HEADER    TRANSFERASE                             30-JUN-03   1PW2              
TITLE     APO STRUCTURE OF HUMAN CYCLIN-DEPENDENT KINASE 2                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HI5;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    PROTEIN KINASE, CELL CYCLE, PHOSPHORYLATION, CELL DIVISION, MITOSIS,  
KEYWDS   2 INHIBITION, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-       
KEYWDS   3 BINDING, 3D-STRUCTURE.                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,K.J.STEWART,S.WANG,  
AUTHOR   2 D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR,P.M.FISCHER,M.D.WALKINSHAW  
REVDAT   3   16-AUG-23 1PW2    1       REMARK                                   
REVDAT   2   24-FEB-09 1PW2    1       VERSN                                    
REVDAT   1   09-DEC-03 1PW2    0                                                
JRNL        AUTH   S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,            
JRNL        AUTH 2 K.J.STEWART,S.WANG,D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR, 
JRNL        AUTH 3 P.M.FISCHER,M.D.WALKINSHAW                                   
JRNL        TITL   DISCOVERY OF A NOVEL FAMILY OF CDK INHIBITORS WITH THE       
JRNL        TITL 2 PROGRAM LIDAEUS: STRUCTURAL BASIS FOR LIGAND-INDUCED         
JRNL        TITL 3 DISORDERING OF THE ACTIVATION LOOP.                          
JRNL        REF    STRUCTURE                     V.  11   399 2003              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12679018                                                     
JRNL        DOI    10.1016/S0969-2126(03)00060-1                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1509856.180                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20265                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 985                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3243                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 153                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2365                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 234                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.61000                                              
REMARK   3    B22 (A**2) : -3.55000                                             
REMARK   3    B33 (A**2) : 1.94000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.770                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.610 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.520 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.170 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.170 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 44.10                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 37 - 40 ARE NOT VISIBLE IN THE   
REMARK   3  ELECTRON DENSITY MAP                                                
REMARK   4                                                                      
REMARK   4 1PW2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019621.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ENRAF-NONIUS FR571                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
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   : 20576                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.610                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 10.45                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HCL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, NA-HEPES, PH 7.8, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.84350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.01600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.89950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.01600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.84350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.89950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  24       12.44    -69.10                                   
REMARK 500    VAL A  44      105.55     61.17                                   
REMARK 500    ARG A 126      -15.45     84.26                                   
REMARK 500    ASP A 127       49.39   -141.87                                   
REMARK 500    PRO A 254       40.10   -100.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 STAUROSPORINE                                                        
REMARK 900 RELATED ID: 1B39   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 PHOSPHORYLATED ON THR 160            
REMARK 900 RELATED ID: 1CKP   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 PURVALANOL B                                                         
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE                          
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR         
REMARK 900 HYMENIALDISINE                                                       
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2058    
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 6027    
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH THE       
REMARK 900 INHIBITOR INDIRUBIN-5-SULPHONATE BOUND                               
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
REMARK 900 CYCLIN A - CYCLIN-DEPENDENT KINASE 2 COMPLEX                         
REMARK 900 RELATED ID: 1FVT   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH    
REMARK 900 AN OXINDOLE INHIBITOR                                                
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE INHIBITOR 
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2) IN       
REMARK 900 COMPLEX WITH THE INHIBITOR H717                                      
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4 INHIBITOR    
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE INHIBITOR 2-      
REMARK 900 AMINO-6-(3'-METHYL-2'-OXO)BUTOXYPURINE                               
REMARK 900 RELATED ID: 1HCK   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1HCL   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2                                      
REMARK 900 RELATED ID: 1JSV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN COMPLEX WITH 4- 
REMARK 900 [(6-AMINO-4-PYRIMIDINYL) AMINO]BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED) IN COMPLEX WITH   
REMARK 900 PKF049-365                                                           
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-1,2-DIHYDRO-3H- INDOL-3-     
REMARK 900 YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE                              
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{4- [2-(7-  
REMARK 900 OXO-6,7-DIHYDRO-8H-[1,3]THIAZOLO[5,4-E]INDOL-8- YLIDENE)HYDRAZINO]   
REMARK 900 PHENYL}METHANESULFONAMIDE                                            
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2- DIOXIDO-1, 
REMARK 900 3-DIHYDRO-2-BENZOTHIEN-5-YL)AMINO]METHYLENE}-5- (1,3-OXAZOL-5-YL)-1, 
REMARK 900 3-DIHYDRO-2H-INDOL-2-ONE                                             
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED 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                                                    
DBREF  1PW2 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              
FORMUL   2  HOH   *234(H2 O)                                                    
HELIX    1   1 PRO A   45  LYS A   56  1                                  12    
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 GLY A  147  PHE A  152  1                                   6    
HELIX    6   6 ALA A  170  LEU A  175  1                                   6    
HELIX    7   7 THR A  182  ARG A  199  1                                  18    
HELIX    8   8 SER A  207  GLY A  220  1                                  14    
HELIX    9   9 GLY A  229  MET A  233  5                                   5    
HELIX   10  10 ASP A  247  VAL A  252  1                                   6    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  ALA A  282  1                                   7    
HELIX   13  13 HIS A  283  GLN A  287  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  O  VAL A  30   N  ALA A  21           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5   A 5 LEU A  66  THR A  72 -1  N  ASP A  68   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0         0.07                     
CRYST1   53.687   71.799   72.032  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      0.018626  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013883        0.00000                         
ATOM      1  N   MET A   1      25.645  56.219  23.709  1.00 66.50           N  
ATOM      2  CA  MET A   1      26.554  57.148  22.979  1.00 65.75           C  
ATOM      3  C   MET A   1      25.990  58.569  22.940  1.00 63.83           C  
ATOM      4  O   MET A   1      24.891  58.827  23.430  1.00 64.81           O  
ATOM      5  CB  MET A   1      26.787  56.641  21.552  1.00 67.08           C  
ATOM      6  CG  MET A   1      27.769  57.482  20.750  1.00 69.37           C  
ATOM      7  SD  MET A   1      28.089  56.856  19.093  1.00 72.80           S  
ATOM      8  CE  MET A   1      29.696  56.082  19.321  1.00 70.66           C  
ATOM      9  N   GLU A   2      26.753  59.485  22.352  1.00 62.26           N  
ATOM     10  CA  GLU A   2      26.356  60.882  22.252  1.00 60.13           C  
ATOM     11  C   GLU A   2      25.264  61.094  21.213  1.00 58.37           C  
ATOM     12  O   GLU A   2      24.588  62.121  21.213  1.00 57.72           O  
ATOM     13  CB  GLU A   2      27.569  61.748  21.896  1.00 60.08           C  
ATOM     14  CG  GLU A   2      28.757  61.576  22.833  1.00 60.56           C  
ATOM     15  CD  GLU A   2      29.396  60.201  22.726  1.00 61.43           C  
ATOM     16  OE1 GLU A   2      29.926  59.872  21.641  1.00 60.85           O  
ATOM     17  OE2 GLU A   2      29.365  59.450  23.725  1.00 62.07           O  
ATOM     18  N   ASN A   3      25.099  60.119  20.325  1.00 55.79           N  
ATOM     19  CA  ASN A   3      24.095  60.204  19.273  1.00 54.00           C  
ATOM     20  C   ASN A   3      22.697  59.830  19.752  1.00 52.97           C  
ATOM     21  O   ASN A   3      21.741  59.883  18.978  1.00 52.78           O  
ATOM     22  CB  ASN A   3      24.483  59.296  18.103  1.00 52.73           C  
ATOM     23  CG  ASN A   3      25.691  59.807  17.344  1.00 52.86           C  
ATOM     24  OD1 ASN A   3      25.648  60.878  16.737  1.00 52.64           O  
ATOM     25  ND2 ASN A   3      26.778  59.044  17.375  1.00 50.81           N  
ATOM     26  N   PHE A   4      22.573  59.457  21.022  1.00 51.26           N  
ATOM     27  CA  PHE A   4      21.274  59.066  21.557  1.00 49.60           C  
ATOM     28  C   PHE A   4      20.920  59.715  22.886  1.00 50.50           C  
ATOM     29  O   PHE A   4      21.751  59.800  23.790  1.00 51.23           O  
ATOM     30  CB  PHE A   4      21.205  57.545  21.735  1.00 46.44           C  
ATOM     31  CG  PHE A   4      21.466  56.771  20.479  1.00 43.24           C  
ATOM     32  CD1 PHE A   4      22.765  56.568  20.029  1.00 41.98           C  
ATOM     33  CD2 PHE A   4      20.410  56.244  19.742  1.00 41.63           C  
ATOM     34  CE1 PHE A   4      23.011  55.849  18.863  1.00 41.49           C  
ATOM     35  CE2 PHE A   4      20.643  55.524  18.575  1.00 41.01           C  
ATOM     36  CZ  PHE A   4      21.947  55.326  18.134  1.00 41.40           C  
ATOM     37  N   GLN A   5      19.674  60.164  22.999  1.00 51.47           N  
ATOM     38  CA  GLN A   5      19.189  60.769  24.233  1.00 51.82           C  
ATOM     39  C   GLN A   5      18.346  59.708  24.936  1.00 49.83           C  
ATOM     40  O   GLN A   5      17.332  59.256  24.401  1.00 49.08           O  
ATOM     41  CB  GLN A   5      18.324  62.003  23.943  1.00 54.13           C  
ATOM     42  CG  GLN A   5      17.040  61.702  23.175  1.00 58.91           C  
ATOM     43  CD  GLN A   5      15.964  62.754  23.390  1.00 61.33           C  
ATOM     44  OE1 GLN A   5      15.586  63.049  24.527  1.00 61.41           O  
ATOM     45  NE2 GLN A   5      15.458  63.319  22.297  1.00 62.34           N  
ATOM     46  N   LYS A   6      18.769  59.299  26.126  1.00 47.91           N  
ATOM     47  CA  LYS A   6      18.038  58.283  26.868  1.00 48.91           C  
ATOM     48  C   LYS A   6      16.711  58.807  27.406  1.00 49.49           C  
ATOM     49  O   LYS A   6      16.679  59.600  28.346  1.00 50.19           O  
ATOM     50  CB  LYS A   6      18.899  57.744  28.014  1.00 48.44           C  
ATOM     51  CG  LYS A   6      20.122  56.965  27.541  1.00 49.83           C  
ATOM     52  CD  LYS A   6      20.895  56.343  28.700  1.00 51.52           C  
ATOM     53  CE  LYS A   6      21.484  57.403  29.622  1.00 52.15           C  
ATOM     54  NZ  LYS A   6      22.263  56.799  30.738  1.00 52.66           N  
ATOM     55  N   VAL A   7      15.618  58.354  26.798  1.00 48.64           N  
ATOM     56  CA  VAL A   7      14.277  58.764  27.202  1.00 47.27           C  
ATOM     57  C   VAL A   7      13.921  58.210  28.574  1.00 47.46           C  
ATOM     58  O   VAL A   7      13.441  58.939  29.439  1.00 48.59           O  
ATOM     59  CB  VAL A   7      13.215  58.274  26.202  1.00 46.44           C  
ATOM     60  CG1 VAL A   7      11.821  58.622  26.713  1.00 45.45           C  
ATOM     61  CG2 VAL A   7      13.460  58.898  24.842  1.00 45.50           C  
ATOM     62  N   GLU A   8      14.151  56.915  28.761  1.00 47.73           N  
ATOM     63  CA  GLU A   8      13.854  56.264  30.029  1.00 47.34           C  
ATOM     64  C   GLU A   8      14.378  54.834  30.043  1.00 46.39           C  
ATOM     65  O   GLU A   8      14.786  54.295  29.013  1.00 44.45           O  
ATOM     66  CB  GLU A   8      12.343  56.258  30.282  1.00 48.13           C  
ATOM     67  CG  GLU A   8      11.567  55.264  29.435  1.00 49.51           C  
ATOM     68  CD  GLU A   8      10.067  55.452  29.544  1.00 51.49           C  
ATOM     69  OE1 GLU A   8       9.550  55.484  30.680  1.00 52.90           O  
ATOM     70  OE2 GLU A   8       9.403  55.567  28.492  1.00 53.38           O  
ATOM     71  N   LYS A   9      14.365  54.226  31.223  1.00 45.82           N  
ATOM     72  CA  LYS A   9      14.826  52.857  31.379  1.00 47.32           C  
ATOM     73  C   LYS A   9      13.682  51.902  31.070  1.00 47.69           C  
ATOM     74  O   LYS A   9      12.629  51.950  31.707  1.00 48.19           O  
ATOM     75  CB  LYS A   9      15.331  52.630  32.807  1.00 47.42           C  
ATOM     76  CG  LYS A   9      15.853  51.228  33.069  1.00 49.41           C  
ATOM     77  CD  LYS A   9      16.576  51.136  34.409  1.00 50.09           C  
ATOM     78  CE  LYS A   9      17.828  52.010  34.426  1.00 51.02           C  
ATOM     79  NZ  LYS A   9      18.578  51.909  35.712  1.00 51.14           N  
ATOM     80  N   ILE A  10      13.888  51.049  30.074  1.00 47.12           N  
ATOM     81  CA  ILE A  10      12.877  50.080  29.678  1.00 47.79           C  
ATOM     82  C   ILE A  10      12.870  48.924  30.665  1.00 48.48           C  
ATOM     83  O   ILE A  10      11.831  48.312  30.909  1.00 49.76           O  
ATOM     84  CB  ILE A  10      13.152  49.539  28.253  1.00 47.28           C  
ATOM     85  CG1 ILE A  10      12.746  50.588  27.219  1.00 47.08           C  
ATOM     86  CG2 ILE A  10      12.397  48.235  28.021  1.00 49.03           C  
ATOM     87  CD1 ILE A  10      12.964  50.152  25.788  1.00 45.97           C  
ATOM     88  N   GLY A  11      14.036  48.632  31.232  1.00 48.64           N  
ATOM     89  CA  GLY A  11      14.137  47.548  32.192  1.00 48.43           C  
ATOM     90  C   GLY A  11      15.536  46.975  32.300  1.00 47.65           C  
ATOM     91  O   GLY A  11      16.493  47.532  31.759  1.00 46.43           O  
ATOM     92  N   GLU A  12      15.651  45.860  33.013  1.00 47.70           N  
ATOM     93  CA  GLU A  12      16.932  45.191  33.200  1.00 46.55           C  
ATOM     94  C   GLU A  12      17.010  44.062  32.178  1.00 44.29           C  
ATOM     95  O   GLU A  12      16.119  43.217  32.115  1.00 44.15           O  
ATOM     96  CB  GLU A  12      17.027  44.597  34.610  1.00 48.97           C  
ATOM     97  CG  GLU A  12      16.507  45.484  35.747  1.00 52.69           C  
ATOM     98  CD  GLU A  12      17.340  46.733  35.974  1.00 55.56           C  
ATOM     99  OE1 GLU A  12      18.581  46.619  36.064  1.00 56.63           O  
ATOM    100  OE2 GLU A  12      16.752  47.831  36.078  1.00 56.09           O  
ATOM    101  N   GLY A  13      18.067  44.046  31.377  1.00 42.07           N  
ATOM    102  CA  GLY A  13      18.209  42.996  30.384  1.00 39.65           C  
ATOM    103  C   GLY A  13      19.073  41.853  30.883  1.00 38.02           C  
ATOM    104  O   GLY A  13      19.574  41.888  32.005  1.00 36.97           O  
ATOM    105  N   THR A  14      19.246  40.833  30.050  1.00 36.87           N  
ATOM    106  CA  THR A  14      20.063  39.680  30.412  1.00 36.48           C  
ATOM    107  C   THR A  14      21.524  40.097  30.530  1.00 35.07           C  
ATOM    108  O   THR A  14      22.238  39.645  31.421  1.00 35.22           O  
ATOM    109  CB  THR A  14      19.979  38.561  29.338  1.00 36.68           C  
ATOM    110  OG1 THR A  14      18.633  38.079  29.238  1.00 38.76           O  
ATOM    111  CG2 THR A  14      20.902  37.403  29.699  1.00 37.00           C  
ATOM    112  N   TYR A  15      21.951  40.978  29.630  1.00 33.04           N  
ATOM    113  CA  TYR A  15      23.335  41.437  29.581  1.00 31.22           C  
ATOM    114  C   TYR A  15      23.587  42.836  30.143  1.00 30.80           C  
ATOM    115  O   TYR A  15      24.734  43.205  30.419  1.00 30.13           O  
ATOM    116  CB  TYR A  15      23.819  41.369  28.134  1.00 30.47           C  
ATOM    117  CG  TYR A  15      23.544  40.031  27.488  1.00 30.66           C  
ATOM    118  CD1 TYR A  15      24.198  38.880  27.924  1.00 32.43           C  
ATOM    119  CD2 TYR A  15      22.594  39.905  26.473  1.00 30.67           C  
ATOM    120  CE1 TYR A  15      23.913  37.636  27.373  1.00 34.13           C  
ATOM    121  CE2 TYR A  15      22.299  38.658  25.911  1.00 33.41           C  
ATOM    122  CZ  TYR A  15      22.963  37.530  26.370  1.00 33.68           C  
ATOM    123  OH  TYR A  15      22.671  36.291  25.846  1.00 35.69           O  
ATOM    124  N   GLY A  16      22.527  43.614  30.311  1.00 28.51           N  
ATOM    125  CA  GLY A  16      22.697  44.956  30.828  1.00 27.64           C  
ATOM    126  C   GLY A  16      21.432  45.780  30.773  1.00 27.76           C  
ATOM    127  O   GLY A  16      20.394  45.304  30.324  1.00 28.17           O  
ATOM    128  N   VAL A  17      21.519  47.024  31.229  1.00 27.76           N  
ATOM    129  CA  VAL A  17      20.362  47.908  31.239  1.00 29.75           C  
ATOM    130  C   VAL A  17      19.845  48.143  29.823  1.00 29.46           C  
ATOM    131  O   VAL A  17      20.622  48.168  28.868  1.00 28.62           O  
ATOM    132  CB  VAL A  17      20.707  49.278  31.861  1.00 31.20           C  
ATOM    133  CG1 VAL A  17      19.432  50.079  32.088  1.00 32.64           C  
ATOM    134  CG2 VAL A  17      21.460  49.084  33.172  1.00 34.03           C  
ATOM    135  N   VAL A  18      18.528  48.299  29.702  1.00 28.80           N  
ATOM    136  CA  VAL A  18      17.879  48.556  28.420  1.00 26.89           C  
ATOM    137  C   VAL A  18      17.194  49.911  28.511  1.00 27.06           C  
ATOM    138  O   VAL A  18      16.408  50.160  29.429  1.00 26.29           O  
ATOM    139  CB  VAL A  18      16.817  47.489  28.097  1.00 27.32           C  
ATOM    140  CG1 VAL A  18      16.154  47.803  26.755  1.00 27.31           C  
ATOM    141  CG2 VAL A  18      17.463  46.110  28.056  1.00 26.98           C  
ATOM    142  N   TYR A  19      17.498  50.788  27.563  1.00 26.67           N  
ATOM    143  CA  TYR A  19      16.918  52.123  27.549  1.00 27.26           C  
ATOM    144  C   TYR A  19      16.133  52.431  26.285  1.00 26.73           C  
ATOM    145  O   TYR A  19      16.437  51.918  25.203  1.00 23.50           O  
ATOM    146  CB  TYR A  19      18.017  53.183  27.672  1.00 33.99           C  
ATOM    147  CG  TYR A  19      18.641  53.319  29.039  1.00 40.83           C  
ATOM    148  CD1 TYR A  19      17.891  53.757  30.131  1.00 45.25           C  
ATOM    149  CD2 TYR A  19      19.990  53.032  29.239  1.00 45.25           C  
ATOM    150  CE1 TYR A  19      18.472  53.909  31.391  1.00 48.27           C  
ATOM    151  CE2 TYR A  19      20.581  53.179  30.493  1.00 48.32           C  
ATOM    152  CZ  TYR A  19      19.817  53.618  31.564  1.00 49.45           C  
ATOM    153  OH  TYR A  19      20.402  53.766  32.803  1.00 51.11           O  
ATOM    154  N   LYS A  20      15.107  53.262  26.435  1.00 24.38           N  
ATOM    155  CA  LYS A  20      14.342  53.725  25.292  1.00 25.02           C  
ATOM    156  C   LYS A  20      15.126  54.992  24.991  1.00 24.81           C  
ATOM    157  O   LYS A  20      15.423  55.760  25.906  1.00 25.08           O  
ATOM    158  CB  LYS A  20      12.901  54.082  25.684  1.00 25.56           C  
ATOM    159  CG  LYS A  20      12.095  54.673  24.540  1.00 24.96           C  
ATOM    160  CD  LYS A  20      10.632  54.867  24.910  1.00 23.52           C  
ATOM    161  CE  LYS A  20       9.823  55.309  23.695  1.00 26.54           C  
ATOM    162  NZ  LYS A  20       8.364  55.450  23.997  1.00 27.99           N  
ATOM    163  N   ALA A  21      15.490  55.209  23.734  1.00 25.64           N  
ATOM    164  CA  ALA A  21      16.256  56.398  23.392  1.00 26.44           C  
ATOM    165  C   ALA A  21      15.891  56.920  22.018  1.00 28.32           C  
ATOM    166  O   ALA A  21      15.260  56.220  21.225  1.00 26.23           O  
ATOM    167  CB  ALA A  21      17.751  56.096  23.457  1.00 26.97           C  
ATOM    168  N   ARG A  22      16.291  58.158  21.749  1.00 28.85           N  
ATOM    169  CA  ARG A  22      16.011  58.792  20.472  1.00 32.38           C  
ATOM    170  C   ARG A  22      17.302  59.136  19.743  1.00 34.45           C  
ATOM    171  O   ARG A  22      18.233  59.686  20.333  1.00 34.26           O  
ATOM    172  CB  ARG A  22      15.195  60.069  20.686  1.00 33.41           C  
ATOM    173  CG  ARG A  22      14.750  60.742  19.396  1.00 34.63           C  
ATOM    174  CD  ARG A  22      14.061  62.062  19.692  1.00 37.05           C  
ATOM    175  NE  ARG A  22      12.972  61.901  20.653  1.00 34.87           N  
ATOM    176  CZ  ARG A  22      11.799  61.349  20.367  1.00 35.39           C  
ATOM    177  NH1 ARG A  22      11.553  60.906  19.140  1.00 35.18           N  
ATOM    178  NH2 ARG A  22      10.876  61.234  21.311  1.00 35.59           N  
ATOM    179  N   ASN A  23      17.351  58.801  18.459  1.00 37.43           N  
ATOM    180  CA  ASN A  23      18.515  59.091  17.634  1.00 41.30           C  
ATOM    181  C   ASN A  23      18.464  60.576  17.293  1.00 43.65           C  
ATOM    182  O   ASN A  23      17.537  61.030  16.621  1.00 45.05           O  
ATOM    183  CB  ASN A  23      18.469  58.265  16.349  1.00 42.00           C  
ATOM    184  CG  ASN A  23      19.741  58.385  15.540  1.00 43.78           C  
ATOM    185  OD1 ASN A  23      20.250  59.485  15.326  1.00 44.33           O  
ATOM    186  ND2 ASN A  23      20.260  57.252  15.079  1.00 45.16           N  
ATOM    187  N   LYS A  24      19.459  61.327  17.754  1.00 45.41           N  
ATOM    188  CA  LYS A  24      19.512  62.768  17.514  1.00 48.00           C  
ATOM    189  C   LYS A  24      19.773  63.162  16.064  1.00 50.21           C  
ATOM    190  O   LYS A  24      20.063  64.324  15.777  1.00 51.40           O  
ATOM    191  CB  LYS A  24      20.573  63.407  18.412  1.00 47.46           C  
ATOM    192  CG  LYS A  24      20.290  63.259  19.897  1.00 47.21           C  
ATOM    193  CD  LYS A  24      21.391  63.879  20.739  1.00 46.38           C  
ATOM    194  CE  LYS A  24      21.130  63.655  22.221  1.00 47.81           C  
ATOM    195  NZ  LYS A  24      22.187  64.254  23.079  1.00 48.39           N  
ATOM    196  N   LEU A  25      19.670  62.204  15.151  1.00 51.43           N  
ATOM    197  CA  LEU A  25      19.893  62.482  13.738  1.00 53.24           C  
ATOM    198  C   LEU A  25      18.709  62.066  12.875  1.00 53.07           C  
ATOM    199  O   LEU A  25      18.244  62.838  12.036  1.00 54.15           O  
ATOM    200  CB  LEU A  25      21.167  61.785  13.255  1.00 54.94           C  
ATOM    201  CG  LEU A  25      22.467  62.500  13.637  1.00 56.31           C  
ATOM    202  CD1 LEU A  25      23.667  61.656  13.236  1.00 55.94           C  
ATOM    203  CD2 LEU A  25      22.511  63.862  12.949  1.00 56.82           C  
ATOM    204  N   THR A  26      18.226  60.845  13.078  1.00 52.23           N  
ATOM    205  CA  THR A  26      17.081  60.353  12.323  1.00 51.67           C  
ATOM    206  C   THR A  26      15.813  60.679  13.103  1.00 50.04           C  
ATOM    207  O   THR A  26      14.712  60.690  12.549  1.00 50.22           O  
ATOM    208  CB  THR A  26      17.159  58.826  12.102  1.00 52.63           C  
ATOM    209  OG1 THR A  26      17.195  58.154  13.367  1.00 53.68           O  
ATOM    210  CG2 THR A  26      18.403  58.468  11.307  1.00 52.05           C  
ATOM    211  N   GLY A  27      15.985  60.950  14.393  1.00 47.79           N  
ATOM    212  CA  GLY A  27      14.863  61.275  15.252  1.00 44.61           C  
ATOM    213  C   GLY A  27      14.065  60.056  15.672  1.00 42.75           C  
ATOM    214  O   GLY A  27      13.082  60.174  16.408  1.00 43.14           O  
ATOM    215  N   GLU A  28      14.484  58.878  15.217  1.00 38.91           N  
ATOM    216  CA  GLU A  28      13.765  57.655  15.549  1.00 36.26           C  
ATOM    217  C   GLU A  28      13.981  57.207  16.989  1.00 33.64           C  
ATOM    218  O   GLU A  28      15.036  57.450  17.577  1.00 32.48           O  
ATOM    219  CB  GLU A  28      14.171  56.520  14.605  1.00 38.63           C  
ATOM    220  CG  GLU A  28      13.415  55.217  14.865  1.00 37.90           C  
ATOM    221  CD  GLU A  28      11.912  55.350  14.644  1.00 40.72           C  
ATOM    222  OE1 GLU A  28      11.476  55.321  13.472  1.00 41.57           O  
ATOM    223  OE2 GLU A  28      11.167  55.494  15.640  1.00 36.08           O  
ATOM    224  N   VAL A  29      12.964  56.567  17.557  1.00 31.57           N  
ATOM    225  CA  VAL A  29      13.059  56.056  18.916  1.00 28.49           C  
ATOM    226  C   VAL A  29      13.501  54.615  18.782  1.00 26.21           C  
ATOM    227  O   VAL A  29      13.013  53.875  17.923  1.00 24.29           O  
ATOM    228  CB  VAL A  29      11.711  56.120  19.673  1.00 29.29           C  
ATOM    229  CG1 VAL A  29      11.289  57.568  19.851  1.00 29.19           C  
ATOM    230  CG2 VAL A  29      10.648  55.345  18.923  1.00 33.83           C  
ATOM    231  N   VAL A  30      14.442  54.222  19.626  1.00 24.46           N  
ATOM    232  CA  VAL A  30      14.973  52.877  19.580  1.00 22.24           C  
