CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 04-JUL-03 1PXL  ***

elNémo ID: 21120614403920577

Job options:

ID        	=	 21120614403920577
JOBID     	=	 TRANSFERASE 04-JUL-03 1PXL
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             04-JUL-03   1PXL              
TITLE     HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                    
TITLE    2 INHIBITOR [4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-            
TITLE    3 (4-TRIFLUOROMETHYL-PHENYL)-AMINE                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HUMAN CYCLIN-DEPENDENT KINASE 2;                           
COMPND   5 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   6 EC: 2.7.1.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 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,           
KEYWDS   2 MITOSIS, INHIBITION, TRANSFERASE, SERINE/THREONINE-PROTEIN           
KEYWDS   3 KINASE, ATP-BINDING, 3D-STRUCTURE.                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.Y.WU,I.MCNAE,G.KONTOPIDIS,S.J.MCCLUE,C.MCINNES,                     
AUTHOR   2 K.J.STEWART,S.WANG,D.I.ZHELEVA,H.MARRIAGE,D.P.LANE,P.TAYLOR,         
AUTHOR   3 P.M.FISCHER,M.D.WALKINSHAW                                           
REVDAT   2   24-FEB-09 1PXL    1       VERSN                                    
REVDAT   1   09-DEC-03 1PXL    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,          
JRNL        AUTH 3 P.TAYLOR,P.M.FISCHER,M.D.WALKINSHAW                          
JRNL        TITL   DISCOVERY OF A NOVEL FAMILY OF CDK INHIBITORS WITH           
JRNL        TITL 2 THE PROGRAM LIDAEUS: STRUCTURAL BASIS FOR                    
JRNL        TITL 3 LIGAND-INDUCED 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   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1092231.390                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 9360                           
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) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 501                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1470                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 83                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2338                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 35                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.00000                                             
REMARK   3    B22 (A**2) : -5.71000                                             
REMARK   3    B33 (A**2) : 6.71000                                              
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) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
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) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.790 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.160 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.180 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 56.24                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : FRA_PAR.TXT                                    
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : FRA_TOP.TXT                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 36 - 43 ARE NOT VISIBLE IN       
REMARK   3  THE ELECTRON DENSITY MAP                                            
REMARK   4                                                                      
REMARK   4 1PXL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019672.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX9.6                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9360                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
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   (%): 37.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
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       26.35450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.21450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.78750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.21450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.35450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.78750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLU A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A   8      145.59   -175.48                                   
REMARK 500    LYS A   9       94.81    -68.45                                   
REMARK 500    GLU A  12       68.97   -161.26                                   
REMARK 500    ASN A  23      104.95    -54.55                                   
REMARK 500    LEU A  25      -83.11    -91.78                                   
REMARK 500    GLU A  73       61.96     34.49                                   
REMARK 500    ARG A 126      -14.31     75.31                                   
REMARK 500    ASP A 127       46.60   -147.75                                   
REMARK 500    PHE A 152      -95.78   -133.69                                   
REMARK 500    VAL A 154       86.67   -162.86                                   
REMARK 500    ARG A 157     -152.77   -134.96                                   
REMARK 500    THR A 158     -170.27   -175.31                                   
REMARK 500    THR A 160        3.91    -59.03                                   
REMARK 500    TYR A 179       56.39   -112.28                                   
REMARK 500    SER A 181     -168.24   -113.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CK4 A 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AQ1   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 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                   
REMARK 900 INHIBITOR PURVALANOL B                                               
REMARK 900 RELATED ID: 1DI8   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CYCLIN-DEPENDENT KINASE 2 (CDK2) IN                 
REMARK 900 COMPLEX WITH 4-[3-HYDROXYANILINO]-6,7-DIMETHOXYQUINAZOLINE           
REMARK 900 RELATED ID: 1DM2   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN-DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR HYMENIALDISINE                                             
REMARK 900 RELATED ID: 1E1V   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 2058                                                       
REMARK 900 RELATED ID: 1E1X   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 6027                                                       
REMARK 900 RELATED ID: 1E9H   RELATED DB: PDB                                   
REMARK 900 THR 160 PHOSPHORYLATED CDK2 - HUMAN CYCLIN A3 COMPLEX WITH           
REMARK 900 THE 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                 
REMARK 900 COMPLEX WITH AN OXINDOLE INHIBITOR                                   
REMARK 900 RELATED ID: 1FVV   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF CDK2/CYCLIN A IN COMPLEX WITH AN OXINDOLE           
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 1G5S   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLIN DEPENDENT KINASE 2 (CDK2)          
REMARK 900 IN COMPLEX WITH THE INHIBITOR H717                                   
REMARK 900 RELATED ID: 1GIH   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4              
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 1GII   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4              
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 1GIJ   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE CDK4              
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 1GZ8   RELATED DB: PDB                                   
REMARK 900 HUMAN CYCLIN DEPENDENT KINASE 2 COMPLEXED WITH THE                   
REMARK 900 INHIBITOR 2-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                 
REMARK 900 COMPLEX WITH 4-[(6-AMINO-4-PYRIMIDINYL) AMINO]                       
REMARK 900 BENZENESULFONAMIDE                                                   
REMARK 900 RELATED ID: 1JVP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CDK2 (UNPHOSPHORYLATED) IN                
REMARK 900 COMPLEX WITH PKF049-365                                              
REMARK 900 RELATED ID: 1KE5   RELATED DB: PDB                                   
REMARK 900 CDK2 COMPLEXED WITH N-METHYL-4-{[(2-OXO-1,2-DIHYDRO-3H-              
REMARK 900 INDOL-3-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDE                      
REMARK 900 RELATED ID: 1KE6   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH N-METHYL-{           
REMARK 900 4-[2-(7-OXO-6,7-DIHYDRO-8H-[1,3]THIAZOLO[5,4-E]INDOL-8-              
REMARK 900 YLIDENE)HYDRAZINO]PHENYL}METHANESULFONAMIDE                          
REMARK 900 RELATED ID: 1KE7   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 3-{[(2,2-            
REMARK 900 DIOXIDO-1,3-DIHYDRO-2-BENZOTHIEN-5-YL)AMINO]METHYLENE}-5-            
REMARK 900 (1,3-OXAZOL-5-YL)-1,3-DIHYDRO-2H-INDOL-2-ONE                         
REMARK 900 RELATED ID: 1KE8   RELATED DB: PDB                                   
REMARK 900 CYCLIN-DEPENDENT KINASE 2 (CDK2) COMPLEXED WITH 4-{[(2-OXO-          
REMARK 900 1,2-DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]AMINO}-N-(1,3-THIAZOL          
REMARK 900 -2-YL)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-          
REMARK 900 2,3-DIHYDRO-1H-INDOLE                                                
DBREF  1PXL A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
HET    CK4  A 500      24                                                       
HETNAM     CK4 4-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-N-[4-                          
HETNAM   2 CK4  (TRIFLUOROMETHYL)PHENYL]PYRIMIDIN-2-AMINE                       
HETSYN     CK4 4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(4-                
HETSYN   2 CK4  TRIFLUOROMETHYL-PHENYL)-AMINE                                   
FORMUL   2  CK4    C16 H13 F3 N4 S                                              
FORMUL   3  HOH   *35(H2 O)                                                     
HELIX    1   1 PRO A   45  LEU A   55  1                                  11    
HELIX    2   2 LYS A   56  LEU A   58  5                                   3    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
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  251  5                                   5    
HELIX   11  11 ASP A  256  LEU A  267  1                                  12    
HELIX   12  12 SER A  276  LEU A  281  1                                   6    
HELIX   13  13 ALA A  282  GLN A  287  5                                   6    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
SHEET    3   A 5 VAL A  29  LYS A  34 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  THR A  72 -1  N  ILE A  70   O  TYR A  77           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
CISPEP   1 PRO A  253    PRO A  254          0         0.27                     
SITE     1 AC1 22 ILE A  10  ALA A  31  LYS A  33  PHE A  80                    
SITE     2 AC1 22 GLU A  81  PHE A  82  LEU A  83  HIS A  84                    
SITE     3 AC1 22 GLN A  85  ASP A  86  LYS A  89  LEU A 134                    
SITE     4 AC1 22 ASP A 145  HOH A 501  HOH A 502  HOH A 503                    
SITE     5 AC1 22 HOH A 504  HOH A 505  HOH A 506  HOH A 507                    
SITE     6 AC1 22 HOH A 508  HOH A 509                                          
CRYST1   52.709   71.575   70.429  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      0.018972  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013971  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014199        0.00000                         
ATOM      1  N   MET A   1      27.913  56.743  20.408  1.00 73.52           N  
ATOM      2  CA  MET A   1      26.862  56.487  21.430  1.00 73.28           C  
ATOM      3  C   MET A   1      26.225  57.786  21.909  1.00 72.77           C  
ATOM      4  O   MET A   1      25.093  57.786  22.387  1.00 72.63           O  
ATOM      5  CB  MET A   1      27.461  55.730  22.618  1.00 75.43           C  
ATOM      6  CG  MET A   1      26.465  55.359  23.716  1.00 77.35           C  
ATOM      7  SD  MET A   1      25.972  56.733  24.792  1.00 81.14           S  
ATOM      8  CE  MET A   1      27.178  56.601  26.120  1.00 79.26           C  
ATOM      9  N   GLU A   2      26.948  58.896  21.783  1.00 72.02           N  
ATOM     10  CA  GLU A   2      26.418  60.191  22.205  1.00 69.69           C  
ATOM     11  C   GLU A   2      25.388  60.669  21.188  1.00 68.19           C  
ATOM     12  O   GLU A   2      25.042  61.848  21.136  1.00 68.10           O  
ATOM     13  CB  GLU A   2      27.545  61.228  22.332  1.00 70.76           C  
ATOM     14  CG  GLU A   2      28.017  61.886  21.028  1.00 71.70           C  
ATOM     15  CD  GLU A   2      28.814  60.957  20.124  1.00 73.48           C  
ATOM     16  OE1 GLU A   2      29.648  60.184  20.650  1.00 74.09           O  
ATOM     17  OE2 GLU A   2      28.621  61.017  18.886  1.00 72.00           O  
ATOM     18  N   ASN A   3      24.901  59.731  20.383  1.00 66.60           N  
ATOM     19  CA  ASN A   3      23.917  60.025  19.350  1.00 64.46           C  
ATOM     20  C   ASN A   3      22.509  59.726  19.846  1.00 63.35           C  
ATOM     21  O   ASN A   3      21.530  60.028  19.169  1.00 63.29           O  
ATOM     22  CB  ASN A   3      24.200  59.175  18.110  1.00 63.22           C  
ATOM     23  CG  ASN A   3      25.685  59.034  17.823  1.00 62.05           C  
ATOM     24  OD1 ASN A   3      26.424  58.392  18.580  1.00 60.28           O  
ATOM     25  ND2 ASN A   3      26.132  59.636  16.726  1.00 59.95           N  
ATOM     26  N   PHE A   4      22.414  59.137  21.034  1.00 61.91           N  
ATOM     27  CA  PHE A   4      21.125  58.770  21.605  1.00 61.26           C  
ATOM     28  C   PHE A   4      20.849  59.408  22.955  1.00 62.35           C  
ATOM     29  O   PHE A   4      21.768  59.685  23.726  1.00 63.69           O  
ATOM     30  CB  PHE A   4      21.048  57.254  21.748  1.00 58.86           C  
ATOM     31  CG  PHE A   4      21.216  56.521  20.455  1.00 57.56           C  
ATOM     32  CD1 PHE A   4      20.165  56.436  19.549  1.00 56.33           C  
ATOM     33  CD2 PHE A   4      22.437  55.937  20.127  1.00 56.09           C  
ATOM     34  CE1 PHE A   4      20.324  55.781  18.332  1.00 56.35           C  
ATOM     35  CE2 PHE A   4      22.608  55.280  18.914  1.00 55.90           C  
ATOM     36  CZ  PHE A   4      21.550  55.200  18.013  1.00 56.16           C  
ATOM     37  N   GLN A   5      19.570  59.631  23.237  1.00 62.83           N  
ATOM     38  CA  GLN A   5      19.152  60.219  24.498  1.00 62.95           C  
ATOM     39  C   GLN A   5      18.261  59.222  25.231  1.00 62.42           C  
ATOM     40  O   GLN A   5      17.092  59.067  24.895  1.00 62.50           O  
ATOM     41  CB  GLN A   5      18.392  61.525  24.244  1.00 64.24           C  
ATOM     42  CG  GLN A   5      18.015  62.282  25.507  1.00 66.67           C  
ATOM     43  CD  GLN A   5      19.227  62.748  26.314  1.00 68.43           C  
ATOM     44  OE1 GLN A   5      19.078  63.350  27.381  1.00 68.24           O  
ATOM     45  NE2 GLN A   5      20.429  62.474  25.806  1.00 67.90           N  
ATOM     46  N   LYS A   6      18.828  58.540  26.221  1.00 62.53           N  
ATOM     47  CA  LYS A   6      18.094  57.550  27.004  1.00 63.18           C  
ATOM     48  C   LYS A   6      16.737  58.123  27.406  1.00 63.63           C  
ATOM     49  O   LYS A   6      16.625  59.314  27.687  1.00 63.87           O  
ATOM     50  CB  LYS A   6      18.897  57.170  28.256  1.00 64.40           C  
ATOM     51  CG  LYS A   6      20.347  56.749  27.977  1.00 66.13           C  
ATOM     52  CD  LYS A   6      21.109  56.446  29.271  1.00 67.18           C  
ATOM     53  CE  LYS A   6      22.633  56.406  29.067  1.00 67.75           C  
ATOM     54  NZ  LYS A   6      23.111  55.300  28.187  1.00 68.42           N  
ATOM     55  N   VAL A   7      15.705  57.281  27.420  1.00 64.38           N  
ATOM     56  CA  VAL A   7      14.361  57.726  27.783  1.00 64.45           C  
ATOM     57  C   VAL A   7      13.781  56.990  28.988  1.00 65.56           C  
ATOM     58  O   VAL A   7      13.100  57.598  29.812  1.00 65.58           O  
ATOM     59  CB  VAL A   7      13.381  57.594  26.584  1.00 63.90           C  
ATOM     60  CG1 VAL A   7      11.940  57.762  27.050  1.00 61.55           C  
ATOM     61  CG2 VAL A   7      13.707  58.651  25.541  1.00 62.42           C  
ATOM     62  N   GLU A   8      14.042  55.689  29.092  1.00 66.74           N  
ATOM     63  CA  GLU A   8      13.537  54.906  30.219  1.00 68.26           C  
ATOM     64  C   GLU A   8      14.043  53.475  30.196  1.00 69.51           C  
ATOM     65  O   GLU A   8      14.219  52.889  29.128  1.00 69.58           O  
ATOM     66  CB  GLU A   8      12.003  54.892  30.229  1.00 68.61           C  
ATOM     67  CG  GLU A   8      11.364  54.247  29.011  1.00 69.15           C  
ATOM     68  CD  GLU A   8       9.867  54.051  29.176  1.00 70.04           C  
ATOM     69  OE1 GLU A   8       9.461  53.261  30.057  1.00 70.24           O  
ATOM     70  OE2 GLU A   8       9.096  54.688  28.427  1.00 71.93           O  
ATOM     71  N   LYS A   9      14.273  52.913  31.379  1.00 70.94           N  
ATOM     72  CA  LYS A   9      14.752  51.542  31.481  1.00 72.30           C  
ATOM     73  C   LYS A   9      13.629  50.625  31.020  1.00 72.82           C  
ATOM     74  O   LYS A   9      12.744  50.268  31.791  1.00 72.92           O  
ATOM     75  CB  LYS A   9      15.139  51.207  32.924  1.00 72.55           C  
ATOM     76  CG  LYS A   9      16.068  50.004  33.039  1.00 74.18           C  
ATOM     77  CD  LYS A   9      16.239  49.537  34.479  1.00 74.77           C  
ATOM     78  CE  LYS A   9      14.973  48.862  34.994  1.00 75.12           C  
ATOM     79  NZ  LYS A   9      15.163  48.248  36.339  1.00 72.74           N  
ATOM     80  N   ILE A  10      13.669  50.257  29.748  1.00 74.26           N  
ATOM     81  CA  ILE A  10      12.657  49.389  29.162  1.00 76.63           C  
ATOM     82  C   ILE A  10      12.735  47.945  29.655  1.00 77.35           C  
ATOM     83  O   ILE A  10      11.717  47.254  29.731  1.00 78.33           O  
ATOM     84  CB  ILE A  10      12.763  49.412  27.619  1.00 76.74           C  
ATOM     85  CG1 ILE A  10      12.229  50.741  27.089  1.00 77.92           C  
ATOM     86  CG2 ILE A  10      12.010  48.250  27.012  1.00 76.86           C  
ATOM     87  CD1 ILE A  10      10.789  51.028  27.477  1.00 78.77           C  
ATOM     88  N   GLY A  11      13.939  47.491  29.992  1.00 78.60           N  
ATOM     89  CA  GLY A  11      14.098  46.127  30.458  1.00 79.07           C  
ATOM     90  C   GLY A  11      15.378  45.880  31.229  1.00 79.52           C  
ATOM     91  O   GLY A  11      16.050  46.817  31.656  1.00 79.23           O  
ATOM     92  N   GLU A  12      15.711  44.604  31.402  1.00 80.98           N  
ATOM     93  CA  GLU A  12      16.906  44.197  32.134  1.00 82.03           C  
ATOM     94  C   GLU A  12      17.242  42.749  31.754  1.00 82.80           C  
ATOM     95  O   GLU A  12      17.110  41.839  32.571  1.00 82.74           O  
ATOM     96  CB  GLU A  12      16.643  44.292  33.641  1.00 82.18           C  
ATOM     97  CG  GLU A  12      17.878  44.482  34.506  1.00 84.45           C  
ATOM     98  CD  GLU A  12      18.344  45.929  34.557  1.00 85.58           C  
ATOM     99  OE1 GLU A  12      17.542  46.798  34.963  1.00 85.23           O  
ATOM    100  OE2 GLU A  12      19.512  46.196  34.195  1.00 86.01           O  
ATOM    101  N   GLY A  13      17.671  42.543  30.510  1.00 83.73           N  
ATOM    102  CA  GLY A  13      18.007  41.207  30.041  1.00 83.77           C  
ATOM    103  C   GLY A  13      19.211  40.563  30.710  1.00 83.88           C  
ATOM    104  O   GLY A  13      19.806  41.126  31.630  1.00 84.10           O  
ATOM    105  N   THR A  14      19.569  39.369  30.245  1.00 83.72           N  
ATOM    106  CA  THR A  14      20.705  38.633  30.793  1.00 84.03           C  
ATOM    107  C   THR A  14      22.032  39.173  30.267  1.00 83.72           C  
ATOM    108  O   THR A  14      23.062  39.090  30.939  1.00 83.61           O  
ATOM    109  CB  THR A  14      20.608  37.128  30.453  1.00 84.45           C  
ATOM    110  OG1 THR A  14      20.175  36.971  29.095  1.00 83.88           O  
ATOM    111  CG2 THR A  14      19.631  36.426  31.387  1.00 85.32           C  
ATOM    112  N   TYR A  15      21.998  39.726  29.060  1.00 83.16           N  
ATOM    113  CA  TYR A  15      23.189  40.287  28.436  1.00 82.01           C  
ATOM    114  C   TYR A  15      23.473  41.650  29.055  1.00 80.00           C  
ATOM    115  O   TYR A  15      24.628  42.015  29.281  1.00 81.44           O  
ATOM    116  CB  TYR A  15      22.964  40.445  26.933  1.00 84.04           C  
ATOM    117  CG  TYR A  15      22.359  39.225  26.281  1.00 85.72           C  
ATOM    118  CD1 TYR A  15      23.086  38.043  26.149  1.00 86.12           C  
ATOM    119  CD2 TYR A  15      21.047  39.248  25.813  1.00 86.25           C  
ATOM    120  CE1 TYR A  15      22.516  36.909  25.566  1.00 87.69           C  
ATOM    121  CE2 TYR A  15      20.468  38.124  25.232  1.00 88.16           C  
ATOM    122  CZ  TYR A  15      21.205  36.957  25.110  1.00 88.33           C  
ATOM    123  OH  TYR A  15      20.621  35.843  24.544  1.00 88.31           O  
ATOM    124  N   GLY A  16      22.407  42.398  29.324  1.00 76.68           N  
ATOM    125  CA  GLY A  16      22.556  43.715  29.914  1.00 73.31           C  
ATOM    126  C   GLY A  16      21.237  44.447  30.061  1.00 70.66           C  
ATOM    127  O   GLY A  16      20.173  43.881  29.817  1.00 70.21           O  
ATOM    128  N   VAL A  17      21.305  45.711  30.461  1.00 68.25           N  
ATOM    129  CA  VAL A  17      20.105  46.512  30.636  1.00 66.65           C  
ATOM    130  C   VAL A  17      19.651  47.071  29.285  1.00 65.80           C  
ATOM    131  O   VAL A  17      20.469  47.275  28.386  1.00 65.24           O  
ATOM    132  CB  VAL A  17      20.358  47.670  31.626  1.00 66.39           C  
ATOM    133  CG1 VAL A  17      21.454  48.577  31.095  1.00 66.67           C  
ATOM    134  CG2 VAL A  17      19.072  48.446  31.868  1.00 65.85           C  
ATOM    135  N   VAL A  18      18.342  47.300  29.148  1.00 64.05           N  
