.234  1.00 17.02           C  
ATOM    765  O   TYR A 107       3.032  33.664  16.880  1.00 15.40           O  
ATOM    766  CB  TYR A 107       0.810  35.161  18.890  1.00 17.39           C  
ATOM    767  CG  TYR A 107       0.453  36.621  19.196  1.00 18.81           C  
ATOM    768  CD1 TYR A 107       0.430  37.611  18.201  1.00 19.40           C  
ATOM    769  CD2 TYR A 107       0.140  37.005  20.499  1.00 19.59           C  
ATOM    770  CE1 TYR A 107       0.097  38.921  18.510  1.00 19.54           C  
ATOM    771  CE2 TYR A 107      -0.166  38.296  20.806  1.00 20.87           C  
ATOM    772  CZ  TYR A 107      -0.152  39.272  19.827  1.00 19.22           C  
ATOM    773  OH  TYR A 107      -0.494  40.554  20.200  1.00 20.33           O  
ATOM    774  N   LEU A 108       1.263  32.396  17.445  1.00 17.00           N  
ATOM    775  CA  LEU A 108       1.989  31.147  17.307  1.00 18.19           C  
ATOM    776  C   LEU A 108       2.506  30.949  15.874  1.00 17.72           C  
ATOM    777  O   LEU A 108       3.647  30.600  15.658  1.00 17.02           O  
ATOM    778  CB  LEU A 108       1.151  29.960  17.743  1.00 18.18           C  
ATOM    779  CG  LEU A 108       1.881  28.627  17.710  1.00 18.11           C  
ATOM    780  CD1 LEU A 108       3.069  28.615  18.686  1.00 19.51           C  
ATOM    781  CD2 LEU A 108       0.880  27.509  17.960  1.00 19.71           C  
ATOM    782  N   PHE A 109       1.628  31.171  14.918  1.00 18.26           N  
ATOM    783  CA  PHE A 109       1.953  31.064  13.502  1.00 17.77           C  
ATOM    784  C   PHE A 109       3.076  32.002  13.100  1.00 18.19           C  
ATOM    785  O   PHE A 109       4.015  31.612  12.393  1.00 18.03           O  
ATOM    786  CB  PHE A 109       0.697  31.435  12.712  1.00 18.61           C  
ATOM    787  CG  PHE A 109       0.806  31.126  11.240  1.00 20.24           C  
ATOM    788  CD1 PHE A 109       0.775  29.832  10.816  1.00 22.11           C  
ATOM    789  CD2 PHE A 109       0.923  32.139  10.300  1.00 26.95           C  
ATOM    790  CE1 PHE A 109       0.865  29.508   9.456  1.00 23.72           C  
ATOM    791  CE2 PHE A 109       1.020  31.809   8.920  1.00 23.83           C  
ATOM    792  CZ  PHE A 109       0.974  30.504   8.532  1.00 24.98           C  
ATOM    793  N   GLN A 110       2.990  33.262  13.531  1.00 18.53           N  
ATOM    794  CA  GLN A 110       4.019  34.254  13.191  1.00 18.16           C  
ATOM    795  C   GLN A 110       5.371  33.868  13.772  1.00 18.69           C  
ATOM    796  O   GLN A 110       6.407  34.022  13.153  1.00 17.40           O  
ATOM    797  CB  GLN A 110       3.645  35.645  13.681  1.00 17.68           C  
ATOM    798  CG  GLN A 110       2.496  36.307  12.938  1.00 18.94           C  
ATOM    799  CD  GLN A 110       2.115  37.607  13.531  1.00 16.49           C  
ATOM    800  OE1 GLN A 110       2.926  38.535  13.501  1.00 17.07           O  
ATOM    801  NE2 GLN A 110       0.852  37.738  14.051  1.00 16.08           N  
ATOM    802  N   LEU A 111       5.350  33.371  15.019  1.00 17.94           N  
ATOM    803  CA  LEU A 111       6.596  32.994  15.661  1.00 18.06           C  
ATOM    804  C   LEU A 111       7.218  31.777  15.014  1.00 16.76           C  
ATOM    805  O   LEU A 111       8.445  31.693  14.896  1.00 17.45           O  
ATOM    806  CB  LEU A 111       6.343  32.771  17.123  1.00 18.56           C  
ATOM    807  CG  LEU A 111       6.018  34.091  17.794  1.00 21.62           C  
ATOM    808  CD1 LEU A 111       5.673  33.811  19.264  1.00 22.55           C  
ATOM    809  CD2 LEU A 111       7.140  35.087  17.678  1.00 24.88           C  
ATOM    810  N   LEU A 112       6.371  30.859  14.599  1.00 16.36           N  
ATOM    811  CA  LEU A 112       6.788  29.723  13.820  1.00 16.94           C  
ATOM    812  C   LEU A 112       7.381  30.200  12.491  1.00 16.40           C  
ATOM    813  O   LEU A 112       8.370  29.629  12.042  1.00 16.64           O  
ATOM    814  CB  LEU A 112       5.682  28.725  13.569  1.00 17.53           C  
ATOM    815  CG  LEU A 112       5.286  27.894  14.815  1.00 16.96           C  
ATOM    816  CD1 LEU A 112       3.949  27.201  14.663  1.00 18.02           C  
ATOM    817  CD2 LEU A 112       6.405  26.922  15.203  1.00 18.61           C  
ATOM    818  N   GLN A 113       6.827  31.235  11.895  1.00 18.36           N  
ATOM    819  CA  GLN A 113       7.465  31.762  10.643  1.00 18.24           C  
ATOM    820  C   GLN A 113       8.851  32.311  10.910  1.00 19.01           C  
ATOM    821  O   GLN A 113       9.794  32.046  10.169  1.00 18.14           O  
ATOM    822  CB  GLN A 113       6.579  32.826   9.998  1.00 19.39           C  
ATOM    823  CG  GLN A 113       5.256  32.314   9.443  1.00 22.67           C  
ATOM    824  CD  GLN A 113       4.443  33.402   8.719  1.00 28.72           C  
ATOM    825  OE1 GLN A 113       4.329  33.398   7.478  1.00 34.22           O  
ATOM    826  NE2 GLN A 113       3.871  34.304   9.480  1.00 27.33           N  
ATOM    827  N   GLY A 114       8.980  33.134  11.955  1.00 17.98           N  
ATOM    828  CA  GLY A 114      10.248  33.639  12.368  1.00 17.93           C  
ATOM    829  C   GLY A 114      11.254  32.550  12.667  1.00 18.41           C  
ATOM    830  O   GLY A 114      12.422  32.603  12.238  1.00 17.03           O  
ATOM    831  N   LEU A 115      10.804  31.529  13.418  1.00 18.15           N  
ATOM    832  CA  LEU A 115      11.659  30.409  13.708  1.00 19.60           C  
ATOM    833  C   LEU A 115      12.055  29.610  12.453  1.00 19.63           C  
ATOM    834  O   LEU A 115      13.204  29.240  12.317  1.00 19.54           O  
ATOM    835  CB  LEU A 115      10.987  29.492  14.710  1.00 19.73           C  
ATOM    836  CG  LEU A 115      11.503  29.468  16.138  1.00 23.49           C  
ATOM    837  CD1 LEU A 115      12.341  30.615  16.684  1.00 24.72           C  
ATOM    838  CD2 LEU A 115      10.365  29.060  17.066  1.00 22.76           C  
ATOM    839  N   ALA A 116      11.109  29.329  11.575  1.00 19.62           N  
ATOM    840  CA  ALA A 116      11.418  28.637  10.311  1.00 21.07           C  
ATOM    841  C   ALA A 116      12.525  29.379   9.547  1.00 21.33           C  
ATOM    842  O   ALA A 116      13.412  28.754   9.003  1.00 22.76           O  
ATOM    843  CB  ALA A 116      10.184  28.502   9.462  1.00 21.48           C  
ATOM    844  N   PHE A 117      12.469  30.695   9.542  1.00 22.83           N  
ATOM    845  CA  PHE A 117      13.477  31.535   8.882  1.00 23.02           C  
ATOM    846  C   PHE A 117      14.832  31.363   9.558  1.00 23.47           C  
ATOM    847  O   PHE A 117      15.795  30.951   8.918  1.00 22.82           O  
ATOM    848  CB  PHE A 117      13.029  32.998   8.858  1.00 22.63           C  
ATOM    849  CG  PHE A 117      14.057  33.942   8.337  1.00 22.66           C  
ATOM    850  CD1 PHE A 117      14.192  34.153   6.962  1.00 26.87           C  
ATOM    851  CD2 PHE A 117      14.907  34.602   9.192  1.00 21.54           C  
ATOM    852  CE1 PHE A 117      15.155  35.020   6.473  1.00 25.39           C  
ATOM    853  CE2 PHE A 117      15.832  35.474   8.708  1.00 26.29           C  
ATOM    854  CZ  PHE A 117      15.971  35.680   7.341  1.00 25.76           C  
ATOM    855  N   CYS A 118      14.916  31.623  10.855  1.00 24.16           N  
ATOM    856  CA  CYS A 118      16.220  31.611  11.524  1.00 25.03           C  
ATOM    857  C   CYS A 118      16.791  30.211  11.467  1.00 22.98           C  
ATOM    858  O   CYS A 118      17.957  30.039  11.175  1.00 23.33           O  
ATOM    859  CB  CYS A 118      16.151  32.061  12.996  1.00 26.61           C  
ATOM    860  SG  CYS A 118      15.393  33.623  13.285  1.00 40.17           S  
ATOM    861  N   HIS A 119      15.966  29.217  11.745  1.00 21.92           N  
ATOM    862  CA  HIS A 119      16.387  27.842  11.690  1.00 20.87           C  
ATOM    863  C   HIS A 119      16.898  27.436  10.271  1.00 22.95           C  
ATOM    864  O   HIS A 119      17.840  26.677  10.169  1.00 22.56           O  
ATOM    865  CB  HIS A 119      15.276  26.905  12.151  1.00 21.22           C  
ATOM    866  CG  HIS A 119      14.961  27.036  13.609  1.00 17.19           C  
ATOM    867  ND1 HIS A 119      13.842  26.478  14.186  1.00 19.78           N  
ATOM    868  CD2 HIS A 119      15.646  27.644  14.613  1.00 19.30           C  
ATOM    869  CE1 HIS A 119      13.845  26.755  15.488  1.00 19.46           C  
ATOM    870  NE2 HIS A 119      14.942  27.440  15.772  1.00 15.17           N  
ATOM    871  N   SER A 120      16.271  27.939   9.211  1.00 23.91           N  
ATOM    872  CA  SER A 120      16.766  27.689   7.833  1.00 24.90           C  
ATOM    873  C   SER A 120      18.197  28.221   7.642  1.00 26.44           C  
ATOM    874  O   SER A 120      18.951  27.672   6.827  1.00 27.74           O  
ATOM    875  CB  SER A 120      15.809  28.265   6.775  1.00 24.43           C  
ATOM    876  OG  SER A 120      15.954  29.660   6.606  1.00 24.41           O  
ATOM    877  N   HIS A 121      18.560  29.278   8.386  1.00 26.41           N  
ATOM    878  CA  HIS A 121      19.896  29.862   8.413  1.00 28.09           C  
ATOM    879  C   HIS A 121      20.812  29.319   9.516  1.00 28.43           C  
ATOM    880  O   HIS A 121      21.882  29.873   9.766  1.00 28.68           O  
ATOM    881  CB  HIS A 121      19.815  31.392   8.474  1.00 28.72           C  
ATOM    882  CG  HIS A 121      19.152  31.988   7.279  1.00 31.62           C  
ATOM    883  ND1 HIS A 121      19.685  31.889   6.009  1.00 37.00           N  
ATOM    884  CD2 HIS A 121      17.979  32.644   7.142  1.00 34.65           C  
ATOM    885  CE1 HIS A 121      18.881  32.491   5.152  1.00 37.63           C  
ATOM    886  NE2 HIS A 121      17.830  32.944   5.810  1.00 35.45           N  
ATOM    887  N   ARG A 122      20.394  28.210  10.114  1.00 28.38           N  
ATOM    888  CA  ARG A 122      21.116  27.522  11.173  1.00 29.66           C  
ATOM    889  C   ARG A 122      21.355  28.430  12.385  1.00 28.54           C  
ATOM    890  O   ARG A 122      22.371  28.330  13.073  1.00 29.34           O  
ATOM    891  CB  ARG A 122      22.437  26.934  10.643  1.00 30.83           C  
ATOM    892  CG  ARG A 122      22.239  25.881   9.564  1.00 35.42           C  
ATOM    893  CD  ARG A 122      21.463  24.622  10.013  1.00 41.06           C  
ATOM    894  NE  ARG A 122      20.437  24.284   9.016  1.00 45.15           N  
ATOM    895  CZ  ARG A 122      19.163  23.962   9.281  1.00 47.47           C  
ATOM    896  NH1 ARG A 122      18.704  23.899  10.538  1.00 46.00           N  
ATOM    897  NH2 ARG A 122      18.339  23.701   8.266  1.00 47.21           N  
ATOM    898  N   VAL A 123      20.410  29.315  12.663  1.00 26.54           N  
ATOM    899  CA  VAL A 123      20.539  30.206  13.819  1.00 25.62           C  
ATOM    900  C   VAL A 123      19.468  29.800  14.821  1.00 24.80           C  
ATOM    901  O   VAL A 123      18.326  29.708  14.442  1.00 22.93           O  
ATOM    902  CB  VAL A 123      20.379  31.687  13.406  1.00 25.12           C  
ATOM    903  CG1 VAL A 123      20.227  32.630  14.611  1.00 26.63           C  
ATOM    904  CG2 VAL A 123      21.597  32.132  12.550  1.00 26.89           C  
ATOM    905  N   LEU A 124      19.865  29.605  16.083  1.00 23.98           N  
ATOM    906  CA  LEU A 124      18.961  29.230  17.161  1.00 24.46           C  
ATOM    907  C   LEU A 124      18.754  30.423  18.068  1.00 23.49           C  
ATOM    908  O   LEU A 124      19.657  31.232  18.243  1.00 22.34           O  
ATOM    909  CB  LEU A 124      19.591  28.160  18.051  1.00 25.41           C  
ATOM    910  CG  LEU A 124      19.879  26.779  17.544  1.00 27.96           C  
ATOM    911  CD1 LEU A 124      20.232  25.816  18.689  1.00 28.07           C  
ATOM    912  CD2 LEU A 124      18.719  26.345  16.829  1.00 33.15           C  
ATOM    913  N   HIS A 125      17.568  30.548  18.645  1.00 22.80           N  
ATOM    914  CA  HIS A 125      17.383  31.540  19.684  1.00 22.48           C  
ATOM    915  C   HIS A 125      18.019  31.090  21.019  1.00 23.44           C  
ATOM    916  O   HIS A 125      18.871  31.795  21.595  1.00 22.98           O  
ATOM    917  CB  HIS A 125      15.917  31.896  19.834  1.00 21.55           C  
ATOM    918  CG  HIS A 125      15.699  33.030  20.772  1.00 22.29           C  
ATOM    919  ND1 HIS A 125      15.295  34.278  20.364  1.00 26.69           N  
ATOM    920  CD2 HIS A 125      15.896  33.115  22.105  1.00 20.24           C  
ATOM    921  CE1 HIS A 125      15.235  35.076  21.410  1.00 20.42           C  
ATOM    922  NE2 HIS A 125      15.612  34.399  22.477  1.00 25.93           N  
ATOM    923  N   ARG A 126      17.627  29.907  21.479  1.00 23.56           N  
ATOM    924  CA  ARG A 126      18.147  29.273  22.704  1.00 24.94           C  
ATOM    925  C   ARG A 126      17.514  29.712  24.022  1.00 24.43           C  
ATOM    926  O   ARG A 126      17.560  28.971  25.006  1.00 24.93           O  
ATOM    927  CB  ARG A 126      19.669  29.402  22.839  1.00 26.53           C  
ATOM    928  CG  ARG A 126      20.462  28.740  21.745  1.00 29.86           C  
ATOM    929  CD  ARG A 126      21.968  29.075  21.832  1.00 36.28           C  
ATOM    930  NE  ARG A 126      22.631  28.972  20.514  1.00 41.66           N  
ATOM    931  CZ  ARG A 126      23.219  27.878  20.029  1.00 44.49           C  
ATOM    932  NH1 ARG A 126      23.259  26.757  20.733  1.00 47.47           N  
ATOM    933  NH2 ARG A 126      23.782  27.898  18.826  1.00 45.43           N  
ATOM    934  N   ASP A 127      16.912  30.886  24.051  1.00 23.31           N  
ATOM    935  CA  ASP A 127      16.259  31.371  25.279  1.00 24.00           C  
ATOM    936  C   ASP A 127      14.925  32.083  25.009  1.00 22.31           C  
ATOM    937  O   ASP A 127      14.669  33.200  25.487  1.00 22.74           O  
ATOM    938  CB  ASP A 127      17.219  32.269  26.041  1.00 23.48           C  
ATOM    939  CG  ASP A 127      16.779  32.531  27.456  1.00 26.60           C  
ATOM    940  OD1 ASP A 127      15.986  31.734  28.030  1.00 24.25           O  
ATOM    941  OD2 ASP A 127      17.185  33.533  28.055  1.00 27.96           O  
ATOM    942  N   LEU A 128      14.046  31.426  24.277  1.00 21.89           N  
ATOM    943  CA  LEU A 128      12.726  31.987  24.057  1.00 21.59           C  
ATOM    944  C   LEU A 128      11.929  31.998  25.357  1.00 21.51           C  
ATOM    945  O   LEU A 128      11.923  31.008  26.111  1.00 21.60           O  
ATOM    946  CB  LEU A 128      11.950  31.221  22.986  1.00 22.42           C  
ATOM    947  CG  LEU A 128      12.442  31.404  21.562  1.00 24.31           C  
ATOM    948  CD1 LEU A 128      11.574  30.597  20.648  1.00 26.27           C  
ATOM    949  CD2 LEU A 128      12.376  32.870  21.240  1.00 26.48           C  
ATOM    950  N   LYS A 129      11.243  33.111  25.579  1.00 20.32           N  
ATOM    951  CA  LYS A 129      10.403  33.305  26.767  1.00 19.95           C  
ATOM    952  C   LYS A 129       9.487  34.481  26.496  1.00 20.28           C  
ATOM    953  O   LYS A 129       9.808  35.336  25.628  1.00 20.26           O  
ATOM    954  CB  LYS A 129      11.257  33.492  28.021  1.00 20.21           C  
ATOM    955  CG  LYS A 129      12.200  34.601  28.003  1.00 23.27           C  
ATOM    956  CD  LYS A 129      13.142  34.543  29.229  1.00 28.23           C  
ATOM    957  CE  LYS A 129      14.364  35.404  29.028  1.00 31.53           C  
ATOM    958  NZ  LYS A 129      15.401  35.285  30.123  1.00 32.54           N  