ATOM    233  C   VAL A  30      15.124  52.307  20.979  1.00 22.87           C  
ATOM    234  O   VAL A  30      14.821  52.966  21.975  1.00 22.62           O  
ATOM    235  CB  VAL A  30      16.362  52.867  18.924  1.00 24.18           C  
ATOM    236  CG1 VAL A  30      16.316  53.593  17.593  1.00 21.07           C  
ATOM    237  CG2 VAL A  30      17.375  53.531  19.859  1.00 23.94           C  
ATOM    238  N   ALA A  31      15.591  51.068  21.033  1.00 23.38           N  
ATOM    239  CA  ALA A  31      15.846  50.386  22.289  1.00 24.10           C  
ATOM    240  C   ALA A  31      17.364  50.189  22.326  1.00 25.03           C  
ATOM    241  O   ALA A  31      17.923  49.474  21.488  1.00 27.56           O  
ATOM    242  CB  ALA A  31      15.130  49.034  22.311  1.00 23.05           C  
ATOM    243  N   LEU A  32      18.025  50.847  23.276  1.00 24.67           N  
ATOM    244  CA  LEU A  32      19.477  50.753  23.433  1.00 24.19           C  
ATOM    245  C   LEU A  32      19.819  49.744  24.511  1.00 23.52           C  
ATOM    246  O   LEU A  32      19.395  49.891  25.654  1.00 22.14           O  
ATOM    247  CB  LEU A  32      20.069  52.102  23.840  1.00 27.69           C  
ATOM    248  CG  LEU A  32      20.518  53.089  22.766  1.00 31.07           C  
ATOM    249  CD1 LEU A  32      21.023  54.358  23.439  1.00 30.84           C  
ATOM    250  CD2 LEU A  32      21.618  52.467  21.919  1.00 32.13           C  
ATOM    251  N   LYS A  33      20.597  48.730  24.150  1.00 23.88           N  
ATOM    252  CA  LYS A  33      20.982  47.708  25.108  1.00 23.84           C  
ATOM    253  C   LYS A  33      22.489  47.680  25.320  1.00 26.32           C  
ATOM    254  O   LYS A  33      23.253  47.489  24.380  1.00 25.04           O  
ATOM    255  CB  LYS A  33      20.504  46.333  24.632  1.00 22.83           C  
ATOM    256  CG  LYS A  33      19.008  46.259  24.347  1.00 21.87           C  
ATOM    257  CD  LYS A  33      18.529  44.817  24.244  1.00 23.76           C  
ATOM    258  CE  LYS A  33      17.012  44.742  24.239  1.00 26.45           C  
ATOM    259  NZ  LYS A  33      16.512  43.342  24.404  1.00 28.12           N  
ATOM    260  N   LYS A  34      22.913  47.881  26.560  1.00 29.02           N  
ATOM    261  CA  LYS A  34      24.331  47.846  26.872  1.00 33.76           C  
ATOM    262  C   LYS A  34      24.693  46.416  27.241  1.00 33.98           C  
ATOM    263  O   LYS A  34      24.028  45.780  28.065  1.00 34.06           O  
ATOM    264  CB  LYS A  34      24.654  48.800  28.023  1.00 36.28           C  
ATOM    265  CG  LYS A  34      23.665  48.745  29.173  1.00 43.98           C  
ATOM    266  CD  LYS A  34      23.022  50.108  29.419  1.00 48.50           C  
ATOM    267  CE  LYS A  34      24.057  51.160  29.803  1.00 51.19           C  
ATOM    268  NZ  LYS A  34      23.448  52.515  29.942  1.00 52.48           N  
ATOM    269  N   ILE A  35      25.741  45.906  26.610  1.00 34.66           N  
ATOM    270  CA  ILE A  35      26.186  44.546  26.856  1.00 35.90           C  
ATOM    271  C   ILE A  35      27.440  44.567  27.711  1.00 37.78           C  
ATOM    272  O   ILE A  35      28.432  45.197  27.349  1.00 35.55           O  
ATOM    273  CB  ILE A  35      26.500  43.824  25.531  1.00 35.11           C  
ATOM    274  CG1 ILE A  35      25.306  43.938  24.577  1.00 35.41           C  
ATOM    275  CG2 ILE A  35      26.844  42.370  25.800  1.00 35.94           C  
ATOM    276  CD1 ILE A  35      24.018  43.373  25.123  1.00 34.84           C  
ATOM    277  N   ARG A  36      27.392  43.886  28.850  1.00 40.33           N  
ATOM    278  CA  ARG A  36      28.546  43.826  29.739  1.00 44.38           C  
ATOM    279  C   ARG A  36      29.483  42.694  29.332  1.00 43.65           C  
ATOM    280  O   ARG A  36      29.034  41.604  28.978  1.00 45.24           O  
ATOM    281  CB  ARG A  36      28.100  43.626  31.190  1.00 46.26           C  
ATOM    282  CG  ARG A  36      27.842  44.916  31.958  1.00 51.65           C  
ATOM    283  CD  ARG A  36      26.568  45.622  31.528  1.00 54.87           C  
ATOM    284  NE  ARG A  36      26.373  46.855  32.289  1.00 59.86           N  
ATOM    285  CZ  ARG A  36      25.268  47.596  32.258  1.00 61.23           C  
ATOM    286  NH1 ARG A  36      24.246  47.234  31.501  1.00 62.84           N  
ATOM    287  NH2 ARG A  36      25.184  48.702  32.986  1.00 63.23           N  
ATOM    288  N   THR A  41      35.653  42.854  31.539  1.00121.78           N  
ATOM    289  CA  THR A  41      35.830  43.845  30.484  1.00121.53           C  
ATOM    290  C   THR A  41      37.289  43.921  30.043  1.00120.73           C  
ATOM    291  O   THR A  41      38.129  44.499  30.734  1.00121.04           O  
ATOM    292  CB  THR A  41      35.381  45.243  30.954  1.00122.30           C  
ATOM    293  OG1 THR A  41      36.167  45.646  32.082  1.00122.74           O  
ATOM    294  CG2 THR A  41      33.912  45.223  31.348  1.00122.96           C  
ATOM    295  N   GLU A  42      37.581  43.334  28.886  1.00119.05           N  
ATOM    296  CA  GLU A  42      38.936  43.323  28.346  1.00116.93           C  
ATOM    297  C   GLU A  42      39.033  44.147  27.066  1.00114.04           C  
ATOM    298  O   GLU A  42      39.974  44.920  26.886  1.00114.06           O  
ATOM    299  CB  GLU A  42      39.370  41.884  28.060  1.00118.66           C  
ATOM    300  CG  GLU A  42      39.343  40.975  29.276  1.00120.85           C  
ATOM    301  CD  GLU A  42      39.599  39.525  28.920  1.00122.05           C  
ATOM    302  OE1 GLU A  42      40.650  39.240  28.309  1.00122.87           O  
ATOM    303  OE2 GLU A  42      38.749  38.671  29.250  1.00122.60           O  
ATOM    304  N   GLY A  43      38.057  43.975  26.179  1.00110.55           N  
ATOM    305  CA  GLY A  43      38.055  44.711  24.928  1.00105.55           C  
ATOM    306  C   GLY A  43      37.103  44.129  23.900  1.00101.75           C  
ATOM    307  O   GLY A  43      37.260  44.357  22.700  1.00101.80           O  
ATOM    308  N   VAL A  44      36.116  43.374  24.373  1.00 97.76           N  
ATOM    309  CA  VAL A  44      35.124  42.749  23.502  1.00 93.09           C  
ATOM    310  C   VAL A  44      35.776  41.777  22.522  1.00 89.23           C  
ATOM    311  O   VAL A  44      36.409  42.194  21.551  1.00 89.14           O  
ATOM    312  CB  VAL A  44      34.344  43.807  22.690  1.00 93.53           C  
ATOM    313  CG1 VAL A  44      33.213  43.141  21.922  1.00 93.37           C  
ATOM    314  CG2 VAL A  44      33.803  44.882  23.616  1.00 93.83           C  
ATOM    315  N   PRO A  45      35.623  40.463  22.761  1.00 84.86           N  
ATOM    316  CA  PRO A  45      36.209  39.448  21.879  1.00 80.86           C  
ATOM    317  C   PRO A  45      35.682  39.550  20.449  1.00 76.77           C  
ATOM    318  O   PRO A  45      34.473  39.631  20.224  1.00 76.20           O  
ATOM    319  CB  PRO A  45      35.821  38.137  22.560  1.00 81.48           C  
ATOM    320  CG  PRO A  45      34.518  38.476  23.209  1.00 82.75           C  
ATOM    321  CD  PRO A  45      34.805  39.831  23.810  1.00 83.84           C  
ATOM    322  N   SER A  46      36.603  39.545  19.490  1.00 72.09           N  
ATOM    323  CA  SER A  46      36.260  39.651  18.076  1.00 66.49           C  
ATOM    324  C   SER A  46      35.188  38.654  17.653  1.00 62.45           C  
ATOM    325  O   SER A  46      34.462  38.890  16.688  1.00 61.74           O  
ATOM    326  CB  SER A  46      37.509  39.445  17.216  1.00 66.71           C  
ATOM    327  OG  SER A  46      38.012  38.129  17.358  1.00 66.77           O  
ATOM    328  N   THR A  47      35.098  37.540  18.375  1.00 58.16           N  
ATOM    329  CA  THR A  47      34.113  36.507  18.070  1.00 53.81           C  
ATOM    330  C   THR A  47      32.694  37.043  18.234  1.00 50.48           C  
ATOM    331  O   THR A  47      31.839  36.829  17.375  1.00 47.99           O  
ATOM    332  CB  THR A  47      34.295  35.276  18.982  1.00 53.67           C  
ATOM    333  OG1 THR A  47      34.163  35.668  20.354  1.00 54.76           O  
ATOM    334  CG2 THR A  47      35.665  34.660  18.766  1.00 54.11           C  
ATOM    335  N   ALA A  48      32.452  37.739  19.341  1.00 47.26           N  
ATOM    336  CA  ALA A  48      31.142  38.319  19.611  1.00 44.52           C  
ATOM    337  C   ALA A  48      30.811  39.362  18.543  1.00 42.33           C  
ATOM    338  O   ALA A  48      29.704  39.385  18.005  1.00 40.13           O  
ATOM    339  CB  ALA A  48      31.130  38.962  20.992  1.00 44.18           C  
ATOM    340  N   ILE A  49      31.783  40.217  18.239  1.00 40.16           N  
ATOM    341  CA  ILE A  49      31.607  41.260  17.234  1.00 39.17           C  
ATOM    342  C   ILE A  49      31.180  40.669  15.891  1.00 39.24           C  
ATOM    343  O   ILE A  49      30.215  41.127  15.284  1.00 37.75           O  
ATOM    344  CB  ILE A  49      32.914  42.070  17.030  1.00 38.68           C  
ATOM    345  CG1 ILE A  49      33.274  42.814  18.319  1.00 37.84           C  
ATOM    346  CG2 ILE A  49      32.755  43.046  15.869  1.00 39.43           C  
ATOM    347  CD1 ILE A  49      32.230  43.829  18.765  1.00 37.55           C  
ATOM    348  N   ARG A  50      31.899  39.654  15.426  1.00 40.42           N  
ATOM    349  CA  ARG A  50      31.558  39.033  14.154  1.00 42.55           C  
ATOM    350  C   ARG A  50      30.181  38.387  14.195  1.00 41.88           C  
ATOM    351  O   ARG A  50      29.406  38.517  13.246  1.00 41.41           O  
ATOM    352  CB  ARG A  50      32.610  37.995  13.752  1.00 45.34           C  
ATOM    353  CG  ARG A  50      33.665  38.533  12.789  1.00 50.45           C  
ATOM    354  CD  ARG A  50      35.042  38.631  13.429  1.00 54.19           C  
ATOM    355  NE  ARG A  50      35.544  37.323  13.841  1.00 58.17           N  
ATOM    356  CZ  ARG A  50      36.763  37.107  14.324  1.00 59.63           C  
ATOM    357  NH1 ARG A  50      37.616  38.115  14.456  1.00 60.73           N  
ATOM    358  NH2 ARG A  50      37.127  35.882  14.681  1.00 59.88           N  
ATOM    359  N   GLU A  51      29.878  37.694  15.291  1.00 40.74           N  
ATOM    360  CA  GLU A  51      28.579  37.044  15.435  1.00 41.37           C  
ATOM    361  C   GLU A  51      27.450  38.060  15.345  1.00 39.39           C  
ATOM    362  O   GLU A  51      26.507  37.892  14.568  1.00 39.11           O  
ATOM    363  CB  GLU A  51      28.486  36.306  16.774  1.00 43.05           C  
ATOM    364  CG  GLU A  51      28.984  34.873  16.731  1.00 47.73           C  
ATOM    365  CD  GLU A  51      28.193  34.019  15.755  1.00 50.43           C  
ATOM    366  OE1 GLU A  51      26.971  33.853  15.958  1.00 52.01           O  
ATOM    367  OE2 GLU A  51      28.791  33.517  14.780  1.00 52.39           O  
ATOM    368  N   ILE A  52      27.556  39.116  16.143  1.00 38.02           N  
ATOM    369  CA  ILE A  52      26.547  40.163  16.168  1.00 38.42           C  
ATOM    370  C   ILE A  52      26.412  40.856  14.821  1.00 37.59           C  
ATOM    371  O   ILE A  52      25.314  41.224  14.415  1.00 35.93           O  
ATOM    372  CB  ILE A  52      26.870  41.215  17.246  1.00 39.43           C  
ATOM    373  CG1 ILE A  52      26.830  40.565  18.627  1.00 39.94           C  
ATOM    374  CG2 ILE A  52      25.870  42.353  17.185  1.00 41.36           C  
ATOM    375  CD1 ILE A  52      27.109  41.531  19.742  1.00 43.47           C  
ATOM    376  N   SER A  53      27.530  41.035  14.126  1.00 37.25           N  
ATOM    377  CA  SER A  53      27.495  41.682  12.824  1.00 36.32           C  
ATOM    378  C   SER A  53      26.649  40.850  11.868  1.00 35.48           C  
ATOM    379  O   SER A  53      25.923  41.389  11.036  1.00 36.02           O  
ATOM    380  CB  SER A  53      28.914  41.850  12.280  1.00 38.85           C  
ATOM    381  OG  SER A  53      29.668  42.699  13.125  1.00 41.50           O  
ATOM    382  N   LEU A  54      26.742  39.532  11.998  1.00 33.50           N  
ATOM    383  CA  LEU A  54      25.969  38.632  11.159  1.00 33.13           C  
ATOM    384  C   LEU A  54      24.482  38.815  11.438  1.00 31.83           C  
ATOM    385  O   LEU A  54      23.655  38.693  10.539  1.00 29.15           O  
ATOM    386  CB  LEU A  54      26.364  37.182  11.432  1.00 35.11           C  
ATOM    387  CG  LEU A  54      27.769  36.765  10.998  1.00 37.82           C  
ATOM    388  CD1 LEU A  54      28.071  35.375  11.529  1.00 39.51           C  
ATOM    389  CD2 LEU A  54      27.870  36.795   9.477  1.00 39.28           C  
ATOM    390  N   LEU A  55      24.149  39.120  12.689  1.00 30.09           N  
ATOM    391  CA  LEU A  55      22.759  39.318  13.083  1.00 29.11           C  
ATOM    392  C   LEU A  55      22.096  40.520  12.426  1.00 28.86           C  
ATOM    393  O   LEU A  55      20.872  40.563  12.290  1.00 27.41           O  
ATOM    394  CB  LEU A  55      22.655  39.442  14.605  1.00 29.75           C  
ATOM    395  CG  LEU A  55      22.933  38.131  15.342  1.00 30.39           C  
ATOM    396  CD1 LEU A  55      22.916  38.362  16.843  1.00 32.20           C  
ATOM    397  CD2 LEU A  55      21.881  37.101  14.945  1.00 31.75           C  
ATOM    398  N   LYS A  56      22.901  41.495  12.021  1.00 28.83           N  
ATOM    399  CA  LYS A  56      22.378  42.694  11.381  1.00 31.48           C  
ATOM    400  C   LYS A  56      21.810  42.355  10.006  1.00 30.90           C  
ATOM    401  O   LYS A  56      21.078  43.143   9.409  1.00 29.83           O  
ATOM    402  CB  LYS A  56      23.485  43.743  11.244  1.00 33.58           C  
ATOM    403  CG  LYS A  56      23.005  45.066  10.671  1.00 40.24           C  
ATOM    404  CD  LYS A  56      24.114  46.112  10.645  1.00 44.42           C  
ATOM    405  CE  LYS A  56      24.629  46.406  12.044  1.00 46.31           C  
ATOM    406  NZ  LYS A  56      25.608  47.532  12.061  1.00 48.81           N  
ATOM    407  N   GLU A  57      22.145  41.167   9.516  1.00 29.41           N  
ATOM    408  CA  GLU A  57      21.683  40.727   8.210  1.00 30.70           C  
ATOM    409  C   GLU A  57      20.450  39.831   8.231  1.00 29.15           C  
ATOM    410  O   GLU A  57      19.747  39.736   7.227  1.00 27.96           O  
ATOM    411  CB  GLU A  57      22.824  40.026   7.472  1.00 35.50           C  
ATOM    412  CG  GLU A  57      23.306  40.781   6.247  1.00 41.88           C  
ATOM    413  CD  GLU A  57      23.369  42.277   6.473  1.00 44.70           C  
ATOM    414  OE1 GLU A  57      24.088  42.713   7.397  1.00 47.67           O  
ATOM    415  OE2 GLU A  57      22.696  43.019   5.725  1.00 48.77           O  
ATOM    416  N   LEU A  58      20.177  39.159   9.347  1.00 27.04           N  
ATOM    417  CA  LEU A  58      18.987  38.316   9.375  1.00 26.31           C  
ATOM    418  C   LEU A  58      17.776  39.142   9.762  1.00 23.34           C  
ATOM    419  O   LEU A  58      17.398  39.242  10.933  1.00 20.04           O  
ATOM    420  CB  LEU A  58      19.135  37.116  10.317  1.00 30.73           C  
ATOM    421  CG  LEU A  58      19.719  37.255  11.711  1.00 32.80           C  
ATOM    422  CD1 LEU A  58      19.094  36.217  12.654  1.00 33.62           C  
ATOM    423  CD2 LEU A  58      21.219  37.067  11.607  1.00 38.71           C  
ATOM    424  N   ASN A  59      17.171  39.720   8.735  1.00 20.90           N  
ATOM    425  CA  ASN A  59      16.008  40.573   8.867  1.00 20.00           C  
ATOM    426  C   ASN A  59      14.739  39.829   8.489  1.00 19.39           C  
ATOM    427  O   ASN A  59      14.682  39.161   7.456  1.00 19.69           O  
ATOM    428  CB  ASN A  59      16.183  41.795   7.964  1.00 20.26           C  
ATOM    429  CG  ASN A  59      17.424  42.593   8.306  1.00 20.58           C  
ATOM    430  OD1 ASN A  59      18.171  43.020   7.423  1.00 22.17           O  
ATOM    431  ND2 ASN A  59      17.649  42.803   9.597  1.00 18.97           N  
ATOM    432  N   HIS A  60      13.720  39.960   9.333  1.00 19.10           N  
ATOM    433  CA  HIS A  60      12.427  39.317   9.111  1.00 18.55           C  
ATOM    434  C   HIS A  60      11.356  40.102   9.865  1.00 17.45           C  
ATOM    435  O   HIS A  60      11.619  40.648  10.937  1.00 19.03           O  
ATOM    436  CB  HIS A  60      12.457  37.870   9.622  1.00 18.61           C  
ATOM    437  CG  HIS A  60      11.185  37.118   9.377  1.00 18.06           C  
ATOM    438  ND1 HIS A  60      10.974  36.355   8.248  1.00 19.49           N  
ATOM    439  CD2 HIS A  60      10.039  37.052  10.095  1.00 17.32           C  
ATOM    440  CE1 HIS A  60       9.753  35.853   8.280  1.00 14.79           C  
ATOM    441  NE2 HIS A  60       9.164  36.262   9.389  1.00 19.41           N  
ATOM    442  N   PRO A  61      10.130  40.164   9.317  1.00 18.31           N  
ATOM    443  CA  PRO A  61       9.025  40.888   9.948  1.00 18.13           C  
ATOM    444  C   PRO A  61       8.751  40.494  11.404  1.00 17.28           C  
ATOM    445  O   PRO A  61       8.266  41.305  12.186  1.00 17.51           O  
ATOM    446  CB  PRO A  61       7.842  40.567   9.039  1.00 19.41           C  
ATOM    447  CG  PRO A  61       8.486  40.438   7.693  1.00 21.24           C  
ATOM    448  CD  PRO A  61       9.726  39.636   8.000  1.00 18.33           C  
ATOM    449  N   ASN A  62       9.066  39.259  11.771  1.00 18.48           N  
ATOM    450  CA  ASN A  62       8.821  38.811  13.140  1.00 17.82           C  
ATOM    451  C   ASN A  62      10.065  38.701  14.022  1.00 18.45           C  
ATOM    452  O   ASN A  62      10.064  38.012  15.044  1.00 18.46           O  
ATOM    453  CB  ASN A  62       8.053  37.494  13.113  1.00 17.72           C  
ATOM    454  CG  ASN A  62       6.717  37.630  12.401  1.00 16.53           C  
ATOM    455  OD1 ASN A  62       6.560  37.215  11.252  1.00 17.85           O  
ATOM    456  ND2 ASN A  62       5.755  38.240  13.078  1.00 15.86           N  
ATOM    457  N   ILE A  63      11.116  39.412  13.622  1.00 16.68           N  
ATOM    458  CA  ILE A  63      12.373  39.456  14.357  1.00 16.34           C  
ATOM    459  C   ILE A  63      12.634  40.933  14.615  1.00 16.63           C  
ATOM    460  O   ILE A  63      12.608  41.740  13.686  1.00 14.63           O  
ATOM    461  CB  ILE A  63      13.537  38.886  13.523  1.00 18.61           C  
ATOM    462  CG1 ILE A  63      13.306  37.404  13.258  1.00 21.20           C  
ATOM    463  CG2 ILE A  63      14.865  39.083  14.249  1.00 15.73           C  
ATOM    464  CD1 ILE A  63      14.324  36.830  12.299  1.00 26.33           C  
ATOM    465  N   VAL A  64      12.846  41.292  15.877  1.00 13.81           N  
ATOM    466  CA  VAL A  64      13.116  42.681  16.230  1.00 15.47           C  
ATOM    467  C   VAL A  64      14.373  43.092  15.482  1.00 17.14           C  
ATOM    468  O   VAL A  64      15.428  42.490  15.652  1.00 17.07           O  
ATOM    469  CB  VAL A  64      13.350  42.846  17.753  1.00 13.21           C  
ATOM    470  CG1 VAL A  64      13.735  44.285  18.071  1.00 15.83           C  
ATOM    471  CG2 VAL A  64      12.089  42.481  18.509  1.00 14.29           C  
ATOM    472  N   LYS A  65      14.264  44.127  14.658  1.00 20.03           N  
ATOM    473  CA  LYS A  65      15.400  44.562  13.863  1.00 18.91           C  
ATOM    474  C   LYS A  65      16.573  45.133  14.641  1.00 18.72           C  
ATOM    475  O   LYS A  65      16.410  45.995  15.496  1.00 18.87           O  
ATOM    476  CB  LYS A  65      14.952  45.589  12.827  1.00 20.11           C  
ATOM    477  CG  LYS A  65      16.045  45.994  11.848  1.00 19.50           C  
ATOM    478  CD  LYS A  65      15.506  47.003  10.850  1.00 21.72           C  
ATOM    479  CE  LYS A  65      16.574  47.444   9.860  1.00 23.02           C  
ATOM    480  NZ  LYS A  65      17.064  46.295   9.065  1.00 20.30           N  
ATOM    481  N   LEU A  66      17.759  44.625  14.336  1.00 19.51           N  
ATOM    482  CA  LEU A  66      18.987  45.102  14.950  1.00 20.56           C  
ATOM    483  C   LEU A  66      19.398  46.262  14.049  1.00 22.79           C  
ATOM    484  O   LEU A  66      19.842  46.048  12.927  1.00 23.64           O  
ATOM    485  CB  LEU A  66      20.049  44.006  14.926  1.00 21.27           C  
ATOM    486  CG  LEU A  66      21.469  44.393  15.347  1.00 22.61           C  
ATOM    487  CD1 LEU A  66      21.453  45.024  16.730  1.00 22.96           C  
ATOM    488  CD2 LEU A  66      22.350  43.153  15.324  1.00 23.84           C  
ATOM    489  N   LEU A  67      19.227  47.484  14.541  1.00 23.23           N  
ATOM    490  CA  LEU A  67      19.539  48.678  13.764  1.00 26.39           C  
ATOM    491  C   LEU A  67      21.028  48.965  13.647  1.00 28.26           C  
ATOM    492  O   LEU A  67      21.529  49.265  12.565  1.00 28.15           O  
ATOM    493  CB  LEU A  67      18.822  49.891  14.365  1.00 27.00           C  
ATOM    494  CG  LEU A  67      17.297  49.970  14.205  1.00 29.34           C  
ATOM    495  CD1 LEU A  67      16.648  48.709  14.712  1.00 33.46           C  
ATOM    496  CD2 LEU A  67      16.761  51.166  14.961  1.00 26.35           C  
ATOM    497  N   ASP A  68      21.741  48.876  14.760  1.00 28.55           N  
ATOM    498  CA  ASP A  68      23.169  49.139  14.739  1.00 31.88           C  
ATOM    499  C   ASP A  68      23.901  48.475  15.882  1.00 32.94           C  
ATOM    500  O   ASP A  68      23.331  48.211  16.941  1.00 28.88           O  
ATOM    501  CB  ASP A  68      23.442  50.646  14.789  1.00 32.29           C  
ATOM    502  CG  ASP A  68      23.535  51.274  13.410  1.00 35.57           C  
ATOM    503  OD1 ASP A  68      24.447  50.893  12.639  1.00 36.52           O  
ATOM    504  OD2 ASP A  68      22.702  52.152  13.105  1.00 34.43           O  
ATOM    505  N   VAL A  69      25.178  48.208  15.641  1.00 34.21           N  
ATOM    506  CA  VAL A  69      26.053  47.598  16.624  1.00 37.20           C  
ATOM    507  C   VAL A  69      27.127  48.640  16.876  1.00 38.83           C  
ATOM    508  O   VAL A  69      28.011  48.844  16.045  1.00 41.34           O  
ATOM    509  CB  VAL A  69      26.696  46.309  16.073  1.00 36.34           C  
ATOM    510  CG1 VAL A  69      27.684  45.740  17.083  1.00 35.35           C  
ATOM    511  CG2 VAL A  69      25.610  45.291  15.756  1.00 35.94           C  
ATOM    512  N   ILE A  70      27.038  49.318  18.014  1.00 40.92           N  
ATOM    513  CA  ILE A  70      28.005  50.351  18.343  1.00 41.62           C  
ATOM    514  C   ILE A  70      29.088  49.864  19.292  1.00 43.23           C  
ATOM    515  O   ILE A  70      28.840  49.614  20.474  1.00 40.24           O  
ATOM    516  CB  ILE A  70      27.317  51.580  18.963  1.00 41.25           C  
ATOM    517  CG1 ILE A  70      26.274  52.136  17.990  1.00 41.05           C  
ATOM    518  CG2 ILE A  70      28.351  52.652  19.276  1.00 41.95           C  
ATOM    519  CD1 ILE A  70      25.527  53.340  18.516  1.00 40.22           C  
ATOM    520  N   HIS A  71      30.293  49.726  18.751  1.00 45.75           N  
ATOM    521  CA  HIS A  71      31.443  49.297  19.527  1.00 48.69           C  
ATOM    522  C   HIS A  71      32.410  50.471  19.559  1.00 51.42           C  
ATOM    523  O   HIS A  71      33.125  50.724  18.588  1.00 51.78           O  
ATOM    524  CB  HIS A  71      32.121  48.097  18.870  1.00 47.80           C  
ATOM    525  CG  HIS A  71      33.231  47.516  19.687  1.00 48.45           C  
ATOM    526  ND1 HIS A  71      34.232  46.742  19.140  1.00 48.10           N  
ATOM    527  CD2 HIS A  71      33.486  47.577  21.016  1.00 48.46           C  
ATOM    528  CE1 HIS A  71      35.055  46.351  20.097  1.00 49.01           C  
ATOM    529  NE2 HIS A  71      34.624  46.844  21.245  1.00 49.04           N  
ATOM    530  N   THR A  72      32.414  51.192  20.673  1.00 54.47           N  
ATOM    531  CA  THR A  72      33.280  52.351  20.845  1.00 57.51           C  
ATOM    532  C   THR A  72      33.773  52.411  22.280  1.00 59.28           C  
ATOM    533  O   THR A  72      33.093  51.947  23.195  1.00 59.36           O  
ATOM    534  CB  THR A  72      32.527  53.664  20.526  1.00 57.28           C  
ATOM    535  OG1 THR A  72      32.298  53.754  19.115  1.00 58.10           O  
ATOM    536  CG2 THR A  72      33.329  54.874  20.986  1.00 57.12           C  
ATOM    537  N   GLU A  73      34.960  52.981  22.469  1.00 61.70           N  
ATOM    538  CA  GLU A  73      35.539  53.108  23.797  1.00 64.06           C  
ATOM    539  C   GLU A  73      35.538  51.740  24.477  1.00 64.03           C  
ATOM    540  O   GLU A  73      35.370  51.631  25.693  1.00 64.15           O  
ATOM    541  CB  GLU A  73      34.728  54.124  24.608  1.00 65.68           C  
ATOM    542  CG  GLU A  73      35.338  54.511  25.942  1.00 69.29           C  
ATOM    543  CD  GLU A  73      34.728  55.782  26.505  1.00 71.38           C  
ATOM    544  OE1 GLU A  73      33.486  55.844  26.636  1.00 71.43           O  
ATOM    545  OE2 GLU A  73      35.494  56.721  26.818  1.00 71.76           O  
ATOM    546  N   ASN A  74      35.734  50.699  23.672  1.00 63.77           N  
ATOM    547  CA  ASN A  74      35.758  49.326  24.162  1.00 63.00           C  
ATOM    548  C   ASN A  74      34.542  48.996  25.018  1.00 61.46           C  
ATOM    549  O   ASN A  74      34.663  48.583  26.172  1.00 61.62           O  
ATOM    550  CB  ASN A  74      37.046  49.066  24.946  1.00 63.97           C  
ATOM    551  CG  ASN A  74      38.254  48.922  24.042  1.00 65.11           C  
ATOM    552  OD1 ASN A  74      38.549  49.803  23.234  1.00 66.14           O  
ATOM    553  ND2 ASN A  74      38.960  47.807  24.173  1.00 66.66           N  
ATOM    554  N   LYS A  75      33.368  49.193  24.428  1.00 59.39           N  
ATOM    555  CA  LYS A  75      32.092  48.913  25.076  1.00 56.18           C  
ATOM    556  C   LYS A  75      31.105  48.525  23.984  1.00 52.23           C  
ATOM    557  O   LYS A  75      31.248  48.951  22.837  1.00 51.54           O  
ATOM    558  CB  LYS A  75      31.587  50.145  25.830  1.00 58.63           C  
ATOM    559  CG  LYS A  75      32.350  50.441  27.109  1.00 61.27           C  
ATOM    560  CD  LYS A  75      32.339  49.250  28.066  1.00 63.86           C  
ATOM    561  CE  LYS A  75      30.930  48.874  28.520  1.00 64.59           C  
ATOM    562  NZ  LYS A  75      30.083  48.316  27.426  1.00 64.96           N  
ATOM    563  N   LEU A  76      30.110  47.716  24.333  1.00 47.37           N  
ATOM    564  CA  LEU A  76      29.132  47.276  23.348  1.00 41.83           C  
ATOM    565  C   LEU A  76      27.719  47.778  23.596  1.00 38.28           C  
ATOM    566  O   LEU A  76      27.183  47.652  24.696  1.00 36.94           O  
ATOM    567  CB  LEU A  76      29.102  45.748  23.269  1.00 41.20           C  
ATOM    568  CG  LEU A  76      29.460  45.122  21.920  1.00 41.38           C  
ATOM    569  CD1 LEU A  76      29.032  43.659  21.920  1.00 40.74           C  
ATOM    570  CD2 LEU A  76      28.765  45.868  20.791  1.00 40.25           C  