ATOM    136  CA  VAL A  18      17.761  47.827  27.912  1.00 60.89           C  
ATOM    137  C   VAL A  18      17.055  49.157  28.137  1.00 59.11           C  
ATOM    138  O   VAL A  18      16.227  49.290  29.035  1.00 58.03           O  
ATOM    139  CB  VAL A  18      16.731  46.860  27.313  1.00 60.05           C  
ATOM    140  CG1 VAL A  18      16.321  47.339  25.926  1.00 59.11           C  
ATOM    141  CG2 VAL A  18      17.303  45.457  27.259  1.00 61.13           C  
ATOM    142  N   TYR A  19      17.380  50.138  27.305  1.00 58.14           N  
ATOM    143  CA  TYR A  19      16.776  51.456  27.418  1.00 56.73           C  
ATOM    144  C   TYR A  19      16.037  51.843  26.144  1.00 55.50           C  
ATOM    145  O   TYR A  19      16.335  51.342  25.060  1.00 53.94           O  
ATOM    146  CB  TYR A  19      17.848  52.517  27.682  1.00 58.42           C  
ATOM    147  CG  TYR A  19      18.517  52.464  29.035  1.00 60.97           C  
ATOM    148  CD1 TYR A  19      17.800  52.715  30.203  1.00 62.68           C  
ATOM    149  CD2 TYR A  19      19.881  52.198  29.144  1.00 62.83           C  
ATOM    150  CE1 TYR A  19      18.427  52.707  31.453  1.00 64.86           C  
ATOM    151  CE2 TYR A  19      20.519  52.187  30.383  1.00 65.01           C  
ATOM    152  CZ  TYR A  19      19.789  52.442  31.533  1.00 65.73           C  
ATOM    153  OH  TYR A  19      20.429  52.439  32.755  1.00 67.21           O  
ATOM    154  N   LYS A  20      15.063  52.735  26.294  1.00 54.06           N  
ATOM    155  CA  LYS A  20      14.318  53.255  25.163  1.00 53.77           C  
ATOM    156  C   LYS A  20      15.119  54.502  24.821  1.00 54.72           C  
ATOM    157  O   LYS A  20      15.374  55.326  25.701  1.00 54.60           O  
ATOM    158  CB  LYS A  20      12.904  53.648  25.577  1.00 52.92           C  
ATOM    159  CG  LYS A  20      12.080  54.242  24.443  1.00 52.17           C  
ATOM    160  CD  LYS A  20      10.628  54.375  24.851  1.00 50.64           C  
ATOM    161  CE  LYS A  20       9.755  54.718  23.672  1.00 47.95           C  
ATOM    162  NZ  LYS A  20       8.328  54.667  24.056  1.00 49.56           N  
ATOM    163  N   ALA A  21      15.529  54.642  23.564  1.00 55.80           N  
ATOM    164  CA  ALA A  21      16.332  55.793  23.173  1.00 58.23           C  
ATOM    165  C   ALA A  21      15.827  56.539  21.943  1.00 59.85           C  
ATOM    166  O   ALA A  21      15.084  55.996  21.123  1.00 58.35           O  
ATOM    167  CB  ALA A  21      17.784  55.361  22.963  1.00 56.48           C  
ATOM    168  N   ARG A  22      16.257  57.793  21.824  1.00 63.13           N  
ATOM    169  CA  ARG A  22      15.863  58.651  20.714  1.00 66.92           C  
ATOM    170  C   ARG A  22      17.085  59.118  19.931  1.00 67.13           C  
ATOM    171  O   ARG A  22      17.822  59.992  20.382  1.00 66.75           O  
ATOM    172  CB  ARG A  22      15.103  59.866  21.252  1.00 69.17           C  
ATOM    173  CG  ARG A  22      14.543  60.783  20.180  1.00 73.88           C  
ATOM    174  CD  ARG A  22      13.855  61.990  20.803  1.00 78.00           C  
ATOM    175  NE  ARG A  22      13.159  62.796  19.804  1.00 82.76           N  
ATOM    176  CZ  ARG A  22      12.140  62.362  19.063  1.00 84.78           C  
ATOM    177  NH1 ARG A  22      11.688  61.120  19.203  1.00 82.41           N  
ATOM    178  NH2 ARG A  22      11.574  63.173  18.176  1.00 86.69           N  
ATOM    179  N   ASN A  23      17.300  58.532  18.760  1.00 68.46           N  
ATOM    180  CA  ASN A  23      18.435  58.915  17.934  1.00 69.69           C  
ATOM    181  C   ASN A  23      18.382  60.418  17.707  1.00 71.66           C  
ATOM    182  O   ASN A  23      17.574  60.898  16.916  1.00 72.90           O  
ATOM    183  CB  ASN A  23      18.384  58.203  16.590  1.00 68.36           C  
ATOM    184  CG  ASN A  23      19.565  58.545  15.717  1.00 68.42           C  
ATOM    185  OD1 ASN A  23      19.969  59.705  15.635  1.00 67.81           O  
ATOM    186  ND2 ASN A  23      20.125  57.542  15.053  1.00 66.73           N  
ATOM    187  N   LYS A  24      19.253  61.149  18.399  1.00 73.83           N  
ATOM    188  CA  LYS A  24      19.311  62.608  18.311  1.00 74.54           C  
ATOM    189  C   LYS A  24      19.310  63.202  16.905  1.00 75.17           C  
ATOM    190  O   LYS A  24      18.995  64.382  16.733  1.00 75.44           O  
ATOM    191  CB  LYS A  24      20.524  63.128  19.082  1.00 75.33           C  
ATOM    192  CG  LYS A  24      20.405  62.975  20.588  1.00 76.87           C  
ATOM    193  CD  LYS A  24      21.644  63.510  21.285  1.00 78.39           C  
ATOM    194  CE  LYS A  24      21.569  63.310  22.789  1.00 79.35           C  
ATOM    195  NZ  LYS A  24      22.821  63.762  23.456  1.00 79.03           N  
ATOM    196  N   LEU A  25      19.666  62.408  15.902  1.00 75.13           N  
ATOM    197  CA  LEU A  25      19.656  62.912  14.530  1.00 75.78           C  
ATOM    198  C   LEU A  25      18.304  62.628  13.875  1.00 74.88           C  
ATOM    199  O   LEU A  25      17.423  63.494  13.848  1.00 74.93           O  
ATOM    200  CB  LEU A  25      20.777  62.275  13.699  1.00 77.19           C  
ATOM    201  CG  LEU A  25      20.744  62.619  12.202  1.00 78.89           C  
ATOM    202  CD1 LEU A  25      20.678  64.129  12.016  1.00 79.49           C  
ATOM    203  CD2 LEU A  25      21.973  62.046  11.507  1.00 80.15           C  
ATOM    204  N   THR A  26      18.146  61.411  13.357  1.00 72.33           N  
ATOM    205  CA  THR A  26      16.909  60.999  12.701  1.00 70.28           C  
ATOM    206  C   THR A  26      15.693  61.105  13.621  1.00 68.16           C  
ATOM    207  O   THR A  26      14.554  61.117  13.158  1.00 67.75           O  
ATOM    208  CB  THR A  26      17.006  59.546  12.196  1.00 70.05           C  
ATOM    209  OG1 THR A  26      17.341  58.683  13.288  1.00 69.70           O  
ATOM    210  CG2 THR A  26      18.070  59.426  11.113  1.00 71.88           C  
ATOM    211  N   GLY A  27      15.938  61.181  14.924  1.00 65.88           N  
ATOM    212  CA  GLY A  27      14.843  61.281  15.871  1.00 63.88           C  
ATOM    213  C   GLY A  27      14.096  59.973  16.057  1.00 62.00           C  
ATOM    214  O   GLY A  27      13.144  59.906  16.835  1.00 61.51           O  
ATOM    215  N   GLU A  28      14.531  58.933  15.349  1.00 59.69           N  
ATOM    216  CA  GLU A  28      13.895  57.628  15.437  1.00 58.01           C  
ATOM    217  C   GLU A  28      14.035  57.018  16.826  1.00 55.80           C  
ATOM    218  O   GLU A  28      15.042  57.214  17.510  1.00 55.62           O  
ATOM    219  CB  GLU A  28      14.473  56.678  14.377  1.00 60.75           C  
ATOM    220  CG  GLU A  28      15.989  56.480  14.436  1.00 65.56           C  
ATOM    221  CD  GLU A  28      16.535  55.686  13.244  1.00 68.08           C  
ATOM    222  OE1 GLU A  28      16.123  54.514  13.061  1.00 67.95           O  
ATOM    223  OE2 GLU A  28      17.375  56.236  12.490  1.00 67.05           O  
ATOM    224  N   VAL A  29      13.000  56.294  17.241  1.00 53.29           N  
ATOM    225  CA  VAL A  29      12.977  55.642  18.544  1.00 49.92           C  
ATOM    226  C   VAL A  29      13.511  54.233  18.389  1.00 48.36           C  
ATOM    227  O   VAL A  29      13.092  53.494  17.495  1.00 49.49           O  
ATOM    228  CB  VAL A  29      11.542  55.581  19.121  1.00 50.03           C  
ATOM    229  CG1 VAL A  29      11.469  54.569  20.243  1.00 49.96           C  
ATOM    230  CG2 VAL A  29      11.142  56.946  19.647  1.00 50.08           C  
ATOM    231  N   VAL A  30      14.443  53.866  19.259  1.00 45.20           N  
ATOM    232  CA  VAL A  30      15.041  52.544  19.206  1.00 43.12           C  
ATOM    233  C   VAL A  30      15.123  51.929  20.600  1.00 43.17           C  
ATOM    234  O   VAL A  30      14.808  52.572  21.601  1.00 41.46           O  
ATOM    235  CB  VAL A  30      16.475  52.606  18.593  1.00 41.74           C  
ATOM    236  CG1 VAL A  30      16.432  53.270  17.230  1.00 38.10           C  
ATOM    237  CG2 VAL A  30      17.413  53.358  19.513  1.00 37.82           C  
ATOM    238  N   ALA A  31      15.514  50.662  20.653  1.00 42.84           N  
ATOM    239  CA  ALA A  31      15.688  49.979  21.924  1.00 43.00           C  
ATOM    240  C   ALA A  31      17.197  49.836  22.019  1.00 43.58           C  
ATOM    241  O   ALA A  31      17.821  49.162  21.196  1.00 43.81           O  
ATOM    242  CB  ALA A  31      15.019  48.621  21.908  1.00 40.00           C  
ATOM    243  N   LEU A  32      17.777  50.500  23.009  1.00 44.83           N  
ATOM    244  CA  LEU A  32      19.218  50.497  23.204  1.00 47.12           C  
ATOM    245  C   LEU A  32      19.643  49.427  24.195  1.00 47.21           C  
ATOM    246  O   LEU A  32      19.286  49.494  25.368  1.00 47.84           O  
ATOM    247  CB  LEU A  32      19.650  51.869  23.719  1.00 48.58           C  
ATOM    248  CG  LEU A  32      21.110  52.298  23.580  1.00 50.86           C  
ATOM    249  CD1 LEU A  32      21.418  52.535  22.110  1.00 51.78           C  
ATOM    250  CD2 LEU A  32      21.355  53.567  24.392  1.00 48.88           C  
ATOM    251  N   LYS A  33      20.406  48.443  23.727  1.00 48.13           N  
ATOM    252  CA  LYS A  33      20.868  47.372  24.605  1.00 49.12           C  
ATOM    253  C   LYS A  33      22.367  47.465  24.866  1.00 49.48           C  
ATOM    254  O   LYS A  33      23.185  47.105  24.025  1.00 49.35           O  
ATOM    255  CB  LYS A  33      20.520  46.000  24.016  1.00 49.06           C  
ATOM    256  CG ALYS A  33      20.440  44.633  24.816  0.59 49.99           C  
ATOM    257  CG BLYS A  33      19.158  45.978  23.333  0.41 48.85           C  
ATOM    258  CD ALYS A  33      21.257  43.498  24.228  0.59 52.00           C  
ATOM    259  CD BLYS A  33      18.188  45.046  24.059  0.41 48.76           C  
ATOM    260  CE ALYS A  33      20.527  42.167  24.309  0.59 52.27           C  
ATOM    261  CE BLYS A  33      16.836  44.962  23.336  0.41 49.64           C  
ATOM    262  NZ ALYS A  33      19.838  41.974  25.642  0.59 54.57           N  
ATOM    263  NZ BLYS A  33      15.958  43.895  23.893  0.41 49.67           N  
ATOM    264  N   LYS A  34      22.701  47.924  26.068  1.00 48.65           N  
ATOM    265  CA  LYS A  34      24.082  48.060  26.501  1.00 51.34           C  
ATOM    266  C   LYS A  34      24.552  46.740  27.118  1.00 50.51           C  
ATOM    267  O   LYS A  34      24.019  46.302  28.137  1.00 49.01           O  
ATOM    268  CB  LYS A  34      24.198  49.173  27.548  1.00 53.86           C  
ATOM    269  CG  LYS A  34      25.570  49.232  28.222  1.00 58.01           C  
ATOM    270  CD  LYS A  34      25.674  50.363  29.246  1.00 60.15           C  
ATOM    271  CE  LYS A  34      27.031  50.342  29.955  1.00 61.81           C  
ATOM    272  NZ  LYS A  34      28.187  50.434  29.008  1.00 61.59           N  
ATOM    273  N   ILE A  35      25.553  46.120  26.500  1.00 50.52           N  
ATOM    274  CA  ILE A  35      26.102  44.856  26.978  1.00 50.24           C  
ATOM    275  C   ILE A  35      27.528  45.041  27.472  1.00 51.01           C  
ATOM    276  O   ILE A  35      27.847  44.687  28.607  1.00 53.48           O  
ATOM    277  CB  ILE A  35      26.110  43.801  25.862  1.00 49.96           C  
ATOM    278  CG1 ILE A  35      24.685  43.569  25.366  1.00 49.58           C  
ATOM    279  CG2 ILE A  35      26.709  42.501  26.373  1.00 49.18           C  
ATOM    280  CD1 ILE A  35      24.607  42.728  24.127  1.00 51.60           C  
ATOM    281  N   VAL A  44      34.641  43.137  24.252  1.00 92.11           N  
ATOM    282  CA  VAL A  44      34.122  41.794  24.011  1.00 91.20           C  
ATOM    283  C   VAL A  44      34.965  41.078  22.958  1.00 90.30           C  
ATOM    284  O   VAL A  44      35.568  41.717  22.093  1.00 91.41           O  
ATOM    285  CB  VAL A  44      32.650  41.838  23.527  1.00 91.18           C  
ATOM    286  CG1 VAL A  44      31.787  42.566  24.548  1.00 91.12           C  
ATOM    287  CG2 VAL A  44      32.565  42.520  22.170  1.00 90.60           C  
ATOM    288  N   PRO A  45      35.016  39.738  23.015  1.00 89.69           N  
ATOM    289  CA  PRO A  45      35.806  38.991  22.033  1.00 87.77           C  
ATOM    290  C   PRO A  45      35.341  39.254  20.604  1.00 86.08           C  
ATOM    291  O   PRO A  45      34.143  39.311  20.325  1.00 86.41           O  
ATOM    292  CB  PRO A  45      35.604  37.539  22.463  1.00 88.28           C  
ATOM    293  CG  PRO A  45      34.229  37.555  23.051  1.00 89.27           C  
ATOM    294  CD  PRO A  45      34.250  38.821  23.877  1.00 88.89           C  
ATOM    295  N   SER A  46      36.304  39.422  19.705  1.00 83.47           N  
ATOM    296  CA  SER A  46      36.021  39.683  18.297  1.00 80.24           C  
ATOM    297  C   SER A  46      35.039  38.661  17.739  1.00 77.62           C  
ATOM    298  O   SER A  46      34.242  38.964  16.849  1.00 77.55           O  
ATOM    299  CB  SER A  46      37.317  39.625  17.493  1.00 80.65           C  
ATOM    300  OG  SER A  46      37.888  38.332  17.570  1.00 79.05           O  
ATOM    301  N   THR A  47      35.119  37.442  18.262  1.00 74.42           N  
ATOM    302  CA  THR A  47      34.246  36.361  17.834  1.00 69.80           C  
ATOM    303  C   THR A  47      32.789  36.792  17.968  1.00 66.51           C  
ATOM    304  O   THR A  47      31.984  36.592  17.060  1.00 65.27           O  
ATOM    305  CB  THR A  47      34.505  35.089  18.678  1.00 69.66           C  
ATOM    306  OG1 THR A  47      33.546  34.082  18.337  1.00 69.89           O  
ATOM    307  CG2 THR A  47      34.418  35.401  20.167  1.00 69.39           C  
ATOM    308  N   ALA A  48      32.464  37.397  19.104  1.00 63.57           N  
ATOM    309  CA  ALA A  48      31.113  37.864  19.359  1.00 62.02           C  
ATOM    310  C   ALA A  48      30.743  38.925  18.328  1.00 60.96           C  
ATOM    311  O   ALA A  48      29.669  38.876  17.727  1.00 58.87           O  
ATOM    312  CB  ALA A  48      31.022  38.439  20.763  1.00 61.51           C  
ATOM    313  N   ILE A  49      31.652  39.877  18.130  1.00 60.71           N  
ATOM    314  CA  ILE A  49      31.459  40.964  17.176  1.00 61.01           C  
ATOM    315  C   ILE A  49      31.118  40.476  15.767  1.00 59.48           C  
ATOM    316  O   ILE A  49      30.223  41.018  15.130  1.00 58.98           O  
ATOM    317  CB  ILE A  49      32.710  41.863  17.110  1.00 62.91           C  
ATOM    318  CG1 ILE A  49      32.950  42.514  18.475  1.00 64.61           C  
ATOM    319  CG2 ILE A  49      32.541  42.926  16.034  1.00 64.01           C  
ATOM    320  CD1 ILE A  49      31.810  43.393  18.954  1.00 65.86           C  
ATOM    321  N   ARG A  50      31.832  39.472  15.269  1.00 59.35           N  
ATOM    322  CA  ARG A  50      31.530  38.948  13.940  1.00 60.23           C  
ATOM    323  C   ARG A  50      30.147  38.332  13.996  1.00 60.23           C  
ATOM    324  O   ARG A  50      29.355  38.452  13.061  1.00 59.15           O  
ATOM    325  CB  ARG A  50      32.503  37.844  13.534  1.00 60.92           C  
ATOM    326  CG  ARG A  50      33.920  38.273  13.305  1.00 63.66           C  
ATOM    327  CD  ARG A  50      34.725  37.092  12.801  1.00 65.41           C  
ATOM    328  NE  ARG A  50      36.134  37.425  12.631  1.00 67.84           N  
ATOM    329  CZ  ARG A  50      36.944  37.770  13.626  1.00 68.76           C  
ATOM    330  NH1 ARG A  50      36.486  37.824  14.869  1.00 69.94           N  
ATOM    331  NH2 ARG A  50      38.211  38.067  13.378  1.00 68.34           N  
ATOM    332  N   GLU A  51      29.878  37.663  15.112  1.00 61.48           N  
ATOM    333  CA  GLU A  51      28.613  36.980  15.330  1.00 62.03           C  
ATOM    334  C   GLU A  51      27.417  37.912  15.407  1.00 59.82           C  
ATOM    335  O   GLU A  51      26.466  37.755  14.652  1.00 60.06           O  
ATOM    336  CB  GLU A  51      28.698  36.127  16.598  1.00 64.64           C  
ATOM    337  CG  GLU A  51      28.451  34.648  16.341  1.00 68.70           C  
ATOM    338  CD  GLU A  51      29.234  34.122  15.140  1.00 71.61           C  
ATOM    339  OE1 GLU A  51      30.483  34.192  15.161  1.00 72.95           O  
ATOM    340  OE2 GLU A  51      28.598  33.641  14.172  1.00 73.06           O  
ATOM    341  N   ILE A  52      27.453  38.880  16.310  1.00 58.47           N  
ATOM    342  CA  ILE A  52      26.333  39.797  16.421  1.00 59.12           C  
ATOM    343  C   ILE A  52      26.254  40.713  15.202  1.00 57.13           C  
ATOM    344  O   ILE A  52      25.252  41.393  15.003  1.00 57.24           O  
ATOM    345  CB  ILE A  52      26.418  40.671  17.696  1.00 60.07           C  
ATOM    346  CG1 ILE A  52      27.628  41.597  17.620  1.00 61.69           C  
ATOM    347  CG2 ILE A  52      26.507  39.791  18.927  1.00 60.31           C  
ATOM    348  CD1 ILE A  52      27.684  42.604  18.747  1.00 63.38           C  
ATOM    349  N   SER A  53      27.306  40.726  14.388  1.00 55.84           N  
ATOM    350  CA  SER A  53      27.319  41.569  13.197  1.00 55.33           C  
ATOM    351  C   SER A  53      26.692  40.868  12.004  1.00 55.06           C  
ATOM    352  O   SER A  53      26.107  41.518  11.140  1.00 54.22           O  
ATOM    353  CB  SER A  53      28.746  42.018  12.861  1.00 55.45           C  
ATOM    354  OG  SER A  53      29.176  43.027  13.762  1.00 52.25           O  
ATOM    355  N   LEU A  54      26.809  39.544  11.958  1.00 55.41           N  
ATOM    356  CA  LEU A  54      26.214  38.772  10.870  1.00 55.82           C  
ATOM    357  C   LEU A  54      24.693  38.840  10.991  1.00 55.48           C  
ATOM    358  O   LEU A  54      23.970  38.687  10.007  1.00 56.69           O  
ATOM    359  CB  LEU A  54      26.650  37.307  10.939  1.00 56.77           C  
ATOM    360  CG  LEU A  54      28.145  36.965  10.934  1.00 59.33           C  
ATOM    361  CD1 LEU A  54      28.313  35.447  10.833  1.00 58.35           C  
ATOM    362  CD2 LEU A  54      28.844  37.654   9.770  1.00 58.93           C  
ATOM    363  N   LEU A  55      24.219  39.065  12.213  1.00 54.71           N  
ATOM    364  CA  LEU A  55      22.795  39.150  12.494  1.00 53.29           C  
ATOM    365  C   LEU A  55      22.172  40.384  11.869  1.00 54.00           C  
ATOM    366  O   LEU A  55      20.977  40.403  11.576  1.00 54.71           O  
ATOM    367  CB  LEU A  55      22.563  39.186  14.000  1.00 52.71           C  
ATOM    368  CG  LEU A  55      23.082  37.996  14.799  1.00 50.96           C  
ATOM    369  CD1 LEU A  55      23.068  38.329  16.284  1.00 51.23           C  
ATOM    370  CD2 LEU A  55      22.230  36.778  14.503  1.00 51.58           C  
ATOM    371  N   LYS A  56      22.981  41.417  11.665  1.00 55.12           N  
ATOM    372  CA  LYS A  56      22.485  42.654  11.077  1.00 56.89           C  
ATOM    373  C   LYS A  56      21.824  42.423   9.724  1.00 56.86           C  
ATOM    374  O   LYS A  56      20.957  43.191   9.306  1.00 58.01           O  
ATOM    375  CB  LYS A  56      23.624  43.656  10.916  1.00 57.98           C  
ATOM    376  CG  LYS A  56      24.383  43.920  12.195  1.00 62.46           C  
ATOM    377  CD  LYS A  56      25.407  45.030  12.017  1.00 65.34           C  
ATOM    378  CE  LYS A  56      24.735  46.366  11.747  1.00 68.30           C  
ATOM    379  NZ  LYS A  56      25.710  47.496  11.776  1.00 69.46           N  
ATOM    380  N   GLU A  57      22.230  41.361   9.043  1.00 56.79           N  
ATOM    381  CA  GLU A  57      21.671  41.049   7.735  1.00 56.99           C  
ATOM    382  C   GLU A  57      20.515  40.053   7.784  1.00 54.35           C  
ATOM    383  O   GLU A  57      19.873  39.786   6.771  1.00 52.94           O  
ATOM    384  CB  GLU A  57      22.779  40.533   6.815  1.00 59.52           C  
ATOM    385  CG  GLU A  57      23.795  41.605   6.451  1.00 65.44           C  
ATOM    386  CD  GLU A  57      23.134  42.858   5.887  1.00 68.79           C  
ATOM    387  OE1 GLU A  57      22.383  42.737   4.892  1.00 71.90           O  
ATOM    388  OE2 GLU A  57      23.363  43.962   6.435  1.00 70.03           O  
ATOM    389  N   LEU A  58      20.253  39.512   8.965  1.00 52.04           N  
ATOM    390  CA  LEU A  58      19.171  38.557   9.141  1.00 51.25           C  
ATOM    391  C   LEU A  58      17.897  39.356   9.417  1.00 50.24           C  
ATOM    392  O   LEU A  58      17.483  39.519  10.568  1.00 51.78           O  
ATOM    393  CB  LEU A  58      19.487  37.633  10.324  1.00 52.41           C  
ATOM    394  CG  LEU A  58      18.505  36.516  10.682  1.00 51.78           C  
ATOM    395  CD1 LEU A  58      18.747  35.307   9.801  1.00 53.83           C  
ATOM    396  CD2 LEU A  58      18.693  36.138  12.138  1.00 52.94           C  
ATOM    397  N   ASN A  59      17.278  39.867   8.360  1.00 47.14           N  
ATOM    398  CA  ASN A  59      16.068  40.660   8.519  1.00 44.60           C  
ATOM    399  C   ASN A  59      14.816  39.888   8.125  1.00 41.27           C  
ATOM    400  O   ASN A  59      14.815  39.154   7.142  1.00 42.34           O  
ATOM    401  CB  ASN A  59      16.175  41.942   7.693  1.00 45.54           C  
ATOM    402  CG  ASN A  59      17.339  42.810   8.118  1.00 45.65           C  
ATOM    403  OD1 ASN A  59      17.390  43.290   9.247  1.00 47.88           O  
ATOM    404  ND2 ASN A  59      18.286  43.014   7.212  1.00 47.87           N  
ATOM    405  N   HIS A  60      13.752  40.067   8.903  1.00 36.53           N  
ATOM    406  CA  HIS A  60      12.482  39.393   8.666  1.00 32.80           C  
ATOM    407  C   HIS A  60      11.411  40.180   9.420  1.00 31.31           C  
ATOM    408  O   HIS A  60      11.651  40.669  10.523  1.00 30.86           O  
ATOM    409  CB  HIS A  60      12.556  37.955   9.193  1.00 32.98           C  
ATOM    410  CG  HIS A  60      11.322  37.146   8.946  1.00 30.87           C  
ATOM    411  ND1 HIS A  60      11.156  36.361   7.826  1.00 31.39           N  
ATOM    412  CD2 HIS A  60      10.199  36.986   9.684  1.00 32.49           C  
ATOM    413  CE1 HIS A  60       9.987  35.749   7.887  1.00 34.06           C  
ATOM    414  NE2 HIS A  60       9.386  36.112   9.006  1.00 32.29           N  
ATOM    415  N   PRO A  61      10.211  40.309   8.836  1.00 30.91           N  