ATOM    959  N   PRO A 130       8.343  34.547  27.178  1.00 19.84           N  
ATOM    960  CA  PRO A 130       7.372  35.612  26.902  1.00 20.45           C  
ATOM    961  C   PRO A 130       8.004  37.005  26.866  1.00 20.36           C  
ATOM    962  O   PRO A 130       7.621  37.837  26.046  1.00 20.20           O  
ATOM    963  CB  PRO A 130       6.374  35.461  28.062  1.00 20.46           C  
ATOM    964  CG  PRO A 130       6.339  33.936  28.260  1.00 21.28           C  
ATOM    965  CD  PRO A 130       7.826  33.592  28.187  1.00 20.90           C  
ATOM    966  N   GLN A 131       8.977  37.220  27.732  1.00 21.40           N  
ATOM    967  CA  GLN A 131       9.657  38.516  27.838  1.00 23.84           C  
ATOM    968  C   GLN A 131      10.445  38.890  26.584  1.00 22.52           C  
ATOM    969  O   GLN A 131      10.702  40.065  26.361  1.00 23.26           O  
ATOM    970  CB  GLN A 131      10.593  38.492  29.042  1.00 25.13           C  
ATOM    971  CG  GLN A 131       9.845  38.386  30.397  1.00 30.54           C  
ATOM    972  CD  GLN A 131       9.618  36.937  30.982  1.00 36.73           C  
ATOM    973  OE1 GLN A 131       9.447  36.825  32.200  1.00 44.12           O  
ATOM    974  NE2 GLN A 131       9.555  35.885  30.149  1.00 28.08           N  
ATOM    975  N   ASN A 132      10.899  37.911  25.820  1.00 22.78           N  
ATOM    976  CA  ASN A 132      11.588  38.192  24.551  1.00 22.59           C  
ATOM    977  C   ASN A 132      10.731  38.076  23.301  1.00 21.58           C  
ATOM    978  O   ASN A 132      11.254  37.896  22.183  1.00 21.00           O  
ATOM    979  CB  ASN A 132      12.703  37.208  24.361  1.00 24.63           C  
ATOM    980  CG  ASN A 132      13.830  37.476  25.233  1.00 26.75           C  
ATOM    981  OD1 ASN A 132      14.052  38.597  25.696  1.00 32.10           O  
ATOM    982  ND2 ASN A 132      14.550  36.399  25.535  1.00 29.40           N  
ATOM    983  N   LEU A 133       9.428  38.152  23.481  1.00 20.20           N  
ATOM    984  CA  LEU A 133       8.487  38.158  22.365  1.00 18.68           C  
ATOM    985  C   LEU A 133       7.789  39.523  22.469  1.00 18.73           C  
ATOM    986  O   LEU A 133       7.161  39.839  23.475  1.00 19.59           O  
ATOM    987  CB  LEU A 133       7.498  37.014  22.469  1.00 18.04           C  
ATOM    988  CG  LEU A 133       8.108  35.625  22.391  1.00 16.81           C  
ATOM    989  CD1 LEU A 133       7.043  34.587  22.589  1.00 18.09           C  
ATOM    990  CD2 LEU A 133       8.878  35.427  21.075  1.00 17.88           C  
ATOM    991  N   LEU A 134       7.944  40.342  21.448  1.00 17.14           N  
ATOM    992  CA  LEU A 134       7.499  41.705  21.468  1.00 18.24           C  
ATOM    993  C   LEU A 134       6.375  41.901  20.474  1.00 17.30           C  
ATOM    994  O   LEU A 134       6.382  41.306  19.378  1.00 17.96           O  
ATOM    995  CB  LEU A 134       8.667  42.621  21.110  1.00 19.31           C  
ATOM    996  CG  LEU A 134       9.911  42.598  21.992  1.00 21.47           C  
ATOM    997  CD1 LEU A 134      10.793  43.728  21.509  1.00 21.83           C  
ATOM    998  CD2 LEU A 134       9.575  42.763  23.471  1.00 21.99           C  
ATOM    999  N   ILE A 135       5.385  42.700  20.870  1.00 18.16           N  
ATOM   1000  CA  ILE A 135       4.175  42.886  20.083  1.00 19.63           C  
ATOM   1001  C   ILE A 135       3.946  44.382  19.754  1.00 20.26           C  
ATOM   1002  O   ILE A 135       4.436  45.274  20.447  1.00 20.97           O  
ATOM   1003  CB  ILE A 135       2.940  42.315  20.793  1.00 20.39           C  
ATOM   1004  CG1 ILE A 135       2.705  42.972  22.174  1.00 20.96           C  
ATOM   1005  CG2 ILE A 135       3.045  40.772  20.938  1.00 20.96           C  
ATOM   1006  CD1 ILE A 135       1.350  42.486  22.912  1.00 23.43           C  
ATOM   1007  N   ASN A 136       3.161  44.617  18.713  1.00 22.28           N  
ATOM   1008  CA  ASN A 136       2.788  45.971  18.324  1.00 23.00           C  
ATOM   1009  C   ASN A 136       1.315  46.058  18.094  1.00 24.94           C  
ATOM   1010  O   ASN A 136       0.602  45.071  18.156  1.00 25.56           O  
ATOM   1011  CB  ASN A 136       3.592  46.443  17.099  1.00 22.10           C  
ATOM   1012  CG  ASN A 136       3.270  45.688  15.840  1.00 20.89           C  
ATOM   1013  OD1 ASN A 136       2.215  45.103  15.713  1.00 20.34           O  
ATOM   1014  ND2 ASN A 136       4.217  45.676  14.903  1.00 19.43           N  
ATOM   1015  N   THR A 137       0.846  47.276  17.835  1.00 26.58           N  
ATOM   1016  CA  THR A 137      -0.580  47.528  17.703  1.00 27.43           C  
ATOM   1017  C   THR A 137      -1.173  46.885  16.461  1.00 28.16           C  
ATOM   1018  O   THR A 137      -2.404  46.765  16.345  1.00 29.07           O  
ATOM   1019  CB  THR A 137      -0.818  49.042  17.621  1.00 27.56           C  
ATOM   1020  OG1 THR A 137      -0.011  49.567  16.563  1.00 27.39           O  
ATOM   1021  CG2 THR A 137      -0.334  49.737  18.812  1.00 27.32           C  
ATOM   1022  N   GLU A 138      -0.327  46.496  15.512  1.00 28.71           N  
ATOM   1023  CA  GLU A 138      -0.784  45.958  14.241  1.00 29.38           C  
ATOM   1024  C   GLU A 138      -1.067  44.454  14.254  1.00 28.68           C  
ATOM   1025  O   GLU A 138      -1.355  43.872  13.207  1.00 30.13           O  
ATOM   1026  CB  GLU A 138       0.275  46.222  13.168  1.00 30.86           C  
ATOM   1027  CG  GLU A 138       0.583  47.683  12.908  1.00 35.58           C  
ATOM   1028  CD  GLU A 138      -0.630  48.510  12.502  1.00 41.75           C  
ATOM   1029  OE1 GLU A 138      -1.726  47.966  12.197  1.00 46.66           O  
ATOM   1030  OE2 GLU A 138      -0.487  49.742  12.474  1.00 47.61           O  
ATOM   1031  N   GLY A 139      -0.956  43.841  15.417  1.00 25.51           N  
ATOM   1032  CA  GLY A 139      -1.058  42.419  15.568  1.00 24.75           C  
ATOM   1033  C   GLY A 139       0.149  41.592  15.229  1.00 23.37           C  
ATOM   1034  O   GLY A 139       0.006  40.395  15.075  1.00 22.57           O  
ATOM   1035  N   ALA A 140       1.319  42.216  15.095  1.00 23.31           N  
ATOM   1036  CA  ALA A 140       2.559  41.501  14.839  1.00 22.02           C  
ATOM   1037  C   ALA A 140       3.159  41.046  16.170  1.00 21.29           C  
ATOM   1038  O   ALA A 140       2.916  41.663  17.215  1.00 19.64           O  
ATOM   1039  CB  ALA A 140       3.542  42.367  14.075  1.00 22.24           C  
ATOM   1040  N   ILE A 141       3.904  39.946  16.127  1.00 20.24           N  
ATOM   1041  CA  ILE A 141       4.744  39.504  17.260  1.00 19.24           C  
ATOM   1042  C   ILE A 141       6.111  39.174  16.725  1.00 19.40           C  
ATOM   1043  O   ILE A 141       6.237  38.695  15.603  1.00 20.75           O  
ATOM   1044  CB  ILE A 141       4.107  38.307  18.010  1.00 18.75           C  
ATOM   1045  CG1 ILE A 141       4.848  38.069  19.303  1.00 18.40           C  
ATOM   1046  CG2 ILE A 141       4.044  37.101  17.165  1.00 18.71           C  
ATOM   1047  CD1 ILE A 141       4.001  37.250  20.317  1.00 19.22           C  
ATOM   1048  N   LYS A 142       7.138  39.465  17.498  1.00 19.68           N  
ATOM   1049  CA  LYS A 142       8.500  39.357  17.010  1.00 20.86           C  
ATOM   1050  C   LYS A 142       9.381  38.692  18.036  1.00 20.64           C  
ATOM   1051  O   LYS A 142       9.295  38.970  19.229  1.00 19.99           O  
ATOM   1052  CB  LYS A 142       9.080  40.708  16.605  1.00 21.16           C  
ATOM   1053  CG  LYS A 142       8.234  41.386  15.543  1.00 21.56           C  
ATOM   1054  CD  LYS A 142       8.910  42.648  14.964  1.00 21.90           C  
ATOM   1055  CE  LYS A 142       7.936  43.540  14.175  1.00 24.00           C  
ATOM   1056  NZ  LYS A 142       8.722  44.395  13.161  1.00 20.50           N  
ATOM   1057  N   LEU A 143      10.267  37.851  17.527  1.00 19.79           N  
ATOM   1058  CA  LEU A 143      11.331  37.252  18.328  1.00 21.32           C  
ATOM   1059  C   LEU A 143      12.415  38.252  18.636  1.00 21.89           C  
ATOM   1060  O   LEU A 143      12.920  38.917  17.727  1.00 21.18           O  
ATOM   1061  CB  LEU A 143      11.923  36.091  17.555  1.00 21.51           C  
ATOM   1062  CG  LEU A 143      10.976  34.950  17.273  1.00 23.85           C  
ATOM   1063  CD1 LEU A 143      11.280  34.303  15.912  1.00 26.14           C  
ATOM   1064  CD2 LEU A 143      11.131  33.953  18.417  1.00 24.96           C  
ATOM   1065  N   ALA A 144      12.801  38.382  19.910  1.00 22.34           N  
ATOM   1066  CA  ALA A 144      13.771  39.399  20.293  1.00 24.47           C  
ATOM   1067  C   ALA A 144      14.980  38.778  20.953  1.00 25.98           C  
ATOM   1068  O   ALA A 144      14.842  37.789  21.624  1.00 24.41           O  
ATOM   1069  CB  ALA A 144      13.127  40.412  21.236  1.00 25.22           C  
ATOM   1070  N   ASP A 145      16.145  39.380  20.788  1.00 29.32           N  
ATOM   1071  CA  ASP A 145      17.380  38.940  21.448  1.00 33.94           C  
ATOM   1072  C   ASP A 145      17.850  37.638  20.821  1.00 35.72           C  
ATOM   1073  O   ASP A 145      18.299  36.732  21.483  1.00 38.50           O  
ATOM   1074  CB  ASP A 145      17.220  38.823  22.976  1.00 34.86           C  
ATOM   1075  CG  ASP A 145      17.533  40.121  23.698  1.00 37.90           C  
ATOM   1076  OD1 ASP A 145      17.349  41.213  23.107  1.00 45.17           O  
ATOM   1077  OD2 ASP A 145      17.939  40.158  24.873  1.00 39.28           O  
ATOM   1078  N   PHE A 146      17.740  37.593  19.504  1.00 39.49           N  
ATOM   1079  CA  PHE A 146      17.871  36.372  18.732  1.00 41.92           C  
ATOM   1080  C   PHE A 146      19.318  36.088  18.409  1.00 43.49           C  
ATOM   1081  O   PHE A 146      19.998  36.949  17.873  1.00 44.04           O  
ATOM   1082  CB  PHE A 146      17.077  36.490  17.437  1.00 41.56           C  
ATOM   1083  CG  PHE A 146      16.578  35.197  16.962  1.00 43.82           C  
ATOM   1084  CD1 PHE A 146      17.443  34.141  16.783  1.00 43.76           C  
ATOM   1085  CD2 PHE A 146      15.243  34.994  16.777  1.00 44.58           C  
ATOM   1086  CE1 PHE A 146      16.988  32.922  16.368  1.00 46.46           C  
ATOM   1087  CE2 PHE A 146      14.775  33.754  16.391  1.00 48.01           C  
ATOM   1088  CZ  PHE A 146      15.655  32.717  16.183  1.00 46.73           C  
ATOM   1089  N   GLY A 147      19.779  34.878  18.725  1.00 46.02           N  
ATOM   1090  CA  GLY A 147      21.160  34.480  18.478  1.00 47.35           C  
ATOM   1091  C   GLY A 147      22.155  35.212  19.366  1.00 48.65           C  
ATOM   1092  O   GLY A 147      23.366  35.116  19.149  1.00 49.22           O  
ATOM   1093  N   LEU A 148      21.660  35.934  20.368  1.00 49.96           N  
ATOM   1094  CA  LEU A 148      22.540  36.615  21.318  1.00 50.84           C  
ATOM   1095  C   LEU A 148      23.246  35.617  22.252  1.00 51.35           C  
ATOM   1096  O   LEU A 148      24.264  35.965  22.861  1.00 51.60           O  
ATOM   1097  CB  LEU A 148      21.769  37.679  22.128  1.00 51.43           C  
ATOM   1098  CG  LEU A 148      21.689  39.126  21.612  1.00 51.91           C  
ATOM   1099  CD1 LEU A 148      23.066  39.648  21.235  1.00 52.48           C  
ATOM   1100  CD2 LEU A 148      20.760  39.256  20.422  1.00 52.37           C  
ATOM   1101  N   ALA A 149      22.733  34.384  22.351  1.00 51.57           N  
ATOM   1102  CA  ALA A 149      23.350  33.371  23.213  1.00 52.10           C  
ATOM   1103  C   ALA A 149      24.340  32.509  22.426  1.00 52.24           C  
ATOM   1104  O   ALA A 149      25.557  32.633  22.604  1.00 53.04           O  
ATOM   1105  CB  ALA A 149      22.281  32.500  23.889  1.00 51.84           C  
ATOM   1106  N   GLU A 162      19.761  39.134  38.583  1.00 52.34           N  
ATOM   1107  CA  GLU A 162      18.474  38.422  38.594  1.00 51.72           C  
ATOM   1108  C   GLU A 162      18.607  36.951  38.135  1.00 50.64           C  
ATOM   1109  O   GLU A 162      19.578  36.577  37.461  1.00 50.80           O  
ATOM   1110  CB  GLU A 162      17.421  39.177  37.755  1.00 52.14           C  
ATOM   1111  CG  GLU A 162      15.999  39.162  38.319  1.00 53.20           C  
ATOM   1112  CD  GLU A 162      15.926  39.448  39.823  1.00 56.05           C  
ATOM   1113  OE1 GLU A 162      15.953  38.467  40.611  1.00 57.50           O  
ATOM   1114  OE2 GLU A 162      15.843  40.642  40.220  1.00 56.90           O  
ATOM   1115  N   VAL A 163      17.628  36.136  38.537  1.00 48.88           N  
ATOM   1116  CA  VAL A 163      17.640  34.681  38.341  1.00 47.16           C  
ATOM   1117  C   VAL A 163      17.150  34.376  36.934  1.00 45.49           C  
ATOM   1118  O   VAL A 163      16.087  34.847  36.551  1.00 44.03           O  
ATOM   1119  CB  VAL A 163      16.681  33.986  39.365  1.00 47.37           C  
ATOM   1120  CG1 VAL A 163      16.453  32.511  39.037  1.00 47.56           C  
ATOM   1121  CG2 VAL A 163      17.206  34.131  40.770  1.00 48.28           C  
ATOM   1122  N   VAL A 164      17.898  33.568  36.182  1.00 43.59           N  
ATOM   1123  CA  VAL A 164      17.482  33.232  34.808  1.00 42.16           C  
ATOM   1124  C   VAL A 164      16.355  32.192  34.848  1.00 39.32           C  
ATOM   1125  O   VAL A 164      16.412  31.221  35.592  1.00 39.43           O  
ATOM   1126  CB  VAL A 164      18.650  32.735  33.930  1.00 43.02           C  
ATOM   1127  CG1 VAL A 164      18.194  32.587  32.435  1.00 43.63           C  
ATOM   1128  CG2 VAL A 164      19.845  33.707  34.025  1.00 44.51           C  
ATOM   1129  N   THR A 165      15.313  32.424  34.070  1.00 35.92           N  
ATOM   1130  CA  THR A 165      14.137  31.579  34.114  1.00 32.85           C  
ATOM   1131  C   THR A 165      14.344  30.279  33.321  1.00 29.92           C  
ATOM   1132  O   THR A 165      14.882  30.254  32.194  1.00 26.74           O  
ATOM   1133  CB  THR A 165      12.892  32.336  33.639  1.00 34.32           C  
ATOM   1134  OG1 THR A 165      11.723  31.510  33.742  1.00 33.89           O  
ATOM   1135  CG2 THR A 165      12.979  32.661  32.119  1.00 35.38           C  
ATOM   1136  N   LEU A 166      13.898  29.200  33.937  1.00 24.64           N  
ATOM   1137  CA  LEU A 166      14.184  27.863  33.439  1.00 24.10           C  
ATOM   1138  C   LEU A 166      12.979  27.279  32.732  1.00 20.71           C  
ATOM   1139  O   LEU A 166      13.064  26.172  32.185  1.00 18.13           O  
ATOM   1140  CB  LEU A 166      14.499  26.964  34.637  1.00 23.66           C  
ATOM   1141  CG  LEU A 166      15.964  26.609  34.942  1.00 27.03           C  
ATOM   1142  CD1 LEU A 166      16.943  27.581  34.454  1.00 25.44           C  
ATOM   1143  CD2 LEU A 166      16.147  26.302  36.458  1.00 27.00           C  
ATOM   1144  N   TRP A 167      11.870  28.024  32.779  1.00 18.44           N  
ATOM   1145  CA  TRP A 167      10.555  27.471  32.582  1.00 17.54           C  
ATOM   1146  C   TRP A 167      10.384  26.993  31.156  1.00 16.40           C  
ATOM   1147  O   TRP A 167       9.584  26.124  30.916  1.00 16.53           O  
ATOM   1148  CB  TRP A 167       9.486  28.496  32.869  1.00 18.45           C  
ATOM   1149  CG  TRP A 167       9.364  28.908  34.300  1.00 18.83           C  
ATOM   1150  CD1 TRP A 167      10.082  28.440  35.367  1.00 23.66           C  
ATOM   1151  CD2 TRP A 167       8.467  29.880  34.810  1.00 23.00           C  
ATOM   1152  NE1 TRP A 167       9.668  29.060  36.531  1.00 21.92           N  
ATOM   1153  CE2 TRP A 167       8.669  29.947  36.219  1.00 23.92           C  