ATOM    571  N   TYR A  77      27.124  48.338  22.547  1.00 33.87           N  
ATOM    572  CA  TYR A  77      25.764  48.852  22.590  1.00 30.68           C  
ATOM    573  C   TYR A  77      25.034  48.310  21.375  1.00 27.81           C  
ATOM    574  O   TYR A  77      25.524  48.422  20.252  1.00 27.86           O  
ATOM    575  CB  TYR A  77      25.759  50.379  22.518  1.00 33.52           C  
ATOM    576  CG  TYR A  77      26.283  51.074  23.748  1.00 36.93           C  
ATOM    577  CD1 TYR A  77      25.517  51.145  24.909  1.00 39.19           C  
ATOM    578  CD2 TYR A  77      27.536  51.685  23.746  1.00 38.93           C  
ATOM    579  CE1 TYR A  77      25.981  51.812  26.039  1.00 41.78           C  
ATOM    580  CE2 TYR A  77      28.011  52.355  24.871  1.00 41.07           C  
ATOM    581  CZ  TYR A  77      27.227  52.415  26.013  1.00 41.79           C  
ATOM    582  OH  TYR A  77      27.682  53.082  27.128  1.00 44.76           O  
ATOM    583  N   LEU A  78      23.876  47.705  21.596  1.00 25.27           N  
ATOM    584  CA  LEU A  78      23.087  47.181  20.492  1.00 24.09           C  
ATOM    585  C   LEU A  78      21.882  48.096  20.360  1.00 23.34           C  
ATOM    586  O   LEU A  78      21.219  48.395  21.352  1.00 23.16           O  
ATOM    587  CB  LEU A  78      22.635  45.745  20.782  1.00 23.14           C  
ATOM    588  CG  LEU A  78      23.756  44.720  20.984  1.00 24.41           C  
ATOM    589  CD1 LEU A  78      23.155  43.354  21.288  1.00 23.78           C  
ATOM    590  CD2 LEU A  78      24.625  44.654  19.732  1.00 24.41           C  
ATOM    591  N   VAL A  79      21.619  48.567  19.146  1.00 22.77           N  
ATOM    592  CA  VAL A  79      20.478  49.444  18.915  1.00 21.26           C  
ATOM    593  C   VAL A  79      19.408  48.639  18.185  1.00 23.25           C  
ATOM    594  O   VAL A  79      19.611  48.194  17.051  1.00 24.48           O  
ATOM    595  CB  VAL A  79      20.868  50.662  18.060  1.00 21.14           C  
ATOM    596  CG1 VAL A  79      19.719  51.651  18.021  1.00 20.34           C  
ATOM    597  CG2 VAL A  79      22.115  51.325  18.633  1.00 21.32           C  
ATOM    598  N   PHE A  80      18.270  48.453  18.843  1.00 23.03           N  
ATOM    599  CA  PHE A  80      17.174  47.681  18.274  1.00 22.00           C  
ATOM    600  C   PHE A  80      15.934  48.521  17.994  1.00 21.51           C  
ATOM    601  O   PHE A  80      15.750  49.617  18.537  1.00 22.13           O  
ATOM    602  CB  PHE A  80      16.762  46.553  19.235  1.00 21.45           C  
ATOM    603  CG  PHE A  80      17.725  45.404  19.296  1.00 19.29           C  
ATOM    604  CD1 PHE A  80      17.691  44.395  18.336  1.00 15.59           C  
ATOM    605  CD2 PHE A  80      18.648  45.309  20.335  1.00 19.10           C  
ATOM    606  CE1 PHE A  80      18.560  43.306  18.412  1.00 19.81           C  
ATOM    607  CE2 PHE A  80      19.524  44.224  20.419  1.00 16.58           C  
ATOM    608  CZ  PHE A  80      19.480  43.221  19.459  1.00 17.62           C  
ATOM    609  N   GLU A  81      15.089  47.973  17.134  1.00 21.91           N  
ATOM    610  CA  GLU A  81      13.811  48.568  16.792  1.00 19.91           C  
ATOM    611  C   GLU A  81      13.053  48.586  18.125  1.00 19.74           C  
ATOM    612  O   GLU A  81      13.190  47.666  18.927  1.00 15.64           O  
ATOM    613  CB  GLU A  81      13.107  47.646  15.796  1.00 20.60           C  
ATOM    614  CG  GLU A  81      11.626  47.864  15.639  1.00 22.76           C  
ATOM    615  CD  GLU A  81      10.959  46.709  14.917  1.00 23.03           C  
ATOM    616  OE1 GLU A  81       9.762  46.824  14.601  1.00 26.01           O  
ATOM    617  OE2 GLU A  81      11.625  45.680  14.672  1.00 19.36           O  
ATOM    618  N   PHE A  82      12.260  49.621  18.364  1.00 18.13           N  
ATOM    619  CA  PHE A  82      11.511  49.728  19.612  1.00 18.94           C  
ATOM    620  C   PHE A  82      10.073  49.247  19.496  1.00 20.10           C  
ATOM    621  O   PHE A  82       9.386  49.581  18.533  1.00 15.67           O  
ATOM    622  CB  PHE A  82      11.488  51.184  20.077  1.00 20.48           C  
ATOM    623  CG  PHE A  82      10.681  51.413  21.329  1.00 22.26           C  
ATOM    624  CD1 PHE A  82      11.213  51.112  22.578  1.00 21.11           C  
ATOM    625  CD2 PHE A  82       9.392  51.931  21.257  1.00 22.48           C  
ATOM    626  CE1 PHE A  82      10.482  51.324  23.737  1.00 21.16           C  
ATOM    627  CE2 PHE A  82       8.645  52.147  22.417  1.00 24.90           C  
ATOM    628  CZ  PHE A  82       9.192  51.843  23.659  1.00 22.55           C  
ATOM    629  N   LEU A  83       9.632  48.453  20.473  1.00 19.91           N  
ATOM    630  CA  LEU A  83       8.247  47.983  20.536  1.00 22.23           C  
ATOM    631  C   LEU A  83       7.784  48.307  21.954  1.00 23.94           C  
ATOM    632  O   LEU A  83       8.529  48.127  22.915  1.00 21.92           O  
ATOM    633  CB  LEU A  83       8.129  46.488  20.242  1.00 23.44           C  
ATOM    634  CG  LEU A  83       8.073  46.204  18.735  1.00 25.81           C  
ATOM    635  CD1 LEU A  83       9.483  46.155  18.189  1.00 24.53           C  
ATOM    636  CD2 LEU A  83       7.364  44.889  18.467  1.00 26.47           C  
ATOM    637  N   HIS A  84       6.553  48.788  22.077  1.00 25.49           N  
ATOM    638  CA  HIS A  84       6.018  49.223  23.363  1.00 26.55           C  
ATOM    639  C   HIS A  84       5.740  48.239  24.492  1.00 26.45           C  
ATOM    640  O   HIS A  84       5.629  48.658  25.642  1.00 27.77           O  
ATOM    641  CB  HIS A  84       4.758  50.058  23.126  1.00 27.36           C  
ATOM    642  CG  HIS A  84       4.994  51.281  22.296  1.00 27.39           C  
ATOM    643  ND1 HIS A  84       5.216  51.227  20.936  1.00 27.09           N  
ATOM    644  CD2 HIS A  84       5.055  52.590  22.637  1.00 28.51           C  
ATOM    645  CE1 HIS A  84       5.402  52.451  20.474  1.00 25.10           C  
ATOM    646  NE2 HIS A  84       5.310  53.297  21.486  1.00 28.39           N  
ATOM    647  N   GLN A  85       5.628  46.950  24.202  1.00 25.84           N  
ATOM    648  CA  GLN A  85       5.336  46.004  25.273  1.00 25.99           C  
ATOM    649  C   GLN A  85       5.725  44.575  24.947  1.00 23.95           C  
ATOM    650  O   GLN A  85       5.811  44.195  23.782  1.00 23.26           O  
ATOM    651  CB  GLN A  85       3.843  46.065  25.623  1.00 28.51           C  
ATOM    652  CG  GLN A  85       3.423  45.180  26.811  1.00 31.68           C  
ATOM    653  CD  GLN A  85       2.056  45.549  27.362  1.00 33.69           C  
ATOM    654  OE1 GLN A  85       1.872  46.632  27.922  1.00 37.12           O  
ATOM    655  NE2 GLN A  85       1.087  44.655  27.201  1.00 33.15           N  
ATOM    656  N   ASP A  86       5.963  43.785  25.987  1.00 23.53           N  
ATOM    657  CA  ASP A  86       6.331  42.387  25.801  1.00 23.12           C  
ATOM    658  C   ASP A  86       5.171  41.477  26.185  1.00 22.59           C  
ATOM    659  O   ASP A  86       4.226  41.908  26.851  1.00 21.65           O  
ATOM    660  CB  ASP A  86       7.572  42.038  26.627  1.00 23.16           C  
ATOM    661  CG  ASP A  86       7.360  42.240  28.114  1.00 27.68           C  
ATOM    662  OD1 ASP A  86       6.454  41.596  28.685  1.00 28.75           O  
ATOM    663  OD2 ASP A  86       8.106  43.043  28.710  1.00 28.56           O  
ATOM    664  N   LEU A  87       5.255  40.217  25.762  1.00 21.41           N  
ATOM    665  CA  LEU A  87       4.211  39.231  26.022  1.00 20.20           C  
ATOM    666  C   LEU A  87       3.987  38.946  27.506  1.00 21.90           C  
ATOM    667  O   LEU A  87       2.870  38.634  27.924  1.00 21.45           O  
ATOM    668  CB  LEU A  87       4.542  37.918  25.302  1.00 20.89           C  
ATOM    669  CG  LEU A  87       3.432  36.856  25.304  1.00 20.26           C  
ATOM    670  CD1 LEU A  87       2.208  37.405  24.585  1.00 21.17           C  
ATOM    671  CD2 LEU A  87       3.918  35.593  24.621  1.00 18.84           C  
ATOM    672  N   LYS A  88       5.042  39.041  28.303  1.00 21.01           N  
ATOM    673  CA  LYS A  88       4.892  38.770  29.723  1.00 25.88           C  
ATOM    674  C   LYS A  88       3.920  39.770  30.326  1.00 25.76           C  
ATOM    675  O   LYS A  88       2.960  39.388  30.994  1.00 27.07           O  
ATOM    676  CB  LYS A  88       6.244  38.849  30.428  1.00 26.34           C  
ATOM    677  CG  LYS A  88       6.197  38.415  31.877  1.00 30.25           C  
ATOM    678  CD  LYS A  88       7.589  38.403  32.494  1.00 34.28           C  
ATOM    679  CE  LYS A  88       7.556  37.908  33.934  1.00 35.80           C  
ATOM    680  NZ  LYS A  88       6.700  38.778  34.792  1.00 40.12           N  
ATOM    681  N   LYS A  89       4.156  41.055  30.073  1.00 27.80           N  
ATOM    682  CA  LYS A  89       3.279  42.099  30.600  1.00 27.31           C  
ATOM    683  C   LYS A  89       1.870  41.969  30.028  1.00 25.52           C  
ATOM    684  O   LYS A  89       0.884  42.171  30.736  1.00 24.88           O  
ATOM    685  CB  LYS A  89       3.844  43.485  30.272  1.00 30.25           C  
ATOM    686  CG  LYS A  89       5.201  43.762  30.903  1.00 35.26           C  
ATOM    687  CD  LYS A  89       5.784  45.100  30.451  1.00 39.70           C  
ATOM    688  CE  LYS A  89       6.043  45.119  28.945  1.00 41.94           C  
ATOM    689  NZ  LYS A  89       6.699  46.377  28.480  1.00 43.51           N  
ATOM    690  N   PHE A  90       1.782  41.617  28.747  1.00 24.00           N  
ATOM    691  CA  PHE A  90       0.496  41.465  28.079  1.00 25.28           C  
ATOM    692  C   PHE A  90      -0.307  40.320  28.698  1.00 25.76           C  
ATOM    693  O   PHE A  90      -1.515  40.436  28.904  1.00 27.40           O  
ATOM    694  CB  PHE A  90       0.704  41.206  26.585  1.00 25.41           C  
ATOM    695  CG  PHE A  90      -0.564  41.230  25.787  1.00 27.19           C  
ATOM    696  CD1 PHE A  90      -1.341  42.384  25.726  1.00 29.59           C  
ATOM    697  CD2 PHE A  90      -0.991  40.097  25.102  1.00 29.50           C  
ATOM    698  CE1 PHE A  90      -2.527  42.408  24.994  1.00 30.22           C  
ATOM    699  CE2 PHE A  90      -2.176  40.112  24.368  1.00 29.79           C  
ATOM    700  CZ  PHE A  90      -2.943  41.268  24.314  1.00 30.72           C  
ATOM    701  N   MET A  91       0.369  39.214  28.987  1.00 26.90           N  
ATOM    702  CA  MET A  91      -0.282  38.062  29.600  1.00 28.01           C  
ATOM    703  C   MET A  91      -0.770  38.435  30.992  1.00 28.97           C  
ATOM    704  O   MET A  91      -1.885  38.089  31.375  1.00 29.11           O  
ATOM    705  CB  MET A  91       0.689  36.888  29.709  1.00 28.19           C  
ATOM    706  CG  MET A  91       1.143  36.328  28.380  1.00 31.22           C  
ATOM    707  SD  MET A  91       2.312  34.972  28.588  1.00 35.57           S  
ATOM    708  CE  MET A  91       1.193  33.649  28.535  1.00 27.32           C  
ATOM    709  N   ASP A  92       0.074  39.132  31.748  1.00 30.49           N  
ATOM    710  CA  ASP A  92      -0.291  39.551  33.099  1.00 33.19           C  
ATOM    711  C   ASP A  92      -1.501  40.470  33.057  1.00 34.07           C  
ATOM    712  O   ASP A  92      -2.382  40.388  33.911  1.00 34.61           O  
ATOM    713  CB  ASP A  92       0.866  40.284  33.783  1.00 34.63           C  
ATOM    714  CG  ASP A  92       2.022  39.365  34.120  1.00 36.42           C  
ATOM    715  OD1 ASP A  92       1.792  38.143  34.238  1.00 38.33           O  
ATOM    716  OD2 ASP A  92       3.157  39.866  34.280  1.00 35.00           O  
ATOM    717  N   ALA A  93      -1.538  41.340  32.055  1.00 33.80           N  
ATOM    718  CA  ALA A  93      -2.637  42.283  31.890  1.00 35.76           C  
ATOM    719  C   ALA A  93      -3.922  41.601  31.431  1.00 36.54           C  
ATOM    720  O   ALA A  93      -5.013  42.141  31.599  1.00 37.47           O  
ATOM    721  CB  ALA A  93      -2.241  43.363  30.890  1.00 34.61           C  
ATOM    722  N   SER A  94      -3.793  40.415  30.850  1.00 37.76           N  
ATOM    723  CA  SER A  94      -4.951  39.677  30.360  1.00 39.43           C  
ATOM    724  C   SER A  94      -5.257  38.477  31.248  1.00 38.50           C  
ATOM    725  O   SER A  94      -5.905  37.529  30.816  1.00 38.74           O  
ATOM    726  CB  SER A  94      -4.693  39.190  28.932  1.00 38.89           C  
ATOM    727  OG  SER A  94      -4.264  40.252  28.102  1.00 41.28           O  
ATOM    728  N   ALA A  95      -4.790  38.523  32.489  1.00 39.88           N  
ATOM    729  CA  ALA A  95      -5.002  37.425  33.425  1.00 40.15           C  
ATOM    730  C   ALA A  95      -6.474  37.104  33.683  1.00 40.79           C  
ATOM    731  O   ALA A  95      -6.889  35.949  33.580  1.00 40.59           O  
ATOM    732  CB  ALA A  95      -4.302  37.732  34.742  1.00 40.72           C  
ATOM    733  N   LEU A  96      -7.258  38.125  34.015  1.00 41.13           N  
ATOM    734  CA  LEU A  96      -8.674  37.937  34.313  1.00 40.96           C  
ATOM    735  C   LEU A  96      -9.500  37.307  33.203  1.00 39.70           C  
ATOM    736  O   LEU A  96     -10.414  36.533  33.475  1.00 40.40           O  
ATOM    737  CB  LEU A  96      -9.320  39.270  34.709  1.00 42.35           C  
ATOM    738  CG  LEU A  96      -8.914  39.906  36.042  1.00 43.87           C  
ATOM    739  CD1 LEU A  96      -9.785  41.131  36.300  1.00 45.28           C  
ATOM    740  CD2 LEU A  96      -9.079  38.900  37.174  1.00 44.74           C  
ATOM    741  N   THR A  97      -9.184  37.630  31.954  1.00 38.48           N  
ATOM    742  CA  THR A  97      -9.947  37.100  30.830  1.00 37.61           C  
ATOM    743  C   THR A  97      -9.156  36.178  29.903  1.00 36.37           C  
ATOM    744  O   THR A  97      -9.738  35.358  29.193  1.00 35.27           O  
ATOM    745  CB  THR A  97     -10.530  38.252  29.990  1.00 39.94           C  
ATOM    746  OG1 THR A  97      -9.461  38.995  29.384  1.00 41.87           O  
ATOM    747  CG2 THR A  97     -11.339  39.192  30.876  1.00 41.05           C  
ATOM    748  N   GLY A  98      -7.834  36.318  29.913  1.00 33.95           N  
ATOM    749  CA  GLY A  98      -6.993  35.502  29.058  1.00 32.94           C  
ATOM    750  C   GLY A  98      -6.962  36.021  27.629  1.00 32.06           C  
ATOM    751  O   GLY A  98      -7.949  36.566  27.137  1.00 32.24           O  
ATOM    752  N   ILE A  99      -5.825  35.865  26.964  1.00 29.06           N  
ATOM    753  CA  ILE A  99      -5.683  36.311  25.587  1.00 26.90           C  
ATOM    754  C   ILE A  99      -6.657  35.510  24.722  1.00 25.59           C  
ATOM    755  O   ILE A  99      -6.691  34.286  24.792  1.00 25.99           O  
ATOM    756  CB  ILE A  99      -4.247  36.067  25.084  1.00 27.31           C  
ATOM    757  CG1 ILE A  99      -3.247  36.750  26.021  1.00 26.11           C  
ATOM    758  CG2 ILE A  99      -4.092  36.591  23.664  1.00 27.60           C  
ATOM    759  CD1 ILE A  99      -1.793  36.421  25.722  1.00 25.19           C  
ATOM    760  N   PRO A 100      -7.471  36.190  23.901  1.00 25.15           N  
ATOM    761  CA  PRO A 100      -8.418  35.453  23.058  1.00 24.89           C  
ATOM    762  C   PRO A 100      -7.677  34.427  22.193  1.00 24.81           C  
ATOM    763  O   PRO A 100      -6.585  34.707  21.695  1.00 23.66           O  
ATOM    764  CB  PRO A 100      -9.069  36.555  22.222  1.00 24.76           C  
ATOM    765  CG  PRO A 100      -8.988  37.753  23.114  1.00 27.41           C  
ATOM    766  CD  PRO A 100      -7.600  37.643  23.697  1.00 24.83           C  
ATOM    767  N   LEU A 101      -8.271  33.249  22.016  1.00 23.74           N  
ATOM    768  CA  LEU A 101      -7.652  32.192  21.221  1.00 24.13           C  
ATOM    769  C   LEU A 101      -7.194  32.656  19.842  1.00 24.01           C  
ATOM    770  O   LEU A 101      -6.110  32.292  19.391  1.00 22.47           O  
ATOM    771  CB  LEU A 101      -8.606  31.005  21.055  1.00 25.64           C  
ATOM    772  CG  LEU A 101      -8.052  29.838  20.227  1.00 28.68           C  
ATOM    773  CD1 LEU A 101      -6.788  29.294  20.891  1.00 28.22           C  
ATOM    774  CD2 LEU A 101      -9.103  28.737  20.107  1.00 30.54           C  
ATOM    775  N   PRO A 102      -8.016  33.464  19.149  1.00 23.43           N  
ATOM    776  CA  PRO A 102      -7.616  33.932  17.818  1.00 21.66           C  
ATOM    777  C   PRO A 102      -6.284  34.674  17.850  1.00 20.27           C  
ATOM    778  O   PRO A 102      -5.467  34.539  16.940  1.00 20.22           O  
ATOM    779  CB  PRO A 102      -8.780  34.835  17.409  1.00 22.50           C  
ATOM    780  CG  PRO A 102      -9.943  34.182  18.078  1.00 22.96           C  
ATOM    781  CD  PRO A 102      -9.389  33.896  19.458  1.00 22.11           C  
ATOM    782  N   LEU A 103      -6.059  35.447  18.907  1.00 20.12           N  
ATOM    783  CA  LEU A 103      -4.817  36.196  19.024  1.00 20.16           C  
ATOM    784  C   LEU A 103      -3.662  35.265  19.402  1.00 19.71           C  
ATOM    785  O   LEU A 103      -2.524  35.477  18.985  1.00 18.76           O  
ATOM    786  CB  LEU A 103      -4.962  37.311  20.061  1.00 20.02           C  
ATOM    787  CG  LEU A 103      -3.795  38.300  20.173  1.00 20.50           C  
ATOM    788  CD1 LEU A 103      -3.511  38.949  18.819  1.00 20.37           C  
ATOM    789  CD2 LEU A 103      -4.132  39.358  21.210  1.00 21.08           C  
ATOM    790  N   ILE A 104      -3.957  34.244  20.202  1.00 18.09           N  
ATOM    791  CA  ILE A 104      -2.944  33.280  20.611  1.00 18.42           C  
ATOM    792  C   ILE A 104      -2.442  32.583  19.357  1.00 19.13           C  
ATOM    793  O   ILE A 104      -1.237  32.476  19.125  1.00 17.19           O  
ATOM    794  CB  ILE A 104      -3.525  32.223  21.591  1.00 17.70           C  
ATOM    795  CG1 ILE A 104      -3.814  32.880  22.943  1.00 19.45           C  
ATOM    796  CG2 ILE A 104      -2.543  31.060  21.771  1.00 17.68           C  
ATOM    797  CD1 ILE A 104      -4.460  31.955  23.958  1.00 21.16           C  
ATOM    798  N   LYS A 105      -3.385  32.134  18.535  1.00 17.32           N  
ATOM    799  CA  LYS A 105      -3.064  31.447  17.298  1.00 17.46           C  
ATOM    800  C   LYS A 105      -2.235  32.337  16.378  1.00 17.66           C  
ATOM    801  O   LYS A 105      -1.250  31.886  15.801  1.00 17.02           O  
ATOM    802  CB  LYS A 105      -4.352  31.010  16.594  1.00 17.46           C  
ATOM    803  CG  LYS A 105      -4.121  30.196  15.329  1.00 19.70           C  
ATOM    804  CD  LYS A 105      -5.405  29.542  14.826  1.00 21.44           C  
ATOM    805  CE  LYS A 105      -5.956  28.532  15.824  1.00 19.47           C  
ATOM    806  NZ  LYS A 105      -7.077  27.728  15.248  1.00 21.39           N  
ATOM    807  N   SER A 106      -2.635  33.599  16.252  1.00 17.26           N  
ATOM    808  CA  SER A 106      -1.924  34.552  15.405  1.00 17.87           C  
ATOM    809  C   SER A 106      -0.490  34.735  15.891  1.00 18.02           C  
ATOM    810  O   SER A 106       0.460  34.719  15.105  1.00 15.86           O  
ATOM    811  CB  SER A 106      -2.633  35.906  15.425  1.00 17.09           C  
ATOM    812  OG  SER A 106      -1.822  36.909  14.835  1.00 16.61           O  
ATOM    813  N   TYR A 107      -0.344  34.924  17.196  1.00 16.30           N  
ATOM    814  CA  TYR A 107       0.971  35.096  17.779  1.00 16.21           C  
ATOM    815  C   TYR A 107       1.854  33.868  17.568  1.00 16.12           C  
ATOM    816  O   TYR A 107       3.009  33.997  17.166  1.00 16.21           O  
ATOM    817  CB  TYR A 107       0.851  35.411  19.277  1.00 16.09           C  
ATOM    818  CG  TYR A 107       0.460  36.848  19.597  1.00 17.80           C  
ATOM    819  CD1 TYR A 107       0.405  37.824  18.599  1.00 17.93           C  
ATOM    820  CD2 TYR A 107       0.191  37.238  20.911  1.00 17.90           C  
ATOM    821  CE1 TYR A 107       0.096  39.158  18.901  1.00 19.39           C  
ATOM    822  CE2 TYR A 107      -0.116  38.563  21.224  1.00 19.57           C  
ATOM    823  CZ  TYR A 107      -0.161  39.517  20.217  1.00 20.21           C  
ATOM    824  OH  TYR A 107      -0.447  40.825  20.537  1.00 20.52           O  
ATOM    825  N   LEU A 108       1.323  32.679  17.832  1.00 15.31           N  
ATOM    826  CA  LEU A 108       2.103  31.451  17.659  1.00 16.86           C  
ATOM    827  C   LEU A 108       2.527  31.289  16.199  1.00 17.89           C  
ATOM    828  O   LEU A 108       3.654  30.894  15.904  1.00 15.56           O  
ATOM    829  CB  LEU A 108       1.280  30.230  18.087  1.00 18.37           C  
ATOM    830  CG  LEU A 108       1.985  28.865  18.045  1.00 19.90           C  
ATOM    831  CD1 LEU A 108       3.208  28.877  18.963  1.00 19.23           C  
ATOM    832  CD2 LEU A 108       1.010  27.781  18.486  1.00 21.81           C  
ATOM    833  N   PHE A 109       1.598  31.595  15.302  1.00 16.29           N  
ATOM    834  CA  PHE A 109       1.816  31.504  13.863  1.00 16.78           C  
ATOM    835  C   PHE A 109       2.959  32.427  13.441  1.00 17.31           C  
ATOM    836  O   PHE A 109       3.876  32.017  12.721  1.00 17.99           O  
ATOM    837  CB  PHE A 109       0.520  31.887  13.149  1.00 15.66           C  
ATOM    838  CG  PHE A 109       0.569  31.738  11.652  1.00 19.39           C  
ATOM    839  CD1 PHE A 109       0.723  30.490  11.066  1.00 19.04           C  
ATOM    840  CD2 PHE A 109       0.405  32.847  10.829  1.00 18.98           C  
ATOM    841  CE1 PHE A 109       0.708  30.346   9.676  1.00 23.92           C  
ATOM    842  CE2 PHE A 109       0.390  32.711   9.443  1.00 20.86           C  
ATOM    843  CZ  PHE A 109       0.541  31.459   8.870  1.00 19.82           C  
ATOM    844  N   GLN A 110       2.919  33.668  13.913  1.00 16.84           N  
ATOM    845  CA  GLN A 110       3.961  34.636  13.574  1.00 15.84           C  
ATOM    846  C   GLN A 110       5.295  34.257  14.194  1.00 17.39           C  
ATOM    847  O   GLN A 110       6.344  34.387  13.560  1.00 15.95           O  
ATOM    848  CB  GLN A 110       3.570  36.032  14.047  1.00 16.60           C  
ATOM    849  CG  GLN A 110       2.400  36.647  13.312  1.00 13.57           C  
ATOM    850  CD  GLN A 110       2.036  37.998  13.887  1.00 18.25           C  
ATOM    851  OE1 GLN A 110       2.832  38.939  13.836  1.00 16.47           O  
ATOM    852  NE2 GLN A 110       0.833  38.100  14.458  1.00 16.25           N  
ATOM    853  N   LEU A 111       5.257  33.802  15.442  1.00 15.87           N  
ATOM    854  CA  LEU A 111       6.471  33.403  16.135  1.00 17.44           C  
ATOM    855  C   LEU A 111       7.147  32.243  15.404  1.00 15.01           C  
ATOM    856  O   LEU A 111       8.366  32.222  15.262  1.00 14.58           O  
ATOM    857  CB  LEU A 111       6.141  33.023  17.585  1.00 18.61           C  
ATOM    858  CG  LEU A 111       6.382  34.098  18.661  1.00 22.57           C  
ATOM    859  CD1 LEU A 111       6.477  35.474  18.050  1.00 24.01           C  
ATOM    860  CD2 LEU A 111       5.284  34.029  19.703  1.00 19.23           C  
ATOM    861  N   LEU A 112       6.355  31.280  14.940  1.00 14.76           N  
ATOM    862  CA  LEU A 112       6.906  30.151  14.206  1.00 16.13           C  
ATOM    863  C   LEU A 112       7.530  30.633  12.892  1.00 16.81           C  
ATOM    864  O   LEU A 112       8.548  30.101  12.453  1.00 14.68           O  
ATOM    865  CB  LEU A 112       5.818  29.108  13.926  1.00 16.56           C  
ATOM    866  CG  LEU A 112       5.446  28.221  15.124  1.00 17.15           C  
ATOM    867  CD1 LEU A 112       4.084  27.583  14.896  1.00 19.18           C  
ATOM    868  CD2 LEU A 112       6.516  27.157  15.319  1.00 17.92           C  
ATOM    869  N   GLN A 113       6.920  31.630  12.261  1.00 17.88           N  
ATOM    870  CA  GLN A 113       7.476  32.167  11.014  1.00 16.88           C  
ATOM    871  C   GLN A 113       8.852  32.749  11.327  1.00 16.97           C  
ATOM    872  O   GLN A 113       9.797  32.573  10.568  1.00 17.63           O  
ATOM    873  CB  GLN A 113       6.574  33.260  10.436  1.00 18.27           C  
ATOM    874  CG  GLN A 113       5.295  32.729   9.808  1.00 20.81           C  
ATOM    875  CD  GLN A 113       4.426  33.827   9.244  1.00 20.27           C  
ATOM    876  OE1 GLN A 113       4.834  34.558   8.345  1.00 24.06           O  
ATOM    877  NE2 GLN A 113       3.215  33.948   9.767  1.00 23.08           N  
ATOM    878  N   GLY A 114       8.958  33.432  12.462  1.00 17.02           N  
ATOM    879  CA  GLY A 114      10.230  34.008  12.866  1.00 16.35           C  
ATOM    880  C   GLY A 114      11.269  32.927  13.105  1.00 17.24           C  
ATOM    881  O   GLY A 114      12.405  33.038  12.650  1.00 19.54           O  
ATOM    882  N   LEU A 115      10.892  31.873  13.822  1.00 17.82           N  
ATOM    883  CA  LEU A 115      11.823  30.779  14.087  1.00 18.19           C  
ATOM    884  C   LEU A 115      12.241  30.086  12.792  1.00 17.86           C  
ATOM    885  O   LEU A 115      13.418  29.801  12.582  1.00 18.53           O  
ATOM    886  CB  LEU A 115      11.198  29.749  15.033  1.00 16.20           C  
ATOM    887  CG  LEU A 115      11.364  29.980  16.541  1.00 21.30           C  
ATOM    888  CD1 LEU A 115      10.830  31.338  16.924  1.00 24.82           C  
ATOM    889  CD2 LEU A 115      10.636  28.889  17.303  1.00 21.99           C  
ATOM    890  N   ALA A 116      11.272  29.812  11.926  1.00 18.77           N  
ATOM    891  CA  ALA A 116      11.566  29.144  10.667  1.00 19.06           C  
ATOM    892  C   ALA A 116      12.628  29.926   9.898  1.00 21.13           C  
ATOM    893  O   ALA A 116      13.543  29.338   9.322  1.00 22.11           O  
ATOM    894  CB  ALA A 116      10.305  29.015   9.837  1.00 19.62           C  
ATOM    895  N   PHE A 117      12.505  31.251   9.897  1.00 20.84           N  
ATOM    896  CA  PHE A 117      13.466  32.097   9.195  1.00 20.53           C  
ATOM    897  C   PHE A 117      14.874  31.958   9.777  1.00 19.74           C  
ATOM    898  O   PHE A 117      15.820  31.627   9.061  1.00 19.17           O  
ATOM    899  CB  PHE A 117      13.038  33.565   9.258  1.00 21.31           C  
ATOM    900  CG  PHE A 117      14.028  34.507   8.631  1.00 21.96           C  
ATOM    901  CD1 PHE A 117      14.171  34.568   7.247  1.00 25.22           C  
ATOM    902  CD2 PHE A 117      14.870  35.279   9.425  1.00 23.42           C  
ATOM    903  CE1 PHE A 117      15.148  35.384   6.658  1.00 23.58           C  
ATOM    904  CE2 PHE A 117      15.848  36.096   8.853  1.00 24.41           C  
ATOM    905  CZ  PHE A 117      15.988  36.146   7.465  1.00 24.43           C  
ATOM    906  N   CYS A 118      15.010  32.216  11.075  1.00 19.56           N  
ATOM    907  CA  CYS A 118      16.304  32.132  11.737  1.00 19.06           C  
ATOM    908  C   CYS A 118      16.884  30.728  11.710  1.00 18.00           C  
ATOM    909  O   CYS A 118      18.095  30.553  11.551  1.00 20.76           O  