ATOM    416  CA  PRO A  61       9.138  41.056   9.497  1.00 30.68           C  
ATOM    417  C   PRO A  61       8.795  40.548  10.886  1.00 31.53           C  
ATOM    418  O   PRO A  61       8.234  41.283  11.693  1.00 32.55           O  
ATOM    419  CB  PRO A  61       7.970  40.944   8.512  1.00 28.50           C  
ATOM    420  CG  PRO A  61       8.245  39.685   7.775  1.00 28.25           C  
ATOM    421  CD  PRO A  61       9.739  39.725   7.567  1.00 29.64           C  
ATOM    422  N   ASN A  62       9.142  39.300  11.178  1.00 33.16           N  
ATOM    423  CA  ASN A  62       8.853  38.750  12.497  1.00 32.50           C  
ATOM    424  C   ASN A  62      10.071  38.647  13.389  1.00 32.18           C  
ATOM    425  O   ASN A  62      10.030  37.994  14.431  1.00 32.57           O  
ATOM    426  CB  ASN A  62       8.182  37.390  12.376  1.00 31.44           C  
ATOM    427  CG  ASN A  62       6.860  37.476  11.671  1.00 29.40           C  
ATOM    428  OD1 ASN A  62       6.719  36.988  10.562  1.00 32.25           O  
ATOM    429  ND2 ASN A  62       5.881  38.120  12.308  1.00 29.07           N  
ATOM    430  N   ILE A  63      11.152  39.299  12.982  1.00 31.05           N  
ATOM    431  CA  ILE A  63      12.362  39.305  13.783  1.00 31.97           C  
ATOM    432  C   ILE A  63      12.657  40.749  14.128  1.00 32.37           C  
ATOM    433  O   ILE A  63      12.733  41.589  13.235  1.00 34.20           O  
ATOM    434  CB  ILE A  63      13.560  38.722  13.006  1.00 32.84           C  
ATOM    435  CG1 ILE A  63      13.267  37.284  12.601  1.00 34.05           C  
ATOM    436  CG2 ILE A  63      14.813  38.759  13.868  1.00 31.67           C  
ATOM    437  CD1 ILE A  63      14.363  36.671  11.770  1.00 38.73           C  
ATOM    438  N   VAL A  64      12.803  41.046  15.416  1.00 33.64           N  
ATOM    439  CA  VAL A  64      13.104  42.412  15.831  1.00 34.54           C  
ATOM    440  C   VAL A  64      14.384  42.849  15.152  1.00 35.94           C  
ATOM    441  O   VAL A  64      15.468  42.356  15.468  1.00 35.42           O  
ATOM    442  CB  VAL A  64      13.306  42.542  17.356  1.00 34.68           C  
ATOM    443  CG1 VAL A  64      13.953  43.897  17.677  1.00 33.67           C  
ATOM    444  CG2 VAL A  64      11.971  42.434  18.068  1.00 31.67           C  
ATOM    445  N   LYS A  65      14.242  43.786  14.225  1.00 37.32           N  
ATOM    446  CA  LYS A  65      15.360  44.318  13.451  1.00 39.49           C  
ATOM    447  C   LYS A  65      16.518  44.897  14.271  1.00 37.69           C  
ATOM    448  O   LYS A  65      16.339  45.796  15.094  1.00 36.54           O  
ATOM    449  CB  LYS A  65      14.818  45.381  12.486  1.00 42.90           C  
ATOM    450  CG  LYS A  65      15.836  46.035  11.574  1.00 44.66           C  
ATOM    451  CD  LYS A  65      15.109  46.929  10.557  1.00 48.61           C  
ATOM    452  CE  LYS A  65      16.080  47.628   9.602  1.00 49.29           C  
ATOM    453  NZ  LYS A  65      17.011  46.673   8.938  1.00 48.02           N  
ATOM    454  N   LEU A  66      17.708  44.355  14.041  1.00 37.79           N  
ATOM    455  CA  LEU A  66      18.917  44.826  14.707  1.00 38.94           C  
ATOM    456  C   LEU A  66      19.456  45.987  13.862  1.00 41.14           C  
ATOM    457  O   LEU A  66      20.192  45.774  12.909  1.00 40.62           O  
ATOM    458  CB  LEU A  66      19.949  43.699  14.769  1.00 34.62           C  
ATOM    459  CG  LEU A  66      21.324  44.049  15.339  1.00 35.35           C  
ATOM    460  CD1 LEU A  66      21.180  44.686  16.729  1.00 34.25           C  
ATOM    461  CD2 LEU A  66      22.174  42.787  15.406  1.00 33.57           C  
ATOM    462  N   LEU A  67      19.075  47.212  14.201  1.00 45.36           N  
ATOM    463  CA  LEU A  67      19.515  48.375  13.436  1.00 49.46           C  
ATOM    464  C   LEU A  67      21.027  48.485  13.320  1.00 53.29           C  
ATOM    465  O   LEU A  67      21.571  48.436  12.215  1.00 54.20           O  
ATOM    466  CB  LEU A  67      18.957  49.661  14.044  1.00 46.25           C  
ATOM    467  CG  LEU A  67      17.429  49.732  14.072  1.00 47.09           C  
ATOM    468  CD1 LEU A  67      16.982  51.014  14.757  1.00 46.58           C  
ATOM    469  CD2 LEU A  67      16.895  49.662  12.657  1.00 45.76           C  
ATOM    470  N   ASP A  68      21.710  48.622  14.453  1.00 57.39           N  
ATOM    471  CA  ASP A  68      23.162  48.765  14.434  1.00 61.08           C  
ATOM    472  C   ASP A  68      23.870  48.156  15.638  1.00 61.36           C  
ATOM    473  O   ASP A  68      23.233  47.651  16.558  1.00 61.43           O  
ATOM    474  CB  ASP A  68      23.524  50.249  14.325  1.00 64.58           C  
ATOM    475  CG  ASP A  68      22.964  50.895  13.066  1.00 67.71           C  
ATOM    476  OD1 ASP A  68      23.414  50.524  11.957  1.00 70.31           O  
ATOM    477  OD2 ASP A  68      22.072  51.765  13.182  1.00 69.37           O  
ATOM    478  N   VAL A  69      25.199  48.211  15.611  1.00 62.29           N  
ATOM    479  CA  VAL A  69      26.038  47.684  16.685  1.00 62.41           C  
ATOM    480  C   VAL A  69      27.104  48.727  16.995  1.00 63.46           C  
ATOM    481  O   VAL A  69      27.826  49.165  16.106  1.00 64.14           O  
ATOM    482  CB  VAL A  69      26.730  46.371  16.267  1.00 60.91           C  
ATOM    483  CG1 VAL A  69      27.542  45.820  17.428  1.00 60.17           C  
ATOM    484  CG2 VAL A  69      25.690  45.355  15.818  1.00 60.66           C  
ATOM    485  N   ILE A  70      27.196  49.125  18.257  1.00 65.77           N  
ATOM    486  CA  ILE A  70      28.162  50.139  18.664  1.00 67.31           C  
ATOM    487  C   ILE A  70      29.157  49.609  19.692  1.00 68.68           C  
ATOM    488  O   ILE A  70      28.800  49.369  20.844  1.00 68.14           O  
ATOM    489  CB  ILE A  70      27.443  51.365  19.277  1.00 67.86           C  
ATOM    490  CG1 ILE A  70      26.256  51.772  18.401  1.00 66.12           C  
ATOM    491  CG2 ILE A  70      28.422  52.520  19.436  1.00 68.24           C  
ATOM    492  CD1 ILE A  70      26.619  52.041  16.970  1.00 68.39           C  
ATOM    493  N   HIS A  71      30.405  49.430  19.273  1.00 70.57           N  
ATOM    494  CA  HIS A  71      31.443  48.941  20.172  1.00 72.79           C  
ATOM    495  C   HIS A  71      32.445  50.060  20.457  1.00 75.20           C  
ATOM    496  O   HIS A  71      33.430  50.229  19.733  1.00 75.51           O  
ATOM    497  CB  HIS A  71      32.168  47.744  19.552  1.00 70.84           C  
ATOM    498  CG  HIS A  71      33.105  47.053  20.493  1.00 69.05           C  
ATOM    499  ND1 HIS A  71      33.977  46.067  20.085  1.00 68.36           N  
ATOM    500  CD2 HIS A  71      33.297  47.197  21.826  1.00 68.52           C  
ATOM    501  CE1 HIS A  71      34.665  45.633  21.126  1.00 68.17           C  
ATOM    502  NE2 HIS A  71      34.271  46.302  22.195  1.00 67.70           N  
ATOM    503  N   THR A  72      32.178  50.824  21.512  1.00 78.10           N  
ATOM    504  CA  THR A  72      33.034  51.934  21.908  1.00 80.70           C  
ATOM    505  C   THR A  72      33.705  51.600  23.228  1.00 82.74           C  
ATOM    506  O   THR A  72      33.052  51.135  24.159  1.00 82.37           O  
ATOM    507  CB  THR A  72      32.222  53.228  22.089  1.00 81.14           C  
ATOM    508  OG1 THR A  72      31.236  53.033  23.112  1.00 81.16           O  
ATOM    509  CG2 THR A  72      31.533  53.613  20.785  1.00 80.59           C  
ATOM    510  N   GLU A  73      35.008  51.853  23.300  1.00 85.43           N  
ATOM    511  CA  GLU A  73      35.801  51.571  24.492  1.00 87.23           C  
ATOM    512  C   GLU A  73      35.317  50.318  25.215  1.00 86.67           C  
ATOM    513  O   GLU A  73      34.887  50.372  26.369  1.00 86.84           O  
ATOM    514  CB  GLU A  73      35.793  52.771  25.446  1.00 89.75           C  
ATOM    515  CG  GLU A  73      34.424  53.221  25.923  1.00 92.77           C  
ATOM    516  CD  GLU A  73      34.522  54.262  27.024  1.00 95.39           C  
ATOM    517  OE1 GLU A  73      35.101  53.945  28.086  1.00 95.58           O  
ATOM    518  OE2 GLU A  73      34.026  55.394  26.829  1.00 96.28           O  
ATOM    519  N   ASN A  74      35.396  49.191  24.514  1.00 85.91           N  
ATOM    520  CA  ASN A  74      34.976  47.898  25.045  1.00 86.07           C  
ATOM    521  C   ASN A  74      33.619  47.925  25.763  1.00 84.90           C  
ATOM    522  O   ASN A  74      33.451  47.350  26.843  1.00 84.66           O  
ATOM    523  CB  ASN A  74      36.069  47.327  25.962  1.00 87.37           C  
ATOM    524  CG  ASN A  74      37.322  46.906  25.190  1.00 89.30           C  
ATOM    525  OD1 ASN A  74      37.982  47.729  24.551  1.00 89.93           O  
ATOM    526  ND2 ASN A  74      37.647  45.616  25.245  1.00 89.09           N  
ATOM    527  N   LYS A  75      32.659  48.608  25.141  1.00 82.32           N  
ATOM    528  CA  LYS A  75      31.287  48.717  25.639  1.00 78.74           C  
ATOM    529  C   LYS A  75      30.445  48.327  24.429  1.00 74.67           C  
ATOM    530  O   LYS A  75      30.545  48.964  23.381  1.00 75.23           O  
ATOM    531  CB  LYS A  75      30.969  50.160  26.048  1.00 81.01           C  
ATOM    532  CG  LYS A  75      31.891  50.736  27.115  1.00 83.47           C  
ATOM    533  CD  LYS A  75      31.768  49.985  28.433  1.00 85.91           C  
ATOM    534  CE  LYS A  75      32.761  50.512  29.457  1.00 86.49           C  
ATOM    535  NZ  LYS A  75      32.572  51.969  29.699  1.00 87.45           N  
ATOM    536  N   LEU A  76      29.627  47.286  24.550  1.00 68.65           N  
ATOM    537  CA  LEU A  76      28.832  46.856  23.405  1.00 63.45           C  
ATOM    538  C   LEU A  76      27.368  47.272  23.472  1.00 59.86           C  
ATOM    539  O   LEU A  76      26.599  46.751  24.269  1.00 59.68           O  
ATOM    540  CB  LEU A  76      28.940  45.335  23.231  1.00 60.77           C  
ATOM    541  CG  LEU A  76      28.487  44.778  21.879  1.00 57.66           C  
ATOM    542  CD1 LEU A  76      29.299  45.414  20.767  1.00 55.70           C  
ATOM    543  CD2 LEU A  76      28.655  43.272  21.858  1.00 56.27           C  
ATOM    544  N   TYR A  77      26.999  48.214  22.612  1.00 56.74           N  
ATOM    545  CA  TYR A  77      25.639  48.732  22.536  1.00 53.95           C  
ATOM    546  C   TYR A  77      24.946  48.147  21.319  1.00 51.20           C  
ATOM    547  O   TYR A  77      25.469  48.235  20.213  1.00 51.53           O  
ATOM    548  CB  TYR A  77      25.662  50.250  22.375  1.00 55.87           C  
ATOM    549  CG  TYR A  77      26.130  51.036  23.578  1.00 59.18           C  
ATOM    550  CD1 TYR A  77      25.265  51.302  24.636  1.00 60.52           C  
ATOM    551  CD2 TYR A  77      27.422  51.558  23.635  1.00 59.99           C  
ATOM    552  CE1 TYR A  77      25.668  52.074  25.719  1.00 61.73           C  
ATOM    553  CE2 TYR A  77      27.838  52.331  24.716  1.00 61.03           C  
ATOM    554  CZ  TYR A  77      26.952  52.587  25.753  1.00 62.26           C  
ATOM    555  OH  TYR A  77      27.340  53.369  26.821  1.00 64.53           O  
ATOM    556  N   LEU A  78      23.773  47.552  21.511  1.00 48.29           N  
ATOM    557  CA  LEU A  78      23.024  46.991  20.387  1.00 45.52           C  
ATOM    558  C   LEU A  78      21.760  47.813  20.172  1.00 43.43           C  
ATOM    559  O   LEU A  78      20.971  48.004  21.101  1.00 42.34           O  
ATOM    560  CB  LEU A  78      22.650  45.526  20.641  1.00 45.29           C  
ATOM    561  CG  LEU A  78      23.788  44.505  20.699  1.00 43.91           C  
ATOM    562  CD1 LEU A  78      23.206  43.110  20.853  1.00 43.48           C  
ATOM    563  CD2 LEU A  78      24.619  44.595  19.433  1.00 43.64           C  
ATOM    564  N   VAL A  79      21.579  48.309  18.951  1.00 41.69           N  
ATOM    565  CA  VAL A  79      20.414  49.121  18.628  1.00 42.36           C  
ATOM    566  C   VAL A  79      19.402  48.317  17.833  1.00 42.21           C  
ATOM    567  O   VAL A  79      19.687  47.845  16.729  1.00 42.75           O  
ATOM    568  CB  VAL A  79      20.801  50.384  17.816  1.00 41.91           C  
ATOM    569  CG1 VAL A  79      19.553  51.141  17.417  1.00 38.85           C  
ATOM    570  CG2 VAL A  79      21.717  51.277  18.640  1.00 41.61           C  
ATOM    571  N   PHE A  80      18.215  48.169  18.407  1.00 41.08           N  
ATOM    572  CA  PHE A  80      17.136  47.421  17.771  1.00 40.39           C  
ATOM    573  C   PHE A  80      15.970  48.351  17.474  1.00 38.25           C  
ATOM    574  O   PHE A  80      15.875  49.439  18.041  1.00 37.47           O  
ATOM    575  CB  PHE A  80      16.649  46.314  18.708  1.00 38.84           C  
ATOM    576  CG  PHE A  80      17.630  45.199  18.906  1.00 39.99           C  
ATOM    577  CD1 PHE A  80      17.695  44.145  18.005  1.00 40.26           C  
ATOM    578  CD2 PHE A  80      18.455  45.170  20.022  1.00 41.21           C  
ATOM    579  CE1 PHE A  80      18.563  43.076  18.218  1.00 40.20           C  
ATOM    580  CE2 PHE A  80      19.327  44.100  20.242  1.00 39.78           C  
ATOM    581  CZ  PHE A  80      19.376  43.052  19.336  1.00 39.30           C  
ATOM    582  N   GLU A  81      15.091  47.928  16.575  1.00 38.04           N  
ATOM    583  CA  GLU A  81      13.910  48.719  16.278  1.00 38.39           C  
ATOM    584  C   GLU A  81      13.106  48.613  17.567  1.00 37.34           C  
ATOM    585  O   GLU A  81      13.249  47.643  18.309  1.00 38.01           O  
ATOM    586  CB  GLU A  81      13.123  48.114  15.116  1.00 39.40           C  
ATOM    587  CG  GLU A  81      12.678  46.697  15.358  1.00 41.01           C  
ATOM    588  CD  GLU A  81      11.691  46.222  14.321  1.00 43.21           C  
ATOM    589  OE1 GLU A  81      10.611  46.843  14.212  1.00 44.26           O  
ATOM    590  OE2 GLU A  81      11.993  45.228  13.621  1.00 44.24           O  
ATOM    591  N   PHE A  82      12.259  49.593  17.834  1.00 36.16           N  
ATOM    592  CA  PHE A  82      11.478  49.605  19.061  1.00 34.03           C  
ATOM    593  C   PHE A  82      10.027  49.156  18.913  1.00 33.76           C  
ATOM    594  O   PHE A  82       9.356  49.539  17.962  1.00 34.60           O  
ATOM    595  CB  PHE A  82      11.509  51.018  19.639  1.00 35.20           C  
ATOM    596  CG  PHE A  82      10.709  51.179  20.887  1.00 35.85           C  
ATOM    597  CD1 PHE A  82      11.250  50.844  22.121  1.00 34.93           C  
ATOM    598  CD2 PHE A  82       9.405  51.655  20.831  1.00 35.86           C  
ATOM    599  CE1 PHE A  82      10.503  50.983  23.287  1.00 35.55           C  
ATOM    600  CE2 PHE A  82       8.651  51.795  21.994  1.00 37.46           C  
ATOM    601  CZ  PHE A  82       9.205  51.458  23.225  1.00 34.92           C  
ATOM    602  N   LEU A  83       9.563  48.322  19.847  1.00 33.41           N  
ATOM    603  CA  LEU A  83       8.174  47.862  19.891  1.00 33.90           C  
ATOM    604  C   LEU A  83       7.674  48.175  21.307  1.00 36.10           C  
ATOM    605  O   LEU A  83       8.412  48.002  22.280  1.00 34.56           O  
ATOM    606  CB  LEU A  83       8.057  46.372  19.558  1.00 32.85           C  
ATOM    607  CG  LEU A  83       8.142  46.163  18.038  1.00 33.67           C  
ATOM    608  CD1 LEU A  83       9.605  46.162  17.645  1.00 34.17           C  
ATOM    609  CD2 LEU A  83       7.475  44.860  17.607  1.00 31.98           C  
ATOM    610  N   HIS A  84       6.429  48.641  21.416  1.00 37.41           N  
ATOM    611  CA  HIS A  84       5.876  49.072  22.700  1.00 40.43           C  
ATOM    612  C   HIS A  84       5.503  48.059  23.748  1.00 41.94           C  
ATOM    613  O   HIS A  84       5.177  48.441  24.876  1.00 42.32           O  
ATOM    614  CB  HIS A  84       4.648  49.964  22.488  1.00 44.06           C  
ATOM    615  CG  HIS A  84       4.942  51.243  21.776  1.00 44.49           C  
ATOM    616  ND1 HIS A  84       5.286  51.289  20.442  1.00 45.53           N  
ATOM    617  CD2 HIS A  84       4.961  52.523  22.215  1.00 47.08           C  
ATOM    618  CE1 HIS A  84       5.506  52.544  20.090  1.00 47.77           C  
ATOM    619  NE2 HIS A  84       5.316  53.313  21.148  1.00 48.14           N  
ATOM    620  N   GLN A  85       5.528  46.778  23.416  1.00 41.98           N  
ATOM    621  CA  GLN A  85       5.139  45.810  24.425  1.00 40.67           C  
ATOM    622  C   GLN A  85       5.618  44.409  24.145  1.00 38.39           C  
ATOM    623  O   GLN A  85       5.784  44.022  22.992  1.00 38.30           O  
ATOM    624  CB  GLN A  85       3.619  45.808  24.547  1.00 42.00           C  
ATOM    625  CG  GLN A  85       3.095  45.080  25.758  1.00 47.27           C  
ATOM    626  CD  GLN A  85       1.620  45.322  25.962  1.00 50.40           C  
ATOM    627  OE1 GLN A  85       0.780  44.768  25.252  1.00 53.37           O  
ATOM    628  NE2 GLN A  85       1.293  46.171  26.926  1.00 53.44           N  
ATOM    629  N   ASP A  86       5.865  43.655  25.209  1.00 36.88           N  
ATOM    630  CA  ASP A  86       6.265  42.268  25.046  1.00 36.70           C  
ATOM    631  C   ASP A  86       5.058  41.416  25.411  1.00 36.77           C  
ATOM    632  O   ASP A  86       4.108  41.903  26.042  1.00 34.67           O  
ATOM    633  CB  ASP A  86       7.485  41.897  25.914  1.00 37.11           C  
ATOM    634  CG  ASP A  86       7.279  42.162  27.396  1.00 36.73           C  
ATOM    635  OD1 ASP A  86       6.176  41.903  27.924  1.00 35.96           O  
ATOM    636  OD2 ASP A  86       8.248  42.612  28.039  1.00 37.38           O  
ATOM    637  N   LEU A  87       5.099  40.154  24.999  1.00 37.08           N  
ATOM    638  CA  LEU A  87       4.017  39.216  25.239  1.00 38.50           C  
ATOM    639  C   LEU A  87       3.757  38.973  26.722  1.00 41.53           C  
ATOM    640  O   LEU A  87       2.601  38.876  27.152  1.00 42.86           O  
ATOM    641  CB  LEU A  87       4.324  37.886  24.542  1.00 36.41           C  
ATOM    642  CG  LEU A  87       3.193  36.851  24.508  1.00 34.79           C  
ATOM    643  CD1 LEU A  87       2.051  37.387  23.643  1.00 33.09           C  
ATOM    644  CD2 LEU A  87       3.713  35.527  23.952  1.00 30.09           C  
ATOM    645  N   LYS A  88       4.825  38.874  27.506  1.00 43.17           N  
ATOM    646  CA  LYS A  88       4.671  38.633  28.932  1.00 45.48           C  
ATOM    647  C   LYS A  88       3.727  39.656  29.536  1.00 44.88           C  
ATOM    648  O   LYS A  88       2.816  39.307  30.283  1.00 45.02           O  
ATOM    649  CB  LYS A  88       6.027  38.695  29.638  1.00 46.24           C  
ATOM    650  CG  LYS A  88       5.927  38.577  31.140  1.00 47.66           C  
ATOM    651  CD  LYS A  88       5.107  37.366  31.538  1.00 51.43           C  
ATOM    652  CE  LYS A  88       4.863  37.353  33.033  1.00 54.07           C  
ATOM    653  NZ  LYS A  88       6.156  37.425  33.768  1.00 56.41           N  
ATOM    654  N   LYS A  89       3.948  40.919  29.185  1.00 45.67           N  
ATOM    655  CA  LYS A  89       3.139  42.035  29.667  1.00 45.70           C  
ATOM    656  C   LYS A  89       1.703  41.984  29.140  1.00 43.66           C  
ATOM    657  O   LYS A  89       0.755  42.206  29.884  1.00 44.49           O  
ATOM    658  CB  LYS A  89       3.796  43.349  29.247  1.00 49.39           C  
ATOM    659  CG  LYS A  89       3.257  44.567  29.956  1.00 54.26           C  
ATOM    660  CD  LYS A  89       3.385  44.398  31.466  1.00 61.98           C  
ATOM    661  CE  LYS A  89       4.828  44.118  31.892  1.00 64.57           C  
ATOM    662  NZ  LYS A  89       4.949  43.921  33.368  1.00 66.44           N  
ATOM    663  N   PHE A  90       1.551  41.697  27.851  1.00 41.74           N  
ATOM    664  CA  PHE A  90       0.236  41.605  27.228  1.00 40.94           C  
ATOM    665  C   PHE A  90      -0.517  40.446  27.877  1.00 41.52           C  
ATOM    666  O   PHE A  90      -1.701  40.538  28.191  1.00 40.47           O  
ATOM    667  CB  PHE A  90       0.406  41.361  25.722  1.00 39.52           C  
ATOM    668  CG  PHE A  90      -0.891  41.235  24.962  1.00 38.39           C  
ATOM    669  CD1 PHE A  90      -1.857  42.235  25.024  1.00 37.89           C  
ATOM    670  CD2 PHE A  90      -1.125  40.134  24.143  1.00 37.41           C  
ATOM    671  CE1 PHE A  90      -3.034  42.142  24.279  1.00 35.83           C  
ATOM    672  CE2 PHE A  90      -2.299  40.033  23.394  1.00 37.29           C  
ATOM    673  CZ  PHE A  90      -3.253  41.039  23.461  1.00 34.94           C  
ATOM    674  N   MET A  91       0.199  39.352  28.082  1.00 43.09           N  
ATOM    675  CA  MET A  91      -0.365  38.164  28.696  1.00 44.59           C  
ATOM    676  C   MET A  91      -0.880  38.492  30.099  1.00 46.35           C  
ATOM    677  O   MET A  91      -1.954  38.039  30.491  1.00 48.32           O  
ATOM    678  CB  MET A  91       0.708  37.086  28.758  1.00 43.06           C  
ATOM    679  CG  MET A  91       0.222  35.704  28.438  1.00 43.41           C  
ATOM    680  SD  MET A  91       1.569  34.711  27.779  1.00 45.52           S  
ATOM    681  CE  MET A  91       2.904  35.101  28.960  1.00 41.27           C  
ATOM    682  N   ASP A  92      -0.115  39.273  30.859  1.00 48.53           N  
ATOM    683  CA  ASP A  92      -0.541  39.657  32.205  1.00 50.64           C  
ATOM    684  C   ASP A  92      -1.734  40.602  32.107  1.00 52.79           C  
ATOM    685  O   ASP A  92      -2.651  40.546  32.925  1.00 52.95           O  
ATOM    686  CB  ASP A  92       0.591  40.353  32.974  1.00 50.62           C  
ATOM    687  CG  ASP A  92       1.776  39.435  33.238  1.00 53.14           C  
ATOM    688  OD1 ASP A  92       1.608  38.197  33.185  1.00 54.36           O  
ATOM    689  OD2 ASP A  92       2.881  39.952  33.513  1.00 54.88           O  
ATOM    690  N   ALA A  93      -1.719  41.462  31.092  1.00 54.83           N  
ATOM    691  CA  ALA A  93      -2.797  42.425  30.873  1.00 55.72           C  
ATOM    692  C   ALA A  93      -4.053  41.777  30.293  1.00 56.17           C  
ATOM    693  O   ALA A  93      -5.089  42.430  30.159  1.00 56.55           O  
ATOM    694  CB  ALA A  93      -2.316  43.539  29.947  1.00 57.08           C  
ATOM    695  N   SER A  94      -3.952  40.499  29.937  1.00 55.96           N  
ATOM    696  CA  SER A  94      -5.078  39.759  29.376  1.00 55.08           C  