ATOM   1154  CE3 TRP A 167       7.483  30.693  34.231  1.00 22.46           C  
ATOM   1155  CZ2 TRP A 167       7.935  30.804  37.041  1.00 27.42           C  
ATOM   1156  CZ3 TRP A 167       6.757  31.544  35.049  1.00 25.45           C  
ATOM   1157  CH2 TRP A 167       6.992  31.586  36.453  1.00 28.27           C  
ATOM   1158  N   TYR A 168      11.204  27.521  30.260  1.00 16.12           N  
ATOM   1159  CA  TYR A 168      11.027  27.269  28.826  1.00 15.86           C  
ATOM   1160  C   TYR A 168      12.165  26.454  28.242  1.00 17.48           C  
ATOM   1161  O   TYR A 168      12.239  26.243  27.027  1.00 15.88           O  
ATOM   1162  CB  TYR A 168      10.854  28.620  28.100  1.00 16.01           C  
ATOM   1163  CG  TYR A 168       9.790  29.460  28.739  1.00 14.58           C  
ATOM   1164  CD1 TYR A 168       8.446  29.263  28.482  1.00 18.12           C  
ATOM   1165  CD2 TYR A 168      10.132  30.421  29.682  1.00 16.50           C  
ATOM   1166  CE1 TYR A 168       7.470  30.005  29.153  1.00 17.26           C  
ATOM   1167  CE2 TYR A 168       9.174  31.145  30.336  1.00 15.90           C  
ATOM   1168  CZ  TYR A 168       7.875  30.943  30.083  1.00 16.17           C  
ATOM   1169  OH  TYR A 168       6.954  31.680  30.750  1.00 16.05           O  
ATOM   1170  N   ARG A 169      13.018  25.919  29.112  1.00 18.15           N  
ATOM   1171  CA  ARG A 169      14.193  25.175  28.688  1.00 19.16           C  
ATOM   1172  C   ARG A 169      13.833  23.757  28.246  1.00 18.56           C  
ATOM   1173  O   ARG A 169      13.158  23.004  28.977  1.00 17.65           O  
ATOM   1174  CB  ARG A 169      15.198  25.113  29.854  1.00 20.88           C  
ATOM   1175  CG  ARG A 169      16.578  24.665  29.477  1.00 24.51           C  
ATOM   1176  CD  ARG A 169      17.666  25.099  30.471  1.00 30.68           C  
ATOM   1177  NE  ARG A 169      17.932  26.548  30.542  1.00 32.82           N  
ATOM   1178  CZ  ARG A 169      18.855  27.051  31.380  1.00 37.69           C  
ATOM   1179  NH1 ARG A 169      19.582  26.222  32.159  1.00 32.76           N  
ATOM   1180  NH2 ARG A 169      19.072  28.372  31.426  1.00 38.83           N  
ATOM   1181  N   ALA A 170      14.344  23.368  27.079  1.00 17.37           N  
ATOM   1182  CA  ALA A 170      14.133  22.026  26.585  1.00 16.79           C  
ATOM   1183  C   ALA A 170      14.833  20.958  27.480  1.00 17.14           C  
ATOM   1184  O   ALA A 170      15.884  21.226  28.062  1.00 15.10           O  
ATOM   1185  CB  ALA A 170      14.654  21.927  25.165  1.00 16.79           C  
ATOM   1186  N   PRO A 171      14.294  19.747  27.526  1.00 17.71           N  
ATOM   1187  CA  PRO A 171      14.882  18.717  28.415  1.00 18.26           C  
ATOM   1188  C   PRO A 171      16.317  18.344  27.999  1.00 18.45           C  
ATOM   1189  O   PRO A 171      17.153  18.075  28.876  1.00 18.72           O  
ATOM   1190  CB  PRO A 171      13.909  17.539  28.306  1.00 17.40           C  
ATOM   1191  CG  PRO A 171      13.091  17.776  27.003  1.00 18.04           C  
ATOM   1192  CD  PRO A 171      13.121  19.258  26.799  1.00 17.76           C  
ATOM   1193  N   GLU A 172      16.641  18.363  26.705  1.00 16.51           N  
ATOM   1194  CA  GLU A 172      18.004  18.055  26.299  1.00 18.41           C  
ATOM   1195  C   GLU A 172      19.036  19.019  26.846  1.00 18.53           C  
ATOM   1196  O   GLU A 172      20.146  18.578  27.150  1.00 19.40           O  
ATOM   1197  CB  GLU A 172      18.166  17.882  24.800  1.00 18.72           C  
ATOM   1198  CG  GLU A 172      17.765  19.112  24.019  1.00 19.61           C  
ATOM   1199  CD  GLU A 172      16.345  19.095  23.583  1.00 20.20           C  
ATOM   1200  OE1 GLU A 172      15.447  18.674  24.386  1.00 18.81           O  
ATOM   1201  OE2 GLU A 172      16.121  19.585  22.445  1.00 15.92           O  
ATOM   1202  N   ILE A 173      18.684  20.293  27.011  1.00 18.45           N  
ATOM   1203  CA  ILE A 173      19.556  21.260  27.682  1.00 20.23           C  
ATOM   1204  C   ILE A 173      19.731  20.912  29.171  1.00 21.22           C  
ATOM   1205  O   ILE A 173      20.856  20.812  29.652  1.00 21.86           O  
ATOM   1206  CB  ILE A 173      19.043  22.717  27.500  1.00 19.85           C  
ATOM   1207  CG1 ILE A 173      18.868  23.040  26.005  1.00 21.74           C  
ATOM   1208  CG2 ILE A 173      20.007  23.730  28.123  1.00 21.90           C  
ATOM   1209  CD1 ILE A 173      18.447  24.415  25.744  1.00 24.64           C  
ATOM   1210  N   LEU A 174      18.619  20.671  29.853  1.00 22.35           N  
ATOM   1211  CA  LEU A 174      18.627  20.298  31.283  1.00 23.22           C  
ATOM   1212  C   LEU A 174      19.378  19.006  31.605  1.00 23.82           C  
ATOM   1213  O   LEU A 174      19.919  18.852  32.725  1.00 24.30           O  
ATOM   1214  CB  LEU A 174      17.191  20.199  31.819  1.00 22.58           C  
ATOM   1215  CG  LEU A 174      16.327  21.467  31.756  1.00 22.15           C  
ATOM   1216  CD1 LEU A 174      14.867  21.061  31.887  1.00 21.16           C  
ATOM   1217  CD2 LEU A 174      16.730  22.480  32.833  1.00 24.32           C  
ATOM   1218  N   LEU A 175      19.396  18.076  30.653  1.00 23.69           N  
ATOM   1219  CA  LEU A 175      20.099  16.794  30.787  1.00 24.78           C  
ATOM   1220  C   LEU A 175      21.541  16.876  30.295  1.00 25.42           C  
ATOM   1221  O   LEU A 175      22.272  15.891  30.330  1.00 25.71           O  
ATOM   1222  CB  LEU A 175      19.338  15.671  30.068  1.00 23.84           C  
ATOM   1223  CG  LEU A 175      18.009  15.282  30.712  1.00 24.50           C  
ATOM   1224  CD1 LEU A 175      17.188  14.354  29.858  1.00 24.13           C  
ATOM   1225  CD2 LEU A 175      18.222  14.674  32.107  1.00 25.76           C  
ATOM   1226  N   GLY A 176      21.950  18.047  29.828  1.00 27.20           N  
ATOM   1227  CA  GLY A 176      23.368  18.373  29.688  1.00 28.70           C  
ATOM   1228  C   GLY A 176      23.950  18.192  28.297  1.00 30.14           C  
ATOM   1229  O   GLY A 176      25.173  18.140  28.113  1.00 28.38           O  
ATOM   1230  N   CYS A 177      23.075  18.094  27.304  1.00 31.83           N  
ATOM   1231  CA  CYS A 177      23.515  17.986  25.914  1.00 33.02           C  
ATOM   1232  C   CYS A 177      24.258  19.284  25.549  1.00 32.85           C  
ATOM   1233  O   CYS A 177      23.801  20.375  25.811  1.00 31.82           O  
ATOM   1234  CB  CYS A 177      22.318  17.666  25.000  1.00 33.76           C  
ATOM   1235  SG  CYS A 177      22.613  17.423  23.218  1.00 40.59           S  
ATOM   1236  N   LYS A 178      25.449  19.114  25.004  1.00 33.97           N  
ATOM   1237  CA  LYS A 178      26.314  20.219  24.625  1.00 35.17           C  
ATOM   1238  C   LYS A 178      25.932  20.763  23.253  1.00 33.82           C  
ATOM   1239  O   LYS A 178      26.112  21.940  22.987  1.00 33.20           O  
ATOM   1240  CB  LYS A 178      27.762  19.723  24.586  1.00 36.48           C  
ATOM   1241  CG  LYS A 178      28.808  20.824  24.783  1.00 40.60           C  
ATOM   1242  CD  LYS A 178      29.305  20.910  26.236  1.00 44.74           C  
ATOM   1243  CE  LYS A 178      28.194  21.242  27.265  1.00 45.97           C  
ATOM   1244  NZ  LYS A 178      28.774  21.446  28.644  1.00 47.69           N  
ATOM   1245  N   TYR A 179      25.404  19.888  22.402  1.00 33.22           N  
ATOM   1246  CA  TYR A 179      25.218  20.191  20.977  1.00 32.82           C  
ATOM   1247  C   TYR A 179      23.779  20.048  20.557  1.00 32.10           C  
ATOM   1248  O   TYR A 179      23.444  19.285  19.654  1.00 32.81           O  
ATOM   1249  CB  TYR A 179      26.091  19.276  20.140  1.00 33.80           C  
ATOM   1250  CG  TYR A 179      27.545  19.450  20.477  1.00 36.93           C  
ATOM   1251  CD1 TYR A 179      28.135  20.699  20.420  1.00 39.80           C  
ATOM   1252  CD2 TYR A 179      28.324  18.369  20.877  1.00 40.70           C  
ATOM   1253  CE1 TYR A 179      29.476  20.873  20.733  1.00 42.60           C  
ATOM   1254  CE2 TYR A 179      29.661  18.534  21.190  1.00 43.53           C  
ATOM   1255  CZ  TYR A 179      30.230  19.796  21.124  1.00 44.98           C  
ATOM   1256  OH  TYR A 179      31.559  19.977  21.463  1.00 47.56           O  
ATOM   1257  N   TYR A 180      22.939  20.800  21.229  1.00 29.91           N  
ATOM   1258  CA  TYR A 180      21.520  20.780  20.953  1.00 29.02           C  
ATOM   1259  C   TYR A 180      21.202  21.581  19.643  1.00 27.05           C  
ATOM   1260  O   TYR A 180      22.036  22.287  19.059  1.00 26.92           O  
ATOM   1261  CB  TYR A 180      20.749  21.286  22.175  1.00 28.67           C  
ATOM   1262  CG  TYR A 180      21.183  22.625  22.659  1.00 31.21           C  
ATOM   1263  CD1 TYR A 180      22.066  22.753  23.725  1.00 32.49           C  
ATOM   1264  CD2 TYR A 180      20.706  23.780  22.047  1.00 33.09           C  
ATOM   1265  CE1 TYR A 180      22.468  23.996  24.152  1.00 36.49           C  
ATOM   1266  CE2 TYR A 180      21.071  25.002  22.476  1.00 35.84           C  
ATOM   1267  CZ  TYR A 180      21.948  25.117  23.523  1.00 37.74           C  
ATOM   1268  OH  TYR A 180      22.301  26.372  23.924  1.00 42.81           O  
ATOM   1269  N   SER A 181      19.997  21.366  19.173  1.00 25.37           N  
ATOM   1270  CA  SER A 181      19.541  21.770  17.865  1.00 24.17           C  
ATOM   1271  C   SER A 181      18.420  22.790  17.948  1.00 22.64           C  
ATOM   1272  O   SER A 181      17.914  23.156  19.035  1.00 22.13           O  
ATOM   1273  CB  SER A 181      18.963  20.530  17.170  1.00 24.26           C  
ATOM   1274  OG  SER A 181      17.708  20.138  17.750  1.00 22.48           O  
ATOM   1275  N   THR A 182      17.952  23.164  16.763  1.00 21.63           N  
ATOM   1276  CA  THR A 182      16.810  24.080  16.623  1.00 20.23           C  
ATOM   1277  C   THR A 182      15.585  23.631  17.373  1.00 18.33           C  
ATOM   1278  O   THR A 182      14.717  24.463  17.664  1.00 19.13           O  
ATOM   1279  CB  THR A 182      16.454  24.242  15.123  1.00 19.75           C  
ATOM   1280  OG1 THR A 182      16.374  22.959  14.533  1.00 18.27           O  
ATOM   1281  CG2 THR A 182      17.586  24.872  14.346  1.00 23.34           C  
ATOM   1282  N   ALA A 183      15.507  22.349  17.679  1.00 18.07           N  
ATOM   1283  CA  ALA A 183      14.379  21.787  18.378  1.00 16.58           C  
ATOM   1284  C   ALA A 183      14.191  22.450  19.724  1.00 16.45           C  
ATOM   1285  O   ALA A 183      13.096  22.473  20.217  1.00 15.70           O  
ATOM   1286  CB  ALA A 183      14.526  20.345  18.541  1.00 17.35           C  
ATOM   1287  N   VAL A 184      15.263  22.962  20.299  1.00 16.06           N  
ATOM   1288  CA  VAL A 184      15.111  23.563  21.640  1.00 16.61           C  
ATOM   1289  C   VAL A 184      14.142  24.769  21.577  1.00 15.85           C  
ATOM   1290  O   VAL A 184      13.422  25.043  22.517  1.00 17.23           O  
ATOM   1291  CB  VAL A 184      16.444  24.011  22.218  1.00 15.77           C  
ATOM   1292  CG1 VAL A 184      17.431  22.857  22.358  1.00 18.39           C  
ATOM   1293  CG2 VAL A 184      17.077  25.163  21.427  1.00 14.59           C  
ATOM   1294  N   ASP A 185      14.152  25.527  20.482  1.00 16.28           N  
ATOM   1295  CA  ASP A 185      13.225  26.646  20.316  1.00 15.46           C  
ATOM   1296  C   ASP A 185      11.766  26.256  20.150  1.00 14.37           C  
ATOM   1297  O   ASP A 185      10.857  26.997  20.602  1.00 14.04           O  
ATOM   1298  CB  ASP A 185      13.636  27.506  19.122  1.00 15.99           C  
ATOM   1299  CG  ASP A 185      14.989  28.216  19.311  1.00 18.52           C  
ATOM   1300  OD1 ASP A 185      15.463  28.450  20.487  1.00 17.37           O  
ATOM   1301  OD2 ASP A 185      15.631  28.586  18.276  1.00 17.38           O  
ATOM   1302  N   ILE A 186      11.520  25.129  19.477  1.00 15.68           N  
ATOM   1303  CA  ILE A 186      10.192  24.602  19.297  1.00 14.75           C  
ATOM   1304  C   ILE A 186       9.645  24.222  20.699  1.00 14.68           C  
ATOM   1305  O   ILE A 186       8.488  24.490  21.023  1.00 14.79           O  
ATOM   1306  CB  ILE A 186      10.203  23.419  18.325  1.00 15.99           C  
ATOM   1307  CG1 ILE A 186      10.596  23.888  16.889  1.00 15.14           C  
ATOM   1308  CG2 ILE A 186       8.856  22.682  18.329  1.00 15.15           C  
ATOM   1309  CD1 ILE A 186       9.656  24.942  16.303  1.00 18.34           C  
ATOM   1310  N   TRP A 187      10.497  23.605  21.509  1.00 13.27           N  
ATOM   1311  CA  TRP A 187      10.107  23.245  22.878  1.00 14.83           C  
ATOM   1312  C   TRP A 187       9.670  24.494  23.609  1.00 14.34           C  
ATOM   1313  O   TRP A 187       8.563  24.543  24.132  1.00 15.84           O  
ATOM   1314  CB  TRP A 187      11.253  22.590  23.641  1.00 15.49           C  
ATOM   1315  CG  TRP A 187      10.857  22.305  25.071  1.00 15.15           C  
ATOM   1316  CD1 TRP A 187      10.863  23.193  26.122  1.00 16.64           C  
ATOM   1317  CD2 TRP A 187      10.400  21.077  25.576  1.00 16.09           C  
ATOM   1318  NE1 TRP A 187      10.436  22.548  27.261  1.00 17.01           N  
ATOM   1319  CE2 TRP A 187      10.132  21.253  26.950  1.00 19.36           C  
ATOM   1320  CE3 TRP A 187      10.200  19.801  25.011  1.00 17.93           C  
ATOM   1321  CZ2 TRP A 187       9.659  20.213  27.755  1.00 19.58           C  
ATOM   1322  CZ3 TRP A 187       9.729  18.787  25.811  1.00 20.16           C  
ATOM   1323  CH2 TRP A 187       9.478  19.000  27.183  1.00 18.63           C  
ATOM   1324  N   SER A 188      10.496  25.514  23.581  1.00 15.10           N  
ATOM   1325  CA  SER A 188      10.238  26.764  24.351  1.00 13.24           C  
ATOM   1326  C   SER A 188       8.952  27.399  23.847  1.00 14.93           C  
ATOM   1327  O   SER A 188       8.124  27.804  24.609  1.00 15.05           O  
ATOM   1328  CB  SER A 188      11.369  27.752  24.218  1.00 14.36           C  
ATOM   1329  OG  SER A 188      12.602  27.211  24.642  1.00 14.73           O  
ATOM   1330  N   LEU A 189       8.742  27.410  22.531  1.00 13.04           N  
ATOM   1331  CA  LEU A 189       7.535  27.977  21.971  1.00 14.38           C  
ATOM   1332  C   LEU A 189       6.272  27.194  22.304  1.00 14.44           C  
ATOM   1333  O   LEU A 189       5.235  27.782  22.541  1.00 15.97           O  
ATOM   1334  CB  LEU A 189       7.696  28.159  20.433  1.00 14.23           C  
ATOM   1335  CG  LEU A 189       6.553  28.924  19.789  1.00 15.47           C  
ATOM   1336  CD1 LEU A 189       6.309  30.313  20.346  1.00 17.75           C  
ATOM   1337  CD2 LEU A 189       6.849  28.989  18.282  1.00 18.22           C  
ATOM   1338  N   GLY A 190       6.376  25.863  22.375  1.00 14.82           N  
ATOM   1339  CA  GLY A 190       5.309  25.039  22.858  1.00 15.09           C  
ATOM   1340  C   GLY A 190       4.918  25.395  24.274  1.00 14.42           C  
ATOM   1341  O   GLY A 190       3.721  25.439  24.608  1.00 15.16           O  
ATOM   1342  N   CYS A 191       5.920  25.602  25.116  1.00 15.65           N  
ATOM   1343  CA  CYS A 191       5.659  25.996  26.519  1.00 15.53           C  
ATOM   1344  C   CYS A 191       4.921  27.338  26.573  1.00 15.62           C  
ATOM   1345  O   CYS A 191       3.984  27.537  27.356  1.00 13.63           O  
ATOM   1346  CB  CYS A 191       6.977  26.070  27.280  1.00 16.03           C  
ATOM   1347  SG  CYS A 191       7.734  24.466  27.557  1.00 16.94           S  
ATOM   1348  N   ILE A 192       5.301  28.260  25.687  1.00 15.21           N  