ATOM    910  CB  CYS A 118      16.196  32.606  13.190  1.00 20.63           C  
ATOM    911  SG  CYS A 118      15.764  34.359  13.396  1.00 23.97           S  
ATOM    912  N   HIS A 119      16.022  29.728  11.867  1.00 16.25           N  
ATOM    913  CA  HIS A 119      16.470  28.349  11.867  1.00 18.35           C  
ATOM    914  C   HIS A 119      16.993  27.947  10.496  1.00 20.21           C  
ATOM    915  O   HIS A 119      17.894  27.116  10.401  1.00 19.33           O  
ATOM    916  CB  HIS A 119      15.339  27.401  12.284  1.00 16.34           C  
ATOM    917  CG  HIS A 119      14.985  27.479  13.738  1.00 14.71           C  
ATOM    918  ND1 HIS A 119      15.702  28.230  14.644  1.00 18.81           N  
ATOM    919  CD2 HIS A 119      13.996  26.882  14.445  1.00 14.74           C  
ATOM    920  CE1 HIS A 119      15.172  28.090  15.849  1.00 15.72           C  
ATOM    921  NE2 HIS A 119      14.134  27.277  15.754  1.00 16.28           N  
ATOM    922  N   SER A 120      16.432  28.540   9.442  1.00 21.06           N  
ATOM    923  CA  SER A 120      16.863  28.224   8.082  1.00 22.04           C  
ATOM    924  C   SER A 120      18.252  28.804   7.838  1.00 24.24           C  
ATOM    925  O   SER A 120      18.958  28.368   6.926  1.00 25.75           O  
ATOM    926  CB  SER A 120      15.867  28.768   7.046  1.00 21.87           C  
ATOM    927  OG  SER A 120      15.967  30.170   6.890  1.00 25.79           O  
ATOM    928  N   HIS A 121      18.642  29.785   8.652  1.00 23.58           N  
ATOM    929  CA  HIS A 121      19.968  30.387   8.541  1.00 26.44           C  
ATOM    930  C   HIS A 121      20.890  29.806   9.611  1.00 26.79           C  
ATOM    931  O   HIS A 121      21.993  30.312   9.845  1.00 26.62           O  
ATOM    932  CB  HIS A 121      19.897  31.915   8.672  1.00 27.02           C  
ATOM    933  CG  HIS A 121      19.357  32.599   7.454  1.00 30.89           C  
ATOM    934  ND1 HIS A 121      18.024  32.556   7.102  1.00 33.06           N  
ATOM    935  CD2 HIS A 121      19.979  33.304   6.480  1.00 31.28           C  
ATOM    936  CE1 HIS A 121      17.850  33.203   5.963  1.00 31.49           C  
ATOM    937  NE2 HIS A 121      19.021  33.665   5.564  1.00 32.05           N  
ATOM    938  N   ARG A 122      20.426  28.736  10.254  1.00 26.97           N  
ATOM    939  CA  ARG A 122      21.194  28.040  11.282  1.00 28.91           C  
ATOM    940  C   ARG A 122      21.463  28.899  12.513  1.00 28.78           C  
ATOM    941  O   ARG A 122      22.484  28.742  13.189  1.00 28.75           O  
ATOM    942  CB  ARG A 122      22.515  27.557  10.684  1.00 31.67           C  
ATOM    943  CG  ARG A 122      22.340  26.776   9.394  1.00 37.37           C  
ATOM    944  CD  ARG A 122      23.672  26.577   8.684  1.00 43.80           C  
ATOM    945  NE  ARG A 122      23.493  26.119   7.308  1.00 48.34           N  
ATOM    946  CZ  ARG A 122      22.952  26.852   6.339  1.00 50.44           C  
ATOM    947  NH1 ARG A 122      22.535  28.087   6.588  1.00 51.08           N  
ATOM    948  NH2 ARG A 122      22.824  26.346   5.119  1.00 52.16           N  
ATOM    949  N   VAL A 123      20.541  29.810  12.797  1.00 24.69           N  
ATOM    950  CA  VAL A 123      20.662  30.687  13.948  1.00 24.31           C  
ATOM    951  C   VAL A 123      19.530  30.348  14.902  1.00 24.37           C  
ATOM    952  O   VAL A 123      18.377  30.265  14.492  1.00 22.39           O  
ATOM    953  CB  VAL A 123      20.529  32.177  13.547  1.00 23.98           C  
ATOM    954  CG1 VAL A 123      20.597  33.055  14.779  1.00 24.26           C  
ATOM    955  CG2 VAL A 123      21.625  32.557  12.573  1.00 23.53           C  
ATOM    956  N   LEU A 124      19.854  30.137  16.170  1.00 23.46           N  
ATOM    957  CA  LEU A 124      18.814  29.836  17.136  1.00 23.21           C  
ATOM    958  C   LEU A 124      18.812  30.870  18.253  1.00 21.96           C  
ATOM    959  O   LEU A 124      19.739  31.672  18.373  1.00 20.61           O  
ATOM    960  CB  LEU A 124      18.989  28.410  17.675  1.00 25.78           C  
ATOM    961  CG  LEU A 124      20.357  27.939  18.161  1.00 26.56           C  
ATOM    962  CD1 LEU A 124      20.655  28.576  19.502  1.00 31.24           C  
ATOM    963  CD2 LEU A 124      20.360  26.426  18.298  1.00 28.96           C  
ATOM    964  N   HIS A 125      17.754  30.882  19.054  1.00 20.40           N  
ATOM    965  CA  HIS A 125      17.683  31.848  20.134  1.00 20.39           C  
ATOM    966  C   HIS A 125      18.337  31.289  21.392  1.00 20.16           C  
ATOM    967  O   HIS A 125      19.260  31.897  21.933  1.00 19.12           O  
ATOM    968  CB  HIS A 125      16.235  32.224  20.429  1.00 19.13           C  
ATOM    969  CG  HIS A 125      16.107  33.383  21.366  1.00 18.76           C  
ATOM    970  ND1 HIS A 125      15.648  34.618  20.965  1.00 21.70           N  
ATOM    971  CD2 HIS A 125      16.418  33.504  22.677  1.00 18.09           C  
ATOM    972  CE1 HIS A 125      15.681  35.450  21.990  1.00 18.52           C  
ATOM    973  NE2 HIS A 125      16.144  34.799  23.041  1.00 21.91           N  
ATOM    974  N   ARG A 126      17.835  30.142  21.848  1.00 18.95           N  
ATOM    975  CA  ARG A 126      18.346  29.452  23.027  1.00 21.65           C  
ATOM    976  C   ARG A 126      17.763  29.973  24.345  1.00 21.29           C  
ATOM    977  O   ARG A 126      17.882  29.311  25.377  1.00 21.93           O  
ATOM    978  CB  ARG A 126      19.882  29.531  23.048  1.00 24.83           C  
ATOM    979  CG  ARG A 126      20.598  28.452  23.858  1.00 33.29           C  
ATOM    980  CD  ARG A 126      20.459  28.668  25.355  1.00 37.41           C  
ATOM    981  NE  ARG A 126      21.303  27.763  26.128  1.00 42.51           N  
ATOM    982  CZ  ARG A 126      21.184  27.576  27.438  1.00 40.98           C  
ATOM    983  NH1 ARG A 126      20.251  28.232  28.115  1.00 40.77           N  
ATOM    984  NH2 ARG A 126      21.995  26.737  28.069  1.00 42.22           N  
ATOM    985  N   ASP A 127      17.136  31.148  24.330  1.00 19.65           N  
ATOM    986  CA  ASP A 127      16.550  31.678  25.562  1.00 19.44           C  
ATOM    987  C   ASP A 127      15.219  32.389  25.344  1.00 19.59           C  
ATOM    988  O   ASP A 127      15.010  33.514  25.814  1.00 18.58           O  
ATOM    989  CB  ASP A 127      17.528  32.620  26.273  1.00 20.06           C  
ATOM    990  CG  ASP A 127      17.090  32.941  27.693  1.00 22.13           C  
ATOM    991  OD1 ASP A 127      16.508  32.045  28.346  1.00 21.86           O  
ATOM    992  OD2 ASP A 127      17.331  34.073  28.161  1.00 21.43           O  
ATOM    993  N   LEU A 128      14.321  31.724  24.627  1.00 17.49           N  
ATOM    994  CA  LEU A 128      12.998  32.273  24.358  1.00 18.66           C  
ATOM    995  C   LEU A 128      12.152  32.280  25.614  1.00 18.23           C  
ATOM    996  O   LEU A 128      12.085  31.278  26.338  1.00 18.80           O  
ATOM    997  CB  LEU A 128      12.273  31.454  23.299  1.00 19.51           C  
ATOM    998  CG  LEU A 128      12.709  31.634  21.854  1.00 23.11           C  
ATOM    999  CD1 LEU A 128      11.677  30.965  20.966  1.00 21.65           C  
ATOM   1000  CD2 LEU A 128      12.825  33.114  21.519  1.00 25.48           C  
ATOM   1001  N   LYS A 129      11.493  33.409  25.858  1.00 16.55           N  
ATOM   1002  CA  LYS A 129      10.654  33.575  27.034  1.00 17.88           C  
ATOM   1003  C   LYS A 129       9.702  34.728  26.746  1.00 17.21           C  
ATOM   1004  O   LYS A 129       9.983  35.570  25.887  1.00 16.73           O  
ATOM   1005  CB  LYS A 129      11.521  33.905  28.252  1.00 18.22           C  
ATOM   1006  CG  LYS A 129      12.189  35.273  28.160  1.00 23.32           C  
ATOM   1007  CD  LYS A 129      13.177  35.531  29.283  1.00 24.60           C  
ATOM   1008  CE  LYS A 129      14.515  34.891  28.989  1.00 24.95           C  
ATOM   1009  NZ  LYS A 129      15.569  35.406  29.911  1.00 25.11           N  
ATOM   1010  N   PRO A 130       8.562  34.782  27.451  1.00 16.60           N  
ATOM   1011  CA  PRO A 130       7.589  35.857  27.234  1.00 17.13           C  
ATOM   1012  C   PRO A 130       8.224  37.240  27.256  1.00 17.25           C  
ATOM   1013  O   PRO A 130       7.802  38.137  26.529  1.00 17.74           O  
ATOM   1014  CB  PRO A 130       6.601  35.657  28.380  1.00 18.97           C  
ATOM   1015  CG  PRO A 130       6.586  34.152  28.526  1.00 16.70           C  
ATOM   1016  CD  PRO A 130       8.063  33.812  28.447  1.00 17.10           C  
ATOM   1017  N   GLN A 131       9.242  37.399  28.093  1.00 17.33           N  
ATOM   1018  CA  GLN A 131       9.933  38.673  28.230  1.00 21.18           C  
ATOM   1019  C   GLN A 131      10.573  39.168  26.933  1.00 20.72           C  
ATOM   1020  O   GLN A 131      10.637  40.377  26.706  1.00 22.73           O  
ATOM   1021  CB  GLN A 131      10.995  38.576  29.329  0.80 19.89           C  
ATOM   1022  CG  GLN A 131      11.546  39.913  29.782  0.80 26.08           C  
ATOM   1023  CD  GLN A 131      12.593  39.766  30.872  0.80 28.38           C  
ATOM   1024  OE1 GLN A 131      12.359  39.103  31.887  0.80 28.12           O  
ATOM   1025  NE2 GLN A 131      13.752  40.387  30.672  0.80 27.64           N  
ATOM   1026  N   ASN A 132      11.056  38.264  26.084  1.00 19.96           N  
ATOM   1027  CA  ASN A 132      11.662  38.725  24.836  1.00 18.19           C  
ATOM   1028  C   ASN A 132      10.818  38.555  23.576  1.00 17.75           C  
ATOM   1029  O   ASN A 132      11.346  38.453  22.465  1.00 16.02           O  
ATOM   1030  CB  ASN A 132      13.064  38.129  24.625  1.00 18.74           C  
ATOM   1031  CG  ASN A 132      13.108  36.631  24.778  1.00 19.90           C  
ATOM   1032  OD1 ASN A 132      12.220  35.916  24.318  1.00 22.98           O  
ATOM   1033  ND2 ASN A 132      14.168  36.139  25.413  1.00 21.71           N  
ATOM   1034  N   LEU A 133       9.503  38.529  23.759  1.00 15.68           N  
ATOM   1035  CA  LEU A 133       8.553  38.448  22.649  1.00 17.36           C  
ATOM   1036  C   LEU A 133       7.842  39.801  22.724  1.00 19.29           C  
ATOM   1037  O   LEU A 133       7.090  40.064  23.661  1.00 19.18           O  
ATOM   1038  CB  LEU A 133       7.568  37.289  22.860  1.00 18.06           C  
ATOM   1039  CG  LEU A 133       7.894  35.931  22.222  1.00 20.72           C  
ATOM   1040  CD1 LEU A 133       9.380  35.680  22.203  1.00 21.93           C  
ATOM   1041  CD2 LEU A 133       7.155  34.819  22.961  1.00 16.19           C  
ATOM   1042  N   LEU A 134       8.097  40.664  21.745  1.00 19.12           N  
ATOM   1043  CA  LEU A 134       7.528  42.005  21.754  1.00 19.67           C  
ATOM   1044  C   LEU A 134       6.341  42.182  20.823  1.00 19.76           C  
ATOM   1045  O   LEU A 134       6.302  41.607  19.740  1.00 19.56           O  
ATOM   1046  CB  LEU A 134       8.630  43.015  21.418  1.00 20.61           C  
ATOM   1047  CG  LEU A 134       9.921  42.855  22.246  1.00 22.52           C  
ATOM   1048  CD1 LEU A 134      10.906  43.956  21.879  1.00 22.02           C  
ATOM   1049  CD2 LEU A 134       9.606  42.922  23.736  1.00 21.62           C  
ATOM   1050  N   ILE A 135       5.372  42.988  21.246  1.00 18.94           N  
ATOM   1051  CA  ILE A 135       4.172  43.201  20.446  1.00 20.38           C  
ATOM   1052  C   ILE A 135       3.890  44.676  20.211  1.00 20.69           C  
ATOM   1053  O   ILE A 135       4.314  45.524  20.994  1.00 21.79           O  
ATOM   1054  CB  ILE A 135       2.927  42.584  21.127  1.00 20.81           C  
ATOM   1055  CG1 ILE A 135       2.629  43.326  22.435  1.00 23.72           C  
ATOM   1056  CG2 ILE A 135       3.170  41.109  21.420  1.00 22.90           C  
ATOM   1057  CD1 ILE A 135       1.330  42.898  23.124  1.00 24.55           C  
ATOM   1058  N   ASN A 136       3.188  44.974  19.118  1.00 21.96           N  
ATOM   1059  CA  ASN A 136       2.812  46.348  18.802  1.00 22.59           C  
ATOM   1060  C   ASN A 136       1.293  46.425  18.693  1.00 24.79           C  
ATOM   1061  O   ASN A 136       0.609  45.403  18.743  1.00 22.27           O  
ATOM   1062  CB  ASN A 136       3.467  46.830  17.503  1.00 23.33           C  
ATOM   1063  CG  ASN A 136       3.005  46.061  16.284  1.00 23.83           C  
ATOM   1064  OD1 ASN A 136       1.909  45.503  16.259  1.00 25.30           O  
ATOM   1065  ND2 ASN A 136       3.836  46.051  15.247  1.00 22.78           N  
ATOM   1066  N   THR A 137       0.765  47.634  18.542  1.00 27.08           N  
ATOM   1067  CA  THR A 137      -0.681  47.834  18.470  1.00 30.10           C  
ATOM   1068  C   THR A 137      -1.353  47.323  17.200  1.00 31.38           C  
ATOM   1069  O   THR A 137      -2.582  47.327  17.102  1.00 33.41           O  
ATOM   1070  CB  THR A 137      -1.026  49.326  18.644  1.00 30.95           C  
ATOM   1071  OG1 THR A 137      -0.330  50.096  17.658  1.00 32.02           O  
ATOM   1072  CG2 THR A 137      -0.616  49.802  20.025  1.00 31.99           C  
ATOM   1073  N   GLU A 138      -0.559  46.872  16.237  1.00 32.96           N  
ATOM   1074  CA  GLU A 138      -1.103  46.378  14.975  1.00 34.08           C  
ATOM   1075  C   GLU A 138      -1.329  44.866  14.906  1.00 32.30           C  
ATOM   1076  O   GLU A 138      -1.704  44.340  13.857  1.00 34.95           O  
ATOM   1077  CB  GLU A 138      -0.190  46.804  13.830  1.00 36.66           C  
ATOM   1078  CG  GLU A 138      -0.093  48.307  13.667  1.00 42.73           C  
ATOM   1079  CD  GLU A 138       1.096  48.711  12.835  1.00 45.67           C  
ATOM   1080  OE1 GLU A 138       1.248  48.166  11.722  1.00 47.73           O  
ATOM   1081  OE2 GLU A 138       1.876  49.572  13.294  1.00 48.74           O  
ATOM   1082  N   GLY A 139      -1.097  44.166  16.010  1.00 28.91           N  
ATOM   1083  CA  GLY A 139      -1.301  42.728  16.010  1.00 23.77           C  
ATOM   1084  C   GLY A 139      -0.057  41.919  15.702  1.00 22.04           C  
ATOM   1085  O   GLY A 139      -0.125  40.700  15.525  1.00 18.65           O  
ATOM   1086  N   ALA A 140       1.091  42.583  15.644  1.00 20.94           N  
ATOM   1087  CA  ALA A 140       2.324  41.868  15.354  1.00 18.01           C  
ATOM   1088  C   ALA A 140       3.041  41.488  16.641  1.00 18.15           C  
ATOM   1089  O   ALA A 140       2.836  42.108  17.681  1.00 16.55           O  
ATOM   1090  CB  ALA A 140       3.241  42.727  14.486  1.00 18.97           C  
ATOM   1091  N   ILE A 141       3.865  40.445  16.555  1.00 18.74           N  
ATOM   1092  CA  ILE A 141       4.674  39.988  17.675  1.00 17.74           C  
ATOM   1093  C   ILE A 141       6.038  39.659  17.072  1.00 16.97           C  
ATOM   1094  O   ILE A 141       6.125  39.093  15.975  1.00 15.50           O  
ATOM   1095  CB  ILE A 141       4.053  38.746  18.390  1.00 18.58           C  
ATOM   1096  CG1 ILE A 141       4.881  38.404  19.628  1.00 17.34           C  
ATOM   1097  CG2 ILE A 141       3.979  37.555  17.444  1.00 15.43           C  
ATOM   1098  CD1 ILE A 141       4.135  37.566  20.683  1.00 18.96           C  
ATOM   1099  N   LYS A 142       7.100  40.039  17.772  1.00 16.41           N  
ATOM   1100  CA  LYS A 142       8.452  39.818  17.267  1.00 16.87           C  
ATOM   1101  C   LYS A 142       9.399  39.225  18.306  1.00 16.12           C  
ATOM   1102  O   LYS A 142       9.285  39.489  19.509  1.00 16.27           O  
ATOM   1103  CB  LYS A 142       9.035  41.147  16.754  1.00 16.61           C  
ATOM   1104  CG  LYS A 142       8.156  41.866  15.729  1.00 18.95           C  
ATOM   1105  CD  LYS A 142       8.869  43.072  15.117  1.00 18.48           C  
ATOM   1106  CE  LYS A 142       8.000  43.771  14.069  1.00 18.14           C  
ATOM   1107  NZ  LYS A 142       8.773  44.772  13.277  1.00 18.23           N  
ATOM   1108  N   LEU A 143      10.342  38.418  17.838  1.00 18.12           N  
ATOM   1109  CA  LEU A 143      11.313  37.816  18.740  1.00 17.72           C  
ATOM   1110  C   LEU A 143      12.495  38.759  18.947  1.00 17.24           C  
ATOM   1111  O   LEU A 143      13.123  39.209  17.981  1.00 13.38           O  
ATOM   1112  CB  LEU A 143      11.798  36.478  18.176  1.00 20.18           C  
ATOM   1113  CG  LEU A 143      10.715  35.396  18.181  1.00 22.45           C  
ATOM   1114  CD1 LEU A 143      10.237  35.138  16.757  1.00 24.54           C  
ATOM   1115  CD2 LEU A 143      11.270  34.124  18.798  1.00 22.79           C  
ATOM   1116  N   ALA A 144      12.786  39.059  20.213  1.00 13.78           N  
ATOM   1117  CA  ALA A 144      13.891  39.939  20.577  1.00 15.06           C  
ATOM   1118  C   ALA A 144      15.107  39.156  21.054  1.00 16.51           C  
ATOM   1119  O   ALA A 144      14.979  38.041  21.561  1.00 14.76           O  
ATOM   1120  CB  ALA A 144      13.456  40.904  21.689  1.00 11.63           C  
ATOM   1121  N   ASP A 145      16.280  39.764  20.909  1.00 18.24           N  
ATOM   1122  CA  ASP A 145      17.541  39.170  21.351  1.00 19.40           C  
ATOM   1123  C   ASP A 145      17.920  37.856  20.689  1.00 20.45           C  
ATOM   1124  O   ASP A 145      18.649  37.050  21.268  1.00 20.26           O  
ATOM   1125  CB  ASP A 145      17.533  38.983  22.873  1.00 21.63           C  
ATOM   1126  CG  ASP A 145      17.482  40.298  23.618  1.00 23.04           C  
ATOM   1127  OD1 ASP A 145      17.719  41.349  22.985  1.00 25.72           O  
ATOM   1128  OD2 ASP A 145      17.212  40.288  24.837  1.00 24.79           O  
ATOM   1129  N   PHE A 146      17.444  37.635  19.473  1.00 20.06           N  
ATOM   1130  CA  PHE A 146      17.774  36.407  18.773  1.00 21.32           C  
ATOM   1131  C   PHE A 146      19.273  36.352  18.496  1.00 21.79           C  
ATOM   1132  O   PHE A 146      19.874  37.351  18.125  1.00 23.02           O  
ATOM   1133  CB  PHE A 146      17.012  36.333  17.454  1.00 24.41           C  
ATOM   1134  CG  PHE A 146      16.500  34.965  17.134  1.00 26.14           C  
ATOM   1135  CD1 PHE A 146      17.366  33.962  16.711  1.00 27.12           C  
ATOM   1136  CD2 PHE A 146      15.147  34.667  17.283  1.00 27.10           C  
ATOM   1137  CE1 PHE A 146      16.891  32.678  16.442  1.00 27.40           C  
ATOM   1138  CE2 PHE A 146      14.663  33.384  17.016  1.00 28.23           C  
ATOM   1139  CZ  PHE A 146      15.540  32.388  16.595  1.00 25.78           C  
ATOM   1140  N   GLY A 147      19.877  35.189  18.709  1.00 22.49           N  
ATOM   1141  CA  GLY A 147      21.297  35.034  18.432  1.00 24.18           C  
ATOM   1142  C   GLY A 147      22.288  35.599  19.429  1.00 24.72           C  
ATOM   1143  O   GLY A 147      23.492  35.432  19.252  1.00 27.10           O  
ATOM   1144  N   LEU A 148      21.808  36.264  20.473  1.00 23.67           N  
ATOM   1145  CA  LEU A 148      22.711  36.825  21.468  1.00 25.69           C  
ATOM   1146  C   LEU A 148      23.307  35.766  22.392  1.00 27.30           C  
ATOM   1147  O   LEU A 148      24.455  35.889  22.823  1.00 27.95           O  
ATOM   1148  CB  LEU A 148      21.982  37.894  22.292  1.00 25.95           C  
ATOM   1149  CG  LEU A 148      21.989  39.310  21.707  1.00 26.16           C  
ATOM   1150  CD1 LEU A 148      21.932  39.276  20.194  1.00 29.06           C  
ATOM   1151  CD2 LEU A 148      20.836  40.092  22.284  1.00 28.27           C  
ATOM   1152  N   ALA A 149      22.539  34.721  22.687  1.00 28.67           N  
ATOM   1153  CA  ALA A 149      23.016  33.659  23.571  1.00 30.45           C  
ATOM   1154  C   ALA A 149      24.329  33.055  23.081  1.00 32.30           C  
ATOM   1155  O   ALA A 149      25.221  32.762  23.881  1.00 31.82           O  
ATOM   1156  CB  ALA A 149      21.955  32.568  23.710  1.00 30.75           C  
ATOM   1157  N   ARG A 150      24.453  32.866  21.772  1.00 33.05           N  
ATOM   1158  CA  ARG A 150      25.677  32.297  21.225  1.00 36.70           C  
ATOM   1159  C   ARG A 150      26.818  33.308  21.275  1.00 37.33           C  
ATOM   1160  O   ARG A 150      27.982  32.935  21.416  1.00 38.17           O  
ATOM   1161  CB  ARG A 150      25.470  31.827  19.784  1.00 37.07           C  
ATOM   1162  CG  ARG A 150      26.711  31.155  19.217  1.00 41.29           C  
ATOM   1163  CD  ARG A 150      26.516  30.587  17.823  1.00 42.99           C  
ATOM   1164  NE  ARG A 150      27.751  29.961  17.362  1.00 46.68           N  
ATOM   1165  CZ  ARG A 150      27.903  29.350  16.192  1.00 48.74           C  
ATOM   1166  NH1 ARG A 150      26.891  29.270  15.338  1.00 50.06           N  
ATOM   1167  NH2 ARG A 150      29.077  28.822  15.873  1.00 49.66           N  
ATOM   1168  N   ALA A 151      26.483  34.589  21.160  1.00 38.15           N  
ATOM   1169  CA  ALA A 151      27.488  35.645  21.207  1.00 38.70           C  
ATOM   1170  C   ALA A 151      27.948  35.844  22.649  1.00 40.44           C  
ATOM   1171  O   ALA A 151      29.128  36.065  22.907  1.00 39.92           O  
ATOM   1172  CB  ALA A 151      26.911  36.939  20.655  1.00 38.86           C  
ATOM   1173  N   PHE A 152      27.002  35.759  23.580  1.00 40.78           N  
ATOM   1174  CA  PHE A 152      27.276  35.915  25.007  1.00 43.85           C  
ATOM   1175  C   PHE A 152      26.502  34.820  25.743  1.00 45.79           C  
ATOM   1176  O   PHE A 152      25.278  34.898  25.865  1.00 47.82           O  
ATOM   1177  CB  PHE A 152      26.777  37.272  25.507  1.00 44.41           C  
ATOM   1178  CG  PHE A 152      26.882  38.373  24.497  1.00 45.46           C  
ATOM   1179  CD1 PHE A 152      28.120  38.840  24.080  1.00 45.29           C  
ATOM   1180  CD2 PHE A 152      25.733  38.953  23.971  1.00 45.78           C  
ATOM   1181  CE1 PHE A 152      28.212  39.870  23.156  1.00 45.72           C  
ATOM   1182  CE2 PHE A 152      25.814  39.982  23.048  1.00 45.62           C  
ATOM   1183  CZ  PHE A 152      27.057  40.442  22.640  1.00 47.06           C  
ATOM   1184  N   GLY A 153      27.207  33.809  26.237  1.00 45.52           N  
ATOM   1185  CA  GLY A 153      26.540  32.724  26.935  1.00 46.47           C  
ATOM   1186  C   GLY A 153      25.483  33.183  27.922  1.00 46.64           C  
ATOM   1187  O   GLY A 153      25.645  34.220  28.570  1.00 50.45           O  
ATOM   1188  N   VAL A 154      24.400  32.416  28.032  1.00 46.23           N  
ATOM   1189  CA  VAL A 154      23.308  32.732  28.952  1.00 44.56           C  
ATOM   1190  C   VAL A 154      23.718  32.410  30.391  1.00 42.67           C  
ATOM   1191  O   VAL A 154      23.880  31.248  30.759  1.00 41.32           O  
ATOM   1192  CB  VAL A 154      22.023  31.942  28.586  1.00 45.89           C  
ATOM   1193  CG1 VAL A 154      22.364  30.491  28.328  1.00 46.87           C  
ATOM   1194  CG2 VAL A 154      21.000  32.046  29.711  1.00 45.14           C  
ATOM   1195  N   PRO A 155      23.889  33.448  31.224  1.00 40.81           N  
ATOM   1196  CA  PRO A 155      24.288  33.303  32.628  1.00 39.55           C  
ATOM   1197  C   PRO A 155      23.191  32.808  33.564  1.00 38.38           C  
ATOM   1198  O   PRO A 155      22.013  32.814  33.211  1.00 38.45           O  
ATOM   1199  CB  PRO A 155      24.750  34.708  32.990  1.00 40.13           C  
ATOM   1200  CG  PRO A 155      23.795  35.560  32.212  1.00 40.99           C  
ATOM   1201  CD  PRO A 155      23.774  34.873  30.860  1.00 40.92           C  
ATOM   1202  N   VAL A 156      23.596  32.375  34.756  1.00 35.60           N  
ATOM   1203  CA  VAL A 156      22.655  31.902  35.763  1.00 34.53           C  
ATOM   1204  C   VAL A 156      21.895  33.122  36.273  1.00 34.86           C  
ATOM   1205  O   VAL A 156      20.677  33.082  36.443  1.00 33.20           O  
ATOM   1206  CB  VAL A 156      23.386  31.230  36.954  1.00 33.63           C  
ATOM   1207  CG1 VAL A 156      22.390  30.864  38.040  1.00 31.19           C  
ATOM   1208  CG2 VAL A 156      24.119  29.986  36.481  1.00 33.29           C  
ATOM   1209  N   ARG A 157      22.636  34.202  36.515  1.00 34.34           N  
ATOM   1210  CA  ARG A 157      22.070  35.464  36.987  1.00 34.06           C  
ATOM   1211  C   ARG A 157      22.462  36.607  36.057  1.00 32.68           C  
ATOM   1212  O   ARG A 157      23.486  36.542  35.377  1.00 32.41           O  
ATOM   1213  CB  ARG A 157      22.566  35.803  38.395  1.00 35.45           C  
ATOM   1214  CG  ARG A 157      21.828  35.110  39.523  1.00 38.16           C  
ATOM   1215  CD  ARG A 157      22.471  33.801  39.900  1.00 39.33           C  
ATOM   1216  NE  ARG A 157      21.864  33.234  41.101  1.00 41.29           N  
ATOM   1217  CZ  ARG A 157      21.758  33.874  42.262  1.00 41.09           C  
ATOM   1218  NH1 ARG A 157      22.213  35.112  42.390  1.00 41.48           N  
ATOM   1219  NH2 ARG A 157      21.209  33.269  43.304  1.00 41.78           N  
ATOM   1220  N   THR A 158      21.644  37.654  36.041  1.00 30.68           N  
ATOM   1221  CA  THR A 158      21.910  38.826  35.215  1.00 30.50           C  
ATOM   1222  C   THR A 158      22.848  39.737  35.999  1.00 30.69           C  
ATOM   1223  O   THR A 158      23.164  39.454  37.155  1.00 28.39           O  
ATOM   1224  CB  THR A 158      20.618  39.607  34.909  1.00 30.48           C  
ATOM   1225  OG1 THR A 158      20.129  40.206  36.116  1.00 30.08           O  
ATOM   1226  CG2 THR A 158      19.548  38.673  34.340  1.00 29.61           C  
ATOM   1227  N   TYR A 159      23.281  40.831  35.375  1.00 30.56           N  
ATOM   1228  CA  TYR A 159      24.180  41.779  36.027  1.00 31.47           C  
ATOM   1229  C   TYR A 159      23.549  42.354  37.296  1.00 31.32           C  
ATOM   1230  O   TYR A 159      24.254  42.850  38.173  1.00 33.61           O  
ATOM   1231  CB  TYR A 159      24.539  42.921  35.068  1.00 32.53           C  
ATOM   1232  CG  TYR A 159      23.389  43.859  34.763  1.00 34.31           C  
ATOM   1233  CD1 TYR A 159      22.215  43.388  34.172  1.00 34.73           C  
ATOM   1234  CD2 TYR A 159      23.469  45.216  35.075  1.00 34.81           C  
ATOM   1235  CE1 TYR A 159      21.150  44.241  33.903  1.00 35.27           C  
ATOM   1236  CE2 TYR A 159      22.408  46.080  34.808  1.00 34.48           C  
ATOM   1237  CZ  TYR A 159      21.252  45.586  34.222  1.00 35.26           C  
ATOM   1238  OH  TYR A 159      20.197  46.435  33.955  1.00 36.25           O  
ATOM   1239  N   THR A 160      22.223  42.288  37.393  1.00 31.35           N  
ATOM   1240  CA  THR A 160      21.516  42.795  38.568  1.00 31.43           C  
ATOM   1241  C   THR A 160      21.258  41.678  39.581  1.00 31.24           C  
ATOM   1242  O   THR A 160      20.559  41.882  40.573  1.00 31.67           O  
ATOM   1243  CB  THR A 160      20.154  43.413  38.196  1.00 33.07           C  
ATOM   1244  OG1 THR A 160      19.362  42.440  37.505  1.00 34.81           O  
ATOM   1245  CG2 THR A 160      20.341  44.634  37.318  1.00 35.34           C  
ATOM   1246  N   HIS A 161      21.819  40.503  39.314  1.00 29.91           N  
ATOM   1247  CA  HIS A 161      21.670  39.341  40.186  1.00 30.34           C  