ATOM    697  C   SER A  94      -5.398  38.610  30.322  1.00 54.88           C  
ATOM    698  O   SER A  94      -6.065  37.650  29.946  1.00 54.59           O  
ATOM    699  CB  SER A  94      -4.714  39.192  27.999  1.00 55.83           C  
ATOM    700  OG  SER A  94      -4.287  40.209  27.108  1.00 56.06           O  
ATOM    701  N   ALA A  95      -4.918  38.723  31.556  1.00 54.69           N  
ATOM    702  CA  ALA A  95      -5.111  37.692  32.573  1.00 55.06           C  
ATOM    703  C   ALA A  95      -6.558  37.292  32.859  1.00 55.79           C  
ATOM    704  O   ALA A  95      -6.870  36.103  32.954  1.00 56.43           O  
ATOM    705  CB  ALA A  95      -4.440  38.124  33.868  1.00 52.49           C  
ATOM    706  N   LEU A  96      -7.436  38.278  33.001  1.00 56.40           N  
ATOM    707  CA  LEU A  96      -8.834  38.010  33.313  1.00 55.41           C  
ATOM    708  C   LEU A  96      -9.630  37.357  32.188  1.00 54.25           C  
ATOM    709  O   LEU A  96     -10.451  36.473  32.438  1.00 53.37           O  
ATOM    710  CB  LEU A  96      -9.532  39.306  33.740  1.00 57.94           C  
ATOM    711  CG  LEU A  96      -8.892  40.155  34.850  1.00 59.09           C  
ATOM    712  CD1 LEU A  96      -9.824  41.314  35.159  1.00 58.96           C  
ATOM    713  CD2 LEU A  96      -8.639  39.327  36.111  1.00 58.43           C  
ATOM    714  N   THR A  97      -9.397  37.788  30.952  1.00 53.30           N  
ATOM    715  CA  THR A  97     -10.129  37.237  29.810  1.00 53.82           C  
ATOM    716  C   THR A  97      -9.311  36.282  28.952  1.00 52.18           C  
ATOM    717  O   THR A  97      -9.854  35.374  28.321  1.00 50.80           O  
ATOM    718  CB  THR A  97     -10.640  38.357  28.888  1.00 54.94           C  
ATOM    719  OG1 THR A  97      -9.541  39.203  28.515  1.00 57.17           O  
ATOM    720  CG2 THR A  97     -11.708  39.181  29.590  1.00 56.31           C  
ATOM    721  N   GLY A  98      -8.002  36.496  28.929  1.00 51.19           N  
ATOM    722  CA  GLY A  98      -7.141  35.658  28.121  1.00 49.46           C  
ATOM    723  C   GLY A  98      -7.107  36.181  26.700  1.00 47.79           C  
ATOM    724  O   GLY A  98      -7.950  36.978  26.297  1.00 49.34           O  
ATOM    725  N   ILE A  99      -6.126  35.731  25.936  1.00 46.08           N  
ATOM    726  CA  ILE A  99      -5.975  36.154  24.554  1.00 43.15           C  
ATOM    727  C   ILE A  99      -6.915  35.337  23.670  1.00 41.75           C  
ATOM    728  O   ILE A  99      -6.975  34.117  23.793  1.00 42.67           O  
ATOM    729  CB  ILE A  99      -4.515  35.939  24.091  1.00 42.71           C  
ATOM    730  CG1 ILE A  99      -3.558  36.540  25.120  1.00 41.31           C  
ATOM    731  CG2 ILE A  99      -4.289  36.584  22.746  1.00 43.59           C  
ATOM    732  CD1 ILE A  99      -2.097  36.355  24.785  1.00 42.97           C  
ATOM    733  N   PRO A 100      -7.675  36.001  22.779  1.00 40.66           N  
ATOM    734  CA  PRO A 100      -8.608  35.303  21.882  1.00 38.87           C  
ATOM    735  C   PRO A 100      -7.867  34.294  21.015  1.00 37.69           C  
ATOM    736  O   PRO A 100      -6.820  34.613  20.462  1.00 38.33           O  
ATOM    737  CB  PRO A 100      -9.205  36.438  21.048  1.00 38.49           C  
ATOM    738  CG  PRO A 100      -9.143  37.612  21.973  1.00 37.51           C  
ATOM    739  CD  PRO A 100      -7.780  37.463  22.609  1.00 39.34           C  
ATOM    740  N   LEU A 101      -8.409  33.087  20.889  1.00 37.47           N  
ATOM    741  CA  LEU A 101      -7.764  32.051  20.088  1.00 37.83           C  
ATOM    742  C   LEU A 101      -7.213  32.581  18.770  1.00 37.31           C  
ATOM    743  O   LEU A 101      -6.046  32.359  18.445  1.00 38.01           O  
ATOM    744  CB  LEU A 101      -8.728  30.894  19.788  1.00 38.38           C  
ATOM    745  CG  LEU A 101      -8.141  29.896  18.770  1.00 42.04           C  
ATOM    746  CD1 LEU A 101      -6.849  29.316  19.322  1.00 40.38           C  
ATOM    747  CD2 LEU A 101      -9.132  28.782  18.455  1.00 42.68           C  
ATOM    748  N   PRO A 102      -8.049  33.287  17.990  1.00 35.70           N  
ATOM    749  CA  PRO A 102      -7.613  33.835  16.706  1.00 33.15           C  
ATOM    750  C   PRO A 102      -6.281  34.560  16.802  1.00 32.54           C  
ATOM    751  O   PRO A 102      -5.450  34.452  15.902  1.00 32.36           O  
ATOM    752  CB  PRO A 102      -8.754  34.779  16.335  1.00 32.93           C  
ATOM    753  CG  PRO A 102      -9.932  34.099  16.890  1.00 32.27           C  
ATOM    754  CD  PRO A 102      -9.444  33.676  18.264  1.00 35.38           C  
ATOM    755  N   LEU A 103      -6.085  35.300  17.894  1.00 31.99           N  
ATOM    756  CA  LEU A 103      -4.850  36.051  18.091  1.00 31.99           C  
ATOM    757  C   LEU A 103      -3.702  35.116  18.458  1.00 32.09           C  
ATOM    758  O   LEU A 103      -2.584  35.288  17.988  1.00 32.58           O  
ATOM    759  CB  LEU A 103      -5.033  37.112  19.175  1.00 33.15           C  
ATOM    760  CG  LEU A 103      -3.896  38.132  19.310  1.00 34.81           C  
ATOM    761  CD1 LEU A 103      -3.792  38.942  18.026  1.00 33.32           C  
ATOM    762  CD2 LEU A 103      -4.147  39.053  20.497  1.00 33.38           C  
ATOM    763  N   ILE A 104      -3.990  34.121  19.289  1.00 30.98           N  
ATOM    764  CA  ILE A 104      -2.993  33.149  19.694  1.00 29.32           C  
ATOM    765  C   ILE A 104      -2.454  32.453  18.453  1.00 29.98           C  
ATOM    766  O   ILE A 104      -1.241  32.381  18.239  1.00 30.16           O  
ATOM    767  CB  ILE A 104      -3.610  32.098  20.623  1.00 28.79           C  
ATOM    768  CG1 ILE A 104      -3.886  32.719  21.986  1.00 26.65           C  
ATOM    769  CG2 ILE A 104      -2.694  30.879  20.740  1.00 29.92           C  
ATOM    770  CD1 ILE A 104      -4.631  31.807  22.926  1.00 23.12           C  
ATOM    771  N   LYS A 105      -3.375  31.955  17.638  1.00 28.56           N  
ATOM    772  CA  LYS A 105      -3.044  31.246  16.411  1.00 29.82           C  
ATOM    773  C   LYS A 105      -2.239  32.101  15.418  1.00 31.43           C  
ATOM    774  O   LYS A 105      -1.360  31.592  14.711  1.00 33.67           O  
ATOM    775  CB  LYS A 105      -4.338  30.739  15.768  1.00 30.80           C  
ATOM    776  CG  LYS A 105      -4.149  29.927  14.505  1.00 31.27           C  
ATOM    777  CD  LYS A 105      -5.483  29.422  13.962  1.00 31.82           C  
ATOM    778  CE  LYS A 105      -6.188  28.537  14.971  1.00 32.20           C  
ATOM    779  NZ  LYS A 105      -7.303  27.778  14.358  1.00 33.22           N  
ATOM    780  N   SER A 106      -2.527  33.397  15.375  1.00 31.93           N  
ATOM    781  CA  SER A 106      -1.822  34.312  14.478  1.00 29.82           C  
ATOM    782  C   SER A 106      -0.390  34.520  14.952  1.00 30.17           C  
ATOM    783  O   SER A 106       0.545  34.491  14.156  1.00 32.62           O  
ATOM    784  CB  SER A 106      -2.542  35.660  14.422  1.00 29.55           C  
ATOM    785  OG  SER A 106      -1.806  36.590  13.642  1.00 30.92           O  
ATOM    786  N   TYR A 107      -0.226  34.738  16.254  1.00 29.43           N  
ATOM    787  CA  TYR A 107       1.088  34.938  16.856  1.00 28.33           C  
ATOM    788  C   TYR A 107       2.003  33.714  16.690  1.00 27.84           C  
ATOM    789  O   TYR A 107       3.165  33.849  16.322  1.00 29.06           O  
ATOM    790  CB  TYR A 107       0.936  35.264  18.345  1.00 27.06           C  
ATOM    791  CG  TYR A 107       0.483  36.683  18.654  1.00 27.68           C  
ATOM    792  CD1 TYR A 107       0.357  37.653  17.650  1.00 26.05           C  
ATOM    793  CD2 TYR A 107       0.222  37.068  19.966  1.00 26.17           C  
ATOM    794  CE1 TYR A 107      -0.013  38.959  17.959  1.00 25.54           C  
ATOM    795  CE2 TYR A 107      -0.142  38.359  20.279  1.00 27.30           C  
ATOM    796  CZ  TYR A 107      -0.261  39.302  19.279  1.00 26.68           C  
ATOM    797  OH  TYR A 107      -0.640  40.576  19.631  1.00 29.13           O  
ATOM    798  N   LEU A 108       1.485  32.522  16.971  1.00 28.30           N  
ATOM    799  CA  LEU A 108       2.287  31.313  16.822  1.00 29.99           C  
ATOM    800  C   LEU A 108       2.690  31.154  15.355  1.00 30.36           C  
ATOM    801  O   LEU A 108       3.825  30.810  15.033  1.00 30.30           O  
ATOM    802  CB  LEU A 108       1.494  30.092  17.276  1.00 27.98           C  
ATOM    803  CG  LEU A 108       2.239  28.753  17.308  1.00 28.39           C  
ATOM    804  CD1 LEU A 108       3.335  28.782  18.363  1.00 23.90           C  
ATOM    805  CD2 LEU A 108       1.239  27.633  17.616  1.00 29.33           C  
ATOM    806  N   PHE A 109       1.748  31.427  14.464  1.00 32.11           N  
ATOM    807  CA  PHE A 109       1.995  31.316  13.034  1.00 30.62           C  
ATOM    808  C   PHE A 109       3.148  32.223  12.606  1.00 30.24           C  
ATOM    809  O   PHE A 109       4.034  31.803  11.864  1.00 31.46           O  
ATOM    810  CB  PHE A 109       0.722  31.682  12.260  1.00 31.95           C  
ATOM    811  CG  PHE A 109       0.792  31.350  10.800  1.00 33.87           C  
ATOM    812  CD1 PHE A 109       0.712  30.027  10.370  1.00 33.35           C  
ATOM    813  CD2 PHE A 109       0.994  32.352   9.853  1.00 34.79           C  
ATOM    814  CE1 PHE A 109       0.834  29.702   9.018  1.00 32.14           C  
ATOM    815  CE2 PHE A 109       1.120  32.036   8.502  1.00 34.91           C  
ATOM    816  CZ  PHE A 109       1.040  30.704   8.085  1.00 32.53           C  
ATOM    817  N   GLN A 110       3.129  33.468  13.077  1.00 28.72           N  
ATOM    818  CA  GLN A 110       4.174  34.445  12.753  1.00 27.66           C  
ATOM    819  C   GLN A 110       5.510  34.076  13.397  1.00 27.69           C  
ATOM    820  O   GLN A 110       6.570  34.273  12.809  1.00 27.21           O  
ATOM    821  CB  GLN A 110       3.767  35.847  13.236  1.00 26.30           C  
ATOM    822  CG  GLN A 110       2.598  36.462  12.504  1.00 23.44           C  
ATOM    823  CD  GLN A 110       2.193  37.782  13.099  1.00 26.13           C  
ATOM    824  OE1 GLN A 110       2.967  38.748  13.099  1.00 29.50           O  
ATOM    825  NE2 GLN A 110       0.976  37.838  13.623  1.00 26.56           N  
ATOM    826  N   LEU A 111       5.446  33.576  14.626  1.00 27.97           N  
ATOM    827  CA  LEU A 111       6.632  33.167  15.352  1.00 27.94           C  
ATOM    828  C   LEU A 111       7.243  31.963  14.633  1.00 26.85           C  
ATOM    829  O   LEU A 111       8.456  31.880  14.457  1.00 27.15           O  
ATOM    830  CB  LEU A 111       6.247  32.837  16.798  1.00 30.19           C  
ATOM    831  CG  LEU A 111       6.505  33.906  17.883  1.00 34.72           C  
ATOM    832  CD1 LEU A 111       6.880  35.259  17.275  1.00 31.31           C  
ATOM    833  CD2 LEU A 111       5.280  34.027  18.779  1.00 32.02           C  
ATOM    834  N   LEU A 112       6.396  31.037  14.203  1.00 26.66           N  
ATOM    835  CA  LEU A 112       6.874  29.877  13.472  1.00 27.97           C  
ATOM    836  C   LEU A 112       7.520  30.374  12.186  1.00 29.10           C  
ATOM    837  O   LEU A 112       8.489  29.781  11.693  1.00 28.94           O  
ATOM    838  CB  LEU A 112       5.718  28.924  13.149  1.00 28.33           C  
ATOM    839  CG  LEU A 112       5.245  28.021  14.286  1.00 27.75           C  
ATOM    840  CD1 LEU A 112       4.085  27.172  13.801  1.00 27.34           C  
ATOM    841  CD2 LEU A 112       6.393  27.136  14.756  1.00 25.67           C  
ATOM    842  N   GLN A 113       6.977  31.462  11.642  1.00 29.87           N  
ATOM    843  CA  GLN A 113       7.532  32.065  10.428  1.00 31.37           C  
ATOM    844  C   GLN A 113       8.921  32.653  10.691  1.00 32.32           C  
ATOM    845  O   GLN A 113       9.851  32.464   9.904  1.00 33.53           O  
ATOM    846  CB  GLN A 113       6.600  33.157   9.910  1.00 34.33           C  
ATOM    847  CG  GLN A 113       5.657  32.685   8.821  1.00 37.18           C  
ATOM    848  CD  GLN A 113       4.618  33.726   8.449  1.00 41.25           C  
ATOM    849  OE1 GLN A 113       4.193  33.800   7.297  1.00 45.60           O  
ATOM    850  NE2 GLN A 113       4.192  34.526   9.424  1.00 43.25           N  
ATOM    851  N   GLY A 114       9.062  33.366  11.803  1.00 32.64           N  
ATOM    852  CA  GLY A 114      10.347  33.937  12.138  1.00 32.66           C  
ATOM    853  C   GLY A 114      11.343  32.816  12.346  1.00 32.87           C  
ATOM    854  O   GLY A 114      12.459  32.848  11.836  1.00 34.15           O  
ATOM    855  N   LEU A 115      10.930  31.804  13.096  1.00 34.18           N  
ATOM    856  CA  LEU A 115      11.792  30.663  13.372  1.00 33.39           C  
ATOM    857  C   LEU A 115      12.233  29.947  12.098  1.00 33.52           C  
ATOM    858  O   LEU A 115      13.426  29.698  11.912  1.00 35.03           O  
ATOM    859  CB  LEU A 115      11.084  29.695  14.313  1.00 33.37           C  
ATOM    860  CG  LEU A 115      11.600  29.660  15.754  1.00 34.30           C  
ATOM    861  CD1 LEU A 115      11.892  31.050  16.261  1.00 35.20           C  
ATOM    862  CD2 LEU A 115      10.570  28.978  16.629  1.00 35.18           C  
ATOM    863  N   ALA A 116      11.292  29.627  11.214  1.00 31.24           N  
ATOM    864  CA  ALA A 116      11.655  28.955   9.973  1.00 30.28           C  
ATOM    865  C   ALA A 116      12.767  29.740   9.268  1.00 32.30           C  
ATOM    866  O   ALA A 116      13.749  29.161   8.809  1.00 34.03           O  
ATOM    867  CB  ALA A 116      10.441  28.821   9.073  1.00 25.57           C  
ATOM    868  N   PHE A 117      12.623  31.061   9.198  1.00 33.50           N  
ATOM    869  CA  PHE A 117      13.631  31.918   8.556  1.00 32.08           C  
ATOM    870  C   PHE A 117      15.012  31.790   9.209  1.00 32.28           C  
ATOM    871  O   PHE A 117      16.014  31.540   8.544  1.00 30.47           O  
ATOM    872  CB  PHE A 117      13.206  33.392   8.630  1.00 29.83           C  
ATOM    873  CG  PHE A 117      14.203  34.342   8.017  1.00 31.48           C  
ATOM    874  CD1 PHE A 117      14.265  34.519   6.633  1.00 31.28           C  
ATOM    875  CD2 PHE A 117      15.097  35.046   8.817  1.00 33.18           C  
ATOM    876  CE1 PHE A 117      15.202  35.380   6.058  1.00 32.56           C  
ATOM    877  CE2 PHE A 117      16.042  35.914   8.250  1.00 35.21           C  
ATOM    878  CZ  PHE A 117      16.094  36.079   6.867  1.00 33.32           C  
ATOM    879  N   CYS A 118      15.059  31.993  10.518  1.00 34.47           N  
ATOM    880  CA  CYS A 118      16.313  31.918  11.246  1.00 37.67           C  
ATOM    881  C   CYS A 118      16.942  30.545  11.126  1.00 37.81           C  
ATOM    882  O   CYS A 118      18.141  30.420  10.876  1.00 37.54           O  
ATOM    883  CB  CYS A 118      16.082  32.249  12.720  1.00 39.07           C  
ATOM    884  SG  CYS A 118      15.560  33.947  12.982  1.00 48.67           S  
ATOM    885  N   HIS A 119      16.123  29.517  11.313  1.00 37.11           N  
ATOM    886  CA  HIS A 119      16.598  28.154  11.231  1.00 38.97           C  
ATOM    887  C   HIS A 119      17.114  27.788   9.842  1.00 41.70           C  
ATOM    888  O   HIS A 119      18.094  27.052   9.723  1.00 42.75           O  
ATOM    889  CB  HIS A 119      15.493  27.196  11.675  1.00 38.09           C  
ATOM    890  CG  HIS A 119      15.182  27.286  13.138  1.00 36.79           C  
ATOM    891  ND1 HIS A 119      14.102  26.652  13.713  1.00 36.14           N  
ATOM    892  CD2 HIS A 119      15.801  27.957  14.139  1.00 35.00           C  
ATOM    893  CE1 HIS A 119      14.068  26.932  15.003  1.00 36.58           C  
ATOM    894  NE2 HIS A 119      15.087  27.723  15.287  1.00 33.42           N  
ATOM    895  N   SER A 120      16.479  28.301   8.793  1.00 42.83           N  
ATOM    896  CA  SER A 120      16.942  27.990   7.446  1.00 44.59           C  
ATOM    897  C   SER A 120      18.340  28.583   7.240  1.00 45.63           C  
ATOM    898  O   SER A 120      19.107  28.095   6.416  1.00 47.74           O  
ATOM    899  CB  SER A 120      15.977  28.537   6.389  1.00 42.96           C  
ATOM    900  OG  SER A 120      16.216  29.908   6.137  1.00 45.41           O  
ATOM    901  N   HIS A 121      18.672  29.630   7.988  1.00 47.48           N  
ATOM    902  CA  HIS A 121      19.994  30.251   7.878  1.00 49.61           C  
ATOM    903  C   HIS A 121      20.921  29.711   8.970  1.00 50.65           C  
ATOM    904  O   HIS A 121      21.977  30.286   9.249  1.00 50.67           O  
ATOM    905  CB  HIS A 121      19.888  31.780   7.984  1.00 50.61           C  
ATOM    906  CG  HIS A 121      19.292  32.433   6.773  1.00 53.14           C  
ATOM    907  ND1 HIS A 121      18.003  32.188   6.350  1.00 54.18           N  
ATOM    908  CD2 HIS A 121      19.817  33.307   5.882  1.00 54.69           C  
ATOM    909  CE1 HIS A 121      17.761  32.878   5.250  1.00 54.27           C  
ATOM    910  NE2 HIS A 121      18.846  33.566   4.945  1.00 55.18           N  
ATOM    911  N   ARG A 122      20.510  28.596   9.573  1.00 50.71           N  
ATOM    912  CA  ARG A 122      21.259  27.934  10.635  1.00 50.58           C  
ATOM    913  C   ARG A 122      21.532  28.801  11.861  1.00 48.25           C  
ATOM    914  O   ARG A 122      22.629  28.770  12.421  1.00 48.47           O  
ATOM    915  CB  ARG A 122      22.584  27.381  10.094  1.00 54.82           C  
ATOM    916  CG  ARG A 122      22.414  26.234   9.104  1.00 58.72           C  
ATOM    917  CD  ARG A 122      22.229  26.746   7.682  1.00 65.08           C  
ATOM    918  NE  ARG A 122      23.497  27.166   7.079  1.00 68.65           N  
ATOM    919  CZ  ARG A 122      23.609  27.709   5.870  1.00 69.75           C  
ATOM    920  NH1 ARG A 122      22.527  27.907   5.125  1.00 69.27           N  
ATOM    921  NH2 ARG A 122      24.804  28.051   5.403  1.00 69.09           N  
ATOM    922  N   VAL A 123      20.531  29.574  12.270  1.00 44.29           N  
ATOM    923  CA  VAL A 123      20.644  30.433  13.441  1.00 41.16           C  
ATOM    924  C   VAL A 123      19.565  30.028  14.433  1.00 40.87           C  
ATOM    925  O   VAL A 123      18.405  29.834  14.059  1.00 39.09           O  
ATOM    926  CB  VAL A 123      20.454  31.925  13.081  1.00 40.43           C  
ATOM    927  CG1 VAL A 123      20.419  32.783  14.341  1.00 37.87           C  
ATOM    928  CG2 VAL A 123      21.579  32.381  12.190  1.00 40.70           C  
ATOM    929  N   LEU A 124      19.958  29.896  15.695  1.00 39.16           N  
ATOM    930  CA  LEU A 124      19.036  29.522  16.750  1.00 38.64           C  
ATOM    931  C   LEU A 124      18.891  30.683  17.717  1.00 37.38           C  
ATOM    932  O   LEU A 124      19.761  31.547  17.787  1.00 37.87           O  
ATOM    933  CB  LEU A 124      19.573  28.324  17.538  1.00 39.52           C  
ATOM    934  CG  LEU A 124      19.854  26.984  16.877  1.00 42.16           C  
ATOM    935  CD1 LEU A 124      20.931  27.132  15.812  1.00 43.57           C  
ATOM    936  CD2 LEU A 124      20.297  26.001  17.957  1.00 41.81           C  
ATOM    937  N   HIS A 125      17.796  30.705  18.469  1.00 36.46           N  
ATOM    938  CA  HIS A 125      17.621  31.747  19.464  1.00 35.47           C  
ATOM    939  C   HIS A 125      18.221  31.210  20.754  1.00 36.29           C  
ATOM    940  O   HIS A 125      18.954  31.914  21.446  1.00 37.39           O  
ATOM    941  CB  HIS A 125      16.156  32.066  19.702  1.00 33.42           C  
ATOM    942  CG  HIS A 125      15.957  33.190  20.667  1.00 32.38           C  
ATOM    943  ND1 HIS A 125      15.529  34.440  20.276  1.00 30.85           N  
ATOM    944  CD2 HIS A 125      16.191  33.270  21.998  1.00 29.68           C  
ATOM    945  CE1 HIS A 125      15.512  35.242  21.325  1.00 30.82           C  
ATOM    946  NE2 HIS A 125      15.910  34.557  22.382  1.00 30.38           N  
ATOM    947  N   ARG A 126      17.890  29.958  21.064  1.00 35.82           N  
ATOM    948  CA  ARG A 126      18.393  29.258  22.237  0.59 36.72           C  
ATOM    949  C   ARG A 126      17.766  29.681  23.557  1.00 37.62           C  
ATOM    950  O   ARG A 126      17.901  28.979  24.556  1.00 39.44           O  
ATOM    951  CB  ARG A 126      19.918  29.392  22.304  0.59 37.61           C  
ATOM    952  CG  ARG A 126      20.629  28.913  21.028  0.59 38.56           C  
ATOM    953  CD  ARG A 126      22.074  29.402  20.959  0.59 39.58           C  
ATOM    954  NE  ARG A 126      22.717  29.099  19.679  0.59 40.58           N  
ATOM    955  CZ  ARG A 126      23.379  27.976  19.406  0.59 41.94           C  
ATOM    956  NH1 ARG A 126      23.500  27.027  20.326  0.59 42.16           N  
ATOM    957  NH2 ARG A 126      23.918  27.799  18.204  0.59 41.72           N  
ATOM    958  N   ASP A 127      17.063  30.807  23.578  1.00 38.33           N  
ATOM    959  CA  ASP A 127      16.438  31.248  24.818  1.00 36.40           C  
ATOM    960  C   ASP A 127      15.116  32.014  24.688  1.00 35.05           C  
ATOM    961  O   ASP A 127      14.921  33.054  25.325  1.00 34.33           O  
ATOM    962  CB  ASP A 127      17.435  32.071  25.625  1.00 40.45           C  
ATOM    963  CG  ASP A 127      16.877  32.510  26.958  1.00 45.66           C  
ATOM    964  OD1 ASP A 127      16.257  31.674  27.656  1.00 48.93           O  
ATOM    965  OD2 ASP A 127      17.062  33.693  27.313  1.00 49.37           O  
ATOM    966  N   LEU A 128      14.200  31.502  23.872  1.00 31.95           N  
ATOM    967  CA  LEU A 128      12.909  32.155  23.717  1.00 31.92           C  
ATOM    968  C   LEU A 128      12.160  32.187  25.047  1.00 31.02           C  
ATOM    969  O   LEU A 128      12.294  31.281  25.864  1.00 32.26           O  
ATOM    970  CB  LEU A 128      12.049  31.430  22.687  1.00 31.93           C  
ATOM    971  CG  LEU A 128      12.561  31.387  21.253  1.00 32.98           C  
ATOM    972  CD1 LEU A 128      11.531  30.693  20.392  1.00 31.85           C  
ATOM    973  CD2 LEU A 128      12.814  32.802  20.750  1.00 35.09           C  
ATOM    974  N   LYS A 129      11.363  33.230  25.242  1.00 30.06           N  
ATOM    975  CA  LYS A 129      10.582  33.410  26.451  1.00 30.83           C  
ATOM    976  C   LYS A 129       9.632  34.550  26.152  1.00 31.99           C  