ATOM   1349  CA  ILE A 192       4.647  29.555  25.630  1.00 14.98           C  
ATOM   1350  C   ILE A 192       3.235  29.435  25.113  1.00 15.52           C  
ATOM   1351  O   ILE A 192       2.369  30.110  25.635  1.00 17.16           O  
ATOM   1352  CB  ILE A 192       5.483  30.529  24.770  1.00 14.56           C  
ATOM   1353  CG1 ILE A 192       6.818  30.731  25.477  1.00 14.96           C  
ATOM   1354  CG2 ILE A 192       4.781  31.854  24.557  1.00 16.44           C  
ATOM   1355  CD1 ILE A 192       7.898  31.245  24.601  1.00 15.94           C  
ATOM   1356  N   PHE A 193       3.022  28.632  24.056  1.00 14.14           N  
ATOM   1357  CA  PHE A 193       1.688  28.295  23.524  1.00 16.41           C  
ATOM   1358  C   PHE A 193       0.742  27.838  24.667  1.00 16.26           C  
ATOM   1359  O   PHE A 193      -0.313  28.413  24.847  1.00 17.41           O  
ATOM   1360  CB  PHE A 193       1.873  27.184  22.460  1.00 16.11           C  
ATOM   1361  CG  PHE A 193       0.610  26.685  21.774  1.00 17.02           C  
ATOM   1362  CD1 PHE A 193      -0.550  27.439  21.715  1.00 16.32           C  
ATOM   1363  CD2 PHE A 193       0.664  25.500  21.061  1.00 17.75           C  
ATOM   1364  CE1 PHE A 193      -1.665  26.968  21.082  1.00 18.67           C  
ATOM   1365  CE2 PHE A 193      -0.455  25.012  20.395  1.00 18.75           C  
ATOM   1366  CZ  PHE A 193      -1.621  25.767  20.392  1.00 19.45           C  
ATOM   1367  N   ALA A 194       1.168  26.823  25.416  1.00 16.67           N  
ATOM   1368  CA  ALA A 194       0.422  26.287  26.565  1.00 16.88           C  
ATOM   1369  C   ALA A 194       0.086  27.377  27.560  1.00 16.10           C  
ATOM   1370  O   ALA A 194      -1.023  27.460  28.044  1.00 19.38           O  
ATOM   1371  CB  ALA A 194       1.202  25.130  27.266  1.00 15.57           C  
ATOM   1372  N   GLU A 195       1.009  28.266  27.809  1.00 17.87           N  
ATOM   1373  CA  GLU A 195       0.814  29.307  28.832  1.00 18.00           C  
ATOM   1374  C   GLU A 195      -0.203  30.352  28.364  1.00 18.07           C  
ATOM   1375  O   GLU A 195      -1.040  30.848  29.126  1.00 17.92           O  
ATOM   1376  CB  GLU A 195       2.151  29.916  29.152  1.00 18.16           C  
ATOM   1377  CG  GLU A 195       2.171  30.898  30.319  1.00 18.96           C  
ATOM   1378  CD  GLU A 195       3.535  31.429  30.641  1.00 22.26           C  
ATOM   1379  OE1 GLU A 195       4.537  30.771  30.295  1.00 18.23           O  
ATOM   1380  OE2 GLU A 195       3.614  32.510  31.288  1.00 22.11           O  
ATOM   1381  N   MET A 196      -0.167  30.674  27.087  1.00 18.99           N  
ATOM   1382  CA  MET A 196      -1.168  31.573  26.520  1.00 19.21           C  
ATOM   1383  C   MET A 196      -2.561  31.005  26.670  1.00 19.67           C  
ATOM   1384  O   MET A 196      -3.522  31.731  26.976  1.00 18.93           O  
ATOM   1385  CB  MET A 196      -0.873  31.862  25.032  1.00 19.06           C  
ATOM   1386  CG  MET A 196       0.272  32.871  24.817  1.00 21.35           C  
ATOM   1387  SD  MET A 196       0.385  33.472  23.056  1.00 22.22           S  
ATOM   1388  CE  MET A 196       0.994  32.104  22.355  1.00 18.28           C  
ATOM   1389  N   VAL A 197      -2.666  29.706  26.445  1.00 18.67           N  
ATOM   1390  CA  VAL A 197      -3.941  29.035  26.431  1.00 19.57           C  
ATOM   1391  C   VAL A 197      -4.487  28.939  27.829  1.00 19.51           C  
ATOM   1392  O   VAL A 197      -5.640  29.334  28.055  1.00 20.49           O  
ATOM   1393  CB  VAL A 197      -3.853  27.655  25.745  1.00 19.56           C  
ATOM   1394  CG1 VAL A 197      -5.107  26.846  25.972  1.00 22.04           C  
ATOM   1395  CG2 VAL A 197      -3.645  27.882  24.250  1.00 18.10           C  
ATOM   1396  N   THR A 198      -3.661  28.497  28.768  1.00 20.14           N  
ATOM   1397  CA  THR A 198      -4.148  28.223  30.115  1.00 20.92           C  
ATOM   1398  C   THR A 198      -4.057  29.358  31.072  1.00 21.78           C  
ATOM   1399  O   THR A 198      -4.687  29.293  32.132  1.00 21.48           O  
ATOM   1400  CB  THR A 198      -3.420  27.029  30.734  1.00 19.84           C  
ATOM   1401  OG1 THR A 198      -2.013  27.280  30.821  1.00 16.84           O  
ATOM   1402  CG2 THR A 198      -3.593  25.794  29.841  1.00 22.09           C  
ATOM   1403  N   ARG A 199      -3.244  30.374  30.738  1.00 22.19           N  
ATOM   1404  CA  ARG A 199      -2.875  31.490  31.618  1.00 23.32           C  
ATOM   1405  C   ARG A 199      -2.117  31.082  32.889  1.00 24.07           C  
ATOM   1406  O   ARG A 199      -2.155  31.779  33.921  1.00 24.02           O  
ATOM   1407  CB  ARG A 199      -4.103  32.374  31.983  1.00 24.53           C  
ATOM   1408  CG  ARG A 199      -5.091  32.602  30.870  1.00 26.80           C  
ATOM   1409  CD  ARG A 199      -6.365  33.330  31.318  1.00 31.19           C  
ATOM   1410  NE  ARG A 199      -7.523  32.709  30.720  1.00 33.81           N  
ATOM   1411  CZ  ARG A 199      -8.758  32.893  31.119  1.00 37.51           C  
ATOM   1412  NH1 ARG A 199      -9.033  33.743  32.109  1.00 40.15           N  
ATOM   1413  NH2 ARG A 199      -9.728  32.249  30.497  1.00 39.87           N  
ATOM   1414  N   ARG A 200      -1.400  29.972  32.800  1.00 24.37           N  
ATOM   1415  CA  ARG A 200      -0.405  29.608  33.768  1.00 25.20           C  
ATOM   1416  C   ARG A 200       0.791  28.992  33.068  1.00 24.31           C  
ATOM   1417  O   ARG A 200       0.655  28.295  32.056  1.00 21.85           O  
ATOM   1418  CB  ARG A 200      -0.989  28.591  34.725  1.00 26.84           C  
ATOM   1419  CG  ARG A 200      -0.480  28.698  36.109  1.00 32.23           C  
ATOM   1420  CD  ARG A 200      -0.680  27.421  36.909  1.00 38.28           C  
ATOM   1421  NE  ARG A 200      -1.303  27.655  38.196  1.00 44.46           N  
ATOM   1422  CZ  ARG A 200      -1.731  26.685  39.003  1.00 47.71           C  
ATOM   1423  NH1 ARG A 200      -1.612  25.415  38.656  1.00 48.19           N  
ATOM   1424  NH2 ARG A 200      -2.280  26.998  40.167  1.00 51.10           N  
ATOM   1425  N   ALA A 201       1.962  29.221  33.633  1.00 22.66           N  
ATOM   1426  CA  ALA A 201       3.150  28.595  33.091  1.00 22.94           C  
ATOM   1427  C   ALA A 201       2.968  27.075  33.061  1.00 22.61           C  
ATOM   1428  O   ALA A 201       2.385  26.486  33.973  1.00 22.25           O  
ATOM   1429  CB  ALA A 201       4.332  28.965  33.903  1.00 22.27           C  
ATOM   1430  N   LEU A 202       3.443  26.442  32.009  1.00 21.56           N  
ATOM   1431  CA  LEU A 202       3.326  24.988  31.909  1.00 20.59           C  
ATOM   1432  C   LEU A 202       4.224  24.250  32.918  1.00 20.16           C  
ATOM   1433  O   LEU A 202       3.773  23.325  33.650  1.00 20.27           O  
ATOM   1434  CB  LEU A 202       3.664  24.536  30.494  1.00 19.48           C  
ATOM   1435  CG  LEU A 202       3.443  23.045  30.147  1.00 19.88           C  
ATOM   1436  CD1 LEU A 202       2.061  22.549  30.464  1.00 22.78           C  
ATOM   1437  CD2 LEU A 202       3.823  22.769  28.633  1.00 20.47           C  
ATOM   1438  N   PHE A 203       5.487  24.622  32.928  1.00 18.95           N  
ATOM   1439  CA  PHE A 203       6.522  23.974  33.758  1.00 20.65           C  
ATOM   1440  C   PHE A 203       7.294  25.024  34.565  1.00 20.53           C  
ATOM   1441  O   PHE A 203       8.408  25.367  34.248  1.00 19.66           O  
ATOM   1442  CB  PHE A 203       7.514  23.188  32.874  1.00 19.73           C  
ATOM   1443  CG  PHE A 203       6.905  22.135  32.005  1.00 21.04           C  
ATOM   1444  CD1 PHE A 203       6.129  21.105  32.538  1.00 23.35           C  
ATOM   1445  CD2 PHE A 203       7.154  22.114  30.637  1.00 20.78           C  
ATOM   1446  CE1 PHE A 203       5.634  20.133  31.753  1.00 23.59           C  
ATOM   1447  CE2 PHE A 203       6.603  21.140  29.843  1.00 22.54           C  
ATOM   1448  CZ  PHE A 203       5.841  20.146  30.402  1.00 20.99           C  
ATOM   1449  N   PRO A 204       6.701  25.594  35.606  1.00 22.32           N  
ATOM   1450  CA  PRO A 204       7.378  26.652  36.361  1.00 23.88           C  
ATOM   1451  C   PRO A 204       8.447  26.195  37.380  1.00 25.17           C  
ATOM   1452  O   PRO A 204       8.322  26.460  38.598  1.00 26.65           O  
ATOM   1453  CB  PRO A 204       6.211  27.394  37.048  1.00 24.67           C  
ATOM   1454  CG  PRO A 204       5.177  26.388  37.185  1.00 23.84           C  
ATOM   1455  CD  PRO A 204       5.352  25.345  36.100  1.00 23.59           C  
ATOM   1456  N   GLY A 205       9.529  25.602  36.886  1.00 24.29           N  
ATOM   1457  CA  GLY A 205      10.630  25.135  37.707  1.00 24.66           C  
ATOM   1458  C   GLY A 205      11.399  26.252  38.368  1.00 25.76           C  
ATOM   1459  O   GLY A 205      11.610  27.317  37.787  1.00 24.53           O  
ATOM   1460  N   ASP A 206      11.802  26.040  39.612  1.00 25.57           N  
ATOM   1461  CA  ASP A 206      12.573  27.087  40.275  1.00 26.77           C  
ATOM   1462  C   ASP A 206      14.001  26.649  40.538  1.00 27.00           C  
ATOM   1463  O   ASP A 206      14.775  27.367  41.203  1.00 28.62           O  
ATOM   1464  CB  ASP A 206      11.884  27.562  41.556  1.00 26.92           C  
ATOM   1465  CG  ASP A 206      11.762  26.480  42.584  1.00 27.97           C  
ATOM   1466  OD1 ASP A 206      12.048  25.302  42.259  1.00 22.80           O  
ATOM   1467  OD2 ASP A 206      11.391  26.718  43.766  1.00 31.29           O  
ATOM   1468  N   SER A 207      14.326  25.475  40.021  1.00 26.57           N  
ATOM   1469  CA  SER A 207      15.682  24.935  39.963  1.00 26.13           C  
ATOM   1470  C   SER A 207      15.782  24.006  38.755  1.00 26.59           C  
ATOM   1471  O   SER A 207      14.784  23.647  38.141  1.00 23.80           O  
ATOM   1472  CB  SER A 207      16.056  24.203  41.254  1.00 26.13           C  
ATOM   1473  OG  SER A 207      15.525  22.910  41.336  1.00 26.95           O  
ATOM   1474  N   GLU A 208      17.003  23.625  38.420  1.00 26.79           N  
ATOM   1475  CA  GLU A 208      17.193  22.743  37.294  1.00 26.61           C  
ATOM   1476  C   GLU A 208      16.518  21.387  37.468  1.00 25.06           C  
ATOM   1477  O   GLU A 208      15.897  20.871  36.528  1.00 24.31           O  
ATOM   1478  CB  GLU A 208      18.665  22.582  37.037  1.00 27.17           C  
ATOM   1479  CG  GLU A 208      19.221  23.628  36.093  1.00 32.12           C  
ATOM   1480  CD  GLU A 208      20.484  23.147  35.424  1.00 36.53           C  
ATOM   1481  OE1 GLU A 208      20.394  22.345  34.465  1.00 40.53           O  
ATOM   1482  OE2 GLU A 208      21.552  23.546  35.891  1.00 43.52           O  
ATOM   1483  N   ILE A 209      16.625  20.817  38.667  1.00 23.69           N  
ATOM   1484  CA  ILE A 209      16.036  19.530  38.922  1.00 23.14           C  
ATOM   1485  C   ILE A 209      14.550  19.662  39.076  1.00 21.96           C  
ATOM   1486  O   ILE A 209      13.831  18.791  38.614  1.00 23.62           O  
ATOM   1487  CB  ILE A 209      16.694  18.777  40.183  1.00 21.69           C  
ATOM   1488  CG1 ILE A 209      16.548  17.272  40.024  1.00 22.33           C  
ATOM   1489  CG2 ILE A 209      16.045  19.252  41.506  1.00 23.73           C  
ATOM   1490  CD1 ILE A 209      16.994  16.714  38.703  1.00 20.22           C  
ATOM   1491  N   ASP A 210      14.079  20.757  39.664  1.00 21.45           N  
ATOM   1492  CA  ASP A 210      12.644  20.998  39.761  1.00 20.88           C  
ATOM   1493  C   ASP A 210      12.024  21.179  38.377  1.00 20.86           C  
ATOM   1494  O   ASP A 210      10.922  20.693  38.113  1.00 19.89           O  
ATOM   1495  CB  ASP A 210      12.343  22.202  40.640  1.00 22.46           C  
ATOM   1496  CG  ASP A 210      10.891  22.354  40.914  1.00 22.64           C  
ATOM   1497  OD1 ASP A 210      10.307  21.417  41.505  1.00 25.31           O  
ATOM   1498  OD2 ASP A 210      10.234  23.371  40.556  1.00 22.71           O  
ATOM   1499  N   GLN A 211      12.772  21.835  37.489  1.00 20.11           N  
ATOM   1500  CA  GLN A 211      12.287  22.041  36.133  1.00 19.59           C  
ATOM   1501  C   GLN A 211      12.166  20.692  35.450  1.00 19.44           C  
ATOM   1502  O   GLN A 211      11.141  20.366  34.853  1.00 19.36           O  
ATOM   1503  CB  GLN A 211      13.242  22.969  35.400  1.00 20.53           C  
ATOM   1504  CG  GLN A 211      12.753  23.320  34.022  1.00 19.70           C  
ATOM   1505  CD  GLN A 211      11.548  24.161  34.029  1.00 20.51           C  
ATOM   1506  OE1 GLN A 211      11.393  25.043  34.905  1.00 21.06           O  
ATOM   1507  NE2 GLN A 211      10.663  23.965  33.019  1.00 18.09           N  
ATOM   1508  N   LEU A 212      13.205  19.890  35.556  1.00 19.79           N  
ATOM   1509  CA  LEU A 212      13.214  18.596  34.935  1.00 20.07           C  
ATOM   1510  C   LEU A 212      12.105  17.740  35.456  1.00 20.39           C  
ATOM   1511  O   LEU A 212      11.401  17.093  34.695  1.00 18.66           O  
ATOM   1512  CB  LEU A 212      14.575  17.942  35.132  1.00 20.35           C  
ATOM   1513  CG  LEU A 212      14.881  16.721  34.312  1.00 23.14           C  
ATOM   1514  CD1 LEU A 212      14.932  17.059  32.816  1.00 25.03           C  
ATOM   1515  CD2 LEU A 212      16.181  16.089  34.775  1.00 27.57           C  
ATOM   1516  N   PHE A 213      11.960  17.694  36.791  1.00 20.24           N  
ATOM   1517  CA  PHE A 213      10.980  16.832  37.368  1.00 20.48           C  
ATOM   1518  C   PHE A 213       9.571  17.335  37.111  1.00 19.75           C  
ATOM   1519  O   PHE A 213       8.661  16.510  37.073  1.00 20.89           O  
ATOM   1520  CB  PHE A 213      11.277  16.611  38.879  1.00 21.09           C  
ATOM   1521  CG  PHE A 213      12.457  15.720  39.137  1.00 22.31           C  
ATOM   1522  CD1 PHE A 213      13.179  15.143  38.113  1.00 24.03           C  
ATOM   1523  CD2 PHE A 213      12.838  15.421  40.444  1.00 25.94           C  
ATOM   1524  CE1 PHE A 213      14.253  14.314  38.382  1.00 27.80           C  
ATOM   1525  CE2 PHE A 213      13.879  14.594  40.702  1.00 24.84           C  
ATOM   1526  CZ  PHE A 213      14.600  14.059  39.709  1.00 28.37           C  
ATOM   1527  N   ARG A 214       9.375  18.640  36.893  1.00 18.87           N  
ATOM   1528  CA  ARG A 214       8.044  19.134  36.551  1.00 18.92           C  
ATOM   1529  C   ARG A 214       7.666  18.617  35.178  1.00 17.73           C  
ATOM   1530  O   ARG A 214       6.504  18.260  34.961  1.00 18.39           O  
ATOM   1531  CB  ARG A 214       7.948  20.646  36.571  1.00 19.57           C  
ATOM   1532  CG  ARG A 214       7.660  21.208  37.961  1.00 22.67           C  
ATOM   1533  CD  ARG A 214       7.833  22.689  38.041  1.00 22.69           C  
ATOM   1534  NE  ARG A 214       7.589  23.165  39.407  1.00 26.22           N  
ATOM   1535  CZ  ARG A 214       6.385  23.433  39.914  1.00 26.69           C  
ATOM   1536  NH1 ARG A 214       5.278  23.278  39.185  1.00 26.50           N  
ATOM   1537  NH2 ARG A 214       6.282  23.869  41.160  1.00 29.09           N  
ATOM   1538  N   ILE A 215       8.637  18.615  34.276  1.00 18.64           N  
ATOM   1539  CA  ILE A 215       8.423  18.054  32.910  1.00 18.43           C  
ATOM   1540  C   ILE A 215       8.058  16.574  33.000  1.00 18.74           C  
ATOM   1541  O   ILE A 215       7.107  16.106  32.379  1.00 19.46           O  
ATOM   1542  CB  ILE A 215       9.656  18.284  32.066  1.00 19.06           C  