ATOM   1248  C   HIS A 161      20.316  38.655  40.051  1.00 30.71           C  
ATOM   1249  O   HIS A 161      20.001  37.728  40.799  1.00 31.14           O  
ATOM   1250  CB  HIS A 161      21.920  39.745  41.642  1.00 33.44           C  
ATOM   1251  CG  HIS A 161      23.224  40.451  41.843  1.00 33.97           C  
ATOM   1252  ND1 HIS A 161      24.438  39.860  41.562  1.00 35.58           N  
ATOM   1253  CD2 HIS A 161      23.503  41.718  42.232  1.00 34.79           C  
ATOM   1254  CE1 HIS A 161      25.408  40.734  41.765  1.00 35.65           C  
ATOM   1255  NE2 HIS A 161      24.867  41.868  42.172  1.00 35.25           N  
ATOM   1256  N   GLU A 162      19.513  39.103  39.095  1.00 28.77           N  
ATOM   1257  CA  GLU A 162      18.213  38.488  38.882  1.00 31.03           C  
ATOM   1258  C   GLU A 162      18.477  37.068  38.388  1.00 27.02           C  
ATOM   1259  O   GLU A 162      19.421  36.835  37.642  1.00 25.62           O  
ATOM   1260  CB  GLU A 162      17.414  39.279  37.842  1.00 33.47           C  
ATOM   1261  CG  GLU A 162      17.148  40.723  38.253  1.00 42.90           C  
ATOM   1262  CD  GLU A 162      16.565  41.565  37.130  1.00 47.47           C  
ATOM   1263  OE1 GLU A 162      17.234  41.717  36.083  1.00 48.97           O  
ATOM   1264  OE2 GLU A 162      15.438  42.078  37.299  1.00 50.98           O  
ATOM   1265  N   VAL A 163      17.660  36.119  38.827  1.00 24.14           N  
ATOM   1266  CA  VAL A 163      17.823  34.731  38.411  1.00 22.15           C  
ATOM   1267  C   VAL A 163      17.263  34.559  36.998  1.00 21.96           C  
ATOM   1268  O   VAL A 163      16.111  34.890  36.746  1.00 20.56           O  
ATOM   1269  CB  VAL A 163      17.064  33.779  39.380  1.00 22.41           C  
ATOM   1270  CG1 VAL A 163      17.099  32.349  38.863  1.00 21.48           C  
ATOM   1271  CG2 VAL A 163      17.686  33.847  40.765  1.00 21.96           C  
ATOM   1272  N   VAL A 164      18.067  34.064  36.063  1.00 22.08           N  
ATOM   1273  CA  VAL A 164      17.527  33.866  34.719  1.00 23.82           C  
ATOM   1274  C   VAL A 164      16.549  32.690  34.820  1.00 22.43           C  
ATOM   1275  O   VAL A 164      16.873  31.647  35.385  1.00 25.16           O  
ATOM   1276  CB  VAL A 164      18.629  33.559  33.684  1.00 24.09           C  
ATOM   1277  CG1 VAL A 164      17.992  33.251  32.339  1.00 24.65           C  
ATOM   1278  CG2 VAL A 164      19.568  34.765  33.543  1.00 22.48           C  
ATOM   1279  N   THR A 165      15.347  32.866  34.289  1.00 22.04           N  
ATOM   1280  CA  THR A 165      14.329  31.826  34.367  1.00 20.56           C  
ATOM   1281  C   THR A 165      14.672  30.539  33.608  1.00 19.26           C  
ATOM   1282  O   THR A 165      15.248  30.569  32.519  1.00 17.62           O  
ATOM   1283  CB  THR A 165      12.966  32.351  33.863  1.00 21.12           C  
ATOM   1284  OG1 THR A 165      11.931  31.440  34.253  1.00 22.75           O  
ATOM   1285  CG2 THR A 165      12.969  32.477  32.342  1.00 20.14           C  
ATOM   1286  N   LEU A 166      14.307  29.408  34.200  1.00 17.04           N  
ATOM   1287  CA  LEU A 166      14.550  28.092  33.604  1.00 17.81           C  
ATOM   1288  C   LEU A 166      13.266  27.516  33.022  1.00 16.53           C  
ATOM   1289  O   LEU A 166      13.292  26.484  32.346  1.00 15.59           O  
ATOM   1290  CB  LEU A 166      15.049  27.118  34.676  1.00 20.54           C  
ATOM   1291  CG  LEU A 166      16.527  26.997  35.058  1.00 25.09           C  
ATOM   1292  CD1 LEU A 166      17.246  28.318  34.922  1.00 27.49           C  
ATOM   1293  CD2 LEU A 166      16.597  26.462  36.491  1.00 21.73           C  
ATOM   1294  N   TRP A 167      12.148  28.189  33.283  1.00 14.45           N  
ATOM   1295  CA  TRP A 167      10.835  27.720  32.863  1.00 14.69           C  
ATOM   1296  C   TRP A 167      10.678  27.290  31.410  1.00 14.88           C  
ATOM   1297  O   TRP A 167       9.883  26.398  31.113  1.00 15.02           O  
ATOM   1298  CB  TRP A 167       9.768  28.776  33.179  1.00 14.91           C  
ATOM   1299  CG  TRP A 167       9.682  29.202  34.625  1.00 17.30           C  
ATOM   1300  CD1 TRP A 167      10.445  28.763  35.665  1.00 17.21           C  
ATOM   1301  CD2 TRP A 167       8.778  30.168  35.171  1.00 17.63           C  
ATOM   1302  NE1 TRP A 167      10.073  29.398  36.831  1.00 19.76           N  
ATOM   1303  CE2 TRP A 167       9.050  30.265  36.552  1.00 19.76           C  
ATOM   1304  CE3 TRP A 167       7.760  30.960  34.624  1.00 17.94           C  
ATOM   1305  CZ2 TRP A 167       8.340  31.126  37.398  1.00 20.89           C  
ATOM   1306  CZ3 TRP A 167       7.051  31.815  35.466  1.00 20.37           C  
ATOM   1307  CH2 TRP A 167       7.348  31.889  36.839  1.00 19.30           C  
ATOM   1308  N   TYR A 168      11.427  27.909  30.504  1.00 12.80           N  
ATOM   1309  CA  TYR A 168      11.303  27.569  29.089  1.00 14.71           C  
ATOM   1310  C   TYR A 168      12.482  26.772  28.525  1.00 16.21           C  
ATOM   1311  O   TYR A 168      12.587  26.572  27.312  1.00 15.25           O  
ATOM   1312  CB  TYR A 168      11.091  28.866  28.296  1.00 13.88           C  
ATOM   1313  CG  TYR A 168      10.030  29.736  28.945  1.00 14.31           C  
ATOM   1314  CD1 TYR A 168       8.674  29.464  28.771  1.00 15.28           C  
ATOM   1315  CD2 TYR A 168      10.388  30.765  29.818  1.00 15.01           C  
ATOM   1316  CE1 TYR A 168       7.697  30.192  29.457  1.00 14.91           C  
ATOM   1317  CE2 TYR A 168       9.426  31.490  30.511  1.00 16.89           C  
ATOM   1318  CZ  TYR A 168       8.081  31.194  30.327  1.00 14.57           C  
ATOM   1319  OH  TYR A 168       7.131  31.891  31.035  1.00 17.72           O  
ATOM   1320  N   ARG A 169      13.352  26.295  29.405  1.00 14.15           N  
ATOM   1321  CA  ARG A 169      14.525  25.545  28.971  1.00 16.08           C  
ATOM   1322  C   ARG A 169      14.228  24.094  28.587  1.00 17.45           C  
ATOM   1323  O   ARG A 169      13.613  23.346  29.350  1.00 17.49           O  
ATOM   1324  CB  ARG A 169      15.607  25.593  30.063  1.00 18.64           C  
ATOM   1325  CG  ARG A 169      16.969  25.084  29.616  1.00 17.44           C  
ATOM   1326  CD  ARG A 169      18.040  25.375  30.650  1.00 19.33           C  
ATOM   1327  NE  ARG A 169      18.267  26.806  30.835  1.00 22.75           N  
ATOM   1328  CZ  ARG A 169      19.084  27.318  31.751  1.00 25.70           C  
ATOM   1329  NH1 ARG A 169      19.757  26.515  32.570  1.00 24.01           N  
ATOM   1330  NH2 ARG A 169      19.225  28.632  31.854  1.00 23.91           N  
ATOM   1331  N   ALA A 170      14.676  23.709  27.394  1.00 15.23           N  
ATOM   1332  CA  ALA A 170      14.483  22.358  26.876  1.00 15.96           C  
ATOM   1333  C   ALA A 170      15.196  21.317  27.749  1.00 16.11           C  
ATOM   1334  O   ALA A 170      16.238  21.597  28.348  1.00 13.98           O  
ATOM   1335  CB  ALA A 170      14.992  22.285  25.433  1.00 13.85           C  
ATOM   1336  N   PRO A 171      14.641  20.097  27.824  1.00 15.76           N  
ATOM   1337  CA  PRO A 171      15.234  19.027  28.634  1.00 15.34           C  
ATOM   1338  C   PRO A 171      16.657  18.631  28.242  1.00 15.48           C  
ATOM   1339  O   PRO A 171      17.478  18.352  29.115  1.00 15.92           O  
ATOM   1340  CB  PRO A 171      14.216  17.880  28.503  1.00 15.14           C  
ATOM   1341  CG  PRO A 171      13.570  18.139  27.170  1.00 15.18           C  
ATOM   1342  CD  PRO A 171      13.416  19.634  27.138  1.00 13.03           C  
ATOM   1343  N   GLU A 172      16.971  18.622  26.947  1.00 14.82           N  
ATOM   1344  CA  GLU A 172      18.329  18.257  26.538  1.00 17.96           C  
ATOM   1345  C   GLU A 172      19.346  19.230  27.132  1.00 17.48           C  
ATOM   1346  O   GLU A 172      20.493  18.857  27.393  1.00 17.58           O  
ATOM   1347  CB  GLU A 172      18.468  18.242  25.012  1.00 18.28           C  
ATOM   1348  CG  GLU A 172      18.096  19.555  24.360  1.00 19.22           C  
ATOM   1349  CD  GLU A 172      16.686  19.557  23.823  1.00 17.53           C  
ATOM   1350  OE1 GLU A 172      15.777  19.080  24.539  1.00 17.38           O  
ATOM   1351  OE2 GLU A 172      16.492  20.040  22.685  1.00 15.54           O  
ATOM   1352  N   ILE A 173      18.935  20.476  27.352  1.00 17.09           N  
ATOM   1353  CA  ILE A 173      19.845  21.456  27.934  1.00 16.75           C  
ATOM   1354  C   ILE A 173      20.027  21.118  29.409  1.00 18.25           C  
ATOM   1355  O   ILE A 173      21.144  21.076  29.915  1.00 18.34           O  
ATOM   1356  CB  ILE A 173      19.301  22.899  27.801  1.00 18.36           C  
ATOM   1357  CG1 ILE A 173      19.245  23.304  26.322  1.00 19.14           C  
ATOM   1358  CG2 ILE A 173      20.196  23.866  28.562  1.00 21.27           C  
ATOM   1359  CD1 ILE A 173      18.723  24.708  26.089  1.00 22.32           C  
ATOM   1360  N   LEU A 174      18.915  20.870  30.092  1.00 17.96           N  
ATOM   1361  CA  LEU A 174      18.943  20.516  31.507  1.00 19.97           C  
ATOM   1362  C   LEU A 174      19.731  19.232  31.772  1.00 20.54           C  
ATOM   1363  O   LEU A 174      20.322  19.074  32.842  1.00 22.15           O  
ATOM   1364  CB  LEU A 174      17.517  20.332  32.030  1.00 20.20           C  
ATOM   1365  CG  LEU A 174      16.701  21.496  32.603  1.00 23.41           C  
ATOM   1366  CD1 LEU A 174      17.341  22.813  32.296  1.00 26.03           C  
ATOM   1367  CD2 LEU A 174      15.283  21.418  32.061  1.00 22.30           C  
ATOM   1368  N   LEU A 175      19.730  18.318  30.804  1.00 20.23           N  
ATOM   1369  CA  LEU A 175      20.433  17.047  30.959  1.00 22.11           C  
ATOM   1370  C   LEU A 175      21.901  17.088  30.545  1.00 23.83           C  
ATOM   1371  O   LEU A 175      22.569  16.053  30.479  1.00 25.49           O  
ATOM   1372  CB  LEU A 175      19.685  15.931  30.218  1.00 19.02           C  
ATOM   1373  CG  LEU A 175      18.351  15.544  30.878  1.00 19.77           C  
ATOM   1374  CD1 LEU A 175      17.565  14.586  29.997  1.00 17.68           C  
ATOM   1375  CD2 LEU A 175      18.626  14.907  32.244  1.00 21.66           C  
ATOM   1376  N   GLY A 176      22.400  18.290  30.270  1.00 24.68           N  
ATOM   1377  CA  GLY A 176      23.802  18.456  29.929  1.00 27.35           C  
ATOM   1378  C   GLY A 176      24.262  18.385  28.486  1.00 28.69           C  
ATOM   1379  O   GLY A 176      25.458  18.269  28.242  1.00 26.79           O  
ATOM   1380  N   CYS A 177      23.346  18.446  27.527  1.00 31.30           N  
ATOM   1381  CA  CYS A 177      23.753  18.395  26.127  1.00 35.57           C  
ATOM   1382  C   CYS A 177      24.563  19.652  25.821  1.00 36.74           C  
ATOM   1383  O   CYS A 177      24.076  20.768  25.997  1.00 38.17           O  
ATOM   1384  CB  CYS A 177      22.529  18.328  25.213  1.00 37.29           C  
ATOM   1385  SG  CYS A 177      22.924  18.046  23.464  1.00 42.14           S  
ATOM   1386  N   LYS A 178      25.799  19.469  25.365  1.00 37.96           N  
ATOM   1387  CA  LYS A 178      26.673  20.595  25.057  1.00 39.73           C  
ATOM   1388  C   LYS A 178      26.390  21.247  23.711  1.00 39.24           C  
ATOM   1389  O   LYS A 178      26.826  22.369  23.456  1.00 40.13           O  
ATOM   1390  CB  LYS A 178      28.133  20.151  25.102  1.00 42.28           C  
ATOM   1391  CG  LYS A 178      28.464  19.011  24.160  1.00 46.82           C  
ATOM   1392  CD  LYS A 178      29.948  18.666  24.215  1.00 50.56           C  
ATOM   1393  CE  LYS A 178      30.389  18.313  25.632  1.00 53.09           C  
ATOM   1394  NZ  LYS A 178      29.596  17.192  26.216  1.00 54.12           N  
ATOM   1395  N   TYR A 179      25.670  20.543  22.847  1.00 38.77           N  
ATOM   1396  CA  TYR A 179      25.336  21.073  21.531  1.00 38.41           C  
ATOM   1397  C   TYR A 179      23.831  21.273  21.417  1.00 36.83           C  
ATOM   1398  O   TYR A 179      23.056  20.335  21.578  1.00 39.30           O  
ATOM   1399  CB  TYR A 179      25.835  20.116  20.452  1.00 40.89           C  
ATOM   1400  CG  TYR A 179      27.321  19.876  20.545  1.00 44.06           C  
ATOM   1401  CD1 TYR A 179      28.221  20.934  20.421  1.00 44.81           C  
ATOM   1402  CD2 TYR A 179      27.831  18.602  20.790  1.00 44.51           C  
ATOM   1403  CE1 TYR A 179      29.590  20.733  20.541  1.00 47.02           C  
ATOM   1404  CE2 TYR A 179      29.205  18.390  20.913  1.00 46.71           C  
ATOM   1405  CZ  TYR A 179      30.077  19.462  20.787  1.00 47.46           C  
ATOM   1406  OH  TYR A 179      31.435  19.272  20.911  1.00 48.62           O  
ATOM   1407  N   TYR A 180      23.420  22.504  21.148  1.00 34.26           N  
ATOM   1408  CA  TYR A 180      22.002  22.814  21.037  1.00 32.13           C  
ATOM   1409  C   TYR A 180      21.552  22.784  19.583  1.00 29.50           C  
ATOM   1410  O   TYR A 180      22.298  23.160  18.688  1.00 29.97           O  
ATOM   1411  CB  TYR A 180      21.720  24.203  21.617  1.00 33.02           C  
ATOM   1412  CG  TYR A 180      22.413  24.480  22.929  1.00 35.33           C  
ATOM   1413  CD1 TYR A 180      22.143  23.713  24.061  1.00 36.41           C  
ATOM   1414  CD2 TYR A 180      23.351  25.505  23.036  1.00 36.87           C  
ATOM   1415  CE1 TYR A 180      22.790  23.959  25.270  1.00 39.49           C  
ATOM   1416  CE2 TYR A 180      24.008  25.759  24.239  1.00 39.28           C  
ATOM   1417  CZ  TYR A 180      23.722  24.982  25.353  1.00 39.86           C  
ATOM   1418  OH  TYR A 180      24.371  25.224  26.544  1.00 41.17           O  
ATOM   1419  N   SER A 181      20.331  22.323  19.352  1.00 25.75           N  
ATOM   1420  CA  SER A 181      19.788  22.289  18.007  1.00 22.62           C  
ATOM   1421  C   SER A 181      18.629  23.271  18.016  1.00 21.30           C  
ATOM   1422  O   SER A 181      18.211  23.733  19.077  1.00 18.46           O  
ATOM   1423  CB  SER A 181      19.271  20.897  17.659  1.00 24.00           C  
ATOM   1424  OG  SER A 181      17.992  20.673  18.224  1.00 21.80           O  
ATOM   1425  N   THR A 182      18.115  23.595  16.838  1.00 18.86           N  
ATOM   1426  CA  THR A 182      16.994  24.518  16.729  1.00 17.76           C  
ATOM   1427  C   THR A 182      15.769  24.014  17.513  1.00 16.95           C  
ATOM   1428  O   THR A 182      14.841  24.782  17.797  1.00 16.27           O  
ATOM   1429  CB  THR A 182      16.613  24.710  15.252  1.00 16.92           C  
ATOM   1430  OG1 THR A 182      16.449  23.428  14.637  1.00 22.97           O  
ATOM   1431  CG2 THR A 182      17.708  25.466  14.513  1.00 19.64           C  
ATOM   1432  N   ALA A 183      15.772  22.733  17.874  1.00 16.85           N  
ATOM   1433  CA  ALA A 183      14.656  22.151  18.621  1.00 15.62           C  
ATOM   1434  C   ALA A 183      14.455  22.800  19.990  1.00 16.01           C  
ATOM   1435  O   ALA A 183      13.343  22.800  20.531  1.00 13.24           O  
ATOM   1436  CB  ALA A 183      14.863  20.656  18.789  1.00 16.47           C  
ATOM   1437  N   VAL A 184      15.515  23.357  20.560  1.00 14.45           N  
ATOM   1438  CA  VAL A 184      15.371  23.984  21.874  1.00 16.23           C  
ATOM   1439  C   VAL A 184      14.397  25.149  21.807  1.00 13.70           C  
ATOM   1440  O   VAL A 184      13.657  25.398  22.749  1.00 14.26           O  
ATOM   1441  CB  VAL A 184      16.728  24.499  22.438  1.00 16.36           C  
ATOM   1442  CG1 VAL A 184      17.717  23.350  22.526  1.00 16.82           C  
ATOM   1443  CG2 VAL A 184      17.272  25.633  21.575  1.00 17.47           C  
ATOM   1444  N   ASP A 185      14.391  25.855  20.683  1.00 14.58           N  
ATOM   1445  CA  ASP A 185      13.498  27.000  20.516  1.00 13.50           C  
ATOM   1446  C   ASP A 185      12.035  26.592  20.386  1.00 15.34           C  
ATOM   1447  O   ASP A 185      11.143  27.312  20.849  1.00 12.85           O  
ATOM   1448  CB  ASP A 185      13.904  27.824  19.290  1.00 14.59           C  
ATOM   1449  CG  ASP A 185      15.182  28.604  19.512  1.00 16.56           C  
ATOM   1450  OD1 ASP A 185      15.511  28.888  20.686  1.00 16.27           O  
ATOM   1451  OD2 ASP A 185      15.847  28.952  18.514  1.00 17.45           O  
ATOM   1452  N   ILE A 186      11.790  25.453  19.745  1.00 14.56           N  
ATOM   1453  CA  ILE A 186      10.428  24.956  19.570  1.00 13.38           C  
ATOM   1454  C   ILE A 186       9.900  24.570  20.945  1.00 14.21           C  
ATOM   1455  O   ILE A 186       8.755  24.855  21.278  1.00 12.90           O  
ATOM   1456  CB  ILE A 186      10.380  23.721  18.646  1.00 13.94           C  
ATOM   1457  CG1 ILE A 186      10.707  24.131  17.201  1.00 15.20           C  
ATOM   1458  CG2 ILE A 186       9.009  23.056  18.738  1.00 12.12           C  
ATOM   1459  CD1 ILE A 186       9.775  25.174  16.612  1.00 17.50           C  
ATOM   1460  N   TRP A 187      10.745  23.920  21.741  1.00 15.47           N  
ATOM   1461  CA  TRP A 187      10.349  23.537  23.090  1.00 14.82           C  
ATOM   1462  C   TRP A 187       9.889  24.777  23.848  1.00 17.18           C  
ATOM   1463  O   TRP A 187       8.777  24.818  24.382  1.00 17.90           O  
ATOM   1464  CB  TRP A 187      11.522  22.898  23.832  1.00 16.96           C  
ATOM   1465  CG  TRP A 187      11.188  22.588  25.249  1.00 14.98           C  
ATOM   1466  CD1 TRP A 187      11.224  23.445  26.313  1.00 16.36           C  
ATOM   1467  CD2 TRP A 187      10.712  21.343  25.753  1.00 15.21           C  
ATOM   1468  NE1 TRP A 187      10.798  22.807  27.455  1.00 15.04           N  
ATOM   1469  CE2 TRP A 187      10.476  21.513  27.137  1.00 17.17           C  
ATOM   1470  CE3 TRP A 187      10.461  20.094  25.170  1.00 16.62           C  
ATOM   1471  CZ2 TRP A 187       9.998  20.481  27.945  1.00 15.19           C  
ATOM   1472  CZ3 TRP A 187       9.988  19.065  25.974  1.00 15.14           C  
ATOM   1473  CH2 TRP A 187       9.762  19.268  27.349  1.00 15.74           C  
ATOM   1474  N   SER A 188      10.749  25.792  23.892  1.00 16.27           N  
ATOM   1475  CA  SER A 188      10.420  27.029  24.591  1.00 14.49           C  
ATOM   1476  C   SER A 188       9.099  27.610  24.114  1.00 16.17           C  
ATOM   1477  O   SER A 188       8.258  28.003  24.921  1.00 14.50           O  
ATOM   1478  CB  SER A 188      11.524  28.070  24.393  1.00 13.34           C  
ATOM   1479  OG  SER A 188      12.750  27.633  24.957  1.00 13.57           O  
ATOM   1480  N   LEU A 189       8.921  27.674  22.800  1.00 14.65           N  
ATOM   1481  CA  LEU A 189       7.697  28.222  22.238  1.00 15.76           C  
ATOM   1482  C   LEU A 189       6.497  27.357  22.617  1.00 16.24           C  
ATOM   1483  O   LEU A 189       5.388  27.860  22.783  1.00 14.80           O  
ATOM   1484  CB  LEU A 189       7.826  28.331  20.718  1.00 15.08           C  
ATOM   1485  CG  LEU A 189       6.691  29.017  19.965  1.00 16.17           C  
ATOM   1486  CD1 LEU A 189       6.386  30.378  20.590  1.00 16.97           C  
ATOM   1487  CD2 LEU A 189       7.099  29.186  18.502  1.00 16.42           C  
ATOM   1488  N   GLY A 190       6.716  26.054  22.752  1.00 16.06           N  
ATOM   1489  CA  GLY A 190       5.625  25.178  23.143  1.00 15.01           C  
ATOM   1490  C   GLY A 190       5.190  25.524  24.558  1.00 14.43           C  
ATOM   1491  O   GLY A 190       3.999  25.577  24.861  1.00 14.10           O  
ATOM   1492  N   CYS A 191       6.163  25.769  25.431  1.00 14.18           N  
ATOM   1493  CA  CYS A 191       5.869  26.130  26.813  1.00 15.46           C  
ATOM   1494  C   CYS A 191       5.107  27.453  26.863  1.00 16.14           C  
ATOM   1495  O   CYS A 191       4.202  27.636  27.681  1.00 14.54           O  
ATOM   1496  CB  CYS A 191       7.169  26.261  27.615  1.00 15.40           C  
ATOM   1497  SG  CYS A 191       8.057  24.713  27.824  1.00 18.68           S  
ATOM   1498  N   ILE A 192       5.482  28.376  25.984  1.00 15.13           N  
ATOM   1499  CA  ILE A 192       4.832  29.682  25.929  1.00 14.58           C  
ATOM   1500  C   ILE A 192       3.407  29.566  25.394  1.00 14.45           C  
ATOM   1501  O   ILE A 192       2.500  30.260  25.864  1.00 14.88           O  
ATOM   1502  CB  ILE A 192       5.670  30.661  25.068  1.00 15.75           C  
ATOM   1503  CG1 ILE A 192       7.034  30.873  25.741  1.00 15.99           C  
ATOM   1504  CG2 ILE A 192       4.933  31.983  24.897  1.00 15.38           C  
ATOM   1505  CD1 ILE A 192       8.048  31.636  24.900  1.00 15.46           C  
ATOM   1506  N   PHE A 193       3.221  28.680  24.420  1.00 13.44           N  
ATOM   1507  CA  PHE A 193       1.920  28.420  23.813  1.00 14.10           C  
ATOM   1508  C   PHE A 193       0.977  27.922  24.908  1.00 15.36           C  
ATOM   1509  O   PHE A 193      -0.141  28.413  25.057  1.00 13.83           O  
ATOM   1510  CB  PHE A 193       2.103  27.363  22.716  1.00 15.90           C  
ATOM   1511  CG  PHE A 193       0.827  26.873  22.084  1.00 16.69           C  
ATOM   1512  CD1 PHE A 193      -0.325  27.656  22.065  1.00 17.85           C  
ATOM   1513  CD2 PHE A 193       0.808  25.637  21.440  1.00 18.00           C  
ATOM   1514  CE1 PHE A 193      -1.476  27.217  21.413  1.00 15.04           C  
ATOM   1515  CE2 PHE A 193      -0.338  25.186  20.783  1.00 20.36           C  
ATOM   1516  CZ  PHE A 193      -1.486  25.983  20.770  1.00 18.69           C  
ATOM   1517  N   ALA A 194       1.446  26.951  25.683  1.00 13.96           N  
ATOM   1518  CA  ALA A 194       0.636  26.390  26.761  1.00 15.54           C  
ATOM   1519  C   ALA A 194       0.279  27.452  27.802  1.00 13.94           C  
ATOM   1520  O   ALA A 194      -0.845  27.484  28.291  1.00 18.23           O  
ATOM   1521  CB  ALA A 194       1.378  25.227  27.425  1.00 12.17           C  
ATOM   1522  N   GLU A 195       1.235  28.318  28.134  1.00 15.31           N  
ATOM   1523  CA  GLU A 195       1.022  29.382  29.123  1.00 15.89           C  
ATOM   1524  C   GLU A 195      -0.025  30.400  28.657  1.00 17.23           C  
ATOM   1525  O   GLU A 195      -0.839  30.865  29.455  1.00 18.62           O  
ATOM   1526  CB  GLU A 195       2.345  30.104  29.420  1.00 13.69           C  
ATOM   1527  CG  GLU A 195       2.337  30.967  30.683  1.00 16.31           C  
ATOM   1528  CD  GLU A 195       3.673  31.635  30.953  1.00 17.74           C  
ATOM   1529  OE1 GLU A 195       4.716  31.045  30.601  1.00 18.30           O  
ATOM   1530  OE2 GLU A 195       3.684  32.745  31.533  1.00 16.19           O  
ATOM   1531  N   MET A 196      -0.011  30.761  27.376  1.00 17.03           N  
ATOM   1532  CA  MET A 196      -1.003  31.718  26.893  1.00 17.51           C  
ATOM   1533  C   MET A 196      -2.402  31.128  27.011  1.00 16.60           C  
ATOM   1534  O   MET A 196      -3.360  31.828  27.337  1.00 15.98           O  
ATOM   1535  CB  MET A 196      -0.749  32.098  25.426  1.00 16.53           C  
ATOM   1536  CG  MET A 196       0.494  32.956  25.186  1.00 19.45           C  
ATOM   1537  SD  MET A 196       0.523  33.620  23.493  1.00 21.89           S  
ATOM   1538  CE  MET A 196       1.187  32.236  22.599  1.00 17.21           C  
ATOM   1539  N   VAL A 197      -2.520  29.833  26.741  1.00 18.76           N  
ATOM   1540  CA  VAL A 197      -3.810  29.163  26.797  1.00 18.28           C  
ATOM   1541  C   VAL A 197      -4.378  28.982  28.204  1.00 20.33           C  
ATOM   1542  O   VAL A 197      -5.557  29.242  28.444  1.00 19.35           O  
ATOM   1543  CB  VAL A 197      -3.736  27.780  26.128  1.00 19.67           C  
ATOM   1544  CG1 VAL A 197      -5.053  27.036  26.309  1.00 23.64           C  
ATOM   1545  CG2 VAL A 197      -3.430  27.937  24.647  1.00 19.48           C  
ATOM   1546  N   THR A 198      -3.543  28.530  29.130  1.00 19.99           N  
ATOM   1547  CA  THR A 198      -3.992  28.282  30.497  1.00 20.20           C  
ATOM   1548  C   THR A 198      -3.845  29.456  31.452  1.00 21.21           C  
ATOM   1549  O   THR A 198      -4.427  29.449  32.536  1.00 22.49           O  
ATOM   1550  CB  THR A 198      -3.245  27.085  31.098  1.00 20.98           C  
ATOM   1551  OG1 THR A 198      -1.846  27.386  31.173  1.00 18.50           O  
ATOM   1552  CG2 THR A 198      -3.453  25.850  30.237  1.00 16.45           C  
ATOM   1553  N   ARG A 199      -3.065  30.454  31.051  1.00 21.98           N  
ATOM   1554  CA  ARG A 199      -2.820  31.644  31.870  1.00 25.19           C  
ATOM   1555  C   ARG A 199      -1.969  31.305  33.085  1.00 26.56           C  
ATOM   1556  O   ARG A 199      -2.021  31.991  34.112  1.00 27.44           O  
ATOM   1557  CB  ARG A 199      -4.134  32.266  32.334  1.00 26.28           C  
ATOM   1558  CG  ARG A 199      -5.098  32.579  31.213  1.00 28.99           C  
ATOM   1559  CD  ARG A 199      -6.378  33.139  31.783  1.00 30.37           C  
ATOM   1560  NE  ARG A 199      -7.555  32.634  31.091  1.00 31.92           N  
ATOM   1561  CZ  ARG A 199      -8.795  32.796  31.539  1.00 33.01           C  
ATOM   1562  NH1 ARG A 199      -9.006  33.450  32.674  1.00 31.23           N  
ATOM   1563  NH2 ARG A 199      -9.818  32.303  30.859  1.00 34.40           N  
ATOM   1564  N   ARG A 200      -1.189  30.238  32.960  1.00 26.06           N  
ATOM   1565  CA  ARG A 200      -0.309  29.796  34.026  1.00 25.51           C  
ATOM   1566  C   ARG A 200       0.916  29.141  33.391  1.00 24.82           C  
ATOM   1567  O   ARG A 200       0.792  28.400  32.418  1.00 21.79           O  
ATOM   1568  CB  ARG A 200      -1.044  28.794  34.923  1.00 27.78           C  
ATOM   1569  CG  ARG A 200      -0.269  28.380  36.158  1.00 34.46           C  
ATOM   1570  CD  ARG A 200      -1.113  27.498  37.067  1.00 38.35           C  
ATOM   1571  NE  ARG A 200      -0.395  27.133  38.286  1.00 43.39           N  
ATOM   1572  CZ  ARG A 200      -0.926  26.445  39.291  1.00 44.51           C  
ATOM   1573  NH1 ARG A 200      -2.187  26.040  39.228  1.00 45.88           N  
ATOM   1574  NH2 ARG A 200      -0.196  26.163  40.363  1.00 45.14           N  
ATOM   1575  N   ALA A 201       2.097  29.425  33.932  1.00 23.70           N  
ATOM   1576  CA  ALA A 201       3.319  28.838  33.398  1.00 23.22           C  
ATOM   1577  C   ALA A 201       3.195  27.315  33.435  1.00 23.73           C  
ATOM   1578  O   ALA A 201       2.674  26.750  34.395  1.00 24.12           O  
ATOM   1579  CB  ALA A 201       4.521  29.294  34.215  1.00 25.07           C  
ATOM   1580  N   LEU A 202       3.679  26.657  32.390  1.00 21.33           N  
ATOM   1581  CA  LEU A 202       3.609  25.203  32.294  1.00 21.39           C  
ATOM   1582  C   LEU A 202       4.525  24.508  33.299  1.00 21.04           C  
ATOM   1583  O   LEU A 202       4.090  23.636  34.049  1.00 19.54           O  
ATOM   1584  CB  LEU A 202       4.004  24.747  30.888  1.00 20.32           C  
ATOM   1585  CG  LEU A 202       3.196  23.671  30.151  1.00 25.17           C  
ATOM   1586  CD1 LEU A 202       4.134  22.965  29.191  1.00 21.80           C  