ATOM    977  O   LYS A 129       9.904  35.373  25.279  1.00 33.46           O  
ATOM    978  CB  LYS A 129      11.483  33.770  27.626  1.00 33.78           C  
ATOM    979  CG  LYS A 129      12.306  35.024  27.412  1.00 39.80           C  
ATOM    980  CD  LYS A 129      12.824  35.558  28.740  1.00 43.77           C  
ATOM    981  CE  LYS A 129      13.894  34.667  29.330  1.00 46.31           C  
ATOM    982  NZ  LYS A 129      15.172  34.813  28.581  1.00 46.37           N  
ATOM    983  N   PRO A 130       8.492  34.608  26.853  1.00 31.53           N  
ATOM    984  CA  PRO A 130       7.503  35.667  26.635  1.00 31.91           C  
ATOM    985  C   PRO A 130       8.049  37.083  26.628  1.00 32.74           C  
ATOM    986  O   PRO A 130       7.551  37.930  25.894  1.00 35.52           O  
ATOM    987  CB  PRO A 130       6.505  35.430  27.758  1.00 31.55           C  
ATOM    988  CG  PRO A 130       6.489  33.928  27.833  1.00 28.37           C  
ATOM    989  CD  PRO A 130       7.976  33.608  27.803  1.00 30.03           C  
ATOM    990  N   GLN A 131       9.069  37.341  27.437  1.00 33.53           N  
ATOM    991  CA  GLN A 131       9.663  38.670  27.503  1.00 34.32           C  
ATOM    992  C   GLN A 131      10.501  38.989  26.272  1.00 33.65           C  
ATOM    993  O   GLN A 131      10.906  40.132  26.089  1.00 36.44           O  
ATOM    994  CB  GLN A 131      10.552  38.830  28.750  1.00 35.21           C  
ATOM    995  CG  GLN A 131       9.927  38.417  30.089  1.00 38.42           C  
ATOM    996  CD  GLN A 131      10.067  36.921  30.365  1.00 40.24           C  
ATOM    997  OE1 GLN A 131       9.262  36.103  29.911  1.00 36.64           O  
ATOM    998  NE2 GLN A 131      11.111  36.561  31.102  1.00 43.15           N  
ATOM    999  N   ASN A 132      10.765  37.985  25.440  1.00 34.81           N  
ATOM   1000  CA  ASN A 132      11.568  38.160  24.217  1.00 36.00           C  
ATOM   1001  C   ASN A 132      10.727  38.208  22.939  1.00 34.69           C  
ATOM   1002  O   ASN A 132      11.264  38.138  21.832  1.00 32.84           O  
ATOM   1003  CB  ASN A 132      12.590  37.025  24.075  1.00 39.29           C  
ATOM   1004  CG  ASN A 132      13.733  37.145  25.051  1.00 44.31           C  
ATOM   1005  OD1 ASN A 132      14.616  36.290  25.094  1.00 49.11           O  
ATOM   1006  ND2 ASN A 132      13.731  38.211  25.841  1.00 48.15           N  
ATOM   1007  N   LEU A 133       9.410  38.293  23.093  1.00 32.76           N  
ATOM   1008  CA  LEU A 133       8.522  38.358  21.949  1.00 32.87           C  
ATOM   1009  C   LEU A 133       7.826  39.711  22.050  1.00 33.11           C  
ATOM   1010  O   LEU A 133       7.152  39.995  23.037  1.00 33.68           O  
ATOM   1011  CB  LEU A 133       7.528  37.188  21.991  1.00 31.32           C  
ATOM   1012  CG  LEU A 133       8.220  35.819  22.130  1.00 31.61           C  
ATOM   1013  CD1 LEU A 133       7.186  34.705  22.280  1.00 27.06           C  
ATOM   1014  CD2 LEU A 133       9.118  35.575  20.921  1.00 27.72           C  
ATOM   1015  N   LEU A 134       8.016  40.557  21.041  1.00 32.71           N  
ATOM   1016  CA  LEU A 134       7.436  41.896  21.063  1.00 31.75           C  
ATOM   1017  C   LEU A 134       6.301  42.079  20.073  1.00 31.06           C  
ATOM   1018  O   LEU A 134       6.339  41.561  18.954  1.00 29.05           O  
ATOM   1019  CB  LEU A 134       8.535  42.913  20.801  1.00 33.93           C  
ATOM   1020  CG  LEU A 134       9.777  42.599  21.641  1.00 34.82           C  
ATOM   1021  CD1 LEU A 134      10.959  43.269  21.028  1.00 35.92           C  
ATOM   1022  CD2 LEU A 134       9.581  43.043  23.072  1.00 32.95           C  
ATOM   1023  N   ILE A 135       5.293  42.828  20.504  1.00 30.74           N  
ATOM   1024  CA  ILE A 135       4.113  43.071  19.691  1.00 33.12           C  
ATOM   1025  C   ILE A 135       3.870  44.553  19.427  1.00 34.07           C  
ATOM   1026  O   ILE A 135       4.256  45.407  20.215  1.00 31.48           O  
ATOM   1027  CB  ILE A 135       2.853  42.514  20.386  1.00 34.37           C  
ATOM   1028  CG1 ILE A 135       2.543  43.356  21.631  1.00 36.31           C  
ATOM   1029  CG2 ILE A 135       3.075  41.046  20.774  1.00 33.77           C  
ATOM   1030  CD1 ILE A 135       1.383  42.850  22.451  1.00 37.81           C  
ATOM   1031  N   ASN A 136       3.233  44.836  18.298  1.00 34.41           N  
ATOM   1032  CA  ASN A 136       2.872  46.191  17.935  1.00 34.56           C  
ATOM   1033  C   ASN A 136       1.352  46.187  17.787  1.00 37.09           C  
ATOM   1034  O   ASN A 136       0.715  45.135  17.793  1.00 39.30           O  
ATOM   1035  CB  ASN A 136       3.526  46.619  16.617  1.00 31.79           C  
ATOM   1036  CG  ASN A 136       3.158  45.715  15.449  1.00 32.87           C  
ATOM   1037  OD1 ASN A 136       2.087  45.093  15.426  1.00 31.98           O  
ATOM   1038  ND2 ASN A 136       4.045  45.649  14.461  1.00 28.71           N  
ATOM   1039  N   THR A 137       0.773  47.366  17.641  1.00 39.60           N  
ATOM   1040  CA  THR A 137      -0.664  47.506  17.509  1.00 40.74           C  
ATOM   1041  C   THR A 137      -1.185  47.045  16.145  1.00 43.16           C  
ATOM   1042  O   THR A 137      -2.388  47.044  15.903  1.00 45.25           O  
ATOM   1043  CB  THR A 137      -1.053  48.966  17.776  1.00 39.45           C  
ATOM   1044  OG1 THR A 137      -0.233  49.831  16.983  1.00 39.45           O  
ATOM   1045  CG2 THR A 137      -0.812  49.312  19.229  1.00 39.01           C  
ATOM   1046  N   GLU A 138      -0.277  46.638  15.264  1.00 44.92           N  
ATOM   1047  CA  GLU A 138      -0.650  46.157  13.932  1.00 46.24           C  
ATOM   1048  C   GLU A 138      -1.056  44.679  13.948  1.00 44.19           C  
ATOM   1049  O   GLU A 138      -1.555  44.156  12.951  1.00 44.45           O  
ATOM   1050  CB  GLU A 138       0.525  46.290  12.961  1.00 50.88           C  
ATOM   1051  CG  GLU A 138       1.293  47.587  13.054  1.00 58.36           C  
ATOM   1052  CD  GLU A 138       0.407  48.779  12.867  1.00 62.02           C  
ATOM   1053  OE1 GLU A 138      -0.395  48.771  11.909  1.00 66.79           O  
ATOM   1054  OE2 GLU A 138       0.512  49.724  13.674  1.00 66.96           O  
ATOM   1055  N   GLY A 139      -0.820  44.000  15.065  1.00 40.88           N  
ATOM   1056  CA  GLY A 139      -1.148  42.588  15.136  1.00 37.12           C  
ATOM   1057  C   GLY A 139       0.072  41.789  14.714  1.00 36.40           C  
ATOM   1058  O   GLY A 139      -0.029  40.656  14.244  1.00 34.78           O  
ATOM   1059  N   ALA A 140       1.238  42.406  14.871  1.00 35.76           N  
ATOM   1060  CA  ALA A 140       2.504  41.779  14.524  1.00 34.57           C  
ATOM   1061  C   ALA A 140       3.211  41.331  15.803  1.00 33.64           C  
ATOM   1062  O   ALA A 140       3.101  41.974  16.844  1.00 35.37           O  
ATOM   1063  CB  ALA A 140       3.375  42.757  13.763  1.00 30.32           C  
ATOM   1064  N   ILE A 141       3.933  40.224  15.718  1.00 32.86           N  
ATOM   1065  CA  ILE A 141       4.653  39.690  16.869  1.00 33.23           C  
ATOM   1066  C   ILE A 141       6.056  39.350  16.344  1.00 32.20           C  
ATOM   1067  O   ILE A 141       6.196  38.710  15.296  1.00 30.62           O  
ATOM   1068  CB  ILE A 141       3.883  38.440  17.440  1.00 31.64           C  
ATOM   1069  CG1 ILE A 141       4.102  38.308  18.953  1.00 31.72           C  
ATOM   1070  CG2 ILE A 141       4.262  37.192  16.684  1.00 31.09           C  
ATOM   1071  CD1 ILE A 141       5.384  37.702  19.359  1.00 33.11           C  
ATOM   1072  N   LYS A 142       7.090  39.821  17.043  1.00 31.62           N  
ATOM   1073  CA  LYS A 142       8.469  39.584  16.606  1.00 31.35           C  
ATOM   1074  C   LYS A 142       9.390  38.979  17.664  1.00 31.11           C  
ATOM   1075  O   LYS A 142       9.216  39.198  18.861  1.00 29.94           O  
ATOM   1076  CB  LYS A 142       9.098  40.896  16.114  1.00 30.16           C  
ATOM   1077  CG  LYS A 142       8.250  41.659  15.122  1.00 31.24           C  
ATOM   1078  CD  LYS A 142       8.954  42.909  14.648  1.00 33.27           C  
ATOM   1079  CE  LYS A 142       8.120  43.639  13.601  1.00 33.32           C  
ATOM   1080  NZ  LYS A 142       8.900  44.673  12.868  1.00 35.28           N  
ATOM   1081  N   LEU A 143      10.383  38.233  17.194  1.00 31.76           N  
ATOM   1082  CA  LEU A 143      11.371  37.598  18.056  1.00 33.58           C  
ATOM   1083  C   LEU A 143      12.500  38.581  18.340  1.00 33.78           C  
ATOM   1084  O   LEU A 143      13.112  39.104  17.420  1.00 33.22           O  
ATOM   1085  CB  LEU A 143      11.940  36.355  17.369  1.00 35.20           C  
ATOM   1086  CG  LEU A 143      10.953  35.199  17.181  1.00 38.75           C  
ATOM   1087  CD1 LEU A 143      11.315  34.376  15.957  1.00 38.53           C  
ATOM   1088  CD2 LEU A 143      10.945  34.342  18.442  1.00 38.98           C  
ATOM   1089  N   ALA A 144      12.771  38.819  19.618  1.00 35.56           N  
ATOM   1090  CA  ALA A 144      13.824  39.732  20.039  1.00 36.10           C  
ATOM   1091  C   ALA A 144      15.024  38.958  20.594  1.00 38.77           C  
ATOM   1092  O   ALA A 144      14.881  37.811  20.997  1.00 38.51           O  
ATOM   1093  CB  ALA A 144      13.278  40.675  21.091  1.00 35.02           C  
ATOM   1094  N   ASP A 145      16.194  39.598  20.617  1.00 40.92           N  
ATOM   1095  CA  ASP A 145      17.440  38.996  21.111  1.00 42.69           C  
ATOM   1096  C   ASP A 145      17.810  37.680  20.453  1.00 43.54           C  
ATOM   1097  O   ASP A 145      18.358  36.778  21.090  1.00 43.34           O  
ATOM   1098  CB  ASP A 145      17.391  38.812  22.626  1.00 43.41           C  
ATOM   1099  CG  ASP A 145      17.276  40.130  23.355  1.00 45.30           C  
ATOM   1100  OD1 ASP A 145      17.467  41.166  22.688  1.00 47.12           O  
ATOM   1101  OD2 ASP A 145      17.002  40.142  24.577  1.00 46.51           O  
ATOM   1102  N   PHE A 146      17.522  37.593  19.163  1.00 44.86           N  
ATOM   1103  CA  PHE A 146      17.812  36.406  18.381  1.00 47.02           C  
ATOM   1104  C   PHE A 146      19.307  36.218  18.137  1.00 47.39           C  
ATOM   1105  O   PHE A 146      20.035  37.178  17.916  1.00 46.79           O  
ATOM   1106  CB  PHE A 146      17.086  36.490  17.039  1.00 48.64           C  
ATOM   1107  CG  PHE A 146      16.553  35.178  16.579  1.00 53.12           C  
ATOM   1108  CD1 PHE A 146      17.418  34.149  16.233  1.00 53.27           C  
ATOM   1109  CD2 PHE A 146      15.183  34.932  16.588  1.00 54.78           C  
ATOM   1110  CE1 PHE A 146      16.926  32.887  15.911  1.00 55.76           C  
ATOM   1111  CE2 PHE A 146      14.682  33.676  16.269  1.00 56.13           C  
ATOM   1112  CZ  PHE A 146      15.555  32.650  15.932  1.00 56.41           C  
ATOM   1113  N   GLY A 147      19.761  34.971  18.179  1.00 49.87           N  
ATOM   1114  CA  GLY A 147      21.166  34.680  17.942  1.00 51.32           C  
ATOM   1115  C   GLY A 147      22.153  35.299  18.916  1.00 52.81           C  
ATOM   1116  O   GLY A 147      23.358  35.104  18.789  1.00 51.13           O  
ATOM   1117  N   LEU A 148      21.653  36.039  19.896  1.00 56.36           N  
ATOM   1118  CA  LEU A 148      22.521  36.676  20.880  1.00 60.48           C  
ATOM   1119  C   LEU A 148      23.057  35.704  21.931  1.00 62.61           C  
ATOM   1120  O   LEU A 148      23.927  36.065  22.717  1.00 62.63           O  
ATOM   1121  CB  LEU A 148      21.778  37.833  21.565  1.00 60.33           C  
ATOM   1122  CG  LEU A 148      22.251  39.256  21.238  1.00 61.33           C  
ATOM   1123  CD1 LEU A 148      22.606  39.384  19.764  1.00 61.12           C  
ATOM   1124  CD2 LEU A 148      21.161  40.241  21.614  1.00 60.53           C  
ATOM   1125  N   ALA A 149      22.544  34.475  21.948  1.00 66.04           N  
ATOM   1126  CA  ALA A 149      23.001  33.480  22.919  1.00 70.50           C  
ATOM   1127  C   ALA A 149      24.309  32.836  22.459  1.00 73.92           C  
ATOM   1128  O   ALA A 149      25.236  32.649  23.247  1.00 73.47           O  
ATOM   1129  CB  ALA A 149      21.931  32.413  23.127  1.00 70.44           C  
ATOM   1130  N   ARG A 150      24.376  32.493  21.179  1.00 78.45           N  
ATOM   1131  CA  ARG A 150      25.577  31.896  20.618  1.00 84.04           C  
ATOM   1132  C   ARG A 150      26.647  32.980  20.560  1.00 88.62           C  
ATOM   1133  O   ARG A 150      27.793  32.758  20.947  1.00 89.43           O  
ATOM   1134  CB  ARG A 150      25.291  31.360  19.213  1.00 83.94           C  
ATOM   1135  CG  ARG A 150      26.513  30.880  18.437  1.00 83.51           C  
ATOM   1136  CD  ARG A 150      26.111  30.453  17.032  1.00 84.45           C  
ATOM   1137  NE  ARG A 150      27.254  30.138  16.180  1.00 85.67           N  
ATOM   1138  CZ  ARG A 150      27.159  29.866  14.881  1.00 86.68           C  
ATOM   1139  NH1 ARG A 150      25.972  29.869  14.287  1.00 87.46           N  
ATOM   1140  NH2 ARG A 150      28.248  29.596  14.172  1.00 86.17           N  
ATOM   1141  N   ALA A 151      26.258  34.159  20.087  1.00 93.92           N  
ATOM   1142  CA  ALA A 151      27.176  35.283  19.975  1.00 99.81           C  
ATOM   1143  C   ALA A 151      27.943  35.523  21.273  1.00103.89           C  
ATOM   1144  O   ALA A 151      29.036  36.088  21.253  1.00104.95           O  
ATOM   1145  CB  ALA A 151      26.412  36.538  19.581  1.00 99.57           C  
ATOM   1146  N   PHE A 152      27.370  35.094  22.397  1.00109.22           N  
ATOM   1147  CA  PHE A 152      28.003  35.265  23.707  1.00114.41           C  
ATOM   1148  C   PHE A 152      27.952  33.973  24.536  1.00118.10           C  
ATOM   1149  O   PHE A 152      28.805  33.096  24.395  1.00117.96           O  
ATOM   1150  CB  PHE A 152      27.313  36.393  24.490  1.00114.73           C  
ATOM   1151  CG  PHE A 152      27.275  37.716  23.764  1.00115.37           C  
ATOM   1152  CD1 PHE A 152      28.451  38.385  23.437  1.00115.79           C  
ATOM   1153  CD2 PHE A 152      26.056  38.297  23.418  1.00115.30           C  
ATOM   1154  CE1 PHE A 152      28.414  39.614  22.775  1.00115.85           C  
ATOM   1155  CE2 PHE A 152      26.007  39.524  22.757  1.00115.26           C  
ATOM   1156  CZ  PHE A 152      27.188  40.183  22.435  1.00115.88           C  
ATOM   1157  N   GLY A 153      26.946  33.874  25.402  1.00122.36           N  
ATOM   1158  CA  GLY A 153      26.782  32.703  26.246  1.00126.97           C  
ATOM   1159  C   GLY A 153      25.531  32.836  27.096  1.00130.40           C  
ATOM   1160  O   GLY A 153      24.757  33.776  26.910  1.00130.77           O  
ATOM   1161  N   VAL A 154      25.323  31.908  28.027  1.00134.01           N  
ATOM   1162  CA  VAL A 154      24.146  31.959  28.893  1.00137.95           C  
ATOM   1163  C   VAL A 154      24.277  31.086  30.143  1.00141.39           C  
ATOM   1164  O   VAL A 154      23.854  29.930  30.155  1.00141.43           O  
ATOM   1165  CB  VAL A 154      22.866  31.549  28.113  1.00137.55           C  
ATOM   1166  CG1 VAL A 154      23.057  30.185  27.465  1.00137.04           C  
ATOM   1167  CG2 VAL A 154      21.662  31.541  29.048  1.00137.04           C  
ATOM   1168  N   PRO A 155      24.869  31.636  31.217  1.00144.38           N  
ATOM   1169  CA  PRO A 155      25.054  30.905  32.476  1.00146.65           C  
ATOM   1170  C   PRO A 155      23.788  30.842  33.335  1.00148.24           C  
ATOM   1171  O   PRO A 155      22.764  31.437  32.996  1.00148.71           O  
ATOM   1172  CB  PRO A 155      26.177  31.682  33.156  1.00146.22           C  
ATOM   1173  CG  PRO A 155      25.890  33.086  32.735  1.00145.67           C  
ATOM   1174  CD  PRO A 155      25.570  32.933  31.260  1.00144.78           C  
ATOM   1175  N   VAL A 156      23.870  30.115  34.446  1.00150.01           N  
ATOM   1176  CA  VAL A 156      22.742  29.970  35.362  1.00151.67           C  
ATOM   1177  C   VAL A 156      22.372  31.325  35.952  1.00152.77           C  
ATOM   1178  O   VAL A 156      21.253  31.529  36.426  1.00152.61           O  
ATOM   1179  CB  VAL A 156      23.085  29.007  36.521  1.00151.58           C  
ATOM   1180  CG1 VAL A 156      24.270  29.544  37.313  1.00151.79           C  
ATOM   1181  CG2 VAL A 156      21.876  28.829  37.426  1.00151.99           C  
ATOM   1182  N   ARG A 157      23.325  32.248  35.923  1.00154.28           N  
ATOM   1183  CA  ARG A 157      23.104  33.584  36.452  1.00155.82           C  
ATOM   1184  C   ARG A 157      23.648  34.616  35.477  1.00156.72           C  
ATOM   1185  O   ARG A 157      23.716  34.364  34.276  1.00157.06           O  
ATOM   1186  CB  ARG A 157      23.800  33.735  37.804  1.00155.68           C  
ATOM   1187  CG  ARG A 157      23.012  34.564  38.787  1.00155.52           C  
ATOM   1188  CD  ARG A 157      21.689  33.886  39.090  1.00155.54           C  
ATOM   1189  NE  ARG A 157      20.859  34.683  39.983  1.00155.96           N  
ATOM   1190  CZ  ARG A 157      21.229  35.070  41.198  1.00156.07           C  
ATOM   1191  NH1 ARG A 157      22.421  34.734  41.671  1.00156.20           N  
ATOM   1192  NH2 ARG A 157      20.405  35.795  41.942  1.00156.28           N  
ATOM   1193  N   THR A 158      24.036  35.773  36.002  1.00158.10           N  
ATOM   1194  CA  THR A 158      24.578  36.858  35.189  1.00159.09           C  
ATOM   1195  C   THR A 158      25.047  38.021  36.064  1.00159.31           C  
ATOM   1196  O   THR A 158      25.113  37.899  37.289  1.00159.30           O  
ATOM   1197  CB  THR A 158      23.527  37.389  34.183  1.00160.00           C  
ATOM   1198  OG1 THR A 158      22.211  37.170  34.705  1.00160.65           O  
ATOM   1199  CG2 THR A 158      23.671  36.697  32.832  1.00160.46           C  
ATOM   1200  N   TYR A 159      25.373  39.144  35.426  1.00159.43           N  
ATOM   1201  CA  TYR A 159      25.833  40.333  36.140  1.00158.83           C  
ATOM   1202  C   TYR A 159      24.630  41.140  36.616  1.00157.38           C  
ATOM   1203  O   TYR A 159      24.720  41.893  37.584  1.00157.20           O  
ATOM   1204  CB  TYR A 159      26.692  41.218  35.227  1.00161.12           C  
ATOM   1205  CG  TYR A 159      25.919  42.359  34.593  1.00163.02           C  
ATOM   1206  CD1 TYR A 159      24.956  42.118  33.612  1.00163.92           C  
ATOM   1207  CD2 TYR A 159      26.110  43.673  35.019  1.00164.04           C  
ATOM   1208  CE1 TYR A 159      24.198  43.159  33.076  1.00164.60           C  
ATOM   1209  CE2 TYR A 159      25.358  44.721  34.489  1.00164.64           C  
ATOM   1210  CZ  TYR A 159      24.404  44.456  33.520  1.00164.80           C  
ATOM   1211  OH  TYR A 159      23.652  45.487  33.003  1.00165.27           O  
ATOM   1212  N   THR A 160      23.511  40.983  35.913  1.00155.04           N  
ATOM   1213  CA  THR A 160      22.277  41.693  36.237  1.00152.17           C  
ATOM   1214  C   THR A 160      21.809  41.379  37.654  1.00150.04           C  
ATOM   1215  O   THR A 160      20.748  41.839  38.084  1.00150.32           O  
ATOM   1216  CB  THR A 160      21.147  41.330  35.238  1.00153.03           C  
ATOM   1217  OG1 THR A 160      19.935  41.999  35.613  1.00152.95           O  
ATOM   1218  CG2 THR A 160      20.907  39.829  35.225  1.00152.91           C  
ATOM   1219  N   HIS A 161      22.612  40.602  38.377  1.00146.69           N  
ATOM   1220  CA  HIS A 161      22.285  40.221  39.744  1.00142.42           C  
ATOM   1221  C   HIS A 161      20.830  39.767  39.744  1.00138.33           C  
ATOM   1222  O   HIS A 161      20.024  40.213  40.563  1.00137.83           O  
ATOM   1223  CB  HIS A 161      22.465  41.421  40.680  1.00144.32           C  
ATOM   1224  CG  HIS A 161      23.744  42.173  40.463  1.00145.07           C  
ATOM   1225  ND1 HIS A 161      24.971  41.550  40.374  1.00145.87           N  
ATOM   1226  CD2 HIS A 161      23.987  43.499  40.337  1.00145.60           C  
ATOM   1227  CE1 HIS A 161      25.914  42.460  40.202  1.00145.85           C  
ATOM   1228  NE2 HIS A 161      25.344  43.651  40.177  1.00145.57           N  
ATOM   1229  N   GLU A 162      20.505  38.879  38.808  1.00132.08           N  
ATOM   1230  CA  GLU A 162      19.145  38.376  38.659  1.00125.89           C  
ATOM   1231  C   GLU A 162      19.140  36.878  38.361  1.00120.45           C  
ATOM   1232  O   GLU A 162      20.193  36.276  38.141  1.00120.60           O  
ATOM   1233  CB  GLU A 162      18.454  39.144  37.530  1.00126.82           C  
ATOM   1234  CG  GLU A 162      16.984  39.412  37.750  1.00126.46           C  
ATOM   1235  CD  GLU A 162      16.499  40.587  36.929  1.00126.68           C  
ATOM   1236  OE1 GLU A 162      17.034  41.701  37.116  1.00126.80           O  
ATOM   1237  OE2 GLU A 162      15.588  40.400  36.096  1.00126.85           O  
ATOM   1238  N   VAL A 163      17.950  36.284  38.347  1.00113.17           N  
ATOM   1239  CA  VAL A 163      17.812  34.854  38.089  1.00105.03           C  
ATOM   1240  C   VAL A 163      17.288  34.518  36.700  1.00 98.65           C  
ATOM   1241  O   VAL A 163      16.359  35.147  36.190  1.00 97.79           O  
ATOM   1242  CB  VAL A 163      16.886  34.185  39.128  1.00105.29           C  
ATOM   1243  CG1 VAL A 163      16.606  32.738  38.733  1.00104.55           C  
ATOM   1244  CG2 VAL A 163      17.537  34.234  40.497  1.00105.26           C  
ATOM   1245  N   VAL A 164      17.898  33.503  36.103  1.00 90.57           N  
ATOM   1246  CA  VAL A 164      17.519  33.040  34.781  1.00 82.35           C  
ATOM   1247  C   VAL A 164      16.228  32.225  34.862  1.00 75.52           C  
ATOM   1248  O   VAL A 164      15.879  31.699  35.917  1.00 74.16           O  
ATOM   1249  CB  VAL A 164      18.632  32.148  34.179  1.00 82.98           C  
ATOM   1250  CG1 VAL A 164      19.935  32.932  34.071  1.00 82.60           C  
ATOM   1251  CG2 VAL A 164      18.829  30.909  35.048  1.00 82.38           C  
ATOM   1252  N   THR A 165      15.518  32.135  33.744  1.00 66.67           N  
ATOM   1253  CA  THR A 165      14.289  31.360  33.687  1.00 59.16           C  
ATOM   1254  C   THR A 165      14.521  30.140  32.803  1.00 53.75           C  
ATOM   1255  O   THR A 165      14.904  30.266  31.643  1.00 53.31           O  
ATOM   1256  CB  THR A 165      13.123  32.194  33.130  1.00 58.73           C  