ATOM   1543  CG1 ILE A 215       9.877  19.790  31.842  1.00 17.92           C  
ATOM   1544  CG2 ILE A 215       9.586  17.539  30.709  1.00 18.87           C  
ATOM   1545  CD1 ILE A 215      11.184  20.141  31.253  1.00 18.29           C  
ATOM   1546  N   PHE A 216       8.834  15.825  33.777  1.00 19.96           N  
ATOM   1547  CA  PHE A 216       8.656  14.377  33.871  1.00 20.81           C  
ATOM   1548  C   PHE A 216       7.308  14.066  34.463  1.00 21.02           C  
ATOM   1549  O   PHE A 216       6.678  13.068  34.071  1.00 21.43           O  
ATOM   1550  CB  PHE A 216       9.742  13.707  34.750  1.00 21.22           C  
ATOM   1551  CG  PHE A 216      11.129  13.723  34.182  1.00 22.05           C  
ATOM   1552  CD1 PHE A 216      11.417  14.289  32.949  1.00 21.91           C  
ATOM   1553  CD2 PHE A 216      12.189  13.196  34.933  1.00 24.24           C  
ATOM   1554  CE1 PHE A 216      12.688  14.281  32.454  1.00 23.54           C  
ATOM   1555  CE2 PHE A 216      13.485  13.193  34.426  1.00 21.04           C  
ATOM   1556  CZ  PHE A 216      13.730  13.728  33.205  1.00 24.47           C  
ATOM   1557  N   ARG A 217       6.870  14.881  35.410  1.00 22.24           N  
ATOM   1558  CA  ARG A 217       5.593  14.631  36.143  1.00 23.92           C  
ATOM   1559  C   ARG A 217       4.395  14.804  35.209  1.00 24.04           C  
ATOM   1560  O   ARG A 217       3.345  14.130  35.340  1.00 23.24           O  
ATOM   1561  CB  ARG A 217       5.440  15.565  37.325  1.00 25.12           C  
ATOM   1562  CG  ARG A 217       6.221  15.113  38.548  1.00 29.27           C  
ATOM   1563  CD  ARG A 217       6.210  16.198  39.695  1.00 36.49           C  
ATOM   1564  NE  ARG A 217       7.312  15.980  40.651  1.00 41.28           N  
ATOM   1565  CZ  ARG A 217       8.168  16.908  41.095  1.00 43.97           C  
ATOM   1566  NH1 ARG A 217       8.083  18.184  40.723  1.00 45.66           N  
ATOM   1567  NH2 ARG A 217       9.119  16.551  41.958  1.00 46.53           N  
ATOM   1568  N   THR A 218       4.584  15.641  34.198  1.00 22.99           N  
ATOM   1569  CA  THR A 218       3.508  15.918  33.236  1.00 23.37           C  
ATOM   1570  C   THR A 218       3.632  14.988  32.014  1.00 21.51           C  
ATOM   1571  O   THR A 218       2.659  14.357  31.609  1.00 22.00           O  
ATOM   1572  CB  THR A 218       3.553  17.381  32.790  1.00 23.35           C  
ATOM   1573  OG1 THR A 218       3.124  18.247  33.861  1.00 26.10           O  
ATOM   1574  CG2 THR A 218       2.544  17.667  31.698  1.00 25.44           C  
ATOM   1575  N   LEU A 219       4.813  14.919  31.434  1.00 20.67           N  
ATOM   1576  CA  LEU A 219       5.040  14.191  30.167  1.00 19.54           C  
ATOM   1577  C   LEU A 219       5.475  12.740  30.313  1.00 20.20           C  
ATOM   1578  O   LEU A 219       5.593  12.002  29.316  1.00 19.41           O  
ATOM   1579  CB  LEU A 219       6.045  14.991  29.316  1.00 20.35           C  
ATOM   1580  CG  LEU A 219       5.639  16.390  28.875  1.00 21.05           C  
ATOM   1581  CD1 LEU A 219       6.636  16.999  27.961  1.00 21.72           C  
ATOM   1582  CD2 LEU A 219       4.259  16.402  28.227  1.00 21.79           C  
ATOM   1583  N   GLY A 220       5.674  12.323  31.575  1.00 20.66           N  
ATOM   1584  CA  GLY A 220       6.227  11.042  31.910  1.00 20.59           C  
ATOM   1585  C   GLY A 220       7.730  11.118  31.944  1.00 20.83           C  
ATOM   1586  O   GLY A 220       8.373  11.849  31.147  1.00 20.02           O  
ATOM   1587  N   THR A 221       8.329  10.406  32.886  1.00 20.12           N  
ATOM   1588  CA  THR A 221       9.784  10.270  32.875  1.00 20.34           C  
ATOM   1589  C   THR A 221      10.203   9.605  31.580  1.00 20.13           C  
ATOM   1590  O   THR A 221       9.729   8.531  31.235  1.00 19.77           O  
ATOM   1591  CB  THR A 221      10.282   9.420  34.038  1.00 20.92           C  
ATOM   1592  OG1 THR A 221       9.883  10.004  35.302  1.00 21.83           O  
ATOM   1593  CG2 THR A 221      11.790   9.396  34.086  1.00 22.89           C  
ATOM   1594  N   PRO A 222      11.112  10.228  30.842  1.00 20.87           N  
ATOM   1595  CA  PRO A 222      11.509   9.689  29.554  1.00 20.05           C  
ATOM   1596  C   PRO A 222      12.407   8.470  29.703  1.00 22.20           C  
ATOM   1597  O   PRO A 222      13.148   8.367  30.671  1.00 21.97           O  
ATOM   1598  CB  PRO A 222      12.265  10.855  28.906  1.00 20.77           C  
ATOM   1599  CG  PRO A 222      12.729  11.669  30.021  1.00 20.35           C  
ATOM   1600  CD  PRO A 222      11.761  11.514  31.128  1.00 20.64           C  
ATOM   1601  N   ASP A 223      12.316   7.558  28.738  1.00 21.13           N  
ATOM   1602  CA  ASP A 223      13.092   6.348  28.725  1.00 22.71           C  
ATOM   1603  C   ASP A 223      13.537   6.088  27.292  1.00 22.22           C  
ATOM   1604  O   ASP A 223      13.303   6.889  26.391  1.00 21.64           O  
ATOM   1605  CB  ASP A 223      12.239   5.171  29.305  1.00 24.16           C  
ATOM   1606  CG  ASP A 223      10.921   4.964  28.544  1.00 28.57           C  
ATOM   1607  OD1 ASP A 223      10.829   5.374  27.364  1.00 28.49           O  
ATOM   1608  OD2 ASP A 223       9.896   4.468  29.075  1.00 34.09           O  
ATOM   1609  N   GLU A 224      14.189   4.963  27.065  1.00 22.76           N  
ATOM   1610  CA  GLU A 224      14.737   4.666  25.759  1.00 24.27           C  
ATOM   1611  C   GLU A 224      13.680   4.432  24.704  1.00 24.09           C  
ATOM   1612  O   GLU A 224      13.965   4.566  23.525  1.00 23.65           O  
ATOM   1613  CB  GLU A 224      15.684   3.470  25.827  1.00 25.06           C  
ATOM   1614  CG  GLU A 224      16.998   3.766  26.544  1.00 26.13           C  
ATOM   1615  CD  GLU A 224      17.949   4.651  25.753  1.00 26.21           C  
ATOM   1616  OE1 GLU A 224      17.906   4.640  24.519  1.00 23.30           O  
ATOM   1617  OE2 GLU A 224      18.760   5.389  26.370  1.00 26.65           O  
ATOM   1618  N   VAL A 225      12.477   4.083  25.124  1.00 24.72           N  
ATOM   1619  CA  VAL A 225      11.373   3.871  24.189  1.00 25.65           C  
ATOM   1620  C   VAL A 225      10.990   5.171  23.497  1.00 25.53           C  
ATOM   1621  O   VAL A 225      10.914   5.231  22.258  1.00 26.93           O  
ATOM   1622  CB  VAL A 225      10.066   3.345  24.878  1.00 26.31           C  
ATOM   1623  CG1 VAL A 225       8.986   3.057  23.786  1.00 27.52           C  
ATOM   1624  CG2 VAL A 225      10.299   2.124  25.781  1.00 29.34           C  
ATOM   1625  N   VAL A 226      10.711   6.206  24.286  1.00 24.07           N  
ATOM   1626  CA  VAL A 226      10.249   7.476  23.721  1.00 24.50           C  
ATOM   1627  C   VAL A 226      11.405   8.384  23.277  1.00 23.46           C  
ATOM   1628  O   VAL A 226      11.274   9.185  22.349  1.00 22.41           O  
ATOM   1629  CB  VAL A 226       9.262   8.207  24.664  1.00 25.23           C  
ATOM   1630  CG1 VAL A 226       8.112   7.295  24.986  1.00 27.47           C  
ATOM   1631  CG2 VAL A 226       9.937   8.646  25.945  1.00 26.27           C  
ATOM   1632  N   TRP A 227      12.564   8.191  23.879  1.00 22.70           N  
ATOM   1633  CA  TRP A 227      13.754   8.997  23.599  1.00 22.32           C  
ATOM   1634  C   TRP A 227      15.030   8.158  23.619  1.00 22.98           C  
ATOM   1635  O   TRP A 227      15.788   8.156  24.631  1.00 21.17           O  
ATOM   1636  CB  TRP A 227      13.855  10.118  24.625  1.00 22.02           C  
ATOM   1637  CG  TRP A 227      14.867  11.169  24.328  1.00 20.97           C  
ATOM   1638  CD1 TRP A 227      15.756  11.207  23.315  1.00 17.86           C  
ATOM   1639  CD2 TRP A 227      15.063  12.367  25.076  1.00 19.23           C  
ATOM   1640  NE1 TRP A 227      16.526  12.341  23.410  1.00 19.63           N  
ATOM   1641  CE2 TRP A 227      16.099  13.076  24.477  1.00 20.26           C  
ATOM   1642  CE3 TRP A 227      14.478  12.886  26.228  1.00 19.13           C  
ATOM   1643  CZ2 TRP A 227      16.539  14.311  24.962  1.00 25.31           C  
ATOM   1644  CZ3 TRP A 227      14.898  14.100  26.705  1.00 24.24           C  
ATOM   1645  CH2 TRP A 227      15.937  14.792  26.093  1.00 22.27           C  
ATOM   1646  N   PRO A 228      15.304   7.519  22.492  1.00 23.84           N  
ATOM   1647  CA  PRO A 228      16.540   6.758  22.302  1.00 24.78           C  
ATOM   1648  C   PRO A 228      17.783   7.609  22.561  1.00 25.09           C  
ATOM   1649  O   PRO A 228      17.878   8.744  22.100  1.00 23.98           O  
ATOM   1650  CB  PRO A 228      16.460   6.284  20.850  1.00 25.03           C  
ATOM   1651  CG  PRO A 228      15.064   6.389  20.470  1.00 25.88           C  
ATOM   1652  CD  PRO A 228      14.417   7.436  21.312  1.00 24.18           C  
ATOM   1653  N   GLY A 229      18.692   7.062  23.372  1.00 25.61           N  
ATOM   1654  CA  GLY A 229      19.855   7.770  23.878  1.00 25.55           C  
ATOM   1655  C   GLY A 229      19.686   8.543  25.178  1.00 26.13           C  
ATOM   1656  O   GLY A 229      20.682   8.982  25.741  1.00 25.96           O  
ATOM   1657  N   VAL A 230      18.453   8.747  25.653  1.00 24.94           N  
ATOM   1658  CA  VAL A 230      18.242   9.607  26.801  1.00 25.13           C  
ATOM   1659  C   VAL A 230      19.065   9.176  28.032  1.00 25.97           C  
ATOM   1660  O   VAL A 230      19.552  10.033  28.773  1.00 25.24           O  
ATOM   1661  CB  VAL A 230      16.755   9.738  27.204  1.00 24.94           C  
ATOM   1662  CG1 VAL A 230      16.143   8.449  27.691  1.00 22.83           C  
ATOM   1663  CG2 VAL A 230      16.557  10.858  28.244  1.00 25.06           C  
ATOM   1664  N   THR A 231      19.188   7.869  28.232  1.00 25.68           N  
ATOM   1665  CA  THR A 231      19.833   7.333  29.455  1.00 26.53           C  
ATOM   1666  C   THR A 231      21.330   7.487  29.431  1.00 28.42           C  
ATOM   1667  O   THR A 231      21.994   7.234  30.450  1.00 30.47           O  
ATOM   1668  CB  THR A 231      19.445   5.842  29.768  1.00 25.98           C  
ATOM   1669  OG1 THR A 231      19.888   4.943  28.718  1.00 25.17           O  
ATOM   1670  CG2 THR A 231      17.977   5.654  29.859  1.00 25.44           C  
ATOM   1671  N   SER A 232      21.860   7.891  28.282  1.00 29.69           N  
ATOM   1672  CA  SER A 232      23.281   8.141  28.088  1.00 31.32           C  
ATOM   1673  C   SER A 232      23.625   9.633  27.989  1.00 31.48           C  
ATOM   1674  O   SER A 232      24.746  10.014  27.613  1.00 33.37           O  
ATOM   1675  CB  SER A 232      23.732   7.399  26.844  1.00 31.17           C  
ATOM   1676  OG  SER A 232      23.541   6.005  27.045  1.00 34.13           O  
ATOM   1677  N   MET A 233      22.690  10.476  28.402  1.00 30.85           N  
ATOM   1678  CA  MET A 233      22.897  11.899  28.407  1.00 30.50           C  
ATOM   1679  C   MET A 233      23.662  12.314  29.661  1.00 29.93           C  
ATOM   1680  O   MET A 233      23.533  11.652  30.689  1.00 29.57           O  
ATOM   1681  CB  MET A 233      21.556  12.579  28.310  1.00 30.35           C  
ATOM   1682  CG  MET A 233      20.894  12.189  26.994  1.00 33.38           C  
ATOM   1683  SD  MET A 233      19.470  13.143  26.697  1.00 37.46           S  
ATOM   1684  CE  MET A 233      20.309  14.584  26.228  1.00 37.70           C  
ATOM   1685  N   PRO A 234      24.493  13.349  29.574  1.00 29.56           N  
ATOM   1686  CA  PRO A 234      25.456  13.658  30.662  1.00 29.03           C  
ATOM   1687  C   PRO A 234      24.880  13.740  32.075  1.00 29.23           C  
ATOM   1688  O   PRO A 234      25.528  13.263  33.027  1.00 27.68           O  
ATOM   1689  CB  PRO A 234      26.032  15.013  30.234  1.00 30.06           C  
ATOM   1690  CG  PRO A 234      26.015  14.912  28.721  1.00 29.37           C  
ATOM   1691  CD  PRO A 234      24.647  14.278  28.440  1.00 29.31           C  
ATOM   1692  N   ASP A 235      23.694  14.331  32.233  1.00 27.47           N  
ATOM   1693  CA  ASP A 235      23.093  14.494  33.544  1.00 27.45           C  
ATOM   1694  C   ASP A 235      21.899  13.605  33.811  1.00 26.59           C  
ATOM   1695  O   ASP A 235      21.178  13.816  34.759  1.00 27.16           O  
ATOM   1696  CB  ASP A 235      22.713  15.944  33.769  1.00 27.74           C  
ATOM   1697  CG  ASP A 235      23.876  16.862  33.606  1.00 30.21           C  
ATOM   1698  OD1 ASP A 235      24.923  16.628  34.247  1.00 33.52           O  
ATOM   1699  OD2 ASP A 235      23.862  17.799  32.822  1.00 29.67           O  
ATOM   1700  N   TYR A 236      21.686  12.615  32.961  1.00 25.67           N  
ATOM   1701  CA  TYR A 236      20.686  11.613  33.216  1.00 25.08           C  
ATOM   1702  C   TYR A 236      21.161  10.720  34.371  1.00 25.71           C  
ATOM   1703  O   TYR A 236      22.331  10.295  34.388  1.00 25.91           O  
ATOM   1704  CB  TYR A 236      20.430  10.737  31.990  1.00 24.28           C  
ATOM   1705  CG  TYR A 236      19.413   9.665  32.288  1.00 25.67           C  
ATOM   1706  CD1 TYR A 236      18.064   9.903  32.145  1.00 24.36           C  
ATOM   1707  CD2 TYR A 236      19.813   8.424  32.789  1.00 26.65           C  
ATOM   1708  CE1 TYR A 236      17.116   8.915  32.466  1.00 26.62           C  
ATOM   1709  CE2 TYR A 236      18.887   7.436  33.102  1.00 28.93           C  
ATOM   1710  CZ  TYR A 236      17.556   7.678  32.943  1.00 27.84           C  
ATOM   1711  OH  TYR A 236      16.676   6.691  33.286  1.00 29.40           O  
ATOM   1712  N   LYS A 237      20.232  10.419  35.278  1.00 25.40           N  
ATOM   1713  CA  LYS A 237      20.465   9.509  36.400  1.00 26.44           C  
ATOM   1714  C   LYS A 237      19.411   8.415  36.412  1.00 25.89           C  
ATOM   1715  O   LYS A 237      18.217   8.696  36.395  1.00 25.40           O  
ATOM   1716  CB  LYS A 237      20.395  10.221  37.766  1.00 26.26           C  
ATOM   1717  CG  LYS A 237      21.203  11.501  37.915  1.00 28.31           C  
ATOM   1718  CD  LYS A 237      22.692  11.241  38.015  1.00 32.99           C  
ATOM   1719  CE  LYS A 237      23.563  12.477  37.795  1.00 34.24           C  
ATOM   1720  NZ  LYS A 237      24.985  12.020  37.455  1.00 32.78           N  
ATOM   1721  N   PRO A 238      19.852   7.159  36.485  1.00 26.44           N  
ATOM   1722  CA  PRO A 238      18.933   6.025  36.622  1.00 25.89           C  
ATOM   1723  C   PRO A 238      18.026   6.146  37.849  1.00 25.71           C  
ATOM   1724  O   PRO A 238      16.935   5.550  37.885  1.00 26.32           O  
ATOM   1725  CB  PRO A 238      19.877   4.829  36.741  1.00 26.46           C  
ATOM   1726  CG  PRO A 238      21.164   5.267  36.189  1.00 26.05           C  
ATOM   1727  CD  PRO A 238      21.266   6.730  36.384  1.00 25.69           C  
ATOM   1728  N   SER A 239      18.475   6.929  38.825  1.00 24.60           N  
ATOM   1729  CA  SER A 239      17.714   7.178  40.046  1.00 23.70           C  
ATOM   1730  C   SER A 239      16.556   8.209  39.892  1.00 23.36           C  
ATOM   1731  O   SER A 239      15.820   8.477  40.832  1.00 22.27           O  
ATOM   1732  CB  SER A 239      18.686   7.599  41.148  1.00 23.28           C  
ATOM   1733  OG  SER A 239      19.389   8.773  40.809  1.00 22.67           O  
ATOM   1734  N   PHE A 240      16.400   8.824  38.722  1.00 24.37           N  
ATOM   1735  CA  PHE A 240      15.259   9.707  38.497  1.00 23.92           C  
ATOM   1736  C   PHE A 240      14.007   8.914  38.775  1.00 24.87           C  
ATOM   1737  O   PHE A 240      13.884   7.754  38.337  1.00 24.40           O  