ATOM   1587  CD2 LEU A 202       2.555  22.668  31.110  1.00 23.49           C  
ATOM   1588  N   PHE A 203       5.797  24.893  33.289  1.00 19.14           N  
ATOM   1589  CA  PHE A 203       6.807  24.301  34.165  1.00 18.67           C  
ATOM   1590  C   PHE A 203       7.584  25.406  34.889  1.00 18.26           C  
ATOM   1591  O   PHE A 203       8.700  25.747  34.498  1.00 18.64           O  
ATOM   1592  CB  PHE A 203       7.797  23.468  33.336  1.00 18.84           C  
ATOM   1593  CG  PHE A 203       7.154  22.423  32.450  1.00 18.90           C  
ATOM   1594  CD1 PHE A 203       6.396  21.384  32.995  1.00 16.30           C  
ATOM   1595  CD2 PHE A 203       7.349  22.454  31.072  1.00 17.46           C  
ATOM   1596  CE1 PHE A 203       5.847  20.396  32.180  1.00 18.69           C  
ATOM   1597  CE2 PHE A 203       6.805  21.472  30.249  1.00 18.13           C  
ATOM   1598  CZ  PHE A 203       6.052  20.440  30.803  1.00 19.39           C  
ATOM   1599  N   PRO A 204       7.007  25.980  35.958  1.00 19.01           N  
ATOM   1600  CA  PRO A 204       7.703  27.047  36.685  1.00 19.59           C  
ATOM   1601  C   PRO A 204       8.755  26.537  37.664  1.00 19.86           C  
ATOM   1602  O   PRO A 204       8.616  26.700  38.875  1.00 22.71           O  
ATOM   1603  CB  PRO A 204       6.562  27.775  37.379  1.00 18.32           C  
ATOM   1604  CG  PRO A 204       5.647  26.651  37.739  1.00 19.15           C  
ATOM   1605  CD  PRO A 204       5.644  25.787  36.485  1.00 18.65           C  
ATOM   1606  N   GLY A 205       9.806  25.922  37.138  1.00 19.55           N  
ATOM   1607  CA  GLY A 205      10.856  25.401  37.999  1.00 20.36           C  
ATOM   1608  C   GLY A 205      11.681  26.492  38.654  1.00 19.96           C  
ATOM   1609  O   GLY A 205      11.868  27.564  38.077  1.00 20.55           O  
ATOM   1610  N   ASP A 206      12.171  26.227  39.864  1.00 19.02           N  
ATOM   1611  CA  ASP A 206      12.976  27.207  40.577  1.00 19.77           C  
ATOM   1612  C   ASP A 206      14.388  26.696  40.847  1.00 19.81           C  
ATOM   1613  O   ASP A 206      15.101  27.213  41.705  1.00 18.94           O  
ATOM   1614  CB  ASP A 206      12.283  27.634  41.882  1.00 19.22           C  
ATOM   1615  CG  ASP A 206      12.154  26.503  42.887  1.00 21.40           C  
ATOM   1616  OD1 ASP A 206      12.376  25.334  42.518  1.00 17.52           O  
ATOM   1617  OD2 ASP A 206      11.814  26.791  44.055  1.00 18.39           O  
ATOM   1618  N   SER A 207      14.777  25.676  40.087  1.00 16.76           N  
ATOM   1619  CA  SER A 207      16.108  25.085  40.152  1.00 18.45           C  
ATOM   1620  C   SER A 207      16.166  24.107  38.990  1.00 18.28           C  
ATOM   1621  O   SER A 207      15.125  23.673  38.497  1.00 18.53           O  
ATOM   1622  CB  SER A 207      16.338  24.354  41.473  1.00 19.13           C  
ATOM   1623  OG  SER A 207      15.716  23.088  41.480  1.00 20.05           O  
ATOM   1624  N   GLU A 208      17.365  23.755  38.543  1.00 17.50           N  
ATOM   1625  CA  GLU A 208      17.467  22.851  37.415  1.00 17.85           C  
ATOM   1626  C   GLU A 208      16.794  21.511  37.654  1.00 18.18           C  
ATOM   1627  O   GLU A 208      16.098  20.997  36.777  1.00 16.50           O  
ATOM   1628  CB  GLU A 208      18.927  22.641  37.034  1.00 21.60           C  
ATOM   1629  CG  GLU A 208      19.581  23.901  36.501  1.00 24.42           C  
ATOM   1630  CD  GLU A 208      20.956  23.644  35.937  1.00 26.98           C  
ATOM   1631  OE1 GLU A 208      21.069  22.834  34.995  1.00 26.91           O  
ATOM   1632  OE2 GLU A 208      21.924  24.251  36.439  1.00 32.58           O  
ATOM   1633  N   ILE A 209      16.980  20.942  38.838  1.00 17.57           N  
ATOM   1634  CA  ILE A 209      16.368  19.648  39.115  1.00 18.39           C  
ATOM   1635  C   ILE A 209      14.856  19.799  39.283  1.00 14.82           C  
ATOM   1636  O   ILE A 209      14.090  18.914  38.893  1.00 16.46           O  
ATOM   1637  CB  ILE A 209      17.004  18.986  40.368  1.00 18.29           C  
ATOM   1638  CG1 ILE A 209      16.663  17.494  40.406  1.00 22.58           C  
ATOM   1639  CG2 ILE A 209      16.529  19.684  41.628  1.00 20.91           C  
ATOM   1640  CD1 ILE A 209      17.213  16.700  39.221  1.00 19.84           C  
ATOM   1641  N   ASP A 210      14.417  20.922  39.851  1.00 15.34           N  
ATOM   1642  CA  ASP A 210      12.981  21.150  40.026  1.00 14.64           C  
ATOM   1643  C   ASP A 210      12.340  21.320  38.651  1.00 15.24           C  
ATOM   1644  O   ASP A 210      11.219  20.865  38.404  1.00 15.14           O  
ATOM   1645  CB  ASP A 210      12.715  22.407  40.858  1.00 15.27           C  
ATOM   1646  CG  ASP A 210      11.227  22.645  41.093  1.00 18.84           C  
ATOM   1647  OD1 ASP A 210      10.584  21.797  41.744  1.00 17.39           O  
ATOM   1648  OD2 ASP A 210      10.692  23.673  40.623  1.00 15.94           O  
ATOM   1649  N   GLN A 211      13.060  21.990  37.759  1.00 12.21           N  
ATOM   1650  CA  GLN A 211      12.564  22.220  36.406  1.00 13.97           C  
ATOM   1651  C   GLN A 211      12.445  20.874  35.700  1.00 14.67           C  
ATOM   1652  O   GLN A 211      11.417  20.550  35.096  1.00 15.62           O  
ATOM   1653  CB  GLN A 211      13.541  23.129  35.654  1.00 15.05           C  
ATOM   1654  CG  GLN A 211      13.079  23.561  34.257  1.00 16.29           C  
ATOM   1655  CD  GLN A 211      11.830  24.432  34.292  1.00 14.65           C  
ATOM   1656  OE1 GLN A 211      11.672  25.275  35.176  1.00 18.74           O  
ATOM   1657  NE2 GLN A 211      10.949  24.247  33.316  1.00 15.14           N  
ATOM   1658  N   LEU A 212      13.501  20.077  35.793  1.00 14.86           N  
ATOM   1659  CA  LEU A 212      13.509  18.775  35.149  1.00 17.27           C  
ATOM   1660  C   LEU A 212      12.392  17.891  35.689  1.00 17.27           C  
ATOM   1661  O   LEU A 212      11.672  17.246  34.923  1.00 17.82           O  
ATOM   1662  CB  LEU A 212      14.870  18.103  35.360  1.00 19.33           C  
ATOM   1663  CG  LEU A 212      15.304  17.005  34.395  1.00 22.79           C  
ATOM   1664  CD1 LEU A 212      15.320  17.542  32.974  1.00 21.24           C  
ATOM   1665  CD2 LEU A 212      16.691  16.512  34.797  1.00 20.34           C  
ATOM   1666  N   PHE A 213      12.226  17.863  37.008  1.00 16.84           N  
ATOM   1667  CA  PHE A 213      11.189  17.025  37.589  1.00 17.44           C  
ATOM   1668  C   PHE A 213       9.766  17.497  37.298  1.00 17.44           C  
ATOM   1669  O   PHE A 213       8.841  16.690  37.268  1.00 18.71           O  
ATOM   1670  CB  PHE A 213      11.438  16.846  39.097  1.00 17.51           C  
ATOM   1671  CG  PHE A 213      12.599  15.924  39.407  1.00 18.85           C  
ATOM   1672  CD1 PHE A 213      13.367  15.381  38.381  1.00 19.70           C  
ATOM   1673  CD2 PHE A 213      12.908  15.580  40.721  1.00 20.00           C  
ATOM   1674  CE1 PHE A 213      14.422  14.508  38.657  1.00 20.64           C  
ATOM   1675  CE2 PHE A 213      13.960  14.708  41.003  1.00 18.37           C  
ATOM   1676  CZ  PHE A 213      14.715  14.172  39.975  1.00 21.74           C  
ATOM   1677  N   ARG A 214       9.583  18.789  37.054  1.00 15.51           N  
ATOM   1678  CA  ARG A 214       8.257  19.284  36.726  1.00 17.17           C  
ATOM   1679  C   ARG A 214       7.919  18.807  35.322  1.00 18.94           C  
ATOM   1680  O   ARG A 214       6.766  18.496  35.013  1.00 20.54           O  
ATOM   1681  CB  ARG A 214       8.210  20.807  36.791  1.00 16.58           C  
ATOM   1682  CG  ARG A 214       8.086  21.334  38.214  1.00 15.72           C  
ATOM   1683  CD  ARG A 214       8.147  22.848  38.247  1.00 17.40           C  
ATOM   1684  NE  ARG A 214       7.815  23.374  39.569  1.00 20.83           N  
ATOM   1685  CZ  ARG A 214       6.575  23.554  40.012  1.00 24.73           C  
ATOM   1686  NH1 ARG A 214       5.537  23.256  39.240  1.00 23.73           N  
ATOM   1687  NH2 ARG A 214       6.373  24.041  41.227  1.00 26.59           N  
ATOM   1688  N   ILE A 215       8.934  18.749  34.473  1.00 18.08           N  
ATOM   1689  CA  ILE A 215       8.735  18.277  33.109  1.00 18.02           C  
ATOM   1690  C   ILE A 215       8.412  16.784  33.169  1.00 19.01           C  
ATOM   1691  O   ILE A 215       7.482  16.310  32.514  1.00 20.12           O  
ATOM   1692  CB  ILE A 215      10.004  18.508  32.268  1.00 15.70           C  
ATOM   1693  CG1 ILE A 215      10.244  20.014  32.102  1.00 14.56           C  
ATOM   1694  CG2 ILE A 215       9.868  17.829  30.903  1.00 15.68           C  
ATOM   1695  CD1 ILE A 215      11.581  20.347  31.461  1.00 15.06           C  
ATOM   1696  N   PHE A 216       9.178  16.058  33.978  1.00 19.57           N  
ATOM   1697  CA  PHE A 216       8.998  14.616  34.140  1.00 20.70           C  
ATOM   1698  C   PHE A 216       7.608  14.239  34.662  1.00 21.25           C  
ATOM   1699  O   PHE A 216       6.999  13.284  34.177  1.00 20.36           O  
ATOM   1700  CB  PHE A 216      10.063  14.050  35.092  1.00 16.84           C  
ATOM   1701  CG  PHE A 216      11.453  14.000  34.511  1.00 20.42           C  
ATOM   1702  CD1 PHE A 216      11.732  14.530  33.249  1.00 21.27           C  
ATOM   1703  CD2 PHE A 216      12.489  13.413  35.230  1.00 19.90           C  
ATOM   1704  CE1 PHE A 216      13.016  14.473  32.720  1.00 20.46           C  
ATOM   1705  CE2 PHE A 216      13.778  13.352  34.709  1.00 21.64           C  
ATOM   1706  CZ  PHE A 216      14.042  13.882  33.450  1.00 22.91           C  
ATOM   1707  N   ARG A 217       7.104  14.980  35.645  1.00 23.83           N  
ATOM   1708  CA  ARG A 217       5.790  14.672  36.211  1.00 26.10           C  
ATOM   1709  C   ARG A 217       4.642  14.898  35.240  1.00 25.81           C  
ATOM   1710  O   ARG A 217       3.576  14.303  35.386  1.00 24.96           O  
ATOM   1711  CB  ARG A 217       5.531  15.496  37.474  1.00 30.11           C  
ATOM   1712  CG  ARG A 217       6.474  15.200  38.627  1.00 34.29           C  
ATOM   1713  CD  ARG A 217       5.922  15.773  39.927  1.00 40.19           C  
ATOM   1714  NE  ARG A 217       6.958  15.933  40.942  1.00 42.88           N  
ATOM   1715  CZ  ARG A 217       7.886  16.883  40.910  1.00 44.12           C  
ATOM   1716  NH1 ARG A 217       7.901  17.759  39.916  1.00 43.46           N  
ATOM   1717  NH2 ARG A 217       8.802  16.955  41.868  1.00 44.93           N  
ATOM   1718  N   THR A 218       4.854  15.755  34.252  1.00 24.45           N  
ATOM   1719  CA  THR A 218       3.808  16.044  33.281  1.00 24.51           C  
ATOM   1720  C   THR A 218       3.921  15.171  32.036  1.00 23.36           C  
ATOM   1721  O   THR A 218       2.961  14.516  31.637  1.00 22.44           O  
ATOM   1722  CB  THR A 218       3.843  17.528  32.852  1.00 25.69           C  
ATOM   1723  OG1 THR A 218       3.664  18.361  34.004  1.00 29.02           O  
ATOM   1724  CG2 THR A 218       2.737  17.824  31.850  1.00 24.73           C  
ATOM   1725  N   LEU A 219       5.101  15.161  31.431  1.00 21.40           N  
ATOM   1726  CA  LEU A 219       5.335  14.394  30.217  1.00 22.63           C  
ATOM   1727  C   LEU A 219       5.845  12.980  30.489  1.00 22.48           C  
ATOM   1728  O   LEU A 219       6.051  12.202  29.560  1.00 22.38           O  
ATOM   1729  CB  LEU A 219       6.337  15.148  29.332  1.00 24.75           C  
ATOM   1730  CG  LEU A 219       5.874  16.303  28.428  1.00 27.93           C  
ATOM   1731  CD1 LEU A 219       4.539  16.859  28.854  1.00 27.81           C  
ATOM   1732  CD2 LEU A 219       6.942  17.382  28.433  1.00 27.17           C  
ATOM   1733  N   GLY A 220       6.043  12.655  31.764  1.00 21.96           N  
ATOM   1734  CA  GLY A 220       6.543  11.343  32.126  1.00 22.29           C  
ATOM   1735  C   GLY A 220       8.062  11.300  32.090  1.00 23.21           C  
ATOM   1736  O   GLY A 220       8.693  11.956  31.257  1.00 21.42           O  
ATOM   1737  N   THR A 221       8.666  10.543  32.998  1.00 23.85           N  
ATOM   1738  CA  THR A 221      10.120  10.436  33.017  1.00 24.46           C  
ATOM   1739  C   THR A 221      10.538   9.806  31.693  1.00 24.72           C  
ATOM   1740  O   THR A 221      10.063   8.729  31.337  1.00 25.89           O  
ATOM   1741  CB  THR A 221      10.605   9.550  34.175  1.00 23.21           C  
ATOM   1742  OG1 THR A 221      10.183  10.122  35.419  1.00 26.09           O  
ATOM   1743  CG2 THR A 221      12.121   9.443  34.162  1.00 24.74           C  
ATOM   1744  N   PRO A 222      11.427  10.474  30.940  1.00 24.90           N  
ATOM   1745  CA  PRO A 222      11.877   9.942  29.652  1.00 23.79           C  
ATOM   1746  C   PRO A 222      12.735   8.689  29.771  1.00 25.21           C  
ATOM   1747  O   PRO A 222      13.510   8.534  30.724  1.00 24.46           O  
ATOM   1748  CB  PRO A 222      12.643  11.116  29.047  1.00 24.57           C  
ATOM   1749  CG  PRO A 222      13.228  11.773  30.251  1.00 24.83           C  
ATOM   1750  CD  PRO A 222      12.062  11.775  31.217  1.00 24.69           C  
ATOM   1751  N   ASP A 223      12.577   7.792  28.803  1.00 24.59           N  
ATOM   1752  CA  ASP A 223      13.337   6.553  28.768  1.00 25.54           C  
ATOM   1753  C   ASP A 223      13.847   6.319  27.359  1.00 25.12           C  
ATOM   1754  O   ASP A 223      13.583   7.114  26.459  1.00 23.46           O  
ATOM   1755  CB  ASP A 223      12.486   5.354  29.208  1.00 29.47           C  
ATOM   1756  CG  ASP A 223      11.232   5.184  28.375  1.00 31.74           C  
ATOM   1757  OD1 ASP A 223      11.296   5.376  27.144  1.00 34.70           O  
ATOM   1758  OD2 ASP A 223      10.179   4.845  28.953  1.00 33.80           O  
ATOM   1759  N   GLU A 224      14.577   5.223  27.179  1.00 24.49           N  
ATOM   1760  CA  GLU A 224      15.146   4.878  25.885  1.00 25.75           C  
ATOM   1761  C   GLU A 224      14.113   4.674  24.789  1.00 26.58           C  
ATOM   1762  O   GLU A 224      14.443   4.742  23.606  1.00 26.92           O  
ATOM   1763  CB  GLU A 224      16.009   3.623  26.014  1.00 26.42           C  
ATOM   1764  CG  GLU A 224      17.330   3.849  26.734  1.00 27.67           C  
ATOM   1765  CD  GLU A 224      18.232   4.825  25.996  1.00 28.07           C  
ATOM   1766  OE1 GLU A 224      18.294   4.754  24.752  1.00 27.15           O  
ATOM   1767  OE2 GLU A 224      18.888   5.656  26.658  1.00 29.05           O  
ATOM   1768  N   VAL A 225      12.865   4.426  25.176  1.00 27.53           N  
ATOM   1769  CA  VAL A 225      11.801   4.215  24.201  1.00 27.13           C  
ATOM   1770  C   VAL A 225      11.400   5.525  23.522  1.00 27.45           C  
ATOM   1771  O   VAL A 225      11.441   5.640  22.297  1.00 25.41           O  
ATOM   1772  CB  VAL A 225      10.553   3.590  24.866  1.00 28.61           C  
ATOM   1773  CG1 VAL A 225       9.379   3.585  23.888  1.00 30.69           C  
ATOM   1774  CG2 VAL A 225      10.868   2.172  25.322  1.00 30.11           C  
ATOM   1775  N   VAL A 226      11.016   6.516  24.320  1.00 27.28           N  
ATOM   1776  CA  VAL A 226      10.607   7.796  23.763  1.00 27.06           C  
ATOM   1777  C   VAL A 226      11.796   8.694  23.415  1.00 24.94           C  
ATOM   1778  O   VAL A 226      11.661   9.604  22.598  1.00 25.29           O  
ATOM   1779  CB  VAL A 226       9.644   8.552  24.726  1.00 29.11           C  
ATOM   1780  CG1 VAL A 226       8.422   7.677  25.029  1.00 31.05           C  
ATOM   1781  CG2 VAL A 226      10.364   8.925  26.017  1.00 29.70           C  
ATOM   1782  N   TRP A 227      12.956   8.429  24.015  1.00 23.38           N  
ATOM   1783  CA  TRP A 227      14.151   9.242  23.765  1.00 19.90           C  
ATOM   1784  C   TRP A 227      15.431   8.409  23.707  1.00 22.75           C  
ATOM   1785  O   TRP A 227      16.167   8.303  24.694  1.00 22.96           O  
ATOM   1786  CB  TRP A 227      14.300  10.308  24.860  1.00 19.01           C  
ATOM   1787  CG  TRP A 227      15.274  11.427  24.540  1.00 18.07           C  
ATOM   1788  CD1 TRP A 227      16.140  11.496  23.488  1.00 20.05           C  
ATOM   1789  CD2 TRP A 227      15.461  12.638  25.290  1.00 18.66           C  
ATOM   1790  NE1 TRP A 227      16.855  12.677  23.533  1.00 18.69           N  
ATOM   1791  CE2 TRP A 227      16.455  13.394  24.630  1.00 18.18           C  
ATOM   1792  CE3 TRP A 227      14.882  13.155  26.456  1.00 15.57           C  
ATOM   1793  CZ2 TRP A 227      16.886  14.645  25.099  1.00 19.30           C  
ATOM   1794  CZ3 TRP A 227      15.311  14.400  26.923  1.00 19.67           C  
ATOM   1795  CH2 TRP A 227      16.302  15.128  26.245  1.00 18.34           C  
ATOM   1796  N   PRO A 228      15.715   7.805  22.547  1.00 23.17           N  
ATOM   1797  CA  PRO A 228      16.920   6.988  22.378  1.00 25.45           C  
ATOM   1798  C   PRO A 228      18.188   7.765  22.729  1.00 25.40           C  
ATOM   1799  O   PRO A 228      18.418   8.859  22.211  1.00 26.08           O  
ATOM   1800  CB  PRO A 228      16.864   6.607  20.905  1.00 25.83           C  
ATOM   1801  CG  PRO A 228      15.388   6.448  20.681  1.00 25.56           C  
ATOM   1802  CD  PRO A 228      14.832   7.684  21.374  1.00 24.97           C  
ATOM   1803  N   GLY A 229      18.997   7.200  23.620  1.00 25.53           N  
ATOM   1804  CA  GLY A 229      20.236   7.845  24.014  1.00 25.94           C  
ATOM   1805  C   GLY A 229      20.131   8.767  25.214  1.00 25.61           C  
ATOM   1806  O   GLY A 229      21.135   9.309  25.665  1.00 27.31           O  
ATOM   1807  N   VAL A 230      18.928   8.940  25.749  1.00 26.51           N  
ATOM   1808  CA  VAL A 230      18.740   9.828  26.893  1.00 26.47           C  
ATOM   1809  C   VAL A 230      19.482   9.384  28.148  1.00 27.62           C  
ATOM   1810  O   VAL A 230      20.016  10.214  28.880  1.00 25.92           O  
ATOM   1811  CB  VAL A 230      17.249   9.977  27.258  1.00 26.02           C  
ATOM   1812  CG1 VAL A 230      16.688   8.645  27.717  1.00 26.49           C  
ATOM   1813  CG2 VAL A 230      17.086  11.029  28.350  1.00 24.15           C  
ATOM   1814  N   THR A 231      19.517   8.077  28.398  1.00 28.53           N  
ATOM   1815  CA  THR A 231      20.175   7.557  29.593  1.00 30.93           C  
ATOM   1816  C   THR A 231      21.692   7.702  29.568  1.00 30.96           C  
ATOM   1817  O   THR A 231      22.363   7.384  30.544  1.00 33.96           O  
ATOM   1818  CB  THR A 231      19.838   6.068  29.816  1.00 32.42           C  
ATOM   1819  OG1 THR A 231      20.464   5.279  28.797  1.00 33.43           O  
ATOM   1820  CG2 THR A 231      18.329   5.850  29.776  1.00 32.60           C  
ATOM   1821  N   SER A 232      22.231   8.188  28.458  1.00 31.65           N  
ATOM   1822  CA  SER A 232      23.673   8.360  28.332  1.00 30.42           C  
ATOM   1823  C   SER A 232      24.074   9.831  28.345  1.00 30.24           C  
ATOM   1824  O   SER A 232      25.230  10.179  28.086  1.00 27.99           O  
ATOM   1825  CB  SER A 232      24.163   7.703  27.038  1.00 33.86           C  
ATOM   1826  OG  SER A 232      23.882   6.313  27.047  1.00 35.97           O  
ATOM   1827  N   MET A 233      23.120  10.703  28.643  1.00 27.24           N  
ATOM   1828  CA  MET A 233      23.421  12.121  28.677  1.00 28.32           C  
ATOM   1829  C   MET A 233      24.153  12.473  29.960  1.00 27.30           C  
ATOM   1830  O   MET A 233      23.950  11.843  30.990  1.00 27.65           O  
ATOM   1831  CB  MET A 233      22.138  12.922  28.519  1.00 28.54           C  
ATOM   1832  CG  MET A 233      21.480  12.632  27.189  1.00 33.35           C  
ATOM   1833  SD  MET A 233      20.238  13.817  26.791  1.00 36.92           S  
ATOM   1834  CE  MET A 233      21.255  15.185  26.301  1.00 35.13           C  
ATOM   1835  N   PRO A 234      25.027  13.486  29.903  1.00 29.11           N  
ATOM   1836  CA  PRO A 234      25.838  13.965  31.026  1.00 28.57           C  
ATOM   1837  C   PRO A 234      25.183  14.019  32.403  1.00 28.27           C  
ATOM   1838  O   PRO A 234      25.716  13.468  33.364  1.00 30.39           O  
ATOM   1839  CB  PRO A 234      26.295  15.340  30.549  1.00 28.94           C  
ATOM   1840  CG  PRO A 234      26.453  15.130  29.084  1.00 29.80           C  
ATOM   1841  CD  PRO A 234      25.182  14.381  28.743  1.00 29.57           C  
ATOM   1842  N   ASP A 235      24.032  14.671  32.504  1.00 26.86           N  
ATOM   1843  CA  ASP A 235      23.367  14.810  33.792  1.00 25.97           C  
ATOM   1844  C   ASP A 235      22.221  13.845  34.058  1.00 24.91           C  
ATOM   1845  O   ASP A 235      21.454  14.023  35.003  1.00 22.68           O  
ATOM   1846  CB  ASP A 235      22.897  16.254  33.964  1.00 25.64           C  
ATOM   1847  CG  ASP A 235      24.043  17.240  33.870  1.00 28.90           C  
ATOM   1848  OD1 ASP A 235      25.067  17.021  34.556  1.00 30.03           O  
ATOM   1849  OD2 ASP A 235      23.929  18.229  33.116  1.00 28.05           O  
ATOM   1850  N   TYR A 236      22.104  12.817  33.226  1.00 24.18           N  
ATOM   1851  CA  TYR A 236      21.052  11.836  33.426  1.00 22.37           C  
ATOM   1852  C   TYR A 236      21.445  10.964  34.616  1.00 23.33           C  
ATOM   1853  O   TYR A 236      22.622  10.653  34.796  1.00 23.99           O  
ATOM   1854  CB  TYR A 236      20.888  10.950  32.190  1.00 22.46           C  
ATOM   1855  CG  TYR A 236      19.829   9.896  32.399  1.00 24.80           C  
ATOM   1856  CD1 TYR A 236      18.476  10.198  32.254  1.00 24.54           C  
ATOM   1857  CD2 TYR A 236      20.175   8.624  32.854  1.00 27.20           C  
ATOM   1858  CE1 TYR A 236      17.495   9.258  32.569  1.00 28.03           C  
ATOM   1859  CE2 TYR A 236      19.205   7.684  33.171  1.00 28.07           C  
ATOM   1860  CZ  TYR A 236      17.872   8.005  33.031  1.00 28.00           C  
ATOM   1861  OH  TYR A 236      16.924   7.072  33.382  1.00 30.74           O  
ATOM   1862  N   LYS A 237      20.467  10.568  35.422  1.00 22.98           N  
ATOM   1863  CA  LYS A 237      20.738   9.721  36.581  1.00 24.62           C  
ATOM   1864  C   LYS A 237      19.741   8.575  36.605  1.00 24.39           C  
ATOM   1865  O   LYS A 237      18.535   8.804  36.630  1.00 23.79           O  
ATOM   1866  CB  LYS A 237      20.588  10.508  37.887  1.00 25.65           C  
ATOM   1867  CG  LYS A 237      21.318  11.844  37.942  1.00 30.53           C  
ATOM   1868  CD  LYS A 237      22.825  11.684  38.074  1.00 30.83           C  
ATOM   1869  CE  LYS A 237      23.496  13.051  38.127  1.00 33.13           C  
ATOM   1870  NZ  LYS A 237      24.982  12.954  38.212  1.00 34.02           N  
ATOM   1871  N   PRO A 238      20.228   7.324  36.599  1.00 25.29           N  
ATOM   1872  CA  PRO A 238      19.323   6.169  36.629  1.00 25.28           C  
ATOM   1873  C   PRO A 238      18.396   6.263  37.836  1.00 26.46           C  
ATOM   1874  O   PRO A 238      17.333   5.644  37.872  1.00 26.45           O  
ATOM   1875  CB  PRO A 238      20.279   4.984  36.748  1.00 25.86           C  
ATOM   1876  CG  PRO A 238      21.503   5.469  36.038  1.00 25.97           C  
ATOM   1877  CD  PRO A 238      21.632   6.889  36.530  1.00 24.93           C  
ATOM   1878  N   SER A 239      18.808   7.049  38.826  1.00 26.40           N  
ATOM   1879  CA  SER A 239      18.015   7.210  40.037  1.00 25.84           C  
ATOM   1880  C   SER A 239      16.873   8.227  39.923  1.00 24.76           C  
ATOM   1881  O   SER A 239      16.182   8.480  40.904  1.00 22.20           O  
ATOM   1882  CB  SER A 239      18.929   7.575  41.212  1.00 26.10           C  
ATOM   1883  OG  SER A 239      19.683   8.742  40.937  1.00 25.29           O  
ATOM   1884  N   PHE A 240      16.674   8.817  38.744  1.00 25.23           N  
ATOM   1885  CA  PHE A 240      15.574   9.775  38.574  1.00 23.82           C  
ATOM   1886  C   PHE A 240      14.280   9.047  38.857  1.00 25.99           C  
ATOM   1887  O   PHE A 240      14.089   7.922  38.401  1.00 27.10           O  
ATOM   1888  CB  PHE A 240      15.466  10.307  37.136  1.00 23.65           C  
ATOM   1889  CG  PHE A 240      16.494  11.328  36.769  1.00 23.93           C  
ATOM   1890  CD1 PHE A 240      17.053  12.163  37.732  1.00 25.10           C  
ATOM   1891  CD2 PHE A 240      16.867  11.493  35.439  1.00 25.80           C  
ATOM   1892  CE1 PHE A 240      17.965  13.144  37.375  1.00 25.72           C  
ATOM   1893  CE2 PHE A 240      17.780  12.473  35.070  1.00 26.93           C  
ATOM   1894  CZ  PHE A 240      18.330  13.300  36.040  1.00 26.69           C  
ATOM   1895  N   PRO A 241      13.365   9.676  39.607  1.00 25.81           N  
ATOM   1896  CA  PRO A 241      12.097   9.006  39.894  1.00 27.99           C  
ATOM   1897  C   PRO A 241      11.387   8.712  38.576  1.00 31.58           C  
ATOM   1898  O   PRO A 241      11.627   9.386  37.572  1.00 29.95           O  
ATOM   1899  CB  PRO A 241      11.354  10.031  40.743  1.00 27.37           C  
ATOM   1900  CG  PRO A 241      12.475  10.712  41.480  1.00 26.86           C  
ATOM   1901  CD  PRO A 241      13.489  10.924  40.379  1.00 26.72           C  
ATOM   1902  N   LYS A 242      10.519   7.706  38.582  1.00 33.13           N  
ATOM   1903  CA  LYS A 242       9.782   7.322  37.383  1.00 35.97           C  
ATOM   1904  C   LYS A 242       8.323   7.757  37.452  1.00 35.25           C  
ATOM   1905  O   LYS A 242       7.511   7.128  38.126  1.00 36.35           O  
ATOM   1906  CB  LYS A 242       9.866   5.805  37.188  1.00 38.90           C  
ATOM   1907  CG  LYS A 242      10.945   5.347  36.210  1.00 43.43           C  
ATOM   1908  CD  LYS A 242      12.304   5.945  36.524  1.00 46.75           C  
ATOM   1909  CE  LYS A 242      13.322   5.582  35.449  1.00 49.07           C  
ATOM   1910  NZ  LYS A 242      14.621   6.294  35.636  1.00 51.23           N  
ATOM   1911  N   TRP A 243       7.997   8.838  36.750  1.00 33.46           N  
ATOM   1912  CA  TRP A 243       6.636   9.362  36.726  1.00 30.91           C  
ATOM   1913  C   TRP A 243       5.950   8.991  35.413  1.00 32.04           C  
ATOM   1914  O   TRP A 243       6.604   8.864  34.375  1.00 28.60           O  
ATOM   1915  CB  TRP A 243       6.655  10.887  36.869  1.00 32.84           C  
ATOM   1916  CG  TRP A 243       6.970  11.400  38.252  1.00 34.50           C  
ATOM   1917  CD1 TRP A 243       6.143  11.392  39.337  1.00 35.38           C  
ATOM   1918  CD2 TRP A 243       8.184  12.036  38.680  1.00 34.12           C  
ATOM   1919  NE1 TRP A 243       6.760  11.989  40.413  1.00 35.87           N  
ATOM   1920  CE2 TRP A 243       8.014  12.393  40.037  1.00 35.51           C  
ATOM   1921  CE3 TRP A 243       9.397  12.339  38.049  1.00 32.69           C  
ATOM   1922  CZ2 TRP A 243       9.013  13.041  40.775  1.00 34.23           C  
ATOM   1923  CZ3 TRP A 243      10.392  12.984  38.784  1.00 33.55           C  
ATOM   1924  CH2 TRP A 243      10.190  13.327  40.134  1.00 33.38           C  
ATOM   1925  N   ALA A 244       4.633   8.818  35.467  1.00 31.98           N  