ATOM   1257  OG1 THR A 165      12.714  33.149  34.118  1.00 59.99           O  
ATOM   1258  CG2 THR A 165      11.942  31.305  32.787  1.00 56.79           C  
ATOM   1259  N   LEU A 166      14.300  28.961  33.372  1.00 46.76           N  
ATOM   1260  CA  LEU A 166      14.489  27.705  32.665  1.00 40.30           C  
ATOM   1261  C   LEU A 166      13.146  27.142  32.228  1.00 36.54           C  
ATOM   1262  O   LEU A 166      13.085  26.069  31.625  1.00 30.67           O  
ATOM   1263  CB  LEU A 166      15.157  26.686  33.583  1.00 42.83           C  
ATOM   1264  CG  LEU A 166      16.314  27.146  34.469  1.00 44.45           C  
ATOM   1265  CD1 LEU A 166      16.546  26.099  35.528  1.00 44.23           C  
ATOM   1266  CD2 LEU A 166      17.575  27.377  33.645  1.00 45.54           C  
ATOM   1267  N   TRP A 167      12.077  27.871  32.538  1.00 33.06           N  
ATOM   1268  CA  TRP A 167      10.725  27.439  32.218  1.00 31.45           C  
ATOM   1269  C   TRP A 167      10.545  26.987  30.774  1.00 31.19           C  
ATOM   1270  O   TRP A 167       9.749  26.083  30.489  1.00 30.15           O  
ATOM   1271  CB  TRP A 167       9.727  28.568  32.508  1.00 33.46           C  
ATOM   1272  CG  TRP A 167       9.651  29.008  33.939  1.00 33.80           C  
ATOM   1273  CD1 TRP A 167      10.377  28.526  34.989  1.00 37.79           C  
ATOM   1274  CD2 TRP A 167       8.785  30.016  34.480  1.00 36.14           C  
ATOM   1275  NE1 TRP A 167      10.016  29.167  36.152  1.00 38.34           N  
ATOM   1276  CE2 TRP A 167       9.041  30.087  35.868  1.00 37.59           C  
ATOM   1277  CE3 TRP A 167       7.817  30.869  33.927  1.00 36.15           C  
ATOM   1278  CZ2 TRP A 167       8.361  30.977  36.712  1.00 36.46           C  
ATOM   1279  CZ3 TRP A 167       7.141  31.752  34.768  1.00 35.49           C  
ATOM   1280  CH2 TRP A 167       7.419  31.799  36.144  1.00 35.15           C  
ATOM   1281  N   TYR A 168      11.298  27.607  29.868  1.00 29.79           N  
ATOM   1282  CA  TYR A 168      11.191  27.323  28.443  1.00 28.16           C  
ATOM   1283  C   TYR A 168      12.373  26.553  27.847  1.00 28.16           C  
ATOM   1284  O   TYR A 168      12.521  26.467  26.622  1.00 28.02           O  
ATOM   1285  CB  TYR A 168      10.991  28.648  27.706  1.00 27.92           C  
ATOM   1286  CG  TYR A 168       9.932  29.524  28.354  1.00 27.83           C  
ATOM   1287  CD1 TYR A 168       8.579  29.329  28.090  1.00 26.96           C  
ATOM   1288  CD2 TYR A 168      10.285  30.503  29.292  1.00 27.88           C  
ATOM   1289  CE1 TYR A 168       7.597  30.079  28.742  1.00 27.10           C  
ATOM   1290  CE2 TYR A 168       9.315  31.252  29.950  1.00 28.72           C  
ATOM   1291  CZ  TYR A 168       7.973  31.037  29.674  1.00 28.84           C  
ATOM   1292  OH  TYR A 168       7.011  31.781  30.330  1.00 28.15           O  
ATOM   1293  N   ARG A 169      13.195  25.967  28.709  1.00 26.95           N  
ATOM   1294  CA  ARG A 169      14.366  25.217  28.263  1.00 28.13           C  
ATOM   1295  C   ARG A 169      14.026  23.761  27.873  1.00 26.93           C  
ATOM   1296  O   ARG A 169      13.408  23.032  28.642  1.00 26.01           O  
ATOM   1297  CB  ARG A 169      15.417  25.262  29.371  1.00 30.22           C  
ATOM   1298  CG  ARG A 169      16.839  25.076  28.914  1.00 37.20           C  
ATOM   1299  CD  ARG A 169      17.789  25.967  29.715  1.00 41.40           C  
ATOM   1300  NE  ARG A 169      17.707  27.374  29.314  1.00 45.39           N  
ATOM   1301  CZ  ARG A 169      18.351  28.367  29.929  1.00 48.16           C  
ATOM   1302  NH1 ARG A 169      19.129  28.108  30.981  1.00 47.63           N  
ATOM   1303  NH2 ARG A 169      18.210  29.619  29.501  1.00 45.03           N  
ATOM   1304  N   ALA A 170      14.422  23.356  26.667  1.00 25.64           N  
ATOM   1305  CA  ALA A 170      14.156  22.001  26.174  1.00 26.76           C  
ATOM   1306  C   ALA A 170      14.912  20.973  27.010  1.00 26.40           C  
ATOM   1307  O   ALA A 170      16.007  21.247  27.505  1.00 29.22           O  
ATOM   1308  CB  ALA A 170      14.556  21.887  24.691  1.00 22.16           C  
ATOM   1309  N   PRO A 171      14.359  19.759  27.149  1.00 27.29           N  
ATOM   1310  CA  PRO A 171      15.028  18.725  27.954  1.00 26.27           C  
ATOM   1311  C   PRO A 171      16.459  18.332  27.558  1.00 26.70           C  
ATOM   1312  O   PRO A 171      17.280  18.029  28.431  1.00 26.46           O  
ATOM   1313  CB  PRO A 171      14.042  17.556  27.903  1.00 26.25           C  
ATOM   1314  CG  PRO A 171      13.378  17.722  26.544  1.00 27.20           C  
ATOM   1315  CD  PRO A 171      13.165  19.225  26.464  1.00 26.91           C  
ATOM   1316  N   GLU A 172      16.773  18.351  26.263  1.00 26.71           N  
ATOM   1317  CA  GLU A 172      18.116  17.989  25.819  1.00 26.38           C  
ATOM   1318  C   GLU A 172      19.165  18.940  26.391  1.00 25.61           C  
ATOM   1319  O   GLU A 172      20.295  18.538  26.659  1.00 27.37           O  
ATOM   1320  CB  GLU A 172      18.198  17.974  24.291  1.00 29.38           C  
ATOM   1321  CG  GLU A 172      17.791  19.280  23.638  1.00 31.65           C  
ATOM   1322  CD  GLU A 172      16.409  19.224  23.020  1.00 32.35           C  
ATOM   1323  OE1 GLU A 172      15.479  18.716  23.685  1.00 30.58           O  
ATOM   1324  OE2 GLU A 172      16.257  19.697  21.870  1.00 32.30           O  
ATOM   1325  N   ILE A 173      18.799  20.203  26.571  1.00 24.90           N  
ATOM   1326  CA  ILE A 173      19.719  21.174  27.147  1.00 24.38           C  
ATOM   1327  C   ILE A 173      19.874  20.850  28.634  1.00 25.34           C  
ATOM   1328  O   ILE A 173      20.979  20.813  29.161  1.00 27.65           O  
ATOM   1329  CB  ILE A 173      19.177  22.628  27.033  1.00 25.67           C  
ATOM   1330  CG1 ILE A 173      19.112  23.067  25.570  1.00 23.97           C  
ATOM   1331  CG2 ILE A 173      20.058  23.569  27.826  1.00 21.42           C  
ATOM   1332  CD1 ILE A 173      18.529  24.471  25.380  1.00 23.28           C  
ATOM   1333  N   LEU A 174      18.755  20.609  29.307  1.00 25.63           N  
ATOM   1334  CA  LEU A 174      18.773  20.295  30.726  1.00 25.69           C  
ATOM   1335  C   LEU A 174      19.481  18.973  31.007  1.00 28.96           C  
ATOM   1336  O   LEU A 174      20.019  18.784  32.100  1.00 30.32           O  
ATOM   1337  CB  LEU A 174      17.348  20.217  31.270  1.00 27.09           C  
ATOM   1338  CG  LEU A 174      16.460  21.462  31.180  1.00 24.86           C  
ATOM   1339  CD1 LEU A 174      15.068  21.102  31.633  1.00 25.91           C  
ATOM   1340  CD2 LEU A 174      17.027  22.574  32.035  1.00 21.81           C  
ATOM   1341  N   LEU A 175      19.483  18.064  30.032  1.00 27.56           N  
ATOM   1342  CA  LEU A 175      20.122  16.768  30.214  1.00 27.86           C  
ATOM   1343  C   LEU A 175      21.598  16.717  29.848  1.00 31.14           C  
ATOM   1344  O   LEU A 175      22.198  15.645  29.843  1.00 31.89           O  
ATOM   1345  CB  LEU A 175      19.351  15.689  29.450  1.00 27.68           C  
ATOM   1346  CG  LEU A 175      18.017  15.347  30.134  1.00 27.91           C  
ATOM   1347  CD1 LEU A 175      17.220  14.377  29.316  1.00 21.52           C  
ATOM   1348  CD2 LEU A 175      18.305  14.775  31.519  1.00 26.91           C  
ATOM   1349  N   GLY A 176      22.189  17.866  29.531  1.00 34.01           N  
ATOM   1350  CA  GLY A 176      23.608  17.884  29.216  1.00 35.86           C  
ATOM   1351  C   GLY A 176      24.040  17.872  27.759  1.00 38.65           C  
ATOM   1352  O   GLY A 176      25.235  17.866  27.481  1.00 39.13           O  
ATOM   1353  N   CYS A 177      23.095  17.864  26.826  1.00 41.64           N  
ATOM   1354  CA  CYS A 177      23.446  17.868  25.406  1.00 43.82           C  
ATOM   1355  C   CYS A 177      24.153  19.188  25.069  1.00 44.88           C  
ATOM   1356  O   CYS A 177      23.614  20.271  25.297  1.00 44.58           O  
ATOM   1357  CB  CYS A 177      22.187  17.716  24.556  1.00 44.20           C  
ATOM   1358  SG  CYS A 177      22.480  17.274  22.843  1.00 45.14           S  
ATOM   1359  N   LYS A 178      25.364  19.092  24.533  1.00 46.89           N  
ATOM   1360  CA  LYS A 178      26.138  20.280  24.188  1.00 48.97           C  
ATOM   1361  C   LYS A 178      25.898  20.752  22.768  1.00 48.32           C  
ATOM   1362  O   LYS A 178      26.075  21.926  22.466  1.00 48.23           O  
ATOM   1363  CB  LYS A 178      27.643  20.020  24.380  1.00 51.64           C  
ATOM   1364  CG  LYS A 178      28.169  20.331  25.783  1.00 56.34           C  
ATOM   1365  CD  LYS A 178      29.673  20.083  25.898  1.00 59.19           C  
ATOM   1366  CE  LYS A 178      29.982  18.652  26.337  1.00 61.50           C  
ATOM   1367  NZ  LYS A 178      29.318  17.626  25.486  1.00 61.93           N  
ATOM   1368  N   TYR A 179      25.489  19.837  21.899  1.00 48.54           N  
ATOM   1369  CA  TYR A 179      25.264  20.179  20.505  1.00 49.24           C  
ATOM   1370  C   TYR A 179      23.802  20.115  20.091  1.00 48.22           C  
ATOM   1371  O   TYR A 179      23.436  19.413  19.145  1.00 48.61           O  
ATOM   1372  CB  TYR A 179      26.113  19.262  19.626  1.00 52.38           C  
ATOM   1373  CG  TYR A 179      27.581  19.302  19.996  1.00 56.77           C  
ATOM   1374  CD1 TYR A 179      28.324  20.480  19.863  1.00 57.47           C  
ATOM   1375  CD2 TYR A 179      28.218  18.179  20.522  1.00 58.60           C  
ATOM   1376  CE1 TYR A 179      29.666  20.539  20.251  1.00 59.71           C  
ATOM   1377  CE2 TYR A 179      29.560  18.227  20.914  1.00 60.65           C  
ATOM   1378  CZ  TYR A 179      30.278  19.407  20.778  1.00 61.43           C  
ATOM   1379  OH  TYR A 179      31.599  19.455  21.182  1.00 62.81           O  
ATOM   1380  N   TYR A 180      22.972  20.865  20.802  1.00 45.93           N  
ATOM   1381  CA  TYR A 180      21.550  20.909  20.509  1.00 44.53           C  
ATOM   1382  C   TYR A 180      21.269  21.699  19.220  1.00 41.81           C  
ATOM   1383  O   TYR A 180      22.094  22.495  18.772  1.00 39.09           O  
ATOM   1384  CB  TYR A 180      20.796  21.506  21.704  1.00 46.06           C  
ATOM   1385  CG  TYR A 180      21.375  22.801  22.220  1.00 48.53           C  
ATOM   1386  CD1 TYR A 180      21.177  23.994  21.535  1.00 49.37           C  
ATOM   1387  CD2 TYR A 180      22.120  22.834  23.399  1.00 49.59           C  
ATOM   1388  CE1 TYR A 180      21.701  25.190  22.012  1.00 52.28           C  
ATOM   1389  CE2 TYR A 180      22.651  24.026  23.884  1.00 50.33           C  
ATOM   1390  CZ  TYR A 180      22.434  25.198  23.186  1.00 51.78           C  
ATOM   1391  OH  TYR A 180      22.936  26.387  23.662  1.00 57.90           O  
ATOM   1392  N   SER A 181      20.094  21.468  18.640  1.00 37.59           N  
ATOM   1393  CA  SER A 181      19.707  22.103  17.395  1.00 35.17           C  
ATOM   1394  C   SER A 181      18.539  23.084  17.479  1.00 34.19           C  
ATOM   1395  O   SER A 181      18.087  23.480  18.552  1.00 32.19           O  
ATOM   1396  CB  SER A 181      19.356  21.026  16.366  1.00 36.22           C  
ATOM   1397  OG  SER A 181      18.192  20.299  16.755  1.00 34.72           O  
ATOM   1398  N   THR A 182      18.058  23.453  16.301  1.00 31.69           N  
ATOM   1399  CA  THR A 182      16.954  24.369  16.142  1.00 31.94           C  
ATOM   1400  C   THR A 182      15.706  23.868  16.870  1.00 33.31           C  
ATOM   1401  O   THR A 182      14.801  24.646  17.157  1.00 35.32           O  
ATOM   1402  CB  THR A 182      16.617  24.503  14.673  1.00 31.59           C  
ATOM   1403  OG1 THR A 182      16.346  23.201  14.149  1.00 31.41           O  
ATOM   1404  CG2 THR A 182      17.774  25.114  13.910  1.00 31.72           C  
ATOM   1405  N   ALA A 183      15.658  22.573  17.166  1.00 32.33           N  
ATOM   1406  CA  ALA A 183      14.508  21.983  17.850  1.00 30.73           C  
ATOM   1407  C   ALA A 183      14.270  22.501  19.272  1.00 30.96           C  
ATOM   1408  O   ALA A 183      13.202  22.267  19.839  1.00 32.25           O  
ATOM   1409  CB  ALA A 183      14.630  20.458  17.869  1.00 31.66           C  
ATOM   1410  N   VAL A 184      15.250  23.197  19.848  1.00 29.42           N  
ATOM   1411  CA  VAL A 184      15.106  23.744  21.196  1.00 24.26           C  
ATOM   1412  C   VAL A 184      14.195  24.965  21.135  1.00 24.76           C  
ATOM   1413  O   VAL A 184      13.463  25.271  22.082  1.00 23.99           O  
ATOM   1414  CB  VAL A 184      16.489  24.134  21.807  1.00 25.19           C  
ATOM   1415  CG1 VAL A 184      17.408  22.935  21.772  1.00 21.36           C  
ATOM   1416  CG2 VAL A 184      17.122  25.312  21.056  1.00 22.42           C  
ATOM   1417  N   ASP A 185      14.239  25.659  20.004  1.00 25.03           N  
ATOM   1418  CA  ASP A 185      13.397  26.824  19.808  1.00 26.47           C  
ATOM   1419  C   ASP A 185      11.939  26.376  19.661  1.00 26.91           C  
ATOM   1420  O   ASP A 185      11.034  27.054  20.145  1.00 26.89           O  
ATOM   1421  CB  ASP A 185      13.838  27.619  18.571  1.00 30.04           C  
ATOM   1422  CG  ASP A 185      15.153  28.364  18.782  1.00 31.66           C  
ATOM   1423  OD1 ASP A 185      15.474  28.706  19.941  1.00 33.27           O  
ATOM   1424  OD2 ASP A 185      15.856  28.626  17.783  1.00 32.60           O  
ATOM   1425  N   ILE A 186      11.706  25.237  19.002  1.00 26.57           N  
ATOM   1426  CA  ILE A 186      10.342  24.736  18.860  1.00 25.30           C  
ATOM   1427  C   ILE A 186       9.782  24.310  20.223  1.00 23.94           C  
ATOM   1428  O   ILE A 186       8.613  24.560  20.516  1.00 25.08           O  
ATOM   1429  CB  ILE A 186      10.240  23.536  17.867  1.00 27.59           C  
ATOM   1430  CG1 ILE A 186      10.322  24.027  16.417  1.00 29.23           C  
ATOM   1431  CG2 ILE A 186       8.927  22.813  18.060  1.00 25.09           C  
ATOM   1432  CD1 ILE A 186      11.716  24.392  15.987  1.00 32.79           C  
ATOM   1433  N   TRP A 187      10.604  23.667  21.052  1.00 21.62           N  
ATOM   1434  CA  TRP A 187      10.150  23.254  22.382  1.00 21.93           C  
ATOM   1435  C   TRP A 187       9.725  24.503  23.149  1.00 22.53           C  
ATOM   1436  O   TRP A 187       8.638  24.553  23.718  1.00 22.63           O  
ATOM   1437  CB  TRP A 187      11.266  22.536  23.144  1.00 22.13           C  
ATOM   1438  CG  TRP A 187      10.899  22.192  24.542  1.00 23.40           C  
ATOM   1439  CD1 TRP A 187      10.892  23.034  25.626  1.00 27.03           C  
ATOM   1440  CD2 TRP A 187      10.414  20.929  25.014  1.00 22.72           C  
ATOM   1441  NE1 TRP A 187      10.426  22.368  26.744  1.00 25.92           N  
ATOM   1442  CE2 TRP A 187      10.125  21.077  26.396  1.00 23.46           C  
ATOM   1443  CE3 TRP A 187      10.191  19.687  24.406  1.00 21.78           C  
ATOM   1444  CZ2 TRP A 187       9.623  20.026  27.178  1.00 21.20           C  
ATOM   1445  CZ3 TRP A 187       9.689  18.638  25.186  1.00 21.30           C  
ATOM   1446  CH2 TRP A 187       9.412  18.820  26.559  1.00 21.52           C  
ATOM   1447  N   SER A 188      10.590  25.513  23.138  1.00 23.34           N  
ATOM   1448  CA  SER A 188      10.313  26.773  23.812  1.00 24.24           C  
ATOM   1449  C   SER A 188       9.019  27.406  23.284  1.00 25.00           C  
ATOM   1450  O   SER A 188       8.166  27.818  24.068  1.00 27.86           O  
ATOM   1451  CB  SER A 188      11.483  27.736  23.617  1.00 25.66           C  
ATOM   1452  OG  SER A 188      12.699  27.124  24.020  1.00 26.98           O  
ATOM   1453  N   LEU A 189       8.851  27.470  21.968  1.00 21.80           N  
ATOM   1454  CA  LEU A 189       7.631  28.049  21.435  1.00 24.09           C  
ATOM   1455  C   LEU A 189       6.401  27.196  21.843  1.00 24.56           C  
ATOM   1456  O   LEU A 189       5.302  27.717  22.048  1.00 23.21           O  
ATOM   1457  CB  LEU A 189       7.745  28.193  19.913  1.00 24.56           C  
ATOM   1458  CG  LEU A 189       6.722  29.084  19.188  1.00 27.78           C  
ATOM   1459  CD1 LEU A 189       6.557  30.431  19.937  1.00 26.65           C  
ATOM   1460  CD2 LEU A 189       7.194  29.317  17.741  1.00 24.11           C  
ATOM   1461  N   GLY A 190       6.586  25.888  21.983  1.00 24.29           N  
ATOM   1462  CA  GLY A 190       5.468  25.063  22.398  1.00 24.49           C  
ATOM   1463  C   GLY A 190       5.018  25.443  23.805  1.00 25.69           C  
ATOM   1464  O   GLY A 190       3.824  25.468  24.099  1.00 26.30           O  
ATOM   1465  N   CYS A 191       5.978  25.746  24.675  1.00 24.82           N  
ATOM   1466  CA  CYS A 191       5.687  26.120  26.055  1.00 25.35           C  
ATOM   1467  C   CYS A 191       4.942  27.444  26.108  1.00 26.63           C  
ATOM   1468  O   CYS A 191       3.973  27.606  26.872  1.00 25.66           O  
ATOM   1469  CB  CYS A 191       6.985  26.244  26.855  1.00 25.73           C  
ATOM   1470  SG  CYS A 191       7.882  24.694  27.095  1.00 26.79           S  
ATOM   1471  N   ILE A 192       5.406  28.392  25.294  1.00 24.89           N  
ATOM   1472  CA  ILE A 192       4.790  29.700  25.212  1.00 23.10           C  
ATOM   1473  C   ILE A 192       3.366  29.531  24.678  1.00 23.93           C  
ATOM   1474  O   ILE A 192       2.427  30.125  25.198  1.00 26.46           O  
ATOM   1475  CB  ILE A 192       5.631  30.624  24.292  1.00 24.07           C  
ATOM   1476  CG1 ILE A 192       7.019  30.815  24.918  1.00 19.84           C  
ATOM   1477  CG2 ILE A 192       4.937  31.968  24.090  1.00 21.73           C  
ATOM   1478  CD1 ILE A 192       7.913  31.724  24.174  1.00 18.84           C  
ATOM   1479  N   PHE A 193       3.210  28.703  23.654  1.00 23.36           N  
ATOM   1480  CA  PHE A 193       1.904  28.438  23.049  1.00 24.98           C  
ATOM   1481  C   PHE A 193       0.930  27.934  24.122  1.00 25.66           C  
ATOM   1482  O   PHE A 193      -0.183  28.441  24.260  1.00 25.78           O  
ATOM   1483  CB  PHE A 193       2.087  27.406  21.922  1.00 24.24           C  
ATOM   1484  CG  PHE A 193       0.806  26.913  21.299  1.00 21.04           C  
ATOM   1485  CD1 PHE A 193      -0.357  27.671  21.333  1.00 22.57           C  
ATOM   1486  CD2 PHE A 193       0.787  25.701  20.620  1.00 19.90           C  
ATOM   1487  CE1 PHE A 193      -1.526  27.226  20.695  1.00 21.41           C  
ATOM   1488  CE2 PHE A 193      -0.370  25.251  19.982  1.00 21.34           C  
ATOM   1489  CZ  PHE A 193      -1.530  26.018  20.021  1.00 19.69           C  
ATOM   1490  N   ALA A 194       1.362  26.940  24.884  1.00 26.40           N  
ATOM   1491  CA  ALA A 194       0.534  26.392  25.946  1.00 26.39           C  
ATOM   1492  C   ALA A 194       0.220  27.480  26.964  1.00 26.22           C  
ATOM   1493  O   ALA A 194      -0.881  27.522  27.509  1.00 27.63           O  
ATOM   1494  CB  ALA A 194       1.257  25.237  26.631  1.00 24.46           C  
ATOM   1495  N   GLU A 195       1.190  28.358  27.222  1.00 26.46           N  
ATOM   1496  CA  GLU A 195       1.009  29.437  28.202  1.00 26.67           C  
ATOM   1497  C   GLU A 195       0.010  30.493  27.733  1.00 26.62           C  
ATOM   1498  O   GLU A 195      -0.687  31.099  28.536  1.00 28.82           O  
ATOM   1499  CB  GLU A 195       2.347  30.107  28.516  1.00 27.07           C  
ATOM   1500  CG  GLU A 195       2.355  30.860  29.830  1.00 29.14           C  
ATOM   1501  CD  GLU A 195       3.707  31.456  30.163  1.00 31.53           C  
ATOM   1502  OE1 GLU A 195       4.733  30.811  29.869  1.00 32.65           O  
ATOM   1503  OE2 GLU A 195       3.749  32.564  30.738  1.00 34.35           O  
ATOM   1504  N   MET A 196      -0.047  30.724  26.431  1.00 27.20           N  
ATOM   1505  CA  MET A 196      -0.981  31.685  25.898  1.00 27.05           C  
ATOM   1506  C   MET A 196      -2.379  31.113  26.044  1.00 29.38           C  
ATOM   1507  O   MET A 196      -3.332  31.842  26.292  1.00 31.82           O  
ATOM   1508  CB  MET A 196      -0.696  31.955  24.422  1.00 27.88           C  
ATOM   1509  CG  MET A 196       0.593  32.706  24.142  1.00 26.57           C  
ATOM   1510  SD  MET A 196       0.596  33.407  22.466  1.00 34.53           S  
ATOM   1511  CE  MET A 196       1.303  32.053  21.477  1.00 24.27           C  
ATOM   1512  N   VAL A 197      -2.504  29.801  25.892  1.00 30.67           N  
ATOM   1513  CA  VAL A 197      -3.807  29.165  26.011  1.00 31.53           C  
ATOM   1514  C   VAL A 197      -4.296  29.042  27.456  1.00 31.21           C  
ATOM   1515  O   VAL A 197      -5.421  29.410  27.762  1.00 31.70           O  
ATOM   1516  CB  VAL A 197      -3.807  27.761  25.360  1.00 31.78           C  
ATOM   1517  CG1 VAL A 197      -5.121  27.047  25.650  1.00 32.57           C  
ATOM   1518  CG2 VAL A 197      -3.631  27.891  23.863  1.00 31.60           C  
ATOM   1519  N   THR A 198      -3.453  28.545  28.351  1.00 33.18           N  
ATOM   1520  CA  THR A 198      -3.873  28.367  29.736  1.00 33.75           C  
ATOM   1521  C   THR A 198      -3.725  29.577  30.640  1.00 36.20           C  
ATOM   1522  O   THR A 198      -4.300  29.602  31.727  1.00 38.14           O  
ATOM   1523  CB  THR A 198      -3.117  27.197  30.407  1.00 32.56           C  
ATOM   1524  OG1 THR A 198      -1.746  27.554  30.611  1.00 31.21           O  
ATOM   1525  CG2 THR A 198      -3.190  25.958  29.540  1.00 31.20           C  
ATOM   1526  N   ARG A 199      -2.961  30.578  30.204  1.00 37.29           N  
ATOM   1527  CA  ARG A 199      -2.729  31.770  31.020  1.00 37.10           C  
ATOM   1528  C   ARG A 199      -1.982  31.343  32.278  1.00 37.33           C  
ATOM   1529  O   ARG A 199      -2.220  31.864  33.370  1.00 38.11           O  
ATOM   1530  CB  ARG A 199      -4.044  32.431  31.423  1.00 36.06           C  
ATOM   1531  CG  ARG A 199      -4.942  32.800  30.256  1.00 38.46           C  
ATOM   1532  CD  ARG A 199      -6.234  33.398  30.752  1.00 38.91           C  
ATOM   1533  NE  ARG A 199      -7.394  32.694  30.217  1.00 41.37           N  
ATOM   1534  CZ  ARG A 199      -8.635  32.893  30.650  1.00 41.97           C  
ATOM   1535  NH1 ARG A 199      -8.850  33.775  31.618  1.00 37.95           N  
ATOM   1536  NH2 ARG A 199      -9.651  32.205  30.131  1.00 40.79           N  