ATOM   1738  CB  PHE A 240      15.149  10.161  37.018  1.00 24.62           C  
ATOM   1739  CG  PHE A 240      16.124  11.186  36.604  1.00 22.06           C  
ATOM   1740  CD1 PHE A 240      16.758  12.026  37.513  1.00 24.64           C  
ATOM   1741  CD2 PHE A 240      16.423  11.318  35.270  1.00 23.75           C  
ATOM   1742  CE1 PHE A 240      17.633  13.005  37.091  1.00 24.31           C  
ATOM   1743  CE2 PHE A 240      17.314  12.293  34.833  1.00 23.59           C  
ATOM   1744  CZ  PHE A 240      17.919  13.140  35.770  1.00 23.55           C  
ATOM   1745  N   PRO A 241      13.087   9.508  39.511  1.00 25.92           N  
ATOM   1746  CA  PRO A 241      11.783   8.890  39.714  1.00 27.44           C  
ATOM   1747  C   PRO A 241      11.079   8.658  38.392  1.00 28.86           C  
ATOM   1748  O   PRO A 241      11.216   9.455  37.458  1.00 28.35           O  
ATOM   1749  CB  PRO A 241      11.035   9.913  40.561  1.00 26.87           C  
ATOM   1750  CG  PRO A 241      12.118  10.635  41.286  1.00 27.67           C  
ATOM   1751  CD  PRO A 241      13.233  10.760  40.278  1.00 25.79           C  
ATOM   1752  N   LYS A 242      10.335   7.568  38.335  1.00 30.20           N  
ATOM   1753  CA  LYS A 242       9.597   7.205  37.144  1.00 31.61           C  
ATOM   1754  C   LYS A 242       8.135   7.597  37.344  1.00 31.77           C  
ATOM   1755  O   LYS A 242       7.402   6.953  38.104  1.00 32.44           O  
ATOM   1756  CB  LYS A 242       9.781   5.714  36.862  1.00 32.53           C  
ATOM   1757  CG  LYS A 242      11.248   5.325  36.752  1.00 34.69           C  
ATOM   1758  CD  LYS A 242      11.510   4.082  35.879  1.00 38.35           C  
ATOM   1759  CE  LYS A 242      12.382   3.044  36.556  1.00 40.47           C  
ATOM   1760  NZ  LYS A 242      13.810   3.167  36.120  1.00 42.70           N  
ATOM   1761  N   TRP A 243       7.730   8.694  36.699  1.00 30.30           N  
ATOM   1762  CA  TRP A 243       6.354   9.176  36.734  1.00 30.44           C  
ATOM   1763  C   TRP A 243       5.671   8.808  35.430  1.00 30.53           C  
ATOM   1764  O   TRP A 243       6.346   8.745  34.389  1.00 27.70           O  
ATOM   1765  CB  TRP A 243       6.323  10.680  36.881  1.00 30.98           C  
ATOM   1766  CG  TRP A 243       6.703  11.235  38.240  1.00 33.02           C  
ATOM   1767  CD1 TRP A 243       5.942  11.246  39.383  1.00 35.70           C  
ATOM   1768  CD2 TRP A 243       7.921  11.891  38.569  1.00 31.39           C  
ATOM   1769  NE1 TRP A 243       6.630  11.862  40.403  1.00 35.66           N  
ATOM   1770  CE2 TRP A 243       7.855  12.253  39.931  1.00 33.58           C  
ATOM   1771  CE3 TRP A 243       9.090  12.173  37.860  1.00 33.26           C  
ATOM   1772  CZ2 TRP A 243       8.889  12.913  40.574  1.00 33.66           C  
ATOM   1773  CZ3 TRP A 243      10.116  12.809  38.501  1.00 34.09           C  
ATOM   1774  CH2 TRP A 243      10.006  13.189  39.848  1.00 33.37           C  
ATOM   1775  N   ALA A 244       4.353   8.589  35.473  1.00 30.96           N  
ATOM   1776  CA  ALA A 244       3.603   8.265  34.247  1.00 32.24           C  
ATOM   1777  C   ALA A 244       3.217   9.536  33.524  1.00 32.47           C  
ATOM   1778  O   ALA A 244       3.073  10.601  34.145  1.00 32.66           O  
ATOM   1779  CB  ALA A 244       2.345   7.433  34.565  1.00 32.62           C  
ATOM   1780  N   ARG A 245       3.048   9.438  32.210  1.00 32.36           N  
ATOM   1781  CA  ARG A 245       2.566  10.588  31.450  1.00 33.40           C  
ATOM   1782  C   ARG A 245       1.119  10.905  31.853  1.00 34.66           C  
ATOM   1783  O   ARG A 245       0.347   9.984  32.150  1.00 33.96           O  
ATOM   1784  CB  ARG A 245       2.658  10.298  29.953  1.00 33.31           C  
ATOM   1785  CG  ARG A 245       2.331  11.454  28.992  1.00 33.03           C  
ATOM   1786  CD  ARG A 245       2.514  11.050  27.520  1.00 33.35           C  
ATOM   1787  NE  ARG A 245       2.384  12.137  26.543  1.00 32.59           N  
ATOM   1788  CZ  ARG A 245       3.362  12.984  26.183  1.00 32.23           C  
ATOM   1789  NH1 ARG A 245       4.576  12.909  26.727  1.00 31.95           N  
ATOM   1790  NH2 ARG A 245       3.127  13.929  25.264  1.00 31.24           N  
ATOM   1791  N   GLN A 246       0.798  12.205  31.894  1.00 36.49           N  
ATOM   1792  CA  GLN A 246      -0.579  12.738  31.894  1.00 38.08           C  
ATOM   1793  C   GLN A 246      -1.124  12.935  30.468  1.00 38.14           C  
ATOM   1794  O   GLN A 246      -0.390  13.299  29.544  1.00 39.24           O  
ATOM   1795  CB  GLN A 246      -0.647  14.131  32.567  1.00 37.74           C  
ATOM   1796  CG  GLN A 246      -0.373  14.202  34.073  1.00 40.83           C  
ATOM   1797  CD  GLN A 246      -0.657  15.594  34.680  1.00 42.99           C  
ATOM   1798  OE1 GLN A 246      -0.788  16.603  33.964  1.00 43.94           O  
ATOM   1799  NE2 GLN A 246      -0.744  15.646  36.004  1.00 47.07           N  
ATOM   1800  N   ASP A 247      -2.448  12.826  30.330  1.00 39.57           N  
ATOM   1801  CA  ASP A 247      -3.158  13.213  29.107  1.00 38.99           C  
ATOM   1802  C   ASP A 247      -3.073  14.704  28.816  1.00 38.57           C  
ATOM   1803  O   ASP A 247      -3.247  15.508  29.716  1.00 38.88           O  
ATOM   1804  CB  ASP A 247      -4.651  12.893  29.263  1.00 40.55           C  
ATOM   1805  CG  ASP A 247      -5.103  11.805  28.372  1.00 42.80           C  
ATOM   1806  OD1 ASP A 247      -5.818  12.120  27.384  1.00 50.08           O  
ATOM   1807  OD2 ASP A 247      -4.791  10.612  28.574  1.00 46.82           O  
ATOM   1808  N   PHE A 248      -2.880  15.080  27.553  1.00 37.17           N  
ATOM   1809  CA  PHE A 248      -2.926  16.495  27.156  1.00 36.99           C  
ATOM   1810  C   PHE A 248      -4.261  17.180  27.398  1.00 35.20           C  
ATOM   1811  O   PHE A 248      -4.324  18.397  27.612  1.00 36.24           O  
ATOM   1812  CB  PHE A 248      -2.496  16.641  25.683  1.00 37.64           C  
ATOM   1813  CG  PHE A 248      -1.062  16.891  25.539  1.00 38.08           C  
ATOM   1814  CD1 PHE A 248      -0.146  16.100  26.205  1.00 40.81           C  
ATOM   1815  CD2 PHE A 248      -0.605  17.961  24.804  1.00 40.39           C  
ATOM   1816  CE1 PHE A 248       1.218  16.353  26.097  1.00 41.01           C  
ATOM   1817  CE2 PHE A 248       0.752  18.214  24.708  1.00 41.97           C  
ATOM   1818  CZ  PHE A 248       1.659  17.409  25.357  1.00 40.57           C  
ATOM   1819  N   SER A 249      -5.338  16.396  27.402  1.00 34.05           N  
ATOM   1820  CA  SER A 249      -6.642  16.917  27.706  1.00 31.86           C  
ATOM   1821  C   SER A 249      -6.646  17.577  29.101  1.00 30.81           C  
ATOM   1822  O   SER A 249      -7.343  18.551  29.292  1.00 30.40           O  
ATOM   1823  CB  SER A 249      -7.714  15.814  27.589  1.00 32.70           C  
ATOM   1824  OG  SER A 249      -7.527  14.795  28.555  1.00 30.48           O  
ATOM   1825  N   LYS A 250      -5.871  17.033  30.044  1.00 30.23           N  
ATOM   1826  CA  LYS A 250      -5.723  17.604  31.388  1.00 30.71           C  
ATOM   1827  C   LYS A 250      -4.726  18.756  31.462  1.00 30.80           C  
ATOM   1828  O   LYS A 250      -4.824  19.611  32.354  1.00 30.44           O  
ATOM   1829  CB  LYS A 250      -5.303  16.528  32.385  1.00 31.86           C  
ATOM   1830  CG  LYS A 250      -5.205  17.022  33.802  1.00 34.43           C  
ATOM   1831  CD  LYS A 250      -5.232  15.877  34.813  1.00 37.84           C  
ATOM   1832  CE  LYS A 250      -3.968  15.799  35.660  1.00 40.85           C  
ATOM   1833  NZ  LYS A 250      -3.487  14.386  35.755  1.00 41.98           N  
ATOM   1834  N   VAL A 251      -3.799  18.798  30.511  1.00 29.66           N  
ATOM   1835  CA  VAL A 251      -2.683  19.756  30.549  1.00 30.17           C  
ATOM   1836  C   VAL A 251      -3.055  21.126  30.007  1.00 29.91           C  
ATOM   1837  O   VAL A 251      -2.719  22.159  30.641  1.00 30.28           O  
ATOM   1838  CB  VAL A 251      -1.413  19.159  29.899  1.00 30.76           C  
ATOM   1839  CG1 VAL A 251      -0.269  20.157  29.801  1.00 32.35           C  
ATOM   1840  CG2 VAL A 251      -0.963  17.993  30.712  1.00 32.17           C  
ATOM   1841  N   VAL A 252      -3.808  21.173  28.910  1.00 28.09           N  
ATOM   1842  CA  VAL A 252      -4.120  22.443  28.311  1.00 28.38           C  
ATOM   1843  C   VAL A 252      -5.585  22.627  27.965  1.00 28.72           C  
ATOM   1844  O   VAL A 252      -5.911  23.183  26.947  1.00 27.77           O  
ATOM   1845  CB  VAL A 252      -3.233  22.693  27.059  1.00 28.80           C  
ATOM   1846  CG1 VAL A 252      -1.801  22.940  27.471  1.00 28.85           C  
ATOM   1847  CG2 VAL A 252      -3.305  21.514  26.098  1.00 28.76           C  
ATOM   1848  N   PRO A 253      -6.498  22.250  28.852  1.00 28.53           N  
ATOM   1849  CA  PRO A 253      -7.899  22.431  28.520  1.00 29.79           C  
ATOM   1850  C   PRO A 253      -8.094  23.942  28.495  1.00 31.02           C  
ATOM   1851  O   PRO A 253      -7.409  24.672  29.224  1.00 29.80           O  
ATOM   1852  CB  PRO A 253      -8.629  21.784  29.717  1.00 29.41           C  
ATOM   1853  CG  PRO A 253      -7.692  21.839  30.793  1.00 28.93           C  
ATOM   1854  CD  PRO A 253      -6.314  21.774  30.222  1.00 28.65           C  
ATOM   1855  N   PRO A 254      -9.028  24.443  27.716  1.00 32.71           N  
ATOM   1856  CA  PRO A 254      -9.871  23.684  26.805  1.00 33.16           C  
ATOM   1857  C   PRO A 254      -9.434  23.765  25.356  1.00 32.61           C  
ATOM   1858  O   PRO A 254     -10.299  23.845  24.488  1.00 33.57           O  
ATOM   1859  CB  PRO A 254     -11.233  24.360  27.007  1.00 34.45           C  
ATOM   1860  CG  PRO A 254     -10.911  25.758  27.363  1.00 34.16           C  
ATOM   1861  CD  PRO A 254      -9.465  25.836  27.827  1.00 33.72           C  
ATOM   1862  N   LEU A 255      -8.125  23.738  25.103  1.00 30.04           N  
ATOM   1863  CA  LEU A 255      -7.580  23.789  23.766  1.00 28.15           C  
ATOM   1864  C   LEU A 255      -8.088  22.598  22.959  1.00 26.41           C  
ATOM   1865  O   LEU A 255      -8.116  21.492  23.463  1.00 24.45           O  
ATOM   1866  CB  LEU A 255      -6.058  23.766  23.828  1.00 27.29           C  
ATOM   1867  CG  LEU A 255      -5.294  23.891  22.501  1.00 27.25           C  
ATOM   1868  CD1 LEU A 255      -5.473  25.238  21.850  1.00 28.81           C  
ATOM   1869  CD2 LEU A 255      -3.874  23.678  22.758  1.00 25.19           C  
ATOM   1870  N   ASP A 256      -8.473  22.871  21.723  1.00 24.34           N  
ATOM   1871  CA  ASP A 256      -9.097  21.890  20.828  1.00 24.22           C  
ATOM   1872  C   ASP A 256      -8.120  20.842  20.328  1.00 22.50           C  
ATOM   1873  O   ASP A 256      -6.940  20.982  20.542  1.00 20.05           O  
ATOM   1874  CB  ASP A 256      -9.788  22.609  19.650  1.00 23.87           C  
ATOM   1875  CG  ASP A 256      -8.813  23.319  18.719  1.00 25.00           C  
ATOM   1876  OD1 ASP A 256      -7.893  22.691  18.168  1.00 22.07           O  
ATOM   1877  OD2 ASP A 256      -8.914  24.520  18.461  1.00 28.06           O  
ATOM   1878  N   GLU A 257      -8.615  19.809  19.623  1.00 21.53           N  
ATOM   1879  CA  GLU A 257      -7.809  18.640  19.313  1.00 21.86           C  
ATOM   1880  C   GLU A 257      -6.681  19.006  18.366  1.00 19.99           C  
ATOM   1881  O   GLU A 257      -5.602  18.430  18.461  1.00 19.81           O  
ATOM   1882  CB  GLU A 257      -8.651  17.477  18.735  1.00 22.76           C  
ATOM   1883  CG  GLU A 257      -7.906  16.148  18.654  1.00 25.72           C  
ATOM   1884  CD  GLU A 257      -7.385  15.684  20.005  1.00 31.85           C  
ATOM   1885  OE1 GLU A 257      -8.211  15.478  20.892  1.00 36.93           O  
ATOM   1886  OE2 GLU A 257      -6.159  15.552  20.179  1.00 35.19           O  
ATOM   1887  N   ASP A 258      -6.914  19.946  17.459  1.00 18.48           N  
ATOM   1888  CA  ASP A 258      -5.838  20.419  16.577  1.00 19.34           C  
ATOM   1889  C   ASP A 258      -4.712  21.072  17.369  1.00 19.08           C  
ATOM   1890  O   ASP A 258      -3.519  20.804  17.156  1.00 17.48           O  
ATOM   1891  CB  ASP A 258      -6.336  21.439  15.562  1.00 19.08           C  
ATOM   1892  CG  ASP A 258      -7.151  20.811  14.434  1.00 22.33           C  
ATOM   1893  OD1 ASP A 258      -6.756  19.736  13.930  1.00 23.08           O  
ATOM   1894  OD2 ASP A 258      -8.189  21.355  13.987  1.00 23.66           O  
ATOM   1895  N   GLY A 259      -5.071  21.981  18.265  1.00 19.12           N  
ATOM   1896  CA  GLY A 259      -4.004  22.596  19.027  1.00 18.69           C  
ATOM   1897  C   GLY A 259      -3.303  21.614  19.935  1.00 18.54           C  
ATOM   1898  O   GLY A 259      -2.101  21.720  20.159  1.00 17.74           O  
ATOM   1899  N   ARG A 260      -4.045  20.692  20.553  1.00 19.15           N  
ATOM   1900  CA  ARG A 260      -3.391  19.716  21.444  1.00 20.07           C  
ATOM   1901  C   ARG A 260      -2.425  18.821  20.662  1.00 19.66           C  
ATOM   1902  O   ARG A 260      -1.332  18.511  21.131  1.00 18.82           O  
ATOM   1903  CB  ARG A 260      -4.422  18.882  22.199  1.00 20.26           C  
ATOM   1904  CG  ARG A 260      -5.292  19.752  23.051  1.00 25.56           C  
ATOM   1905  CD  ARG A 260      -6.122  19.059  24.150  1.00 26.80           C  
ATOM   1906  NE  ARG A 260      -6.828  17.863  23.691  1.00 32.97           N  
ATOM   1907  CZ  ARG A 260      -8.108  17.787  23.296  1.00 34.52           C  
ATOM   1908  NH1 ARG A 260      -8.611  16.615  22.943  1.00 37.15           N  
ATOM   1909  NH2 ARG A 260      -8.885  18.850  23.215  1.00 37.52           N  
ATOM   1910  N   SER A 261      -2.876  18.356  19.494  1.00 19.22           N  
ATOM   1911  CA  SER A 261      -2.029  17.624  18.560  1.00 19.63           C  
ATOM   1912  C   SER A 261      -0.738  18.355  18.264  1.00 18.63           C  
ATOM   1913  O   SER A 261       0.370  17.775  18.409  1.00 17.84           O  
ATOM   1914  CB  SER A 261      -2.794  17.380  17.258  1.00 20.01           C  
ATOM   1915  OG  SER A 261      -2.021  16.582  16.424  1.00 24.46           O  
ATOM   1916  N   LEU A 262      -0.851  19.628  17.847  1.00 18.03           N  
ATOM   1917  CA  LEU A 262       0.337  20.417  17.520  1.00 17.65           C  
ATOM   1918  C   LEU A 262       1.228  20.585  18.764  1.00 17.32           C  
ATOM   1919  O   LEU A 262       2.440  20.390  18.685  1.00 18.09           O  
ATOM   1920  CB  LEU A 262      -0.014  21.790  16.950  1.00 16.48           C  
ATOM   1921  CG  LEU A 262       1.115  22.802  16.819  1.00 18.42           C  
ATOM   1922  CD1 LEU A 262       2.204  22.216  15.967  1.00 21.69           C  
ATOM   1923  CD2 LEU A 262       0.579  24.111  16.243  1.00 17.91           C  
ATOM   1924  N   LEU A 263       0.618  20.886  19.897  1.00 17.48           N  
ATOM   1925  CA  LEU A 263       1.426  21.118  21.093  1.00 17.25           C  
ATOM   1926  C   LEU A 263       2.182  19.829  21.464  1.00 16.54           C  
ATOM   1927  O   LEU A 263       3.344  19.861  21.852  1.00 16.55           O  
ATOM   1928  CB  LEU A 263       0.548  21.614  22.238  1.00 16.91           C  
ATOM   1929  CG  LEU A 263       1.353  21.711  23.536  1.00 16.72           C  
ATOM   1930  CD1 LEU A 263       2.235  22.923  23.457  1.00 16.09           C  
ATOM   1931  CD2 LEU A 263       0.432  21.761  24.741  1.00 18.49           C  
ATOM   1932  N   SER A 264       1.505  18.693  21.368  1.00 17.40           N  