ATOM   1926  CA  ALA A 244       3.853   8.469  34.287  1.00 33.90           C  
ATOM   1927  C   ALA A 244       3.371   9.738  33.605  1.00 33.92           C  
ATOM   1928  O   ALA A 244       3.065  10.733  34.261  1.00 34.60           O  
ATOM   1929  CB  ALA A 244       2.660   7.599  34.681  1.00 34.12           C  
ATOM   1930  N   ARG A 245       3.299   9.697  32.283  1.00 34.89           N  
ATOM   1931  CA  ARG A 245       2.864  10.847  31.505  1.00 36.16           C  
ATOM   1932  C   ARG A 245       1.395  11.165  31.763  1.00 38.53           C  
ATOM   1933  O   ARG A 245       0.582  10.260  31.962  1.00 38.50           O  
ATOM   1934  CB  ARG A 245       3.075  10.563  30.018  1.00 36.34           C  
ATOM   1935  CG  ARG A 245       2.781  11.723  29.084  1.00 34.49           C  
ATOM   1936  CD  ARG A 245       2.694  11.217  27.652  1.00 35.93           C  
ATOM   1937  NE  ARG A 245       2.550  12.292  26.675  1.00 35.48           N  
ATOM   1938  CZ  ARG A 245       3.534  13.106  26.308  1.00 36.33           C  
ATOM   1939  NH1 ARG A 245       4.747  12.975  26.837  1.00 33.03           N  
ATOM   1940  NH2 ARG A 245       3.309  14.047  25.401  1.00 35.37           N  
ATOM   1941  N   GLN A 246       1.067  12.455  31.770  1.00 39.45           N  
ATOM   1942  CA  GLN A 246      -0.305  12.903  31.972  1.00 41.15           C  
ATOM   1943  C   GLN A 246      -0.901  13.131  30.587  1.00 41.29           C  
ATOM   1944  O   GLN A 246      -0.167  13.291  29.611  1.00 41.67           O  
ATOM   1945  CB  GLN A 246      -0.342  14.220  32.754  1.00 42.50           C  
ATOM   1946  CG  GLN A 246       0.451  14.225  34.054  1.00 46.40           C  
ATOM   1947  CD  GLN A 246      -0.067  13.232  35.078  1.00 48.95           C  
ATOM   1948  OE1 GLN A 246      -0.059  12.021  34.849  1.00 50.13           O  
ATOM   1949  NE2 GLN A 246      -0.520  13.742  36.220  1.00 50.44           N  
ATOM   1950  N   ASP A 247      -2.227  13.153  30.503  1.00 40.94           N  
ATOM   1951  CA  ASP A 247      -2.906  13.371  29.233  1.00 39.61           C  
ATOM   1952  C   ASP A 247      -3.009  14.874  28.997  1.00 38.12           C  
ATOM   1953  O   ASP A 247      -3.325  15.625  29.917  1.00 38.05           O  
ATOM   1954  CB  ASP A 247      -4.305  12.744  29.281  1.00 42.62           C  
ATOM   1955  CG  ASP A 247      -4.962  12.678  27.920  1.00 43.77           C  
ATOM   1956  OD1 ASP A 247      -5.155  13.742  27.293  1.00 47.51           O  
ATOM   1957  OD2 ASP A 247      -5.286  11.559  27.473  1.00 47.43           O  
ATOM   1958  N   PHE A 248      -2.740  15.315  27.772  1.00 35.79           N  
ATOM   1959  CA  PHE A 248      -2.807  16.739  27.456  1.00 34.84           C  
ATOM   1960  C   PHE A 248      -4.186  17.343  27.678  1.00 32.34           C  
ATOM   1961  O   PHE A 248      -4.308  18.538  27.935  1.00 31.38           O  
ATOM   1962  CB  PHE A 248      -2.351  16.999  26.015  1.00 36.72           C  
ATOM   1963  CG  PHE A 248      -0.861  17.093  25.868  1.00 36.59           C  
ATOM   1964  CD1 PHE A 248      -0.055  15.989  26.107  1.00 37.94           C  
ATOM   1965  CD2 PHE A 248      -0.258  18.303  25.543  1.00 36.96           C  
ATOM   1966  CE1 PHE A 248       1.335  16.089  26.028  1.00 39.39           C  
ATOM   1967  CE2 PHE A 248       1.129  18.416  25.463  1.00 37.00           C  
ATOM   1968  CZ  PHE A 248       1.927  17.308  25.707  1.00 37.49           C  
ATOM   1969  N   SER A 249      -5.227  16.524  27.581  1.00 29.95           N  
ATOM   1970  CA  SER A 249      -6.573  17.025  27.806  1.00 26.78           C  
ATOM   1971  C   SER A 249      -6.603  17.607  29.222  1.00 24.36           C  
ATOM   1972  O   SER A 249      -7.371  18.517  29.520  1.00 24.35           O  
ATOM   1973  CB  SER A 249      -7.595  15.889  27.685  1.00 25.69           C  
ATOM   1974  OG  SER A 249      -7.362  14.894  28.666  1.00 26.52           O  
ATOM   1975  N   LYS A 250      -5.750  17.079  30.090  1.00 23.26           N  
ATOM   1976  CA  LYS A 250      -5.689  17.559  31.469  1.00 24.70           C  
ATOM   1977  C   LYS A 250      -4.709  18.724  31.625  1.00 25.32           C  
ATOM   1978  O   LYS A 250      -4.887  19.587  32.488  1.00 25.87           O  
ATOM   1979  CB  LYS A 250      -5.265  16.429  32.408  1.00 25.10           C  
ATOM   1980  CG  LYS A 250      -5.247  16.846  33.870  1.00 27.95           C  
ATOM   1981  CD  LYS A 250      -4.652  15.773  34.761  1.00 34.29           C  
ATOM   1982  CE  LYS A 250      -4.768  16.183  36.221  1.00 34.81           C  
ATOM   1983  NZ  LYS A 250      -4.216  15.160  37.146  1.00 38.49           N  
ATOM   1984  N   VAL A 251      -3.683  18.745  30.780  1.00 24.15           N  
ATOM   1985  CA  VAL A 251      -2.660  19.782  30.840  1.00 26.21           C  
ATOM   1986  C   VAL A 251      -3.074  21.141  30.288  1.00 26.34           C  
ATOM   1987  O   VAL A 251      -2.817  22.174  30.917  1.00 25.70           O  
ATOM   1988  CB  VAL A 251      -1.377  19.340  30.096  1.00 28.28           C  
ATOM   1989  CG1 VAL A 251      -0.340  20.457  30.130  1.00 29.92           C  
ATOM   1990  CG2 VAL A 251      -0.813  18.079  30.732  1.00 28.58           C  
ATOM   1991  N   VAL A 252      -3.724  21.157  29.128  1.00 24.65           N  
ATOM   1992  CA  VAL A 252      -4.094  22.435  28.539  1.00 24.67           C  
ATOM   1993  C   VAL A 252      -5.535  22.692  28.116  1.00 26.43           C  
ATOM   1994  O   VAL A 252      -5.790  23.151  27.000  1.00 26.01           O  
ATOM   1995  CB  VAL A 252      -3.178  22.760  27.334  1.00 25.76           C  
ATOM   1996  CG1 VAL A 252      -1.786  23.120  27.820  1.00 26.61           C  
ATOM   1997  CG2 VAL A 252      -3.109  21.571  26.395  1.00 24.31           C  
ATOM   1998  N   PRO A 253      -6.506  22.409  28.996  1.00 25.88           N  
ATOM   1999  CA  PRO A 253      -7.878  22.685  28.567  1.00 26.72           C  
ATOM   2000  C   PRO A 253      -7.982  24.217  28.521  1.00 27.69           C  
ATOM   2001  O   PRO A 253      -7.289  24.902  29.271  1.00 27.99           O  
ATOM   2002  CB  PRO A 253      -8.709  22.072  29.693  1.00 27.82           C  
ATOM   2003  CG  PRO A 253      -7.849  22.324  30.901  1.00 25.87           C  
ATOM   2004  CD  PRO A 253      -6.464  21.945  30.394  1.00 26.52           C  
ATOM   2005  N   PRO A 254      -8.845  24.779  27.659  1.00 28.42           N  
ATOM   2006  CA  PRO A 254      -9.759  24.159  26.700  1.00 28.18           C  
ATOM   2007  C   PRO A 254      -9.217  24.169  25.274  1.00 27.03           C  
ATOM   2008  O   PRO A 254      -9.961  24.411  24.325  1.00 26.91           O  
ATOM   2009  CB  PRO A 254     -10.998  25.025  26.831  1.00 29.19           C  
ATOM   2010  CG  PRO A 254     -10.383  26.392  26.901  1.00 28.56           C  
ATOM   2011  CD  PRO A 254      -9.169  26.209  27.817  1.00 28.76           C  
ATOM   2012  N   LEU A 255      -7.924  23.916  25.123  1.00 24.98           N  
ATOM   2013  CA  LEU A 255      -7.317  23.900  23.800  1.00 25.18           C  
ATOM   2014  C   LEU A 255      -7.928  22.740  23.025  1.00 22.56           C  
ATOM   2015  O   LEU A 255      -8.015  21.627  23.545  1.00 20.49           O  
ATOM   2016  CB  LEU A 255      -5.805  23.718  23.926  1.00 24.49           C  
ATOM   2017  CG  LEU A 255      -4.976  23.866  22.651  1.00 25.43           C  
ATOM   2018  CD1 LEU A 255      -5.148  25.263  22.087  1.00 27.43           C  
ATOM   2019  CD2 LEU A 255      -3.521  23.611  22.970  1.00 24.30           C  
ATOM   2020  N   ASP A 256      -8.353  22.993  21.789  1.00 23.66           N  
ATOM   2021  CA  ASP A 256      -8.971  21.939  20.991  1.00 22.89           C  
ATOM   2022  C   ASP A 256      -7.974  20.862  20.584  1.00 22.47           C  
ATOM   2023  O   ASP A 256      -6.784  20.967  20.877  1.00 20.31           O  
ATOM   2024  CB  ASP A 256      -9.672  22.521  19.752  1.00 24.75           C  
ATOM   2025  CG  ASP A 256      -8.720  23.223  18.805  1.00 27.43           C  
ATOM   2026  OD1 ASP A 256      -7.682  22.626  18.457  1.00 22.70           O  
ATOM   2027  OD2 ASP A 256      -9.022  24.369  18.397  1.00 29.65           O  
ATOM   2028  N   GLU A 257      -8.462  19.831  19.899  1.00 20.69           N  
ATOM   2029  CA  GLU A 257      -7.609  18.723  19.495  1.00 21.65           C  
ATOM   2030  C   GLU A 257      -6.450  19.107  18.580  1.00 19.12           C  
ATOM   2031  O   GLU A 257      -5.365  18.539  18.693  1.00 18.63           O  
ATOM   2032  CB  GLU A 257      -8.444  17.624  18.834  1.00 25.19           C  
ATOM   2033  CG  GLU A 257      -7.718  16.302  18.745  1.00 31.34           C  
ATOM   2034  CD  GLU A 257      -7.457  15.711  20.115  1.00 33.54           C  
ATOM   2035  OE1 GLU A 257      -8.446  15.397  20.808  1.00 37.50           O  
ATOM   2036  OE2 GLU A 257      -6.273  15.573  20.499  1.00 35.66           O  
ATOM   2037  N   ASP A 258      -6.670  20.051  17.671  1.00 19.60           N  
ATOM   2038  CA  ASP A 258      -5.597  20.477  16.768  1.00 18.18           C  
ATOM   2039  C   ASP A 258      -4.483  21.133  17.583  1.00 19.06           C  
ATOM   2040  O   ASP A 258      -3.297  20.851  17.381  1.00 19.68           O  
ATOM   2041  CB  ASP A 258      -6.117  21.473  15.725  1.00 20.37           C  
ATOM   2042  CG  ASP A 258      -7.019  20.822  14.683  1.00 21.73           C  
ATOM   2043  OD1 ASP A 258      -6.681  19.727  14.201  1.00 22.86           O  
ATOM   2044  OD2 ASP A 258      -8.060  21.415  14.333  1.00 24.37           O  
ATOM   2045  N   GLY A 259      -4.871  22.012  18.501  1.00 17.64           N  
ATOM   2046  CA  GLY A 259      -3.890  22.682  19.335  1.00 20.26           C  
ATOM   2047  C   GLY A 259      -3.106  21.695  20.187  1.00 20.41           C  
ATOM   2048  O   GLY A 259      -1.879  21.777  20.274  1.00 17.34           O  
ATOM   2049  N   ARG A 260      -3.814  20.762  20.823  1.00 19.92           N  
ATOM   2050  CA  ARG A 260      -3.168  19.758  21.663  1.00 21.11           C  
ATOM   2051  C   ARG A 260      -2.224  18.882  20.841  1.00 19.27           C  
ATOM   2052  O   ARG A 260      -1.146  18.506  21.307  1.00 19.07           O  
ATOM   2053  CB  ARG A 260      -4.223  18.886  22.359  1.00 22.65           C  
ATOM   2054  CG  ARG A 260      -4.983  19.598  23.477  1.00 29.83           C  
ATOM   2055  CD  ARG A 260      -6.059  18.696  24.080  1.00 35.85           C  
ATOM   2056  NE  ARG A 260      -7.205  18.552  23.188  1.00 40.70           N  
ATOM   2057  CZ  ARG A 260      -8.063  17.540  23.228  1.00 43.65           C  
ATOM   2058  NH1 ARG A 260      -7.907  16.569  24.117  1.00 45.96           N  
ATOM   2059  NH2 ARG A 260      -9.081  17.498  22.380  1.00 45.96           N  
ATOM   2060  N   SER A 261      -2.628  18.561  19.616  1.00 19.19           N  
ATOM   2061  CA  SER A 261      -1.796  17.744  18.745  1.00 18.86           C  
ATOM   2062  C   SER A 261      -0.492  18.472  18.451  1.00 19.95           C  
ATOM   2063  O   SER A 261       0.591  17.902  18.581  1.00 17.73           O  
ATOM   2064  CB  SER A 261      -2.516  17.453  17.428  1.00 20.95           C  
ATOM   2065  OG  SER A 261      -1.629  16.856  16.499  1.00 26.75           O  
ATOM   2066  N   LEU A 262      -0.595  19.739  18.057  1.00 17.04           N  
ATOM   2067  CA  LEU A 262       0.601  20.527  17.744  1.00 18.07           C  
ATOM   2068  C   LEU A 262       1.474  20.739  18.972  1.00 17.29           C  
ATOM   2069  O   LEU A 262       2.699  20.629  18.902  1.00 17.07           O  
ATOM   2070  CB  LEU A 262       0.208  21.889  17.166  1.00 17.49           C  
ATOM   2071  CG  LEU A 262       1.298  22.953  17.022  1.00 20.31           C  
ATOM   2072  CD1 LEU A 262       2.406  22.454  16.110  1.00 18.79           C  
ATOM   2073  CD2 LEU A 262       0.671  24.231  16.480  1.00 18.32           C  
ATOM   2074  N   LEU A 263       0.854  21.048  20.102  1.00 15.98           N  
ATOM   2075  CA  LEU A 263       1.640  21.270  21.311  1.00 16.60           C  
ATOM   2076  C   LEU A 263       2.421  20.012  21.672  1.00 17.77           C  
ATOM   2077  O   LEU A 263       3.597  20.081  22.045  1.00 16.12           O  
ATOM   2078  CB  LEU A 263       0.739  21.674  22.475  1.00 14.89           C  
ATOM   2079  CG  LEU A 263       1.467  21.889  23.808  1.00 17.76           C  
ATOM   2080  CD1 LEU A 263       2.414  23.077  23.695  1.00 15.29           C  
ATOM   2081  CD2 LEU A 263       0.454  22.121  24.913  1.00 14.61           C  
ATOM   2082  N   SER A 264       1.769  18.859  21.559  1.00 17.19           N  
ATOM   2083  CA  SER A 264       2.427  17.598  21.884  1.00 18.95           C  
ATOM   2084  C   SER A 264       3.684  17.422  21.032  1.00 18.70           C  
ATOM   2085  O   SER A 264       4.724  16.977  21.517  1.00 18.13           O  
ATOM   2086  CB  SER A 264       1.473  16.426  21.647  1.00 20.75           C  
ATOM   2087  OG  SER A 264       2.067  15.208  22.053  0.66 22.57           O  
ATOM   2088  N   GLN A 265       3.584  17.771  19.756  1.00 16.69           N  
ATOM   2089  CA  GLN A 265       4.727  17.638  18.861  1.00 18.65           C  
ATOM   2090  C   GLN A 265       5.837  18.634  19.173  1.00 15.79           C  
ATOM   2091  O   GLN A 265       7.007  18.353  18.923  1.00 18.47           O  
ATOM   2092  CB  GLN A 265       4.274  17.776  17.404  1.00 16.05           C  
ATOM   2093  CG  GLN A 265       3.441  16.598  16.940  1.00 22.19           C  
ATOM   2094  CD  GLN A 265       3.090  16.667  15.465  1.00 21.72           C  
ATOM   2095  OE1 GLN A 265       2.180  17.383  15.064  1.00 25.61           O  
ATOM   2096  NE2 GLN A 265       3.821  15.921  14.651  1.00 25.97           N  
ATOM   2097  N   MET A 266       5.477  19.787  19.731  1.00 15.71           N  
ATOM   2098  CA  MET A 266       6.473  20.798  20.070  1.00 15.33           C  
ATOM   2099  C   MET A 266       7.160  20.439  21.383  1.00 17.11           C  
ATOM   2100  O   MET A 266       8.249  20.932  21.674  1.00 16.00           O  
ATOM   2101  CB  MET A 266       5.822  22.175  20.205  1.00 14.93           C  
ATOM   2102  CG  MET A 266       5.137  22.678  18.940  1.00 15.96           C  
ATOM   2103  SD  MET A 266       4.390  24.287  19.263  1.00 16.79           S  
ATOM   2104  CE  MET A 266       5.826  25.337  19.263  1.00 14.33           C  
ATOM   2105  N   LEU A 267       6.514  19.575  22.162  1.00 16.31           N  
ATOM   2106  CA  LEU A 267       7.044  19.139  23.452  1.00 17.80           C  
ATOM   2107  C   LEU A 267       7.613  17.713  23.473  1.00 18.24           C  
ATOM   2108  O   LEU A 267       7.826  17.143  24.543  1.00 15.65           O  
ATOM   2109  CB  LEU A 267       5.956  19.275  24.521  1.00 17.72           C  
ATOM   2110  CG  LEU A 267       5.971  20.502  25.436  1.00 23.58           C  
ATOM   2111  CD1 LEU A 267       6.666  21.686  24.794  1.00 23.31           C  
ATOM   2112  CD2 LEU A 267       4.551  20.834  25.816  1.00 20.52           C  
ATOM   2113  N   HIS A 268       7.856  17.134  22.301  1.00 19.25           N  
ATOM   2114  CA  HIS A 268       8.433  15.795  22.230  1.00 20.05           C  
ATOM   2115  C   HIS A 268       9.818  15.817  22.903  1.00 19.13           C  
ATOM   2116  O   HIS A 268      10.589  16.764  22.735  1.00 16.97           O  
ATOM   2117  CB  HIS A 268       8.561  15.346  20.765  1.00 22.98           C  
ATOM   2118  CG  HIS A 268       7.340  14.662  20.229  1.00 27.10           C  
ATOM   2119  ND1 HIS A 268       7.019  14.654  18.888  1.00 27.10           N  
ATOM   2120  CD2 HIS A 268       6.365  13.959  20.854  1.00 28.85           C  
ATOM   2121  CE1 HIS A 268       5.897  13.980  18.710  1.00 26.78           C  
ATOM   2122  NE2 HIS A 268       5.479  13.547  19.887  1.00 29.91           N  
ATOM   2123  N   TYR A 269      10.115  14.780  23.681  1.00 18.87           N  
ATOM   2124  CA  TYR A 269      11.388  14.697  24.381  1.00 19.06           C  
ATOM   2125  C   TYR A 269      12.572  14.654  23.440  1.00 17.96           C  
ATOM   2126  O   TYR A 269      13.476  15.472  23.547  1.00 17.67           O  
ATOM   2127  CB  TYR A 269      11.427  13.463  25.284  1.00 17.88           C  
ATOM   2128  CG  TYR A 269      10.913  13.709  26.675  1.00 17.15           C  
ATOM   2129  CD1 TYR A 269      11.522  14.650  27.504  1.00 15.53           C  
ATOM   2130  CD2 TYR A 269       9.841  12.973  27.183  1.00 17.64           C  
ATOM   2131  CE1 TYR A 269      11.085  14.851  28.805  1.00 17.84           C  
ATOM   2132  CE2 TYR A 269       9.390  13.168  28.493  1.00 18.46           C  
ATOM   2133  CZ  TYR A 269      10.020  14.108  29.295  1.00 15.19           C  
ATOM   2134  OH  TYR A 269       9.599  14.301  30.586  1.00 18.07           O  
ATOM   2135  N   ASP A 270      12.575  13.691  22.526  1.00 17.97           N  
ATOM   2136  CA  ASP A 270      13.675  13.565  21.587  1.00 20.02           C  
ATOM   2137  C   ASP A 270      13.756  14.806  20.700  1.00 21.38           C  
ATOM   2138  O   ASP A 270      12.856  15.060  19.897  1.00 22.08           O  
ATOM   2139  CB  ASP A 270      13.485  12.328  20.706  1.00 21.23           C  
ATOM   2140  CG  ASP A 270      14.730  11.990  19.917  1.00 23.26           C  
ATOM   2141  OD1 ASP A 270      15.528  12.915  19.658  1.00 22.05           O  
ATOM   2142  OD2 ASP A 270      14.909  10.809  19.555  1.00 26.51           O  
ATOM   2143  N   PRO A 271      14.843  15.588  20.823  1.00 20.14           N  
ATOM   2144  CA  PRO A 271      15.002  16.797  20.012  1.00 22.90           C  
ATOM   2145  C   PRO A 271      14.773  16.515  18.532  1.00 22.40           C  
ATOM   2146  O   PRO A 271      14.243  17.355  17.814  1.00 24.29           O  
ATOM   2147  CB  PRO A 271      16.443  17.217  20.295  1.00 22.02           C  
ATOM   2148  CG  PRO A 271      16.670  16.712  21.682  1.00 23.63           C  
ATOM   2149  CD  PRO A 271      16.036  15.356  21.653  1.00 21.46           C  
ATOM   2150  N   ASN A 272      15.169  15.326  18.083  1.00 23.60           N  
ATOM   2151  CA  ASN A 272      15.014  14.956  16.676  1.00 26.53           C  
ATOM   2152  C   ASN A 272      13.586  14.653  16.261  1.00 27.28           C  
ATOM   2153  O   ASN A 272      13.246  14.758  15.080  1.00 32.61           O  
ATOM   2154  CB  ASN A 272      15.898  13.756  16.337  1.00 29.09           C  
ATOM   2155  CG  ASN A 272      17.359  14.041  16.553  1.00 31.82           C  
ATOM   2156  OD1 ASN A 272      17.858  13.993  17.683  1.00 36.24           O  
ATOM   2157  ND2 ASN A 272      18.060  14.361  15.472  1.00 33.05           N  
ATOM   2158  N   LYS A 273      12.746  14.267  17.214  1.00 26.11           N  
ATOM   2159  CA  LYS A 273      11.352  13.972  16.899  1.00 26.22           C  
ATOM   2160  C   LYS A 273      10.510  15.238  17.010  1.00 24.06           C  
ATOM   2161  O   LYS A 273       9.437  15.332  16.414  1.00 24.66           O  
ATOM   2162  CB  LYS A 273      10.787  12.914  17.855  1.00 28.85           C  
ATOM   2163  CG  LYS A 273      11.465  11.554  17.786  1.00 31.72           C  
ATOM   2164  CD  LYS A 273      10.842  10.590  18.793  1.00 34.63           C  
ATOM   2165  CE  LYS A 273      11.461   9.197  18.708  1.00 36.85           C  
ATOM   2166  NZ  LYS A 273      12.926   9.208  18.978  1.00 34.38           N  
ATOM   2167  N   ARG A 274      11.003  16.207  17.776  1.00 21.43           N  
ATOM   2168  CA  ARG A 274      10.290  17.464  17.997  1.00 18.71           C  
ATOM   2169  C   ARG A 274      10.059  18.162  16.656  1.00 18.57           C  
ATOM   2170  O   ARG A 274      10.976  18.294  15.844  1.00 18.57           O  
ATOM   2171  CB  ARG A 274      11.102  18.359  18.944  1.00 17.85           C  
ATOM   2172  CG  ARG A 274      10.296  19.407  19.713  1.00 18.59           C  
ATOM   2173  CD  ARG A 274      11.185  20.112  20.751  1.00 17.18           C  
ATOM   2174  NE  ARG A 274      11.755  19.157  21.704  1.00 17.58           N  
ATOM   2175  CZ  ARG A 274      12.915  19.319  22.342  1.00 17.98           C  
ATOM   2176  NH1 ARG A 274      13.653  20.405  22.144  1.00 16.37           N  
ATOM   2177  NH2 ARG A 274      13.347  18.378  23.172  1.00 18.59           N  
ATOM   2178  N   ILE A 275       8.825  18.604  16.438  1.00 17.49           N  
ATOM   2179  CA  ILE A 275       8.438  19.261  15.196  1.00 17.48           C  
ATOM   2180  C   ILE A 275       9.274  20.505  14.886  1.00 15.77           C  
ATOM   2181  O   ILE A 275       9.691  21.228  15.787  1.00 17.80           O  
ATOM   2182  CB  ILE A 275       6.926  19.632  15.232  1.00 18.62           C  
ATOM   2183  CG1 ILE A 275       6.422  19.930  13.817  1.00 19.61           C  
ATOM   2184  CG2 ILE A 275       6.695  20.830  16.151  1.00 15.39           C  
ATOM   2185  CD1 ILE A 275       4.922  20.077  13.725  1.00 21.85           C  
ATOM   2186  N   SER A 276       9.540  20.732  13.605  1.00 15.80           N  
ATOM   2187  CA  SER A 276      10.307  21.896  13.179  1.00 16.02           C  
ATOM   2188  C   SER A 276       9.361  23.087  13.057  1.00 15.78           C  
ATOM   2189  O   SER A 276       8.144  22.917  13.013  1.00 16.24           O  
ATOM   2190  CB  SER A 276      10.966  21.638  11.821  1.00 18.15           C  
ATOM   2191  OG  SER A 276       9.986  21.525  10.802  1.00 18.88           O  
ATOM   2192  N   ALA A 277       9.918  24.291  12.993  1.00 16.99           N  
ATOM   2193  CA  ALA A 277       9.092  25.490  12.869  1.00 16.95           C  
ATOM   2194  C   ALA A 277       8.345  25.437  11.543  1.00 18.33           C  
ATOM   2195  O   ALA A 277       7.147  25.718  11.480  1.00 17.79           O  
ATOM   2196  CB  ALA A 277       9.959  26.740  12.924  1.00 16.70           C  
ATOM   2197  N   LYS A 278       9.056  25.056  10.486  1.00 19.04           N  
ATOM   2198  CA  LYS A 278       8.445  24.985   9.162  1.00 22.16           C  
ATOM   2199  C   LYS A 278       7.274  24.005   9.120  1.00 22.15           C  
ATOM   2200  O   LYS A 278       6.200  24.334   8.625  1.00 22.88           O  
ATOM   2201  CB  LYS A 278       9.488  24.592   8.116  1.00 24.97           C  
ATOM   2202  CG  LYS A 278       8.950  24.579   6.690  1.00 31.77           C  
ATOM   2203  CD  LYS A 278      10.060  24.378   5.665  1.00 35.87           C  
ATOM   2204  CE  LYS A 278       9.492  24.305   4.249  1.00 38.07           C  
ATOM   2205  NZ  LYS A 278       8.675  25.514   3.912  1.00 36.90           N  
ATOM   2206  N   ALA A 279       7.477  22.802   9.647  1.00 21.96           N  
ATOM   2207  CA  ALA A 279       6.422  21.796   9.650  1.00 21.61           C  
ATOM   2208  C   ALA A 279       5.242  22.227  10.511  1.00 22.05           C  
ATOM   2209  O   ALA A 279       4.089  21.912  10.206  1.00 20.72           O  
ATOM   2210  CB  ALA A 279       6.969  20.468  10.147  1.00 22.29           C  
ATOM   2211  N   ALA A 280       5.525  22.948  11.590  1.00 20.36           N  
ATOM   2212  CA  ALA A 280       4.464  23.401  12.482  1.00 18.91           C  
ATOM   2213  C   ALA A 280       3.559  24.406  11.782  1.00 19.44           C  
ATOM   2214  O   ALA A 280       2.362  24.445  12.035  1.00 19.66           O  
ATOM   2215  CB  ALA A 280       5.068  24.017  13.755  1.00 17.84           C  
ATOM   2216  N   LEU A 281       4.128  25.208  10.886  1.00 19.39           N  
ATOM   2217  CA  LEU A 281       3.338  26.197  10.164  1.00 19.57           C  
ATOM   2218  C   LEU A 281       2.287  25.541   9.268  1.00 20.73           C  
ATOM   2219  O   LEU A 281       1.282  26.163   8.913  1.00 21.82           O  
ATOM   2220  CB  LEU A 281       4.260  27.091   9.324  1.00 20.76           C  
ATOM   2221  CG  LEU A 281       5.146  28.055  10.121  1.00 19.01           C  
ATOM   2222  CD1 LEU A 281       6.108  28.780   9.186  1.00 18.71           C  
ATOM   2223  CD2 LEU A 281       4.266  29.055  10.861  1.00 17.93           C  
ATOM   2224  N   ALA A 282       2.509  24.279   8.915  1.00 19.63           N  
ATOM   2225  CA  ALA A 282       1.574  23.555   8.054  1.00 20.65           C  
ATOM   2226  C   ALA A 282       0.524  22.771   8.837  1.00 21.25           C  
ATOM   2227  O   ALA A 282      -0.360  22.142   8.244  1.00 19.93           O  
ATOM   2228  CB  ALA A 282       2.345  22.606   7.139  1.00 21.42           C  
ATOM   2229  N   HIS A 283       0.619  22.813  10.163  1.00 18.81           N  
ATOM   2230  CA  HIS A 283      -0.305  22.076  11.021  1.00 20.72           C  
ATOM   2231  C   HIS A 283      -1.746  22.577  10.901  1.00 20.60           C  
ATOM   2232  O   HIS A 283      -1.995  23.777  10.792  1.00 21.31           O  
ATOM   2233  CB  HIS A 283       0.166  22.149  12.480  1.00 20.85           C  
ATOM   2234  CG  HIS A 283      -0.486  21.144  13.382  1.00 21.30           C  
ATOM   2235  ND1 HIS A 283      -1.771  21.290  13.858  1.00 20.80           N  
ATOM   2236  CD2 HIS A 283      -0.032  19.968  13.880  1.00 21.47           C  
ATOM   2237  CE1 HIS A 283      -2.081  20.248  14.611  1.00 21.73           C  
ATOM   2238  NE2 HIS A 283      -1.042  19.431  14.642  1.00 20.84           N  
ATOM   2239  N   PRO A 284      -2.715  21.648  10.912  1.00 20.81           N  
ATOM   2240  CA  PRO A 284      -4.144  21.971  10.804  1.00 21.85           C  
ATOM   2241  C   PRO A 284      -4.615  23.022  11.808  1.00 21.45           C  
ATOM   2242  O   PRO A 284      -5.647  23.656  11.610  1.00 22.95           O  
ATOM   2243  CB  PRO A 284      -4.817  20.621  11.033  1.00 20.55           C  
ATOM   2244  CG  PRO A 284      -3.838  19.659  10.431  1.00 23.22           C  
ATOM   2245  CD  PRO A 284      -2.507  20.187  10.938  1.00 21.45           C  
ATOM   2246  N   PHE A 285      -3.864  23.199  12.891  1.00 21.03           N  
ATOM   2247  CA  PHE A 285      -4.231  24.175  13.917  1.00 20.02           C  
ATOM   2248  C   PHE A 285      -4.296  25.590  13.353  1.00 20.68           C  
ATOM   2249  O   PHE A 285      -5.056  26.428  13.841  1.00 21.20           O  
ATOM   2250  CB  PHE A 285      -3.223  24.135  15.071  1.00 20.60           C  
ATOM   2251  CG  PHE A 285      -3.527  25.105  16.181  1.00 18.39           C  
ATOM   2252  CD1 PHE A 285      -4.718  25.016  16.895  1.00 19.40           C  
ATOM   2253  CD2 PHE A 285      -2.612  26.091  16.529  1.00 18.67           C  
ATOM   2254  CE1 PHE A 285      -4.991  25.896  17.947  1.00 19.58           C  
ATOM   2255  CE2 PHE A 285      -2.876  26.973  17.577  1.00 20.42           C  
ATOM   2256  CZ  PHE A 285      -4.074  26.869  18.288  1.00 19.99           C  
ATOM   2257  N   PHE A 286      -3.504  25.850  12.319  1.00 20.46           N  
ATOM   2258  CA  PHE A 286      -3.460  27.172  11.710  1.00 19.05           C  
ATOM   2259  C   PHE A 286      -4.384  27.362  10.509  1.00 23.39           C  
ATOM   2260  O   PHE A 286      -4.332  28.395   9.845  1.00 23.39           O  
ATOM   2261  CB  PHE A 286      -2.015  27.503  11.322  1.00 19.35           C  
ATOM   2262  CG  PHE A 286      -1.090  27.602  12.504  1.00 16.96           C  
ATOM   2263  CD1 PHE A 286      -1.276  28.598  13.458  1.00 16.20           C  