ATOM   1537  N   ARG A 200      -1.079  30.387  32.111  1.00 37.03           N  
ATOM   1538  CA  ARG A 200      -0.292  29.865  33.217  1.00 37.60           C  
ATOM   1539  C   ARG A 200       0.916  29.160  32.607  1.00 36.06           C  
ATOM   1540  O   ARG A 200       0.777  28.464  31.600  1.00 34.61           O  
ATOM   1541  CB  ARG A 200      -1.126  28.863  34.007  1.00 38.79           C  
ATOM   1542  CG  ARG A 200      -0.833  28.867  35.470  1.00 43.42           C  
ATOM   1543  CD  ARG A 200      -1.430  27.657  36.133  1.00 50.21           C  
ATOM   1544  NE  ARG A 200      -1.173  27.661  37.570  1.00 54.62           N  
ATOM   1545  CZ  ARG A 200      -1.407  26.627  38.372  1.00 56.54           C  
ATOM   1546  NH1 ARG A 200      -1.904  25.501  37.876  1.00 57.10           N  
ATOM   1547  NH2 ARG A 200      -1.145  26.719  39.669  1.00 57.41           N  
ATOM   1548  N   ALA A 201       2.095  29.344  33.197  1.00 33.94           N  
ATOM   1549  CA  ALA A 201       3.290  28.701  32.666  1.00 32.32           C  
ATOM   1550  C   ALA A 201       3.126  27.185  32.673  1.00 30.85           C  
ATOM   1551  O   ALA A 201       2.560  26.612  33.602  1.00 32.01           O  
ATOM   1552  CB  ALA A 201       4.517  29.102  33.473  1.00 32.32           C  
ATOM   1553  N   LEU A 202       3.620  26.539  31.628  1.00 28.47           N  
ATOM   1554  CA  LEU A 202       3.519  25.091  31.516  1.00 29.75           C  
ATOM   1555  C   LEU A 202       4.407  24.331  32.512  1.00 29.07           C  
ATOM   1556  O   LEU A 202       3.925  23.472  33.246  1.00 29.42           O  
ATOM   1557  CB  LEU A 202       3.866  24.670  30.084  1.00 27.18           C  
ATOM   1558  CG  LEU A 202       3.441  23.258  29.711  1.00 28.34           C  
ATOM   1559  CD1 LEU A 202       1.967  23.055  30.083  1.00 24.30           C  
ATOM   1560  CD2 LEU A 202       3.678  23.043  28.221  1.00 27.53           C  
ATOM   1561  N   PHE A 203       5.701  24.648  32.515  1.00 28.93           N  
ATOM   1562  CA  PHE A 203       6.684  24.014  33.397  1.00 27.54           C  
ATOM   1563  C   PHE A 203       7.503  25.101  34.105  1.00 27.91           C  
ATOM   1564  O   PHE A 203       8.659  25.349  33.751  1.00 29.23           O  
ATOM   1565  CB  PHE A 203       7.634  23.147  32.577  1.00 24.58           C  
ATOM   1566  CG  PHE A 203       6.945  22.128  31.709  1.00 26.95           C  
ATOM   1567  CD1 PHE A 203       6.121  21.153  32.268  1.00 24.64           C  
ATOM   1568  CD2 PHE A 203       7.150  22.124  30.328  1.00 26.16           C  
ATOM   1569  CE1 PHE A 203       5.515  20.191  31.467  1.00 25.28           C  
ATOM   1570  CE2 PHE A 203       6.549  21.168  29.520  1.00 24.45           C  
ATOM   1571  CZ  PHE A 203       5.729  20.195  30.089  1.00 25.06           C  
ATOM   1572  N   PRO A 204       6.921  25.754  35.119  1.00 27.93           N  
ATOM   1573  CA  PRO A 204       7.598  26.820  35.862  1.00 30.99           C  
ATOM   1574  C   PRO A 204       8.607  26.345  36.907  1.00 34.67           C  
ATOM   1575  O   PRO A 204       8.496  26.691  38.090  1.00 36.68           O  
ATOM   1576  CB  PRO A 204       6.431  27.577  36.487  1.00 27.97           C  
ATOM   1577  CG  PRO A 204       5.521  26.488  36.851  1.00 26.79           C  
ATOM   1578  CD  PRO A 204       5.538  25.593  35.602  1.00 29.07           C  
ATOM   1579  N   GLY A 205       9.594  25.567  36.468  1.00 35.11           N  
ATOM   1580  CA  GLY A 205      10.595  25.055  37.387  1.00 34.84           C  
ATOM   1581  C   GLY A 205      11.387  26.143  38.073  1.00 35.29           C  
ATOM   1582  O   GLY A 205      11.495  27.249  37.556  1.00 36.09           O  
ATOM   1583  N   ASP A 206      11.943  25.832  39.240  1.00 38.16           N  
ATOM   1584  CA  ASP A 206      12.742  26.799  39.988  1.00 40.81           C  
ATOM   1585  C   ASP A 206      14.192  26.351  40.162  1.00 40.77           C  
ATOM   1586  O   ASP A 206      14.943  26.955  40.924  1.00 42.30           O  
ATOM   1587  CB  ASP A 206      12.127  27.060  41.361  1.00 43.12           C  
ATOM   1588  CG  ASP A 206      12.112  25.833  42.225  1.00 45.48           C  
ATOM   1589  OD1 ASP A 206      11.006  25.387  42.578  1.00 46.67           O  
ATOM   1590  OD2 ASP A 206      13.202  25.313  42.548  1.00 47.83           O  
ATOM   1591  N   SER A 207      14.561  25.277  39.472  1.00 39.23           N  
ATOM   1592  CA  SER A 207      15.919  24.746  39.488  1.00 38.41           C  
ATOM   1593  C   SER A 207      15.945  23.795  38.304  1.00 38.16           C  
ATOM   1594  O   SER A 207      14.883  23.452  37.775  1.00 37.92           O  
ATOM   1595  CB  SER A 207      16.229  24.005  40.792  1.00 37.42           C  
ATOM   1596  OG  SER A 207      15.634  22.724  40.835  1.00 40.04           O  
ATOM   1597  N   GLU A 208      17.132  23.372  37.875  1.00 36.24           N  
ATOM   1598  CA  GLU A 208      17.216  22.494  36.716  1.00 36.07           C  
ATOM   1599  C   GLU A 208      16.570  21.143  36.939  1.00 35.05           C  
ATOM   1600  O   GLU A 208      15.995  20.559  36.022  1.00 37.04           O  
ATOM   1601  CB  GLU A 208      18.672  22.304  36.278  1.00 38.21           C  
ATOM   1602  CG  GLU A 208      19.360  23.587  35.811  1.00 43.36           C  
ATOM   1603  CD  GLU A 208      20.505  23.335  34.836  1.00 45.15           C  
ATOM   1604  OE1 GLU A 208      20.285  23.426  33.607  1.00 48.10           O  
ATOM   1605  OE2 GLU A 208      21.628  23.039  35.299  1.00 49.44           O  
ATOM   1606  N   ILE A 209      16.645  20.648  38.162  1.00 33.91           N  
ATOM   1607  CA  ILE A 209      16.083  19.351  38.456  1.00 32.42           C  
ATOM   1608  C   ILE A 209      14.578  19.468  38.623  1.00 33.90           C  
ATOM   1609  O   ILE A 209      13.825  18.564  38.239  1.00 34.42           O  
ATOM   1610  CB  ILE A 209      16.755  18.725  39.717  1.00 31.42           C  
ATOM   1611  CG1 ILE A 209      16.537  17.212  39.706  1.00 29.46           C  
ATOM   1612  CG2 ILE A 209      16.213  19.355  40.990  1.00 29.37           C  
ATOM   1613  CD1 ILE A 209      17.002  16.564  38.419  1.00 28.73           C  
ATOM   1614  N   ASP A 210      14.131  20.590  39.179  1.00 32.95           N  
ATOM   1615  CA  ASP A 210      12.701  20.789  39.343  1.00 33.94           C  
ATOM   1616  C   ASP A 210      12.090  21.000  37.959  1.00 33.53           C  
ATOM   1617  O   ASP A 210      10.984  20.531  37.671  1.00 33.49           O  
ATOM   1618  CB  ASP A 210      12.411  22.003  40.220  1.00 34.96           C  
ATOM   1619  CG  ASP A 210      10.930  22.192  40.461  1.00 38.45           C  
ATOM   1620  OD1 ASP A 210      10.299  21.240  40.963  1.00 38.45           O  
ATOM   1621  OD2 ASP A 210      10.395  23.279  40.144  1.00 40.87           O  
ATOM   1622  N   GLN A 211      12.834  21.706  37.110  1.00 32.08           N  
ATOM   1623  CA  GLN A 211      12.408  21.997  35.747  1.00 30.51           C  
ATOM   1624  C   GLN A 211      12.228  20.695  34.988  1.00 30.16           C  
ATOM   1625  O   GLN A 211      11.212  20.456  34.340  1.00 29.76           O  
ATOM   1626  CB  GLN A 211      13.468  22.849  35.052  1.00 29.20           C  
ATOM   1627  CG  GLN A 211      13.109  23.269  33.646  1.00 27.62           C  
ATOM   1628  CD  GLN A 211      11.796  23.997  33.595  1.00 28.17           C  
ATOM   1629  OE1 GLN A 211      11.498  24.811  34.463  1.00 32.38           O  
ATOM   1630  NE2 GLN A 211      11.000  23.718  32.576  1.00 28.11           N  
ATOM   1631  N   LEU A 212      13.237  19.849  35.086  1.00 31.67           N  
ATOM   1632  CA  LEU A 212      13.230  18.569  34.414  1.00 32.80           C  
ATOM   1633  C   LEU A 212      12.120  17.676  34.975  1.00 32.26           C  
ATOM   1634  O   LEU A 212      11.441  16.974  34.237  1.00 32.40           O  
ATOM   1635  CB  LEU A 212      14.600  17.914  34.600  1.00 33.76           C  
ATOM   1636  CG  LEU A 212      15.055  16.873  33.585  1.00 34.86           C  
ATOM   1637  CD1 LEU A 212      15.243  17.524  32.226  1.00 33.86           C  
ATOM   1638  CD2 LEU A 212      16.359  16.257  34.059  1.00 37.96           C  
ATOM   1639  N   PHE A 213      11.918  17.717  36.283  1.00 32.25           N  
ATOM   1640  CA  PHE A 213      10.895  16.880  36.876  1.00 31.16           C  
ATOM   1641  C   PHE A 213       9.474  17.320  36.597  1.00 30.63           C  
ATOM   1642  O   PHE A 213       8.568  16.488  36.544  1.00 30.01           O  
ATOM   1643  CB  PHE A 213      11.146  16.733  38.370  1.00 32.57           C  
ATOM   1644  CG  PHE A 213      12.232  15.754  38.688  1.00 33.04           C  
ATOM   1645  CD1 PHE A 213      12.890  15.081  37.669  1.00 32.81           C  
ATOM   1646  CD2 PHE A 213      12.589  15.481  40.003  1.00 35.41           C  
ATOM   1647  CE1 PHE A 213      13.885  14.151  37.953  1.00 34.04           C  
ATOM   1648  CE2 PHE A 213      13.585  14.549  40.293  1.00 31.39           C  
ATOM   1649  CZ  PHE A 213      14.229  13.887  39.267  1.00 32.47           C  
ATOM   1650  N   ARG A 214       9.268  18.619  36.422  1.00 29.81           N  
ATOM   1651  CA  ARG A 214       7.938  19.103  36.090  1.00 30.70           C  
ATOM   1652  C   ARG A 214       7.624  18.618  34.669  1.00 31.55           C  
ATOM   1653  O   ARG A 214       6.488  18.258  34.362  1.00 31.61           O  
ATOM   1654  CB  ARG A 214       7.881  20.622  36.165  1.00 30.86           C  
ATOM   1655  CG  ARG A 214       7.755  21.168  37.567  1.00 29.40           C  
ATOM   1656  CD  ARG A 214       7.939  22.668  37.527  1.00 35.03           C  
ATOM   1657  NE  ARG A 214       7.830  23.296  38.836  1.00 37.97           N  
ATOM   1658  CZ  ARG A 214       6.683  23.493  39.474  1.00 40.16           C  
ATOM   1659  NH1 ARG A 214       5.536  23.108  38.925  1.00 39.75           N  
ATOM   1660  NH2 ARG A 214       6.684  24.097  40.651  1.00 42.09           N  
ATOM   1661  N   ILE A 215       8.641  18.589  33.811  1.00 30.58           N  
ATOM   1662  CA  ILE A 215       8.459  18.100  32.448  1.00 30.37           C  
ATOM   1663  C   ILE A 215       8.123  16.610  32.540  1.00 32.58           C  
ATOM   1664  O   ILE A 215       7.187  16.121  31.896  1.00 32.94           O  
ATOM   1665  CB  ILE A 215       9.747  18.294  31.601  1.00 28.33           C  
ATOM   1666  CG1 ILE A 215      10.031  19.796  31.417  1.00 28.36           C  
ATOM   1667  CG2 ILE A 215       9.597  17.622  30.246  1.00 25.12           C  
ATOM   1668  CD1 ILE A 215      11.354  20.111  30.713  1.00 24.04           C  
ATOM   1669  N   PHE A 216       8.883  15.895  33.365  1.00 33.60           N  
ATOM   1670  CA  PHE A 216       8.678  14.462  33.561  1.00 34.12           C  
ATOM   1671  C   PHE A 216       7.283  14.107  34.064  1.00 35.64           C  
ATOM   1672  O   PHE A 216       6.671  13.155  33.575  1.00 35.54           O  
ATOM   1673  CB  PHE A 216       9.713  13.908  34.541  1.00 32.37           C  
ATOM   1674  CG  PHE A 216      11.104  13.809  33.974  1.00 33.03           C  
ATOM   1675  CD1 PHE A 216      11.383  14.242  32.676  1.00 33.07           C  
ATOM   1676  CD2 PHE A 216      12.138  13.282  34.742  1.00 32.73           C  
ATOM   1677  CE1 PHE A 216      12.665  14.150  32.156  1.00 33.05           C  
ATOM   1678  CE2 PHE A 216      13.422  13.185  34.233  1.00 32.06           C  
ATOM   1679  CZ  PHE A 216      13.688  13.619  32.936  1.00 34.50           C  
ATOM   1680  N   ARG A 217       6.784  14.866  35.038  1.00 37.19           N  
ATOM   1681  CA  ARG A 217       5.466  14.607  35.611  1.00 38.74           C  
ATOM   1682  C   ARG A 217       4.346  14.800  34.602  1.00 40.72           C  
ATOM   1683  O   ARG A 217       3.282  14.198  34.721  1.00 43.50           O  
ATOM   1684  CB  ARG A 217       5.202  15.530  36.801  1.00 39.97           C  
ATOM   1685  CG  ARG A 217       6.216  15.436  37.931  1.00 45.77           C  
ATOM   1686  CD  ARG A 217       6.034  16.589  38.918  1.00 48.26           C  
ATOM   1687  NE  ARG A 217       7.305  17.019  39.504  1.00 49.15           N  
ATOM   1688  CZ  ARG A 217       7.468  18.143  40.199  1.00 49.72           C  
ATOM   1689  NH1 ARG A 217       6.439  18.963  40.402  1.00 50.69           N  
ATOM   1690  NH2 ARG A 217       8.663  18.455  40.684  1.00 46.91           N  
ATOM   1691  N   THR A 218       4.580  15.642  33.605  1.00 41.06           N  
ATOM   1692  CA  THR A 218       3.556  15.921  32.612  1.00 38.99           C  
ATOM   1693  C   THR A 218       3.648  15.087  31.340  1.00 38.43           C  
ATOM   1694  O   THR A 218       2.641  14.581  30.860  1.00 38.00           O  
ATOM   1695  CB  THR A 218       3.583  17.405  32.220  1.00 39.31           C  
ATOM   1696  OG1 THR A 218       3.389  18.208  33.389  1.00 41.34           O  
ATOM   1697  CG2 THR A 218       2.490  17.713  31.216  1.00 40.15           C  
ATOM   1698  N   LEU A 219       4.847  14.962  30.785  1.00 36.39           N  
ATOM   1699  CA  LEU A 219       5.030  14.204  29.552  1.00 37.24           C  
ATOM   1700  C   LEU A 219       5.535  12.774  29.781  1.00 35.47           C  
ATOM   1701  O   LEU A 219       5.630  11.985  28.841  1.00 34.15           O  
ATOM   1702  CB  LEU A 219       6.008  14.944  28.638  1.00 37.21           C  
ATOM   1703  CG  LEU A 219       5.698  16.406  28.321  1.00 35.01           C  
ATOM   1704  CD1 LEU A 219       6.849  16.998  27.532  1.00 34.59           C  
ATOM   1705  CD2 LEU A 219       4.412  16.507  27.530  1.00 33.11           C  
ATOM   1706  N   GLY A 220       5.858  12.454  31.031  1.00 34.33           N  
ATOM   1707  CA  GLY A 220       6.357  11.134  31.355  1.00 34.96           C  
ATOM   1708  C   GLY A 220       7.874  11.086  31.341  1.00 35.50           C  
ATOM   1709  O   GLY A 220       8.511  11.770  30.538  1.00 34.25           O  
ATOM   1710  N   THR A 221       8.461  10.286  32.230  1.00 35.32           N  
ATOM   1711  CA  THR A 221       9.911  10.164  32.292  1.00 33.58           C  
ATOM   1712  C   THR A 221      10.340   9.546  30.979  1.00 35.20           C  
ATOM   1713  O   THR A 221       9.855   8.483  30.593  1.00 37.64           O  
ATOM   1714  CB  THR A 221      10.344   9.285  33.471  1.00 32.27           C  
ATOM   1715  OG1 THR A 221       9.864   9.866  34.689  1.00 29.97           O  
ATOM   1716  CG2 THR A 221      11.865   9.200  33.547  1.00 34.70           C  
ATOM   1717  N   PRO A 222      11.253  10.207  30.258  1.00 34.86           N  
ATOM   1718  CA  PRO A 222      11.663   9.628  28.985  1.00 34.04           C  
ATOM   1719  C   PRO A 222      12.592   8.445  29.162  1.00 35.06           C  
ATOM   1720  O   PRO A 222      13.335   8.370  30.139  1.00 36.18           O  
ATOM   1721  CB  PRO A 222      12.343  10.800  28.299  1.00 33.65           C  
ATOM   1722  CG  PRO A 222      13.074  11.429  29.436  1.00 33.73           C  
ATOM   1723  CD  PRO A 222      12.046  11.412  30.564  1.00 34.14           C  
ATOM   1724  N   ASP A 223      12.525   7.511  28.223  1.00 35.48           N  
ATOM   1725  CA  ASP A 223      13.403   6.358  28.238  1.00 38.10           C  
ATOM   1726  C   ASP A 223      13.796   6.068  26.803  1.00 38.14           C  
ATOM   1727  O   ASP A 223      13.438   6.818  25.890  1.00 37.75           O  
ATOM   1728  CB  ASP A 223      12.739   5.127  28.872  1.00 41.87           C  
ATOM   1729  CG  ASP A 223      11.426   4.759  28.217  1.00 45.08           C  
ATOM   1730  OD1 ASP A 223      11.237   5.059  27.021  1.00 47.36           O  
ATOM   1731  OD2 ASP A 223      10.583   4.148  28.907  1.00 48.75           O  
ATOM   1732  N   GLU A 224      14.536   4.986  26.604  1.00 36.82           N  
ATOM   1733  CA  GLU A 224      14.992   4.621  25.278  1.00 35.53           C  
ATOM   1734  C   GLU A 224      13.851   4.382  24.321  1.00 35.41           C  
ATOM   1735  O   GLU A 224      14.042   4.422  23.111  1.00 35.33           O  
ATOM   1736  CB  GLU A 224      15.862   3.370  25.346  1.00 36.38           C  
ATOM   1737  CG  GLU A 224      17.222   3.594  25.972  1.00 36.06           C  
ATOM   1738  CD  GLU A 224      18.027   4.651  25.251  1.00 35.92           C  
ATOM   1739  OE1 GLU A 224      18.097   4.613  24.006  1.00 34.98           O  
ATOM   1740  OE2 GLU A 224      18.606   5.516  25.935  1.00 40.04           O  
ATOM   1741  N   VAL A 225      12.666   4.124  24.861  1.00 36.88           N  
ATOM   1742  CA  VAL A 225      11.498   3.861  24.028  1.00 37.35           C  
ATOM   1743  C   VAL A 225      11.058   5.100  23.258  1.00 37.91           C  
ATOM   1744  O   VAL A 225      11.003   5.088  22.029  1.00 39.21           O  
ATOM   1745  CB  VAL A 225      10.290   3.342  24.871  1.00 40.20           C  
ATOM   1746  CG1 VAL A 225       9.016   3.338  24.004  1.00 39.15           C  
ATOM   1747  CG2 VAL A 225      10.576   1.922  25.405  1.00 35.96           C  
ATOM   1748  N   VAL A 226      10.749   6.168  23.978  1.00 35.88           N  
ATOM   1749  CA  VAL A 226      10.298   7.384  23.333  1.00 37.82           C  
ATOM   1750  C   VAL A 226      11.435   8.312  22.929  1.00 37.57           C  
ATOM   1751  O   VAL A 226      11.250   9.201  22.098  1.00 38.11           O  
ATOM   1752  CB  VAL A 226       9.305   8.135  24.243  1.00 41.44           C  
ATOM   1753  CG1 VAL A 226       8.185   7.173  24.656  1.00 40.62           C  
ATOM   1754  CG2 VAL A 226      10.022   8.696  25.489  1.00 41.79           C  
ATOM   1755  N   TRP A 227      12.617   8.092  23.496  1.00 37.34           N  
ATOM   1756  CA  TRP A 227      13.765   8.934  23.183  1.00 35.68           C  
ATOM   1757  C   TRP A 227      15.061   8.138  23.075  1.00 37.59           C  
ATOM   1758  O   TRP A 227      15.852   8.080  24.025  1.00 40.39           O  
ATOM   1759  CB  TRP A 227      13.916  10.024  24.252  1.00 31.10           C  
ATOM   1760  CG  TRP A 227      14.896  11.098  23.902  1.00 27.89           C  
ATOM   1761  CD1 TRP A 227      15.762  11.114  22.840  1.00 26.64           C  
ATOM   1762  CD2 TRP A 227      15.130  12.309  24.628  1.00 25.42           C  
ATOM   1763  NE1 TRP A 227      16.518  12.257  22.867  1.00 24.39           N  
ATOM   1764  CE2 TRP A 227      16.149  13.009  23.952  1.00 24.96           C  
ATOM   1765  CE3 TRP A 227      14.575  12.870  25.786  1.00 25.37           C  
ATOM   1766  CZ2 TRP A 227      16.626  14.247  24.396  1.00 26.05           C  
ATOM   1767  CZ3 TRP A 227      15.049  14.097  26.227  1.00 26.17           C  
ATOM   1768  CH2 TRP A 227      16.065  14.774  25.534  1.00 24.58           C  
ATOM   1769  N   PRO A 228      15.303   7.512  21.913  1.00 38.43           N  
ATOM   1770  CA  PRO A 228      16.527   6.728  21.721  1.00 38.02           C  
ATOM   1771  C   PRO A 228      17.820   7.485  22.025  1.00 38.56           C  
ATOM   1772  O   PRO A 228      18.106   8.532  21.431  1.00 38.73           O  
ATOM   1773  CB  PRO A 228      16.442   6.295  20.255  1.00 37.19           C  
ATOM   1774  CG  PRO A 228      15.522   7.315  19.632  1.00 37.58           C  
ATOM   1775  CD  PRO A 228      14.479   7.492  20.695  1.00 37.07           C  
ATOM   1776  N   GLY A 229      18.598   6.941  22.955  1.00 37.13           N  
ATOM   1777  CA  GLY A 229      19.859   7.553  23.317  1.00 34.98           C  
ATOM   1778  C   GLY A 229      19.785   8.410  24.558  1.00 34.96           C  
ATOM   1779  O   GLY A 229      20.816   8.802  25.088  1.00 34.55           O  
ATOM   1780  N   VAL A 230      18.571   8.688  25.030  1.00 35.47           N  
ATOM   1781  CA  VAL A 230      18.368   9.533  26.205  1.00 35.26           C  
ATOM   1782  C   VAL A 230      19.189   9.137  27.433  1.00 35.57           C  
ATOM   1783  O   VAL A 230      19.672   9.997  28.165  1.00 34.91           O  
ATOM   1784  CB  VAL A 230      16.872   9.584  26.603  1.00 33.78           C  
ATOM   1785  CG1 VAL A 230      16.390   8.214  27.055  1.00 32.29           C  
ATOM   1786  CG2 VAL A 230      16.673  10.598  27.691  1.00 34.70           C  
ATOM   1787  N   THR A 231      19.346   7.838  27.663  1.00 37.75           N  
ATOM   1788  CA  THR A 231      20.111   7.357  28.816  1.00 38.93           C  
ATOM   1789  C   THR A 231      21.625   7.557  28.641  1.00 40.36           C  
ATOM   1790  O   THR A 231      22.391   7.369  29.577  1.00 40.65           O  
ATOM   1791  CB  THR A 231      19.835   5.855  29.085  1.00 38.20           C  
ATOM   1792  OG1 THR A 231      20.237   5.084  27.945  1.00 39.48           O  
ATOM   1793  CG2 THR A 231      18.344   5.614  29.358  1.00 34.69           C  
ATOM   1794  N   SER A 232      22.053   7.934  27.442  1.00 41.40           N  
ATOM   1795  CA  SER A 232      23.471   8.168  27.182  1.00 42.86           C  
ATOM   1796  C   SER A 232      23.787   9.625  27.524  1.00 42.41           C  
ATOM   1797  O   SER A 232      24.938   9.991  27.756  1.00 42.07           O  
ATOM   1798  CB  SER A 232      23.796   7.898  25.702  1.00 44.88           C  
ATOM   1799  OG  SER A 232      23.355   6.607  25.291  1.00 50.85           O  
ATOM   1800  N   MET A 233      22.744  10.450  27.543  1.00 42.07           N  
ATOM   1801  CA  MET A 233      22.856  11.868  27.852  1.00 40.72           C  
ATOM   1802  C   MET A 233      23.677  12.073  29.121  1.00 40.51           C  
ATOM   1803  O   MET A 233      23.521  11.344  30.104  1.00 40.91           O  
ATOM   1804  CB  MET A 233      21.458  12.465  28.031  1.00 43.00           C  
ATOM   1805  CG  MET A 233      20.576  12.385  26.790  1.00 45.04           C  
ATOM   1806  SD  MET A 233      20.465  13.955  25.913  1.00 46.26           S  
ATOM   1807  CE  MET A 233      22.080  14.043  25.158  1.00 49.82           C  
ATOM   1808  N   PRO A 234      24.560  13.079  29.116  1.00 39.80           N  
ATOM   1809  CA  PRO A 234      25.444  13.434  30.230  1.00 38.76           C  
ATOM   1810  C   PRO A 234      24.812  13.551  31.622  1.00 38.52           C  
ATOM   1811  O   PRO A 234      25.351  13.015  32.592  1.00 38.94           O  
ATOM   1812  CB  PRO A 234      26.057  14.755  29.767  1.00 38.33           C  
ATOM   1813  CG  PRO A 234      26.145  14.570  28.292  1.00 38.05           C  
ATOM   1814  CD  PRO A 234      24.790  13.979  27.970  1.00 39.69           C  
ATOM   1815  N   ASP A 235      23.689  14.256  31.730  1.00 36.31           N  
ATOM   1816  CA  ASP A 235      23.045  14.439  33.032  1.00 36.08           C  
ATOM   1817  C   ASP A 235      21.885  13.502  33.289  1.00 35.83           C  