ATOM   1933  CA  SER A 264       2.137  17.389  21.641  1.00 18.51           C  
ATOM   1934  C   SER A 264       3.365  17.164  20.778  1.00 18.06           C  
ATOM   1935  O   SER A 264       4.374  16.667  21.231  1.00 16.75           O  
ATOM   1936  CB  SER A 264       1.122  16.231  21.558  1.00 19.23           C  
ATOM   1937  OG  SER A 264       0.817  15.867  20.216  1.00 23.17           O  
ATOM   1938  N   GLN A 265       3.298  17.572  19.522  1.00 16.59           N  
ATOM   1939  CA  GLN A 265       4.437  17.430  18.636  1.00 17.42           C  
ATOM   1940  C   GLN A 265       5.578  18.425  18.938  1.00 17.30           C  
ATOM   1941  O   GLN A 265       6.722  18.122  18.675  1.00 17.59           O  
ATOM   1942  CB  GLN A 265       3.980  17.526  17.191  1.00 18.14           C  
ATOM   1943  CG  GLN A 265       3.038  16.413  16.806  1.00 18.27           C  
ATOM   1944  CD  GLN A 265       2.814  16.351  15.285  1.00 20.94           C  
ATOM   1945  OE1 GLN A 265       2.266  17.256  14.727  1.00 23.81           O  
ATOM   1946  NE2 GLN A 265       3.295  15.314  14.651  1.00 24.72           N  
ATOM   1947  N   MET A 266       5.261  19.573  19.527  1.00 16.25           N  
ATOM   1948  CA  MET A 266       6.266  20.552  19.870  1.00 16.47           C  
ATOM   1949  C   MET A 266       6.935  20.134  21.193  1.00 16.92           C  
ATOM   1950  O   MET A 266       7.975  20.653  21.508  1.00 16.22           O  
ATOM   1951  CB  MET A 266       5.645  21.952  20.032  1.00 17.38           C  
ATOM   1952  CG  MET A 266       4.966  22.494  18.737  1.00 17.24           C  
ATOM   1953  SD  MET A 266       4.155  24.076  18.990  1.00 18.00           S  
ATOM   1954  CE  MET A 266       5.562  25.143  19.051  1.00 16.53           C  
ATOM   1955  N   LEU A 267       6.308  19.222  21.942  1.00 17.29           N  
ATOM   1956  CA  LEU A 267       6.800  18.831  23.270  1.00 17.99           C  
ATOM   1957  C   LEU A 267       7.318  17.387  23.306  1.00 18.85           C  
ATOM   1958  O   LEU A 267       7.533  16.813  24.388  1.00 18.58           O  
ATOM   1959  CB  LEU A 267       5.705  19.029  24.301  1.00 18.10           C  
ATOM   1960  CG  LEU A 267       5.365  20.504  24.592  1.00 18.71           C  
ATOM   1961  CD1 LEU A 267       4.433  20.583  25.778  1.00 19.56           C  
ATOM   1962  CD2 LEU A 267       6.608  21.363  24.830  1.00 21.02           C  
ATOM   1963  N   HIS A 268       7.529  16.788  22.140  1.00 19.23           N  
ATOM   1964  CA  HIS A 268       8.137  15.456  22.093  1.00 20.10           C  
ATOM   1965  C   HIS A 268       9.504  15.522  22.756  1.00 18.77           C  
ATOM   1966  O   HIS A 268      10.314  16.477  22.580  1.00 16.79           O  
ATOM   1967  CB  HIS A 268       8.268  14.914  20.662  1.00 21.52           C  
ATOM   1968  CG  HIS A 268       7.022  14.254  20.156  1.00 25.42           C  
ATOM   1969  ND1 HIS A 268       6.656  14.282  18.821  1.00 31.29           N  
ATOM   1970  CD2 HIS A 268       6.027  13.602  20.804  1.00 28.59           C  
ATOM   1971  CE1 HIS A 268       5.504  13.653  18.670  1.00 27.76           C  
ATOM   1972  NE2 HIS A 268       5.088  13.254  19.863  1.00 31.58           N  
ATOM   1973  N   TYR A 269       9.761  14.513  23.565  1.00 18.98           N  
ATOM   1974  CA  TYR A 269      11.055  14.440  24.236  1.00 18.60           C  
ATOM   1975  C   TYR A 269      12.210  14.373  23.273  1.00 18.66           C  
ATOM   1976  O   TYR A 269      13.185  15.059  23.440  1.00 18.82           O  
ATOM   1977  CB  TYR A 269      11.105  13.209  25.140  1.00 17.86           C  
ATOM   1978  CG  TYR A 269      10.585  13.490  26.497  1.00 18.32           C  
ATOM   1979  CD1 TYR A 269      11.220  14.419  27.320  1.00 17.64           C  
ATOM   1980  CD2 TYR A 269       9.487  12.793  26.994  1.00 16.76           C  
ATOM   1981  CE1 TYR A 269      10.743  14.650  28.596  1.00 18.67           C  
ATOM   1982  CE2 TYR A 269       9.040  12.977  28.284  1.00 20.66           C  
ATOM   1983  CZ  TYR A 269       9.659  13.919  29.075  1.00 19.15           C  
ATOM   1984  OH  TYR A 269       9.132  14.116  30.322  1.00 18.16           O  
ATOM   1985  N   ASP A 270      12.148  13.487  22.279  1.00 19.85           N  
ATOM   1986  CA  ASP A 270      13.286  13.246  21.407  1.00 20.26           C  
ATOM   1987  C   ASP A 270      13.353  14.460  20.488  1.00 21.44           C  
ATOM   1988  O   ASP A 270      12.382  14.692  19.725  1.00 21.53           O  
ATOM   1989  CB  ASP A 270      13.032  11.993  20.570  1.00 20.06           C  
ATOM   1990  CG  ASP A 270      14.183  11.595  19.723  1.00 20.31           C  
ATOM   1991  OD1 ASP A 270      15.053  12.419  19.418  1.00 20.27           O  
ATOM   1992  OD2 ASP A 270      14.254  10.436  19.269  1.00 22.51           O  
ATOM   1993  N   PRO A 271      14.446  15.219  20.515  1.00 22.34           N  
ATOM   1994  CA  PRO A 271      14.553  16.406  19.666  1.00 23.34           C  
ATOM   1995  C   PRO A 271      14.376  16.071  18.193  1.00 25.13           C  
ATOM   1996  O   PRO A 271      13.958  16.923  17.394  1.00 24.50           O  
ATOM   1997  CB  PRO A 271      15.976  16.893  19.926  1.00 24.15           C  
ATOM   1998  CG  PRO A 271      16.352  16.297  21.269  1.00 23.31           C  
ATOM   1999  CD  PRO A 271      15.630  15.062  21.393  1.00 23.13           C  
ATOM   2000  N   ASN A 272      14.679  14.834  17.825  1.00 26.16           N  
ATOM   2001  CA  ASN A 272      14.522  14.405  16.440  1.00 28.69           C  
ATOM   2002  C   ASN A 272      13.115  14.068  15.998  1.00 28.38           C  
ATOM   2003  O   ASN A 272      12.817  14.059  14.791  1.00 30.73           O  
ATOM   2004  CB  ASN A 272      15.524  13.288  16.115  1.00 29.15           C  
ATOM   2005  CG  ASN A 272      16.628  13.796  15.274  1.00 32.90           C  
ATOM   2006  OD1 ASN A 272      17.519  14.490  15.777  1.00 41.50           O  
ATOM   2007  ND2 ASN A 272      16.543  13.569  13.959  1.00 36.30           N  
ATOM   2008  N   LYS A 273      12.259  13.747  16.960  1.00 27.04           N  
ATOM   2009  CA  LYS A 273      10.848  13.537  16.725  1.00 26.92           C  
ATOM   2010  C   LYS A 273      10.101  14.851  16.795  1.00 23.44           C  
ATOM   2011  O   LYS A 273       9.036  14.974  16.237  1.00 21.57           O  
ATOM   2012  CB  LYS A 273      10.269  12.596  17.795  1.00 27.78           C  
ATOM   2013  CG  LYS A 273       9.257  11.637  17.294  1.00 34.42           C  
ATOM   2014  CD  LYS A 273       9.905  10.383  16.669  1.00 39.33           C  
ATOM   2015  CE  LYS A 273       9.150   9.105  17.023  1.00 41.14           C  
ATOM   2016  NZ  LYS A 273       8.998   8.203  15.875  1.00 41.00           N  
ATOM   2017  N   ARG A 274      10.670  15.828  17.501  1.00 21.13           N  
ATOM   2018  CA  ARG A 274      10.000  17.081  17.767  1.00 19.46           C  
ATOM   2019  C   ARG A 274       9.719  17.796  16.428  1.00 19.41           C  
ATOM   2020  O   ARG A 274      10.558  17.811  15.570  1.00 18.21           O  
ATOM   2021  CB  ARG A 274      10.877  17.968  18.649  1.00 19.05           C  
ATOM   2022  CG  ARG A 274      10.113  18.997  19.497  1.00 18.24           C  
ATOM   2023  CD  ARG A 274      10.974  19.718  20.513  1.00 18.11           C  
ATOM   2024  NE  ARG A 274      11.469  18.786  21.514  1.00 16.02           N  
ATOM   2025  CZ  ARG A 274      12.618  18.917  22.141  1.00 13.19           C  
ATOM   2026  NH1 ARG A 274      13.361  19.987  21.924  1.00 14.37           N  
ATOM   2027  NH2 ARG A 274      13.007  17.994  23.038  1.00 16.09           N  
ATOM   2028  N   ILE A 275       8.540  18.372  16.284  1.00 19.31           N  
ATOM   2029  CA  ILE A 275       8.154  18.972  14.994  1.00 18.82           C  
ATOM   2030  C   ILE A 275       9.057  20.169  14.690  1.00 18.76           C  
ATOM   2031  O   ILE A 275       9.463  20.912  15.584  1.00 18.31           O  
ATOM   2032  CB  ILE A 275       6.647  19.310  14.998  1.00 18.85           C  
ATOM   2033  CG1 ILE A 275       6.153  19.647  13.590  1.00 19.74           C  
ATOM   2034  CG2 ILE A 275       6.320  20.467  15.940  1.00 18.78           C  
ATOM   2035  CD1 ILE A 275       4.670  19.761  13.486  1.00 20.36           C  
ATOM   2036  N   SER A 276       9.399  20.331  13.419  1.00 17.64           N  
ATOM   2037  CA  SER A 276      10.115  21.500  12.962  1.00 18.50           C  
ATOM   2038  C   SER A 276       9.152  22.681  12.800  1.00 17.58           C  
ATOM   2039  O   SER A 276       7.949  22.475  12.680  1.00 17.65           O  
ATOM   2040  CB  SER A 276      10.829  21.208  11.651  1.00 19.31           C  
ATOM   2041  OG  SER A 276       9.877  21.188  10.615  1.00 20.24           O  
ATOM   2042  N   ALA A 277       9.673  23.892  12.810  1.00 18.50           N  
ATOM   2043  CA  ALA A 277       8.864  25.098  12.597  1.00 18.93           C  
ATOM   2044  C   ALA A 277       8.146  25.003  11.266  1.00 20.00           C  
ATOM   2045  O   ALA A 277       6.945  25.240  11.177  1.00 20.65           O  
ATOM   2046  CB  ALA A 277       9.688  26.358  12.675  1.00 17.85           C  
ATOM   2047  N   LYS A 278       8.899  24.649  10.232  1.00 21.46           N  
ATOM   2048  CA  LYS A 278       8.340  24.553   8.894  1.00 22.90           C  
ATOM   2049  C   LYS A 278       7.204  23.567   8.805  1.00 22.00           C  
ATOM   2050  O   LYS A 278       6.173  23.888   8.286  1.00 20.83           O  
ATOM   2051  CB  LYS A 278       9.435  24.261   7.869  1.00 24.78           C  
ATOM   2052  CG  LYS A 278       9.011  24.580   6.444  1.00 29.32           C  
ATOM   2053  CD  LYS A 278       8.593  26.054   6.232  1.00 34.06           C  
ATOM   2054  CE  LYS A 278       7.896  26.240   4.875  1.00 36.73           C  
ATOM   2055  NZ  LYS A 278       7.156  27.530   4.717  1.00 36.08           N  
ATOM   2056  N   ALA A 279       7.351  22.376   9.375  1.00 22.45           N  
ATOM   2057  CA  ALA A 279       6.248  21.414   9.411  1.00 21.84           C  
ATOM   2058  C   ALA A 279       5.071  21.870  10.273  1.00 21.76           C  
ATOM   2059  O   ALA A 279       3.883  21.621   9.962  1.00 19.71           O  
ATOM   2060  CB  ALA A 279       6.758  20.086   9.877  1.00 22.01           C  
ATOM   2061  N   ALA A 280       5.380  22.582  11.360  1.00 20.44           N  
ATOM   2062  CA  ALA A 280       4.326  23.034  12.235  1.00 20.10           C  
ATOM   2063  C   ALA A 280       3.393  24.025  11.505  1.00 20.22           C  
ATOM   2064  O   ALA A 280       2.190  24.027  11.714  1.00 18.43           O  
ATOM   2065  CB  ALA A 280       4.931  23.666  13.462  1.00 20.21           C  
ATOM   2066  N   LEU A 281       3.962  24.836  10.623  1.00 20.30           N  
ATOM   2067  CA  LEU A 281       3.217  25.807   9.872  1.00 20.56           C  
ATOM   2068  C   LEU A 281       2.154  25.133   8.973  1.00 21.69           C  
ATOM   2069  O   LEU A 281       1.156  25.780   8.605  1.00 21.25           O  
ATOM   2070  CB  LEU A 281       4.160  26.651   8.989  1.00 20.83           C  
ATOM   2071  CG  LEU A 281       5.104  27.557   9.786  1.00 21.12           C  
ATOM   2072  CD1 LEU A 281       6.182  28.100   8.867  1.00 23.26           C  
ATOM   2073  CD2 LEU A 281       4.310  28.670  10.392  1.00 23.23           C  
ATOM   2074  N   ALA A 282       2.388  23.879   8.613  1.00 20.85           N  
ATOM   2075  CA  ALA A 282       1.458  23.114   7.772  1.00 21.79           C  
ATOM   2076  C   ALA A 282       0.427  22.362   8.600  1.00 21.51           C  
ATOM   2077  O   ALA A 282      -0.474  21.745   8.054  1.00 20.96           O  
ATOM   2078  CB  ALA A 282       2.219  22.168   6.846  1.00 22.27           C  
ATOM   2079  N   HIS A 283       0.489  22.459   9.924  1.00 20.68           N  
ATOM   2080  CA  HIS A 283      -0.397  21.645  10.776  1.00 21.15           C  
ATOM   2081  C   HIS A 283      -1.856  22.108  10.598  1.00 21.49           C  
ATOM   2082  O   HIS A 283      -2.100  23.277  10.374  1.00 20.12           O  
ATOM   2083  CB  HIS A 283       0.029  21.727  12.223  1.00 21.75           C  
ATOM   2084  CG  HIS A 283      -0.749  20.846  13.150  1.00 19.06           C  
ATOM   2085  ND1 HIS A 283      -0.216  19.719  13.745  1.00 22.55           N  
ATOM   2086  CD2 HIS A 283      -2.011  20.948  13.614  1.00 19.09           C  
ATOM   2087  CE1 HIS A 283      -1.128  19.164  14.523  1.00 17.38           C  
ATOM   2088  NE2 HIS A 283      -2.229  19.890  14.452  1.00 21.97           N  
ATOM   2089  N   PRO A 284      -2.818  21.196  10.634  1.00 21.92           N  
ATOM   2090  CA  PRO A 284      -4.248  21.574  10.546  1.00 22.09           C  
ATOM   2091  C   PRO A 284      -4.760  22.655  11.525  1.00 23.00           C  
ATOM   2092  O   PRO A 284      -5.808  23.264  11.301  1.00 22.14           O  
ATOM   2093  CB  PRO A 284      -4.969  20.258  10.804  1.00 22.28           C  
ATOM   2094  CG  PRO A 284      -4.025  19.201  10.284  1.00 22.85           C  
ATOM   2095  CD  PRO A 284      -2.628  19.739  10.559  1.00 22.83           C  
ATOM   2096  N   PHE A 285      -4.036  22.865  12.623  1.00 22.36           N  
ATOM   2097  CA  PHE A 285      -4.351  23.928  13.571  1.00 21.38           C  
ATOM   2098  C   PHE A 285      -4.370  25.295  12.896  1.00 21.75           C  
ATOM   2099  O   PHE A 285      -5.179  26.127  13.266  1.00 21.91           O  
ATOM   2100  CB  PHE A 285      -3.338  23.936  14.711  1.00 21.58           C  
ATOM   2101  CG  PHE A 285      -3.664  24.887  15.841  1.00 19.65           C  
ATOM   2102  CD1 PHE A 285      -4.837  24.783  16.565  1.00 21.13           C  
ATOM   2103  CD2 PHE A 285      -2.775  25.865  16.199  1.00 21.02           C  
ATOM   2104  CE1 PHE A 285      -5.104  25.643  17.651  1.00 18.94           C  
ATOM   2105  CE2 PHE A 285      -3.051  26.719  17.269  1.00 18.71           C  
ATOM   2106  CZ  PHE A 285      -4.231  26.606  17.980  1.00 17.29           C  
ATOM   2107  N   PHE A 286      -3.515  25.504  11.907  1.00 21.17           N  
ATOM   2108  CA  PHE A 286      -3.465  26.778  11.208  1.00 23.05           C  
ATOM   2109  C   PHE A 286      -4.373  26.916   9.954  1.00 24.75           C  
ATOM   2110  O   PHE A 286      -4.283  27.937   9.251  1.00 24.25           O  
ATOM   2111  CB  PHE A 286      -2.031  27.134  10.873  1.00 21.73           C  
ATOM   2112  CG  PHE A 286      -1.143  27.203  12.097  1.00 21.68           C  
ATOM   2113  CD1 PHE A 286      -1.381  28.132  13.089  1.00 19.72           C  
ATOM   2114  CD2 PHE A 286      -0.110  26.290  12.271  1.00 20.05           C  
ATOM   2115  CE1 PHE A 286      -0.569  28.177  14.236  1.00 21.45           C  
ATOM   2116  CE2 PHE A 286       0.689  26.327  13.423  1.00 20.69           C  
ATOM   2117  CZ  PHE A 286       0.477  27.258  14.379  1.00 19.84           C  
ATOM   2118  N   GLN A 287      -5.268  25.955   9.724  1.00 26.53           N  
ATOM   2119  CA  GLN A 287      -6.159  26.006   8.526  1.00 29.03           C  
ATOM   2120  C   GLN A 287      -6.960  27.311   8.500  1.00 28.60           C  
ATOM   2121  O   GLN A 287      -7.182  27.893   7.428  1.00 30.73           O  
ATOM   2122  CB  GLN A 287      -7.109  24.809   8.506  1.00 29.52           C  
ATOM   2123  CG  GLN A 287      -8.202  24.826   7.378  1.00 35.27           C  
ATOM   2124  CD  GLN A 287      -9.554  25.441   7.818  1.00 39.82           C  
ATOM   2125  OE1 GLN A 287      -9.790  25.716   9.014  1.00 43.05           O  
ATOM   2126  NE2 GLN A 287     -10.436  25.659   6.844  1.00 43.17           N  