ATOM   2264  CD2 PHE A 286      -0.076  26.667  12.696  1.00 17.91           C  
ATOM   2265  CE1 PHE A 286      -0.469  28.659  14.590  1.00 16.23           C  
ATOM   2266  CE2 PHE A 286       0.743  26.714  13.828  1.00 15.93           C  
ATOM   2267  CZ  PHE A 286       0.548  27.707  14.776  1.00 15.34           C  
ATOM   2268  N   GLN A 287      -5.246  26.381  10.257  1.00 24.16           N  
ATOM   2269  CA  GLN A 287      -6.163  26.440   9.125  1.00 28.26           C  
ATOM   2270  C   GLN A 287      -6.999  27.720   9.095  1.00 26.68           C  
ATOM   2271  O   GLN A 287      -7.196  28.317   8.042  1.00 29.19           O  
ATOM   2272  CB  GLN A 287      -7.099  25.228   9.139  1.00 30.10           C  
ATOM   2273  CG  GLN A 287      -7.858  25.031   7.837  1.00 36.91           C  
ATOM   2274  CD  GLN A 287      -6.960  24.569   6.703  1.00 41.47           C  
ATOM   2275  OE1 GLN A 287      -7.301  24.716   5.525  1.00 45.41           O  
ATOM   2276  NE2 GLN A 287      -5.811  23.995   7.052  1.00 43.34           N  
ATOM   2277  N   ASP A 288      -7.477  28.143  10.256  1.00 26.98           N  
ATOM   2278  CA  ASP A 288      -8.313  29.335  10.343  1.00 29.26           C  
ATOM   2279  C   ASP A 288      -7.592  30.496  11.015  1.00 27.05           C  
ATOM   2280  O   ASP A 288      -8.222  31.332  11.659  1.00 27.94           O  
ATOM   2281  CB  ASP A 288      -9.586  29.007  11.128  1.00 29.76           C  
ATOM   2282  CG  ASP A 288      -9.299  28.686  12.589  1.00 33.06           C  
ATOM   2283  OD1 ASP A 288      -8.109  28.584  12.955  1.00 33.18           O  
ATOM   2284  OD2 ASP A 288     -10.261  28.530  13.370  1.00 34.56           O  
ATOM   2285  N   VAL A 289      -6.274  30.551  10.874  1.00 26.41           N  
ATOM   2286  CA  VAL A 289      -5.525  31.626  11.504  1.00 24.41           C  
ATOM   2287  C   VAL A 289      -5.852  32.967  10.856  1.00 25.38           C  
ATOM   2288  O   VAL A 289      -6.043  33.054   9.638  1.00 24.33           O  
ATOM   2289  CB  VAL A 289      -4.000  31.378  11.428  1.00 24.18           C  
ATOM   2290  CG1 VAL A 289      -3.507  31.569  10.006  1.00 23.61           C  
ATOM   2291  CG2 VAL A 289      -3.276  32.314  12.390  1.00 22.36           C  
ATOM   2292  N   THR A 290      -5.930  34.001  11.688  1.00 25.51           N  
ATOM   2293  CA  THR A 290      -6.223  35.361  11.248  1.00 25.59           C  
ATOM   2294  C   THR A 290      -5.266  36.282  11.997  1.00 26.56           C  
ATOM   2295  O   THR A 290      -4.459  35.817  12.803  1.00 24.89           O  
ATOM   2296  CB  THR A 290      -7.672  35.774  11.611  1.00 25.52           C  
ATOM   2297  OG1 THR A 290      -7.812  35.838  13.038  1.00 24.39           O  
ATOM   2298  CG2 THR A 290      -8.673  34.764  11.057  1.00 25.59           C  
ATOM   2299  N   LYS A 291      -5.345  37.582  11.736  1.00 25.78           N  
ATOM   2300  CA  LYS A 291      -4.477  38.526  12.431  1.00 25.93           C  
ATOM   2301  C   LYS A 291      -5.301  39.585  13.163  1.00 26.64           C  
ATOM   2302  O   LYS A 291      -5.526  40.685  12.650  1.00 26.04           O  
ATOM   2303  CB  LYS A 291      -3.513  39.197  11.452  1.00 27.74           C  
ATOM   2304  CG  LYS A 291      -2.573  40.179  12.127  1.00 30.75           C  
ATOM   2305  CD  LYS A 291      -1.606  40.816  11.143  1.00 34.14           C  
ATOM   2306  CE  LYS A 291      -0.676  41.780  11.867  1.00 35.71           C  
ATOM   2307  NZ  LYS A 291       0.330  42.378  10.952  1.00 37.53           N  
ATOM   2308  N   PRO A 292      -5.767  39.257  14.378  1.00 24.43           N  
ATOM   2309  CA  PRO A 292      -6.571  40.160  15.204  1.00 25.97           C  
ATOM   2310  C   PRO A 292      -5.735  41.293  15.774  1.00 27.35           C  
ATOM   2311  O   PRO A 292      -4.527  41.152  15.959  1.00 28.76           O  
ATOM   2312  CB  PRO A 292      -7.088  39.252  16.322  1.00 25.33           C  
ATOM   2313  CG  PRO A 292      -6.949  37.861  15.767  1.00 24.46           C  
ATOM   2314  CD  PRO A 292      -5.660  37.934  15.013  1.00 24.05           C  
ATOM   2315  N   VAL A 293      -6.381  42.418  16.052  1.00 29.96           N  
ATOM   2316  CA  VAL A 293      -5.681  43.544  16.645  1.00 34.05           C  
ATOM   2317  C   VAL A 293      -5.872  43.403  18.153  1.00 36.64           C  
ATOM   2318  O   VAL A 293      -6.998  43.295  18.644  1.00 37.37           O  
ATOM   2319  CB  VAL A 293      -6.251  44.907  16.154  1.00 35.04           C  
ATOM   2320  CG1 VAL A 293      -6.321  44.918  14.638  1.00 34.79           C  
ATOM   2321  CG2 VAL A 293      -7.627  45.169  16.751  1.00 35.97           C  
ATOM   2322  N   PRO A 294      -4.769  43.358  18.906  1.00 39.03           N  
ATOM   2323  CA  PRO A 294      -4.877  43.225  20.357  1.00 40.77           C  
ATOM   2324  C   PRO A 294      -5.244  44.581  20.932  1.00 44.53           C  
ATOM   2325  O   PRO A 294      -4.922  45.615  20.341  1.00 45.52           O  
ATOM   2326  CB  PRO A 294      -3.477  42.796  20.757  1.00 39.19           C  
ATOM   2327  CG  PRO A 294      -2.634  43.593  19.813  1.00 39.00           C  
ATOM   2328  CD  PRO A 294      -3.358  43.428  18.490  1.00 39.20           C  
ATOM   2329  N   HIS A 295      -5.924  44.594  22.069  1.00 47.47           N  
ATOM   2330  CA  HIS A 295      -6.277  45.869  22.656  1.00 51.10           C  
ATOM   2331  C   HIS A 295      -5.200  46.269  23.648  1.00 51.05           C  
ATOM   2332  O   HIS A 295      -5.115  45.725  24.749  1.00 52.22           O  
ATOM   2333  CB  HIS A 295      -7.645  45.808  23.336  1.00 53.37           C  
ATOM   2334  CG  HIS A 295      -8.391  47.105  23.279  1.00 57.01           C  
ATOM   2335  ND1 HIS A 295      -7.969  48.236  23.946  1.00 59.57           N  
ATOM   2336  CD2 HIS A 295      -9.495  47.469  22.584  1.00 59.12           C  
ATOM   2337  CE1 HIS A 295      -8.779  49.241  23.662  1.00 60.53           C  
ATOM   2338  NE2 HIS A 295      -9.713  48.802  22.837  1.00 60.89           N  
ATOM   2339  N   LEU A 296      -4.357  47.205  23.225  1.00 51.27           N  
ATOM   2340  CA  LEU A 296      -3.270  47.714  24.049  1.00 51.93           C  
ATOM   2341  C   LEU A 296      -3.550  49.151  24.457  1.00 52.63           C  
ATOM   2342  O   LEU A 296      -3.925  49.976  23.621  1.00 51.65           O  
ATOM   2343  CB  LEU A 296      -1.948  47.682  23.279  1.00 51.48           C  
ATOM   2344  CG  LEU A 296      -1.178  46.374  23.136  1.00 50.88           C  
ATOM   2345  CD1 LEU A 296      -2.056  45.320  22.501  1.00 52.40           C  
ATOM   2346  CD2 LEU A 296       0.064  46.623  22.300  1.00 50.13           C  
ATOM   2347  N   ARG A 297      -3.369  49.447  25.741  1.00 52.81           N  
ATOM   2348  CA  ARG A 297      -3.574  50.801  26.235  1.00 54.45           C  
ATOM   2349  C   ARG A 297      -2.264  51.300  26.841  1.00 53.09           C  
ATOM   2350  O   ARG A 297      -2.020  51.164  28.041  1.00 53.08           O  
ATOM   2351  CB  ARG A 297      -4.697  50.842  27.275  1.00 56.65           C  
ATOM   2352  CG  ARG A 297      -5.188  52.255  27.557  1.00 62.79           C  
ATOM   2353  CD  ARG A 297      -6.473  52.267  28.369  1.00 67.32           C  
ATOM   2354  NE  ARG A 297      -7.032  53.614  28.470  1.00 70.28           N  
ATOM   2355  CZ  ARG A 297      -8.152  53.914  29.120  1.00 71.95           C  
ATOM   2356  NH1 ARG A 297      -8.842  52.961  29.733  1.00 73.47           N  
ATOM   2357  NH2 ARG A 297      -8.583  55.168  29.158  1.00 72.87           N  
ATOM   2358  N   LEU A 298      -1.426  51.872  25.982  1.00 51.29           N  
ATOM   2359  CA  LEU A 298      -0.120  52.396  26.365  1.00 49.56           C  
ATOM   2360  C   LEU A 298      -0.232  53.689  27.169  1.00 49.09           C  
ATOM   2361  O   LEU A 298       0.547  53.923  28.094  1.00 47.51           O  
ATOM   2362  CB  LEU A 298       0.715  52.638  25.105  1.00 48.38           C  
ATOM   2363  CG  LEU A 298       0.816  51.435  24.161  1.00 48.20           C  
ATOM   2364  CD1 LEU A 298       1.375  51.870  22.818  1.00 47.69           C  
ATOM   2365  CD2 LEU A 298       1.689  50.362  24.794  1.00 48.49           C  
TER    2366      LEU A 298                                                      
HETATM 2367  O   HOH A 501      13.242  46.379  21.217  1.00 27.89           O  
HETATM 2368  O   HOH A 502      11.885  47.715  22.906  1.00 32.19           O  
HETATM 2369  O   HOH A 503      15.022  44.446  21.988  1.00 35.55           O  
HETATM 2370  O   HOH A 504      16.509  42.548  20.786  1.00 31.21           O  
HETATM 2371  O   HOH A 505       9.373  48.501  25.540  1.00 44.68           O  
HETATM 2372  O   HOH A 506      13.729  43.646  24.320  1.00 31.98           O  
HETATM 2373  O   HOH A 507      12.326  45.583  25.583  1.00 45.24           O  
HETATM 2374  O   HOH A 508      15.218  42.438  27.809  1.00 41.07           O  
HETATM 2375  O   HOH A 509      13.322  41.739  25.890  1.00 45.83           O  
HETATM 2376  O   HOH A 510      14.905  29.052  23.339  1.00 15.59           O  
HETATM 2377  O   HOH A 511       5.029  28.216  30.371  1.00 12.02           O  
HETATM 2378  O   HOH A 512      13.362  28.422  45.486  1.00 18.83           O  
HETATM 2379  O   HOH A 513      14.439  41.798  11.593  1.00 15.86           O  
HETATM 2380  O   HOH A 514       7.238  53.832  25.713  1.00 24.47           O  
HETATM 2381  O   HOH A 515      -2.551  39.419  15.546  1.00 21.80           O  
HETATM 2382  O   HOH A 516      12.373  20.991  16.329  1.00 20.28           O  
HETATM 2383  O   HOH A 517      19.704  34.681  22.479  1.00 19.83           O  
HETATM 2384  O   HOH A 518      15.164  25.796  25.341  1.00 15.22           O  
HETATM 2385  O   HOH A 519       9.459  18.361  11.644  1.00 22.28           O  
HETATM 2386  O   HOH A 520       0.350  42.547  18.577  1.00 23.96           O  
HETATM 2387  O   HOH A 521       7.941  12.556  23.790  1.00 20.09           O  
HETATM 2388  O   HOH A 522      -6.489  33.767  14.427  1.00 19.17           O  
HETATM 2389  O   HOH A 523      20.573  23.708  32.459  1.00 23.40           O  
HETATM 2390  O   HOH A 524       5.076  34.598  32.570  1.00 35.67           O  
HETATM 2391  O   HOH A 525      15.778  28.126  26.648  1.00 16.63           O  
HETATM 2392  O   HOH A 526       4.978  22.069  36.443  1.00 21.53           O  
HETATM 2393  O   HOH A 527      13.719  18.649  15.511  1.00 20.92           O  
HETATM 2394  O   HOH A 528      12.578  24.778  13.188  1.00 18.59           O  
HETATM 2395  O   HOH A 529     -10.058  36.162  14.077  1.00 28.07           O  
HETATM 2396  O   HOH A 530      13.349  26.691   8.964  1.00 20.93           O  
HETATM 2397  O   HOH A 531      18.506  20.375  20.819  1.00 18.22           O  
HETATM 2398  O   HOH A 532      13.562  29.444  37.036  1.00 18.78           O  
HETATM 2399  O   HOH A 533      17.559  40.803  15.904  1.00 25.18           O  
HETATM 2400  O   HOH A 534      -8.154  24.121  15.067  1.00 34.78           O  
HETATM 2401  O   HOH A 535       8.269  57.803  25.140  1.00 33.54           O  
HETATM 2402  O   HOH A 536      14.870  35.439  32.681  1.00 21.48           O  
HETATM 2403  O   HOH A 537      -7.750  14.280  31.351  1.00 19.54           O  
HETATM 2404  O   HOH A 538      15.930  39.590  17.892  1.00 30.85           O  
HETATM 2405  O   HOH A 539       7.034  13.443  15.840  1.00 40.80           O  
HETATM 2406  O   HOH A 540      -8.325  25.540  20.858  1.00 31.06           O  
HETATM 2407  O   HOH A 541      11.999  24.991  10.698  1.00 19.18           O  
HETATM 2408  O   HOH A 542      17.366  42.436  12.328  1.00 21.67           O  
HETATM 2409  O   HOH A 543       6.938  14.595  25.517  1.00 22.46           O  
HETATM 2410  O   HOH A 544       3.170  36.864  32.331  1.00 28.56           O  
HETATM 2411  O   HOH A 545      12.266  51.623  16.349  1.00 21.19           O  
HETATM 2412  O   HOH A 546      19.475  37.416  43.258  1.00 26.92           O  
HETATM 2413  O   HOH A 547      19.156  45.201  10.527  1.00 26.85           O  
HETATM 2414  O   HOH A 548       7.634  34.411  32.109  1.00 23.19           O  
HETATM 2415  O   HOH A 549      21.362  30.759  41.524  1.00 46.40           O  
HETATM 2416  O   HOH A 550      22.846  31.200  17.337  1.00 29.26           O  
HETATM 2417  O   HOH A 551      33.883  58.419  21.163  1.00 24.21           O  
HETATM 2418  O   HOH A 552      20.016  24.527  40.093  1.00 34.83           O  
HETATM 2419  O   HOH A 553      -8.148  11.724  27.369  1.00 39.14           O  
HETATM 2420  O   HOH A 554       4.546  19.498  36.282  1.00 29.11           O  
HETATM 2421  O   HOH A 555       6.996  26.640  31.497  1.00 17.84           O  
HETATM 2422  O   HOH A 556      13.764  22.480  14.288  1.00 17.06           O  
HETATM 2423  O   HOH A 557      14.231  30.310  27.749  1.00 22.63           O  
HETATM 2424  O   HOH A 558      13.732  23.756  43.968  1.00 22.49           O  
HETATM 2425  O   HOH A 559      17.292  28.457  28.925  1.00 25.07           O  
HETATM 2426  O   HOH A 560      10.973  43.634  12.355  1.00 26.63           O  
HETATM 2427  O   HOH A 561      -9.538  42.445  15.795  1.00 28.72           O  
HETATM 2428  O   HOH A 562       0.056  25.787  32.530  1.00 25.04           O  
HETATM 2429  O   HOH A 563      19.620  35.724  25.145  1.00 26.58           O  
HETATM 2430  O   HOH A 564      -3.658  34.299  28.238  1.00 32.19           O  
HETATM 2431  O   HOH A 565       5.608  25.714   6.480  1.00 25.96           O  
HETATM 2432  O   HOH A 566      16.551  38.923   5.502  1.00 24.62           O  
HETATM 2433  O   HOH A 567      10.332  11.982  22.161  1.00 26.39           O  
HETATM 2434  O   HOH A 568      12.857  40.934   4.947  1.00 26.89           O  
HETATM 2435  O   HOH A 569      15.559  29.392  38.858  1.00 25.25           O  
HETATM 2436  O   HOH A 570       9.447  29.238  40.520  1.00 31.64           O  
HETATM 2437  O   HOH A 571       8.977  44.598   9.095  1.00 33.11           O  
HETATM 2438  O   HOH A 572      -1.366  36.160  11.924  1.00 24.18           O  
HETATM 2439  O   HOH A 573       5.220  35.002  35.218  1.00 33.08           O  
HETATM 2440  O   HOH A 574      -6.159  32.372  27.278  1.00 35.74           O  
HETATM 2441  O   HOH A 575      12.289  31.959  37.438  1.00 29.04           O  
HETATM 2442  O   HOH A 576      17.358  30.491  30.407  1.00 28.24           O  
HETATM 2443  O   HOH A 577     -10.602  37.796  16.417  1.00 28.06           O  
HETATM 2444  O   HOH A 578      19.261  40.099  18.233  1.00 28.00           O  
HETATM 2445  O   HOH A 579     -11.224  33.145  23.098  1.00 44.92           O  
HETATM 2446  O   HOH A 580      21.250  45.369  27.573  1.00 27.89           O  
HETATM 2447  O   HOH A 581      -3.343  12.057  32.524  1.00 45.70           O  
HETATM 2448  O   HOH A 582      22.362  34.021  45.860  1.00 24.64           O  
HETATM 2449  O   HOH A 583      11.409  44.828  10.015  1.00 29.96           O  
HETATM 2450  O   HOH A 584       5.751  42.298  11.622  1.00 27.70           O  
HETATM 2451  O   HOH A 585      19.281  40.842   4.809  1.00 34.30           O  
HETATM 2452  O   HOH A 586      12.073  36.226  32.399  1.00 38.58           O  
HETATM 2453  O   HOH A 587       2.292  31.205  36.269  1.00 33.78           O  
HETATM 2454  O   HOH A 588      13.691  34.474  37.276  1.00 26.12           O  
HETATM 2455  O   HOH A 589      -9.943  13.677  27.988  1.00 31.42           O  
HETATM 2456  O   HOH A 590      -9.210  19.012  27.778  1.00 34.86           O  
HETATM 2457  O   HOH A 591      10.155  61.976  26.911  1.00 49.01           O  
HETATM 2458  O   HOH A 592      23.680  21.885  28.704  1.00 29.57           O  
HETATM 2459  O   HOH A 593       9.027  25.117  42.211  1.00 27.37           O  
HETATM 2460  O   HOH A 594      19.218  30.703  36.091  1.00 26.42           O  
HETATM 2461  O   HOH A 595      -8.462  31.938  14.424  1.00 22.55           O  
HETATM 2462  O   HOH A 596      17.675  28.007  42.273  1.00 32.55           O  
HETATM 2463  O   HOH A 597      23.295  24.999  34.065  1.00 42.76           O  
HETATM 2464  O   HOH A 598      23.658  29.075  25.081  1.00 43.18           O  
HETATM 2465  O   HOH A 599      -4.244  15.484  23.942  1.00 42.49           O  
HETATM 2466  O   HOH A 600      17.359   9.751  19.804  1.00 41.45           O  
HETATM 2467  O   HOH A 601      11.498  30.928  39.762  1.00 19.95           O  
HETATM 2468  O   HOH A 602       0.065  37.860  10.320  1.00 27.56           O  
HETATM 2469  O   HOH A 604      -9.264  44.458  19.406  1.00 35.51           O  
HETATM 2470  O   HOH A 606      22.882  65.763  16.406  1.00 46.23           O  
HETATM 2471  O   HOH A 607      17.784   4.086  33.749  1.00 34.71           O  
HETATM 2472  O   HOH A 608      -9.060  38.020  18.975  1.00 24.77           O  
HETATM 2473  O   HOH A 609      11.164  17.443  13.360  1.00 35.97           O  
HETATM 2474  O   HOH A 610      -7.768  13.260  24.754  1.00 51.99           O  
HETATM 2475  O   HOH A 611      -2.633  29.361  39.000  1.00 37.71           O  
HETATM 2476  O   HOH A 612      -8.568  13.278  22.192  1.00 39.82           O  
HETATM 2477  O   HOH A 613      20.446  42.477  27.546  1.00 31.78           O  
HETATM 2478  O   HOH A 614      10.195  61.271  24.334  1.00 40.03           O  
HETATM 2479  O   HOH A 616      23.017  24.553  31.136  1.00 37.60           O  
HETATM 2480  O   HOH A 617     -10.822  32.926  14.127  1.00 42.19           O  
HETATM 2481  O   HOH A 618      11.400  62.128  15.669  1.00 42.52           O  
HETATM 2482  O   HOH A 619      12.773  38.147   5.664  1.00 21.09           O  
HETATM 2483  O   HOH A 620       3.467  45.532  12.538  1.00 38.99           O  
HETATM 2484  O   HOH A 621      16.594  54.689  13.446  1.00 46.99           O  
HETATM 2485  O   HOH A 622      21.924  41.138   3.648  1.00 44.16           O  
HETATM 2486  O   HOH A 624      18.227  40.101  13.415  1.00 26.79           O  
HETATM 2487  O   HOH A 625      22.124  31.983  20.063  1.00 29.06           O  
HETATM 2488  O   HOH A 626      15.491  36.942  40.488  1.00 37.98           O  
HETATM 2489  O   HOH A 627       5.288  49.194  19.392  1.00 36.89           O  
HETATM 2490  O   HOH A 628     -11.022  29.061  23.716  1.00 41.74           O  
HETATM 2491  O   HOH A 629       6.480  46.288  12.193  1.00 41.45           O  
HETATM 2492  O   HOH A 630      20.756  45.953   8.543  1.00 44.41           O  
HETATM 2493  O   HOH A 631      23.298  45.017   7.559  1.00 36.45           O  
HETATM 2494  O   HOH A 632      -7.669  40.344  20.291  1.00 33.93           O  
HETATM 2495  O   HOH A 633     -12.399  29.842  13.112  1.00 50.02           O  
HETATM 2496  O   HOH A 634      -0.647  33.669  31.135  1.00 40.61           O  
HETATM 2497  O   HOH A 635      28.424  60.387  15.547  1.00 31.48           O  
HETATM 2498  O   HOH A 637      -8.885  30.609  17.048  1.00 34.78           O  
HETATM 2499  O   HOH A 639      -6.969  40.867  33.195  1.00 42.03           O  
HETATM 2500  O   HOH A 640      -7.955  39.763  27.484  1.00 30.26           O  
HETATM 2501  O   HOH A 641       4.556  15.078  23.456  1.00 25.93           O  
HETATM 2502  O   HOH A 642      26.746  16.389  25.168  1.00 37.27           O  
HETATM 2503  O   HOH A 643      22.406  30.271  43.913  1.00 48.40           O  
HETATM 2504  O   HOH A 644      22.889  20.447  32.307  1.00 40.32           O  
HETATM 2505  O   HOH A 645      13.969   6.519  32.636  1.00 34.65           O  
HETATM 2506  O   HOH A 646      24.966  16.087  37.389  1.00 33.67           O  
HETATM 2507  O   HOH A 648      25.599  37.780  34.486  1.00 31.28           O  
HETATM 2508  O   HOH A 649      19.104  29.800  40.969  1.00 39.05           O  
HETATM 2509  O   HOH A 650      -5.959  20.286  34.966  1.00 30.84           O  
HETATM 2510  O   HOH A 651       2.895  50.468  16.043  1.00 42.49           O  
HETATM 2511  O   HOH A 652      -8.507  29.500  24.108  1.00 42.82           O  
HETATM 2512  O   HOH A 653       1.471  33.646  32.741  1.00 36.25           O  
HETATM 2513  O   HOH A 654      12.596  22.369   8.567  1.00 38.93           O  
HETATM 2514  O   HOH A 655      -3.004  29.017   7.364  1.00 42.49           O  
HETATM 2515  O   HOH A 656      -6.435  41.499   9.455  1.00 50.36           O  
HETATM 2516  O   HOH A 657      14.830   7.295  42.672  1.00 38.90           O  
HETATM 2517  O   HOH A 658      36.785  43.158  18.507  1.00 37.36           O  
HETATM 2518  O   HOH A 659      16.488  38.031  25.958  1.00 31.99           O  
HETATM 2519  O   HOH A 660       8.717   8.184  29.345  1.00 45.86           O  
HETATM 2520  O   HOH A 661      27.362  14.744  38.069  1.00 60.61           O  
HETATM 2521  O   HOH A 662      11.060  18.798  42.408  1.00 40.76           O  
HETATM 2522  O   HOH A 664      19.555   2.607  30.309  1.00 38.73           O  
HETATM 2523  O   HOH A 665      33.028  60.126  23.328  1.00 39.75           O  
HETATM 2524  O   HOH A 666      14.648   4.011  31.879  1.00 37.80           O  
HETATM 2525  O   HOH A 667      23.666  50.463  34.751  1.00 57.98           O  
HETATM 2526  O   HOH A 668      16.632  23.190  11.934  1.00 31.27           O  
HETATM 2527  O   HOH A 670      -1.167  45.726  28.198  1.00 38.34           O  
HETATM 2528  O   HOH A 671     -11.158  32.459  11.607  1.00 42.46           O  
HETATM 2529  O   HOH A 672      28.393  13.487  33.999  1.00 33.29           O  
HETATM 2530  O   HOH A 675       2.281  44.135  10.724  1.00 45.96           O  
HETATM 2531  O   HOH A 677      -9.895  40.859  25.558  1.00 49.71           O  
HETATM 2532  O   HOH A 678      -7.723  29.681  26.860  1.00 38.58           O  
HETATM 2533  O   HOH A 679     -11.582  30.783  18.551  1.00 51.19           O  
HETATM 2534  O   HOH A 680      20.506  18.781  21.291  1.00 29.37           O  
HETATM 2535  O   HOH A 681      27.393  18.264  32.806  1.00 48.60           O  
HETATM 2536  O   HOH A 682      15.028  64.722  19.127  1.00 61.39           O  
HETATM 2537  O   HOH A 683      12.532  62.345  23.448  1.00 59.60           O  
HETATM 2538  O   HOH A 684       1.932  27.016   6.195  1.00 48.59           O  
HETATM 2539  O   HOH A 685      14.847  39.414  28.271  1.00 35.38           O  
HETATM 2540  O   HOH A 686      -2.181  34.803   7.432  1.00 46.27           O  
HETATM 2541  O   HOH A 687      -2.221  31.608   6.602  1.00 43.57           O  
HETATM 2542  O   HOH A 688      29.737  19.592  33.237  1.00 46.74           O  
HETATM 2543  O   HOH A 689       3.717  22.840   3.250  1.00 46.04           O  
HETATM 2544  O   HOH A 691      37.834  40.080  26.108  1.00 48.79           O  
HETATM 2545  O   HOH A 692      35.941  36.141  10.027  1.00 44.39           O  
HETATM 2546  O   HOH A 694      13.062  51.359  13.768  1.00 46.21           O  
HETATM 2547  O   HOH A 695      -0.873  47.171  30.573  1.00 40.54           O  
HETATM 2548  O   HOH A 696      23.788  36.973   8.389  1.00 41.00           O  
HETATM 2549  O   HOH A 697       3.202   8.813  37.798  1.00 42.80           O  
HETATM 2550  O   HOH A 698      -2.769  55.557  25.832  1.00 36.87           O  
HETATM 2551  O   HOH A 700      11.790  47.368  10.103  1.00 42.50           O  
HETATM 2552  O   HOH A 701      19.082  60.171   8.249  1.00 47.22           O  
HETATM 2553  O   HOH A 702       3.960  12.708  41.860  1.00 45.13           O  
HETATM 2554  O   HOH A 703      -2.656  53.505  23.924  1.00 31.78           O  
HETATM 2555  O   HOH A 705      -2.478  13.891  25.634  1.00 38.80           O  
HETATM 2556  O   HOH A 706       4.929  51.989  25.708  1.00 41.71           O  
HETATM 2557  O   HOH A 707      23.177  28.010  30.061  1.00 42.97           O  
HETATM 2558  O   HOH A 708       7.315  35.601  36.510  1.00 52.55           O  
HETATM 2559  O   HOH A 710      14.661  20.932  12.243  1.00 37.91           O  
HETATM 2560  O   HOH A 712       0.725   7.183  37.447  1.00 56.25           O  
HETATM 2561  O   HOH A 713       9.337  48.853  30.459  1.00 38.07           O  
HETATM 2562  O   HOH A 715       1.050  46.390   8.851  1.00 45.00           O  
HETATM 2563  O   HOH A 716      -3.600  21.738   6.733  1.00 47.67           O  
HETATM 2564  O   HOH A 717       6.657  56.430  31.163  1.00 47.41           O  
HETATM 2565  O   HOH A 718      14.859  29.683  43.469  1.00 14.89           O  
HETATM 2566  O   HOH A 719      10.898  23.922  30.230  1.00 13.49           O  
HETATM 2567  O   HOH A 720      13.814  29.471  30.313  1.00 15.50           O  
HETATM 2568  O   HOH A 721       9.180  31.868   7.974  1.00 30.44           O  
HETATM 2569  O   HOH A 722     -10.551  54.985  26.973  1.00 40.35           O  
HETATM 2570  O   HOH A 723      23.995  33.746  16.549  1.00 31.97           O  
HETATM 2571  O   HOH A 724       2.810  11.955  36.703  1.00 34.65           O  
HETATM 2572  O   HOH A 725      17.554  18.165  16.479  1.00 39.23           O  
HETATM 2573  O   HOH A 727      25.171  11.508  34.993  1.00 41.03           O  
HETATM 2574  O   HOH A 728      -3.009  35.605  30.560  1.00 37.29           O  
HETATM 2575  O   HOH A 729      20.422  16.430  22.814  1.00 39.87           O  
HETATM 2576  O   HOH A 730      24.592  39.575  32.592  1.00 50.46           O  
HETATM 2577  O   HOH A 731      18.760  29.378  38.348  1.00 33.32           O  
HETATM 2578  O   HOH A 732      -4.662  37.194   8.088  1.00 39.65           O  
HETATM 2579  O   HOH A 733      -3.297   9.561  33.165  1.00 36.40           O  
HETATM 2580  O   HOH A 734      -6.793  41.252  23.209  1.00 34.97           O  
HETATM 2581  O   HOH A 735       1.871  14.567  43.618  1.00 51.30           O  
HETATM 2582  O   HOH A 736      18.293  13.088  20.598  1.00 41.75           O  
HETATM 2583  O   HOH A 737       6.239  34.470  39.475  1.00 46.30           O  
HETATM 2584  O   HOH A 738     -10.322  28.133  16.335  1.00 45.65           O  
HETATM 2585  O   HOH A 739      -3.310  24.712   6.783  1.00 46.79           O  
HETATM 2586  O   HOH A 740       8.168  42.409  31.374  1.00 45.10           O  
HETATM 2587  O   HOH A 741      25.895  30.041  28.181  1.00 48.85           O  
HETATM 2588  O   HOH A 742      -9.375  21.086  26.032  1.00 35.34           O  
HETATM 2589  O   HOH A 743      27.622  19.174  29.601  1.00 41.88           O  
HETATM 2590  O   HOH A 744      18.911  53.598  12.305  1.00 35.49           O  
HETATM 2591  O   HOH A 745      12.547   3.979  20.336  1.00 37.47           O  
HETATM 2592  O   HOH A 746      20.044  10.801  22.140  1.00 43.76           O  
HETATM 2593  O   HOH A 747      -6.796  38.359   9.430  1.00 40.09           O  
HETATM 2594  O   HOH A 748       7.087  10.012  28.260  1.00 40.01           O  
HETATM 2595  O   HOH A 749       9.856  35.963  30.583  1.00 25.44           O  
HETATM 2596  O   HOH A 750      19.521  64.903  10.678  1.00 47.39           O  
HETATM 2597  O   HOH A 751       4.004  52.033  28.070  1.00 43.21           O  
HETATM 2598  O   HOH A 752     -11.850  33.810  32.198  1.00 46.73           O  
HETATM 2599  O   HOH A 753      33.885  51.133  15.633  1.00 44.12           O  
HETATM 2600  O   HOH A 754      -9.198  41.894  32.190  1.00 45.98           O  
MASTER      313    0    0   13    8    0    0    6 2599    1    0   23          
END                                                                             