ATOM   2127  N   ASP A 288      -7.355  27.779   9.673  1.00 28.02           N  
ATOM   2128  CA  ASP A 288      -8.157  28.998   9.812  1.00 28.25           C  
ATOM   2129  C   ASP A 288      -7.472  30.152  10.544  1.00 27.14           C  
ATOM   2130  O   ASP A 288      -8.134  31.001  11.167  1.00 28.46           O  
ATOM   2131  CB  ASP A 288      -9.471  28.664  10.509  1.00 27.87           C  
ATOM   2132  CG  ASP A 288      -9.282  28.231  11.945  1.00 31.65           C  
ATOM   2133  OD1 ASP A 288      -8.105  28.055  12.382  1.00 32.64           O  
ATOM   2134  OD2 ASP A 288     -10.260  28.018  12.693  1.00 32.77           O  
ATOM   2135  N   VAL A 289      -6.154  30.204  10.454  1.00 26.55           N  
ATOM   2136  CA  VAL A 289      -5.384  31.290  11.023  1.00 25.21           C  
ATOM   2137  C   VAL A 289      -5.743  32.597  10.323  1.00 25.58           C  
ATOM   2138  O   VAL A 289      -5.937  32.637   9.100  1.00 24.93           O  
ATOM   2139  CB  VAL A 289      -3.840  31.051  10.945  1.00 24.62           C  
ATOM   2140  CG1 VAL A 289      -3.320  31.128   9.526  1.00 26.05           C  
ATOM   2141  CG2 VAL A 289      -3.075  32.041  11.861  1.00 23.50           C  
ATOM   2142  N   THR A 290      -5.812  33.635  11.138  1.00 24.54           N  
ATOM   2143  CA  THR A 290      -6.093  34.997  10.732  1.00 25.42           C  
ATOM   2144  C   THR A 290      -5.165  35.891  11.510  1.00 25.83           C  
ATOM   2145  O   THR A 290      -4.384  35.400  12.357  1.00 25.49           O  
ATOM   2146  CB  THR A 290      -7.524  35.380  11.101  1.00 25.17           C  
ATOM   2147  OG1 THR A 290      -7.702  35.302  12.534  1.00 25.06           O  
ATOM   2148  CG2 THR A 290      -8.546  34.424  10.479  1.00 25.68           C  
ATOM   2149  N   LYS A 291      -5.251  37.195  11.255  1.00 25.23           N  
ATOM   2150  CA  LYS A 291      -4.418  38.151  11.940  1.00 25.83           C  
ATOM   2151  C   LYS A 291      -5.255  39.211  12.652  1.00 25.83           C  
ATOM   2152  O   LYS A 291      -5.481  40.305  12.104  1.00 24.82           O  
ATOM   2153  CB  LYS A 291      -3.456  38.794  10.940  1.00 27.19           C  
ATOM   2154  CG  LYS A 291      -2.367  39.624  11.611  1.00 29.66           C  
ATOM   2155  CD  LYS A 291      -1.550  40.467  10.582  1.00 33.04           C  
ATOM   2156  CE  LYS A 291      -0.213  40.864  11.178  1.00 36.24           C  
ATOM   2157  NZ  LYS A 291       0.762  41.512  10.228  1.00 37.75           N  
ATOM   2158  N   PRO A 292      -5.712  38.894  13.859  1.00 25.78           N  
ATOM   2159  CA  PRO A 292      -6.413  39.853  14.697  1.00 25.43           C  
ATOM   2160  C   PRO A 292      -5.547  41.000  15.217  1.00 27.17           C  
ATOM   2161  O   PRO A 292      -4.338  40.860  15.277  1.00 26.41           O  
ATOM   2162  CB  PRO A 292      -6.896  38.994  15.873  1.00 25.64           C  
ATOM   2163  CG  PRO A 292      -6.896  37.630  15.369  1.00 25.81           C  
ATOM   2164  CD  PRO A 292      -5.665  37.565  14.509  1.00 25.71           C  
ATOM   2165  N   VAL A 293      -6.194  42.115  15.535  1.00 27.90           N  
ATOM   2166  CA  VAL A 293      -5.576  43.226  16.265  1.00 31.34           C  
ATOM   2167  C   VAL A 293      -5.784  42.988  17.768  1.00 31.10           C  
ATOM   2168  O   VAL A 293      -6.902  42.702  18.217  1.00 33.43           O  
ATOM   2169  CB  VAL A 293      -6.134  44.648  15.897  1.00 31.64           C  
ATOM   2170  CG1 VAL A 293      -4.955  45.594  15.479  1.00 34.66           C  
ATOM   2171  CG2 VAL A 293      -7.172  44.627  14.784  1.00 33.08           C  
ATOM   2172  N   PRO A 294      -4.737  43.108  18.552  1.00 31.98           N  
ATOM   2173  CA  PRO A 294      -4.873  42.955  20.004  1.00 32.65           C  
ATOM   2174  C   PRO A 294      -5.377  44.260  20.617  1.00 33.94           C  
ATOM   2175  O   PRO A 294      -5.177  45.312  20.003  1.00 33.16           O  
ATOM   2176  CB  PRO A 294      -3.445  42.736  20.449  1.00 32.37           C  
ATOM   2177  CG  PRO A 294      -2.616  43.511  19.448  1.00 31.38           C  
ATOM   2178  CD  PRO A 294      -3.356  43.445  18.166  1.00 31.99           C  
ATOM   2179  N   HIS A 295      -5.999  44.220  21.791  1.00 35.56           N  
ATOM   2180  CA  HIS A 295      -6.207  45.496  22.457  1.00 36.87           C  
ATOM   2181  C   HIS A 295      -5.045  45.766  23.367  1.00 35.43           C  
ATOM   2182  O   HIS A 295      -4.802  45.030  24.337  1.00 36.30           O  
ATOM   2183  CB  HIS A 295      -7.564  45.707  23.140  1.00 38.44           C  
ATOM   2184  CG  HIS A 295      -7.903  47.167  23.243  1.00 41.65           C  
ATOM   2185  ND1 HIS A 295      -8.048  47.825  24.446  1.00 47.94           N  
ATOM   2186  CD2 HIS A 295      -7.970  48.122  22.285  1.00 46.09           C  
ATOM   2187  CE1 HIS A 295      -8.262  49.112  24.217  1.00 49.10           C  
ATOM   2188  NE2 HIS A 295      -8.220  49.316  22.912  1.00 48.33           N  
ATOM   2189  N   LEU A 296      -4.278  46.774  22.954  1.00 35.29           N  
ATOM   2190  CA  LEU A 296      -3.080  47.228  23.643  1.00 34.43           C  
ATOM   2191  C   LEU A 296      -3.346  48.617  24.202  1.00 34.50           C  
ATOM   2192  O   LEU A 296      -3.717  49.552  23.472  1.00 33.05           O  
ATOM   2193  CB  LEU A 296      -1.889  47.318  22.704  1.00 34.35           C  
ATOM   2194  CG  LEU A 296      -1.362  46.081  22.000  1.00 35.54           C  
ATOM   2195  CD1 LEU A 296      -0.011  46.429  21.367  1.00 35.92           C  
ATOM   2196  CD2 LEU A 296      -1.233  44.945  23.007  1.00 36.06           C  
ATOM   2197  N   ARG A 297      -3.164  48.734  25.508  1.00 34.76           N  
ATOM   2198  CA  ARG A 297      -3.237  50.011  26.182  1.00 35.99           C  
ATOM   2199  C   ARG A 297      -1.821  50.374  26.583  1.00 35.49           C  
ATOM   2200  O   ARG A 297      -1.240  49.738  27.476  1.00 35.14           O  
ATOM   2201  CB  ARG A 297      -4.118  49.909  27.425  1.00 36.77           C  
ATOM   2202  CG  ARG A 297      -4.193  51.202  28.210  1.00 41.59           C  
ATOM   2203  CD  ARG A 297      -3.307  51.259  29.471  1.00 46.24           C  
ATOM   2204  NE  ARG A 297      -3.981  51.992  30.545  1.00 49.40           N  
ATOM   2205  CZ  ARG A 297      -4.322  51.495  31.740  1.00 52.82           C  
ATOM   2206  NH1 ARG A 297      -4.032  50.229  32.079  1.00 53.67           N  
ATOM   2207  NH2 ARG A 297      -4.947  52.286  32.620  1.00 53.82           N  
ATOM   2208  N   LEU A 298      -1.279  51.397  25.928  1.00 33.70           N  
ATOM   2209  CA  LEU A 298       0.104  51.782  26.106  1.00 33.84           C  
ATOM   2210  C   LEU A 298       0.221  53.033  26.951  1.00 34.40           C  
ATOM   2211  O   LEU A 298       1.335  53.319  27.411  1.00 35.36           O  
ATOM   2212  CB  LEU A 298       0.782  52.011  24.764  1.00 33.79           C  
ATOM   2213  CG  LEU A 298       0.815  50.815  23.813  1.00 33.74           C  
ATOM   2214  CD1 LEU A 298       1.368  51.222  22.470  1.00 34.87           C  
ATOM   2215  CD2 LEU A 298       1.614  49.617  24.379  1.00 34.99           C  
TER    2216      LEU A 298                                                      
HETATM 2217  O11 U73 A 300      10.880  45.713  25.963  1.00 27.72           O  
HETATM 2218  C10 U73 A 300      10.089  46.361  25.281  1.00 26.38           C  
HETATM 2219  N9  U73 A 300      10.341  46.684  24.019  1.00 22.35           N  
HETATM 2220  C3  U73 A 300      11.636  46.427  23.299  1.00 21.80           C  
HETATM 2221  N4  U73 A 300      11.853  46.738  21.973  1.00 19.31           N  
HETATM 2222  C5  U73 A 300      13.042  46.341  21.695  1.00 20.64           C  
HETATM 2223  S2  U73 A 300      12.887  45.492  24.088  1.00 22.16           S  
HETATM 2224  C1  U73 A 300      13.723  45.673  22.640  1.00 22.12           C  
HETATM 2225  C6  U73 A 300      15.104  45.097  22.395  1.00 22.14           C  
HETATM 2226  C8  U73 A 300      14.965  43.633  21.927  1.00 23.60           C  
HETATM 2227  C7  U73 A 300      16.056  45.231  23.578  1.00 24.18           C  
HETATM 2228  C12 U73 A 300       8.724  46.722  25.823  1.00 26.71           C  
HETATM 2229  C13 U73 A 300       8.710  47.876  26.770  1.00 28.45           C  
HETATM 2230  C14 U73 A 300       8.915  47.679  28.124  1.00 28.31           C  
HETATM 2231  C15 U73 A 300       8.916  48.790  28.967  1.00 27.35           C  
HETATM 2232  C16 U73 A 300       8.715  50.033  28.428  1.00 30.73           C  
HETATM 2233  N17 U73 A 300       8.500  50.183  27.116  1.00 31.26           N  
HETATM 2234  C18 U73 A 300       8.491  49.142  26.283  1.00 30.63           C  
HETATM 2235  O   HOH A2001       6.945  54.107  28.035  1.00 36.64           O  
HETATM 2236  O   HOH A2002       7.217  52.836  25.792  1.00 22.42           O  
HETATM 2237  O   HOH A2003      12.360  51.456  16.323  1.00 25.77           O  
HETATM 2238  O   HOH A2004      11.410  55.228  15.484  1.00 30.83           O  
HETATM 2239  O   HOH A2005      18.466  39.695  13.508  1.00 25.94           O  
HETATM 2240  O   HOH A2006      17.442  42.255  12.223  1.00 26.34           O  
HETATM 2241  O   HOH A2007       5.761  41.936  11.460  1.00 30.74           O  
HETATM 2242  O   HOH A2008      14.419  41.650  11.533  1.00 21.71           O  
HETATM 2243  O   HOH A2009      17.573  40.449  15.983  1.00 33.63           O  
HETATM 2244  O   HOH A2010      19.323  44.903  10.348  1.00 27.36           O  
HETATM 2245  O   HOH A2011      14.543  20.377  12.426  1.00 33.11           O  
HETATM 2246  O   HOH A2012       5.091  51.210  25.601  1.00 32.96           O  
HETATM 2247  O   HOH A2013       4.412  48.088  27.479  1.00 37.27           O  
HETATM 2248  O   HOH A2014       5.165  49.009  18.992  1.00 22.18           O  
HETATM 2249  O   HOH A2015       6.160  45.395  27.954  1.00 25.46           O  
HETATM 2250  O   HOH A2016      -6.406  33.245  14.004  1.00 23.97           O  
HETATM 2251  O   HOH A2017      -9.153  30.319  16.337  1.00 37.00           O  
HETATM 2252  O   HOH A2018      -1.262  35.807  11.606  1.00 25.91           O  
HETATM 2253  O   HOH A2019      13.350  26.085   8.654  1.00 26.41           O  
HETATM 2254  O   HOH A2020     -10.813  32.861  13.852  1.00 29.82           O  
HETATM 2255  O   HOH A2021     -10.676  37.089  15.797  1.00 31.12           O  
HETATM 2256  O   HOH A2022      12.515  24.318  13.061  1.00 17.73           O  
HETATM 2257  O   HOH A2023      22.763  29.675  16.450  1.00 32.35           O  
HETATM 2258  O   HOH A2024      19.752  34.334  21.839  1.00 34.04           O  
HETATM 2259  O   HOH A2025      15.638  27.772  26.465  1.00 19.53           O  
HETATM 2260  O   HOH A2026      14.033  29.916  27.459  1.00 20.69           O  
HETATM 2261  O   HOH A2027       0.407  42.345  18.292  1.00 25.44           O  
HETATM 2262  O   HOH A2028      11.064  43.520  12.302  1.00 26.84           O  
HETATM 2263  O   HOH A2029      13.575  29.075  30.119  1.00 19.11           O  
HETATM 2264  O   HOH A2030      10.929  30.322  39.500  1.00 27.83           O  
HETATM 2265  O   HOH A2031      10.609  23.574  29.970  1.00 18.70           O  
HETATM 2266  O   HOH A2032      16.735  28.495  28.797  1.00 31.20           O  
HETATM 2267  O   HOH A2033      14.973  25.387  25.191  1.00 15.60           O  
HETATM 2268  O   HOH A2034      18.034  19.735  20.434  1.00 22.40           O  
HETATM 2269  O   HOH A2035      13.689  21.995  14.282  1.00 19.38           O  
HETATM 2270  O   HOH A2036      19.946  22.545  14.841  1.00 32.99           O  
HETATM 2271  O   HOH A2037      14.490  28.739  23.119  1.00 17.49           O  
HETATM 2272  O   HOH A2038       1.307  33.911  31.901  1.00 30.43           O  
HETATM 2273  O   HOH A2039       4.806  28.103  30.009  1.00 15.79           O  
HETATM 2274  O   HOH A2040       6.701  26.418  31.266  1.00 15.95           O  
HETATM 2275  O   HOH A2041       7.119  27.367  40.843  1.00 30.23           O  
HETATM 2276  O   HOH A2042      13.067  28.452  45.094  1.00 22.10           O  
HETATM 2277  O   HOH A2043       4.430  19.149  36.176  1.00 29.42           O  
HETATM 2278  O   HOH A2044       6.681   9.961  27.862  1.00 32.02           O  
HETATM 2279  O   HOH A2045      15.063   3.161  29.284  1.00 28.89           O  
HETATM 2280  O   HOH A2046      12.185   3.561  20.376  1.00 28.59           O  
HETATM 2281  O   HOH A2047       9.150   6.169  20.329  1.00 27.62           O  
HETATM 2282  O   HOH A2048       9.822  11.600  22.097  1.00 21.77           O  
HETATM 2283  O   HOH A2049      20.336  15.526  36.846  1.00 35.65           O  
HETATM 2284  O   HOH A2050      -7.930  14.277  31.161  1.00 29.91           O  
HETATM 2285  O   HOH A2051      -8.470  25.690  16.411  1.00 33.66           O  
HETATM 2286  O   HOH A2052      -3.246  14.655  19.992  1.00 28.86           O  
HETATM 2287  O   HOH A2053      -8.608  23.839  14.152  1.00 30.77           O  
HETATM 2288  O   HOH A2054       2.641  17.215  11.928  1.00 27.98           O  
HETATM 2289  O   HOH A2055       4.593  13.095  15.733  1.00 35.21           O  
HETATM 2290  O   HOH A2056       6.422  14.442  25.179  1.00 28.42           O  
HETATM 2291  O   HOH A2057       7.649  12.359  23.379  1.00 26.66           O  
HETATM 2292  O   HOH A2058      13.515  18.411  15.364  1.00 21.52           O  
HETATM 2293  O   HOH A2059      12.234  20.779  16.040  1.00 20.42           O  
HETATM 2294  O   HOH A2060       9.190  18.027  11.590  1.00 25.92           O  
HETATM 2295  O   HOH A2061      11.898  24.381  10.320  1.00 17.80           O  
HETATM 2296  O   HOH A2062       2.267  19.442  10.440  1.00 29.29           O  
HETATM 2297  O   HOH A2063      -8.221  21.835  10.197  1.00 33.55           O  
HETATM 2298  O   HOH A2064      -8.426  31.548  13.830  1.00 35.69           O  
HETATM 2299  O   HOH A2065     -10.142  35.891  13.651  1.00 29.45           O  
HETATM 2300  O   HOH A2066      -2.386  39.054  15.173  1.00 23.48           O  
HETATM 2301  O   HOH A2067       3.495  51.469  27.576  1.00 32.01           O  
CONECT 2217 2218                                                                
CONECT 2218 2217 2219 2228                                                      
CONECT 2219 2218 2220                                                           
CONECT 2220 2219 2221 2223                                                      
CONECT 2221 2220 2222                                                           
CONECT 2222 2221 2224                                                           
CONECT 2223 2220 2224                                                           
CONECT 2224 2222 2223 2225                                                      
CONECT 2225 2224 2226 2227                                                      
CONECT 2226 2225                                                                
CONECT 2227 2225                                                                
CONECT 2228 2218 2229                                                           
CONECT 2229 2228 2230 2234                                                      
CONECT 2230 2229 2231                                                           
CONECT 2231 2230 2232                                                           
CONECT 2232 2231 2233                                                           
CONECT 2233 2232 2234                                                           
CONECT 2234 2229 2233                                                           
MASTER      574    0    1   12    8    0    3    6 2300    1   18   23          
END                                                                             