ATOM   1818  O   ASP A 235      21.054  13.765  34.160  1.00 36.02           O  
ATOM   1819  CB  ASP A 235      22.544  15.875  33.195  1.00 36.26           C  
ATOM   1820  CG  ASP A 235      23.643  16.887  33.076  1.00 34.82           C  
ATOM   1821  OD1 ASP A 235      24.766  16.604  33.525  1.00 34.80           O  
ATOM   1822  OD2 ASP A 235      23.381  17.975  32.542  1.00 40.83           O  
ATOM   1823  N   TYR A 236      21.814  12.421  32.522  1.00 34.91           N  
ATOM   1824  CA  TYR A 236      20.747  11.453  32.698  1.00 34.49           C  
ATOM   1825  C   TYR A 236      21.089  10.579  33.880  1.00 34.65           C  
ATOM   1826  O   TYR A 236      22.218  10.117  34.008  1.00 36.72           O  
ATOM   1827  CB  TYR A 236      20.603  10.566  31.474  1.00 33.09           C  
ATOM   1828  CG  TYR A 236      19.447   9.620  31.604  1.00 37.09           C  
ATOM   1829  CD1 TYR A 236      18.158  10.014  31.253  1.00 37.20           C  
ATOM   1830  CD2 TYR A 236      19.627   8.343  32.129  1.00 38.14           C  
ATOM   1831  CE1 TYR A 236      17.078   9.158  31.421  1.00 39.04           C  
ATOM   1832  CE2 TYR A 236      18.550   7.482  32.305  1.00 39.28           C  
ATOM   1833  CZ  TYR A 236      17.280   7.894  31.946  1.00 39.38           C  
ATOM   1834  OH  TYR A 236      16.215   7.030  32.090  1.00 44.56           O  
ATOM   1835  N   LYS A 237      20.121  10.342  34.750  1.00 34.38           N  
ATOM   1836  CA  LYS A 237      20.383   9.509  35.905  1.00 32.47           C  
ATOM   1837  C   LYS A 237      19.375   8.381  35.911  1.00 33.67           C  
ATOM   1838  O   LYS A 237      18.165   8.625  35.994  1.00 31.70           O  
ATOM   1839  CB  LYS A 237      20.249  10.328  37.181  1.00 32.88           C  
ATOM   1840  CG  LYS A 237      21.070  11.611  37.192  1.00 36.66           C  
ATOM   1841  CD  LYS A 237      22.565  11.318  37.172  1.00 35.85           C  
ATOM   1842  CE  LYS A 237      23.361  12.588  37.392  1.00 37.82           C  
ATOM   1843  NZ  LYS A 237      24.831  12.336  37.383  1.00 40.70           N  
ATOM   1844  N   PRO A 238      19.857   7.125  35.814  1.00 33.41           N  
ATOM   1845  CA  PRO A 238      18.992   5.942  35.814  1.00 32.20           C  
ATOM   1846  C   PRO A 238      18.075   5.983  37.030  1.00 33.92           C  
ATOM   1847  O   PRO A 238      17.099   5.238  37.115  1.00 35.72           O  
ATOM   1848  CB  PRO A 238      19.982   4.785  35.895  1.00 31.38           C  
ATOM   1849  CG  PRO A 238      21.221   5.342  35.229  1.00 31.58           C  
ATOM   1850  CD  PRO A 238      21.282   6.739  35.772  1.00 33.52           C  
ATOM   1851  N   SER A 239      18.389   6.876  37.964  1.00 33.76           N  
ATOM   1852  CA  SER A 239      17.605   7.023  39.178  1.00 35.02           C  
ATOM   1853  C   SER A 239      16.455   8.040  39.120  1.00 36.36           C  
ATOM   1854  O   SER A 239      15.842   8.327  40.149  1.00 37.79           O  
ATOM   1855  CB  SER A 239      18.529   7.382  40.339  1.00 32.40           C  
ATOM   1856  OG  SER A 239      19.148   8.628  40.101  1.00 31.95           O  
ATOM   1857  N   PHE A 240      16.165   8.602  37.949  1.00 37.56           N  
ATOM   1858  CA  PHE A 240      15.051   9.553  37.849  1.00 37.21           C  
ATOM   1859  C   PHE A 240      13.742   8.825  38.154  1.00 36.47           C  
ATOM   1860  O   PHE A 240      13.537   7.695  37.712  1.00 35.26           O  
ATOM   1861  CB  PHE A 240      14.906  10.135  36.437  1.00 36.70           C  
ATOM   1862  CG  PHE A 240      15.960  11.121  36.054  1.00 36.79           C  
ATOM   1863  CD1 PHE A 240      16.487  12.002  36.988  1.00 37.01           C  
ATOM   1864  CD2 PHE A 240      16.392  11.199  34.733  1.00 36.51           C  
ATOM   1865  CE1 PHE A 240      17.429  12.948  36.617  1.00 38.00           C  
ATOM   1866  CE2 PHE A 240      17.332  12.138  34.346  1.00 37.59           C  
ATOM   1867  CZ  PHE A 240      17.855  13.018  35.291  1.00 39.72           C  
ATOM   1868  N   PRO A 241      12.838   9.465  38.906  1.00 35.93           N  
ATOM   1869  CA  PRO A 241      11.562   8.820  39.220  1.00 37.24           C  
ATOM   1870  C   PRO A 241      10.823   8.505  37.932  1.00 40.51           C  
ATOM   1871  O   PRO A 241      10.823   9.313  37.005  1.00 42.28           O  
ATOM   1872  CB  PRO A 241      10.850   9.871  40.052  1.00 35.12           C  
ATOM   1873  CG  PRO A 241      11.994  10.496  40.803  1.00 36.02           C  
ATOM   1874  CD  PRO A 241      13.015  10.688  39.700  1.00 35.33           C  
ATOM   1875  N   LYS A 242      10.200   7.332  37.865  1.00 43.61           N  
ATOM   1876  CA  LYS A 242       9.463   6.939  36.668  1.00 45.62           C  
ATOM   1877  C   LYS A 242       8.017   7.456  36.699  1.00 45.82           C  
ATOM   1878  O   LYS A 242       7.155   6.852  37.318  1.00 46.67           O  
ATOM   1879  CB  LYS A 242       9.468   5.409  36.523  1.00 47.83           C  
ATOM   1880  CG  LYS A 242      10.856   4.773  36.407  1.00 50.53           C  
ATOM   1881  CD  LYS A 242      11.590   5.278  35.177  1.00 54.59           C  
ATOM   1882  CE  LYS A 242      13.041   4.817  35.150  1.00 56.80           C  
ATOM   1883  NZ  LYS A 242      13.808   5.542  34.092  1.00 59.39           N  
ATOM   1884  N   TRP A 243       7.760   8.575  36.031  1.00 46.93           N  
ATOM   1885  CA  TRP A 243       6.420   9.163  35.980  1.00 46.82           C  
ATOM   1886  C   TRP A 243       5.677   8.750  34.717  1.00 47.05           C  
ATOM   1887  O   TRP A 243       6.267   8.660  33.648  1.00 47.46           O  
ATOM   1888  CB  TRP A 243       6.504  10.687  35.994  1.00 46.93           C  
ATOM   1889  CG  TRP A 243       6.623  11.320  37.333  1.00 47.51           C  
ATOM   1890  CD1 TRP A 243       5.628  11.489  38.249  1.00 47.36           C  
ATOM   1891  CD2 TRP A 243       7.791  11.939  37.886  1.00 46.94           C  
ATOM   1892  NE1 TRP A 243       6.101  12.184  39.338  1.00 48.53           N  
ATOM   1893  CE2 TRP A 243       7.426  12.470  39.141  1.00 46.96           C  
ATOM   1894  CE3 TRP A 243       9.111  12.096  37.441  1.00 46.27           C  
ATOM   1895  CZ2 TRP A 243       8.331  13.150  39.958  1.00 47.25           C  
ATOM   1896  CZ3 TRP A 243      10.011  12.770  38.252  1.00 47.45           C  
ATOM   1897  CH2 TRP A 243       9.615  13.290  39.499  1.00 47.63           C  
ATOM   1898  N   ALA A 244       4.377   8.518  34.844  1.00 49.71           N  
ATOM   1899  CA  ALA A 244       3.543   8.139  33.709  1.00 51.88           C  
ATOM   1900  C   ALA A 244       3.170   9.386  32.923  1.00 52.46           C  
ATOM   1901  O   ALA A 244       3.091  10.479  33.482  1.00 53.92           O  
ATOM   1902  CB  ALA A 244       2.277   7.448  34.195  1.00 53.38           C  
ATOM   1903  N   ARG A 245       2.937   9.223  31.627  1.00 52.90           N  
ATOM   1904  CA  ARG A 245       2.558  10.352  30.793  1.00 54.36           C  
ATOM   1905  C   ARG A 245       1.106  10.733  31.085  1.00 55.55           C  
ATOM   1906  O   ARG A 245       0.223   9.873  31.139  1.00 53.99           O  
ATOM   1907  CB  ARG A 245       2.717   9.993  29.313  1.00 54.71           C  
ATOM   1908  CG  ARG A 245       2.505  11.158  28.362  1.00 56.93           C  
ATOM   1909  CD  ARG A 245       2.669  10.711  26.922  1.00 58.50           C  
ATOM   1910  NE  ARG A 245       2.433  11.790  25.963  1.00 62.40           N  
ATOM   1911  CZ  ARG A 245       3.261  12.811  25.746  1.00 63.92           C  
ATOM   1912  NH1 ARG A 245       4.402  12.908  26.427  1.00 63.13           N  
ATOM   1913  NH2 ARG A 245       2.954  13.729  24.832  1.00 61.78           N  
ATOM   1914  N   GLN A 246       0.872  12.026  31.287  1.00 56.95           N  
ATOM   1915  CA  GLN A 246      -0.463  12.542  31.564  1.00 57.65           C  
ATOM   1916  C   GLN A 246      -1.095  12.971  30.240  1.00 57.42           C  
ATOM   1917  O   GLN A 246      -0.460  13.644  29.431  1.00 57.54           O  
ATOM   1918  CB  GLN A 246      -0.373  13.734  32.523  1.00 59.14           C  
ATOM   1919  CG  GLN A 246      -1.654  14.007  33.290  1.00 64.53           C  
ATOM   1920  CD  GLN A 246      -1.496  15.083  34.356  1.00 66.65           C  
ATOM   1921  OE1 GLN A 246      -2.408  15.312  35.163  1.00 67.70           O  
ATOM   1922  NE2 GLN A 246      -0.343  15.753  34.364  1.00 65.67           N  
ATOM   1923  N   ASP A 247      -2.344  12.576  30.020  1.00 57.32           N  
ATOM   1924  CA  ASP A 247      -3.044  12.905  28.784  1.00 55.90           C  
ATOM   1925  C   ASP A 247      -3.039  14.407  28.497  1.00 53.85           C  
ATOM   1926  O   ASP A 247      -3.366  15.221  29.357  1.00 53.28           O  
ATOM   1927  CB  ASP A 247      -4.475  12.378  28.859  1.00 60.37           C  
ATOM   1928  CG  ASP A 247      -5.068  12.128  27.496  1.00 63.87           C  
ATOM   1929  OD1 ASP A 247      -4.394  11.461  26.678  1.00 65.01           O  
ATOM   1930  OD2 ASP A 247      -6.205  12.588  27.246  1.00 65.50           O  
ATOM   1931  N   PHE A 248      -2.664  14.759  27.274  1.00 52.05           N  
ATOM   1932  CA  PHE A 248      -2.578  16.153  26.832  1.00 50.70           C  
ATOM   1933  C   PHE A 248      -3.864  16.963  26.970  1.00 49.10           C  
ATOM   1934  O   PHE A 248      -3.832  18.193  26.995  1.00 48.33           O  
ATOM   1935  CB  PHE A 248      -2.107  16.196  25.373  1.00 50.16           C  
ATOM   1936  CG  PHE A 248      -0.811  16.904  25.183  1.00 49.93           C  
ATOM   1937  CD1 PHE A 248      -0.775  18.279  25.026  1.00 51.61           C  
ATOM   1938  CD2 PHE A 248       0.386  16.203  25.216  1.00 50.74           C  
ATOM   1939  CE1 PHE A 248       0.437  18.943  24.908  1.00 52.06           C  
ATOM   1940  CE2 PHE A 248       1.599  16.860  25.099  1.00 49.96           C  
ATOM   1941  CZ  PHE A 248       1.625  18.230  24.946  1.00 51.44           C  
ATOM   1942  N   SER A 249      -4.995  16.271  27.038  1.00 47.99           N  
ATOM   1943  CA  SER A 249      -6.291  16.930  27.176  1.00 46.75           C  
ATOM   1944  C   SER A 249      -6.323  17.690  28.503  1.00 43.85           C  
ATOM   1945  O   SER A 249      -6.994  18.705  28.644  1.00 40.63           O  
ATOM   1946  CB  SER A 249      -7.410  15.883  27.168  1.00 47.79           C  
ATOM   1947  OG  SER A 249      -7.347  15.070  28.337  1.00 50.29           O  
ATOM   1948  N   LYS A 250      -5.582  17.170  29.469  1.00 42.12           N  
ATOM   1949  CA  LYS A 250      -5.511  17.751  30.797  1.00 42.80           C  
ATOM   1950  C   LYS A 250      -4.432  18.831  30.900  1.00 42.15           C  
ATOM   1951  O   LYS A 250      -4.346  19.532  31.904  1.00 42.15           O  
ATOM   1952  CB  LYS A 250      -5.244  16.624  31.800  1.00 42.52           C  
ATOM   1953  CG  LYS A 250      -4.880  17.056  33.200  1.00 45.96           C  
ATOM   1954  CD  LYS A 250      -6.097  17.239  34.075  1.00 47.47           C  
ATOM   1955  CE  LYS A 250      -5.677  17.412  35.526  1.00 47.93           C  
ATOM   1956  NZ  LYS A 250      -4.780  16.294  35.964  1.00 47.10           N  
ATOM   1957  N   VAL A 251      -3.623  18.972  29.854  1.00 41.56           N  
ATOM   1958  CA  VAL A 251      -2.544  19.953  29.856  1.00 41.56           C  
ATOM   1959  C   VAL A 251      -2.924  21.331  29.324  1.00 41.28           C  
ATOM   1960  O   VAL A 251      -2.680  22.344  29.981  1.00 43.14           O  
ATOM   1961  CB  VAL A 251      -1.327  19.457  29.035  1.00 42.59           C  
ATOM   1962  CG1 VAL A 251      -0.296  20.566  28.931  1.00 42.67           C  
ATOM   1963  CG2 VAL A 251      -0.704  18.219  29.687  1.00 40.02           C  
ATOM   1964  N   VAL A 252      -3.505  21.378  28.132  1.00 40.16           N  
ATOM   1965  CA  VAL A 252      -3.871  22.659  27.540  1.00 40.66           C  
ATOM   1966  C   VAL A 252      -5.344  22.831  27.202  1.00 42.62           C  
ATOM   1967  O   VAL A 252      -5.705  23.044  26.043  1.00 41.49           O  
ATOM   1968  CB  VAL A 252      -3.049  22.942  26.270  1.00 37.99           C  
ATOM   1969  CG1 VAL A 252      -1.610  23.232  26.652  1.00 40.25           C  
ATOM   1970  CG2 VAL A 252      -3.107  21.752  25.332  1.00 35.01           C  
ATOM   1971  N   PRO A 253      -6.220  22.726  28.210  1.00 42.99           N  
ATOM   1972  CA  PRO A 253      -7.640  22.897  27.929  1.00 44.20           C  
ATOM   1973  C   PRO A 253      -7.856  24.409  27.904  1.00 45.17           C  
ATOM   1974  O   PRO A 253      -7.175  25.146  28.614  1.00 47.46           O  
ATOM   1975  CB  PRO A 253      -8.293  22.223  29.125  1.00 45.23           C  
ATOM   1976  CG  PRO A 253      -7.365  22.595  30.239  1.00 43.41           C  
ATOM   1977  CD  PRO A 253      -6.002  22.370  29.624  1.00 43.28           C  
ATOM   1978  N   PRO A 254      -8.801  24.896  27.096  1.00 44.88           N  
ATOM   1979  CA  PRO A 254      -9.660  24.111  26.229  1.00 43.54           C  
ATOM   1980  C   PRO A 254      -9.212  24.162  24.770  1.00 42.31           C  
ATOM   1981  O   PRO A 254     -10.040  24.208  23.869  1.00 44.99           O  
ATOM   1982  CB  PRO A 254     -11.018  24.758  26.460  1.00 44.11           C  
ATOM   1983  CG  PRO A 254     -10.659  26.224  26.505  1.00 44.55           C  
ATOM   1984  CD  PRO A 254      -9.269  26.295  27.153  1.00 45.35           C  
ATOM   1985  N   LEU A 255      -7.904  24.167  24.541  1.00 39.52           N  
ATOM   1986  CA  LEU A 255      -7.370  24.179  23.180  1.00 37.49           C  
ATOM   1987  C   LEU A 255      -8.032  23.023  22.422  1.00 37.60           C  
ATOM   1988  O   LEU A 255      -8.261  21.968  22.999  1.00 37.86           O  
ATOM   1989  CB  LEU A 255      -5.851  23.989  23.223  1.00 31.66           C  
ATOM   1990  CG  LEU A 255      -5.070  24.003  21.915  1.00 27.59           C  
ATOM   1991  CD1 LEU A 255      -5.303  25.280  21.160  1.00 28.64           C  
ATOM   1992  CD2 LEU A 255      -3.614  23.848  22.231  1.00 25.07           C  
ATOM   1993  N   ASP A 256      -8.348  23.216  21.142  1.00 39.09           N  
ATOM   1994  CA  ASP A 256      -9.001  22.164  20.357  1.00 39.73           C  
ATOM   1995  C   ASP A 256      -8.035  21.071  19.900  1.00 39.60           C  
ATOM   1996  O   ASP A 256      -6.816  21.202  20.034  1.00 41.62           O  
ATOM   1997  CB  ASP A 256      -9.741  22.770  19.149  1.00 41.43           C  
ATOM   1998  CG  ASP A 256      -8.802  23.248  18.048  1.00 44.44           C  
ATOM   1999  OD1 ASP A 256      -8.160  22.394  17.400  1.00 47.39           O  
ATOM   2000  OD2 ASP A 256      -8.711  24.475  17.820  1.00 45.79           O  
ATOM   2001  N   GLU A 257      -8.584  19.997  19.349  1.00 38.88           N  
ATOM   2002  CA  GLU A 257      -7.786  18.860  18.906  1.00 37.73           C  
ATOM   2003  C   GLU A 257      -6.641  19.189  17.953  1.00 35.99           C  
ATOM   2004  O   GLU A 257      -5.584  18.566  18.030  1.00 35.09           O  
ATOM   2005  CB  GLU A 257      -8.699  17.802  18.279  1.00 39.88           C  
ATOM   2006  CG  GLU A 257      -8.025  16.477  17.985  1.00 42.48           C  
ATOM   2007  CD  GLU A 257      -7.480  15.800  19.236  1.00 46.96           C  
ATOM   2008  OE1 GLU A 257      -8.219  15.728  20.247  1.00 46.44           O  
ATOM   2009  OE2 GLU A 257      -6.318  15.329  19.203  1.00 47.08           O  
ATOM   2010  N   ASP A 258      -6.842  20.146  17.050  1.00 36.45           N  
ATOM   2011  CA  ASP A 258      -5.779  20.517  16.105  1.00 36.28           C  
ATOM   2012  C   ASP A 258      -4.592  21.141  16.840  1.00 35.89           C  
ATOM   2013  O   ASP A 258      -3.435  20.830  16.563  1.00 36.20           O  
ATOM   2014  CB  ASP A 258      -6.286  21.516  15.054  1.00 36.11           C  
ATOM   2015  CG  ASP A 258      -7.058  20.852  13.920  1.00 36.56           C  
ATOM   2016  OD1 ASP A 258      -6.569  19.845  13.366  1.00 36.69           O  
ATOM   2017  OD2 ASP A 258      -8.149  21.352  13.566  1.00 36.27           O  
ATOM   2018  N   GLY A 259      -4.893  22.033  17.773  1.00 34.74           N  
ATOM   2019  CA  GLY A 259      -3.849  22.687  18.526  1.00 35.49           C  
ATOM   2020  C   GLY A 259      -3.117  21.722  19.431  1.00 36.68           C  
ATOM   2021  O   GLY A 259      -1.888  21.760  19.508  1.00 38.97           O  
ATOM   2022  N   ARG A 260      -3.859  20.854  20.117  1.00 35.30           N  
ATOM   2023  CA  ARG A 260      -3.234  19.888  21.014  1.00 36.03           C  
ATOM   2024  C   ARG A 260      -2.330  18.937  20.259  1.00 34.86           C  
ATOM   2025  O   ARG A 260      -1.387  18.390  20.819  1.00 35.64           O  
ATOM   2026  CB  ARG A 260      -4.288  19.089  21.772  1.00 37.24           C  
ATOM   2027  CG  ARG A 260      -5.040  19.896  22.808  1.00 41.51           C  
ATOM   2028  CD  ARG A 260      -5.678  18.964  23.800  1.00 43.60           C  
ATOM   2029  NE  ARG A 260      -6.565  18.034  23.119  1.00 45.01           N  
ATOM   2030  CZ  ARG A 260      -7.826  18.313  22.827  1.00 46.75           C  
ATOM   2031  NH1 ARG A 260      -8.329  19.489  23.170  1.00 48.82           N  
ATOM   2032  NH2 ARG A 260      -8.574  17.430  22.184  1.00 47.73           N  
ATOM   2033  N   SER A 261      -2.635  18.746  18.982  1.00 35.37           N  
ATOM   2034  CA  SER A 261      -1.863  17.876  18.107  1.00 34.16           C  
ATOM   2035  C   SER A 261      -0.578  18.586  17.715  1.00 32.19           C  
ATOM   2036  O   SER A 261       0.479  17.973  17.642  1.00 34.54           O  
ATOM   2037  CB  SER A 261      -2.675  17.547  16.851  1.00 35.16           C  
ATOM   2038  OG  SER A 261      -1.961  16.693  15.970  1.00 37.43           O  
ATOM   2039  N   LEU A 262      -0.674  19.883  17.458  1.00 30.38           N  
ATOM   2040  CA  LEU A 262       0.494  20.664  17.086  1.00 28.75           C  
ATOM   2041  C   LEU A 262       1.414  20.762  18.294  1.00 29.64           C  
ATOM   2042  O   LEU A 262       2.621  20.544  18.190  1.00 31.11           O  
ATOM   2043  CB  LEU A 262       0.078  22.067  16.626  1.00 25.35           C  
ATOM   2044  CG  LEU A 262       1.226  23.031  16.299  1.00 25.92           C  
ATOM   2045  CD1 LEU A 262       2.134  22.430  15.240  1.00 24.56           C  
ATOM   2046  CD2 LEU A 262       0.669  24.356  15.823  1.00 24.24           C  
ATOM   2047  N   LEU A 263       0.831  21.074  19.446  1.00 29.88           N  
ATOM   2048  CA  LEU A 263       1.593  21.213  20.678  1.00 29.95           C  
ATOM   2049  C   LEU A 263       2.367  19.944  21.030  1.00 30.12           C  
ATOM   2050  O   LEU A 263       3.560  20.001  21.328  1.00 30.98           O  
ATOM   2051  CB  LEU A 263       0.662  21.584  21.830  1.00 28.42           C  
ATOM   2052  CG  LEU A 263       1.328  21.841  23.179  1.00 29.14           C  
ATOM   2053  CD1 LEU A 263       2.186  23.105  23.091  1.00 29.34           C  
ATOM   2054  CD2 LEU A 263       0.262  22.002  24.248  1.00 29.64           C  
ATOM   2055  N   SER A 264       1.692  18.801  20.989  1.00 30.42           N  
ATOM   2056  CA  SER A 264       2.333  17.531  21.325  1.00 32.00           C  
ATOM   2057  C   SER A 264       3.517  17.229  20.413  1.00 29.93           C  
ATOM   2058  O   SER A 264       4.476  16.584  20.822  1.00 29.79           O  
ATOM   2059  CB  SER A 264       1.316  16.382  21.266  1.00 30.87           C  
ATOM   2060  OG  SER A 264       0.760  16.279  19.976  1.00 34.46           O  
ATOM   2061  N   GLN A 265       3.448  17.696  19.175  1.00 30.21           N  
ATOM   2062  CA  GLN A 265       4.539  17.488  18.238  1.00 29.77           C  
ATOM   2063  C   GLN A 265       5.690  18.462  18.503  1.00 30.00           C  
ATOM   2064  O   GLN A 265       6.846  18.180  18.178  1.00 29.24           O  
ATOM   2065  CB  GLN A 265       4.029  17.645  16.810  1.00 33.07           C  
ATOM   2066  CG  GLN A 265       3.251  16.446  16.314  1.00 34.91           C  
ATOM   2067  CD  GLN A 265       2.721  16.646  14.918  1.00 37.32           C  
ATOM   2068  OE1 GLN A 265       1.742  17.365  14.710  1.00 42.63           O  
ATOM   2069  NE2 GLN A 265       3.368  16.021  13.948  1.00 38.93           N  
ATOM   2070  N   MET A 266       5.371  19.610  19.093  1.00 29.13           N  
ATOM   2071  CA  MET A 266       6.391  20.603  19.412  1.00 29.17           C  
ATOM   2072  C   MET A 266       7.038  20.216  20.733  1.00 29.28           C  
ATOM   2073  O   MET A 266       8.102  20.718  21.078  1.00 29.21           O  
ATOM   2074  CB  MET A 266       5.777  22.003  19.541  1.00 29.11           C  
ATOM   2075  CG  MET A 266       5.196  22.576  18.259  1.00 27.64           C  
ATOM   2076  SD  MET A 266       4.317  24.138  18.549  1.00 30.75           S  
ATOM   2077  CE  MET A 266       5.620  25.326  18.248  1.00 26.32           C  
ATOM   2078  N   LEU A 267       6.389  19.325  21.476  1.00 29.57           N  
ATOM   2079  CA  LEU A 267       6.935  18.887  22.755  1.00 31.23           C  
ATOM   2080  C   LEU A 267       7.397  17.436  22.786  1.00 32.79           C  
ATOM   2081  O   LEU A 267       7.388  16.815  23.840  1.00 34.80           O  
ATOM   2082  CB  LEU A 267       5.930  19.121  23.889  1.00 30.00           C  
ATOM   2083  CG  LEU A 267       5.471  20.558  24.170  1.00 29.76           C  
ATOM   2084  CD1 LEU A 267       4.516  20.544  25.353  1.00 29.48           C  
ATOM   2085  CD2 LEU A 267       6.665  21.458  24.449  1.00 25.77           C  
ATOM   2086  N   HIS A 268       7.787  16.883  21.640  1.00 34.78           N  
ATOM   2087  CA  HIS A 268       8.285  15.514  21.626  1.00 35.59           C  
ATOM   2088  C   HIS A 268       9.648  15.522  22.307  1.00 34.82           C  
ATOM   2089  O   HIS A 268      10.454  16.442  22.107  1.00 33.87           O  
ATOM   2090  CB  HIS A 268       8.452  14.979  20.196  1.00 40.10           C  
ATOM   2091  CG  HIS A 268       7.198  14.413  19.608  1.00 44.24           C  
ATOM   2092  ND1 HIS A 268       6.308  13.658  20.341  1.00 46.51           N  
ATOM   2093  CD2 HIS A 268       6.683  14.490  18.357  1.00 45.25           C  
ATOM   2094  CE1 HIS A 268       5.296  13.298  19.570  1.00 44.79           C  
ATOM   2095  NE2 HIS A 268       5.500  13.790  18.362  1.00 44.78           N  
ATOM   2096  N   TYR A 269       9.906  14.505  23.118  1.00 32.80           N  
ATOM   2097  CA  TYR A 269      11.185  14.399  23.802  1.00 29.59           C  
ATOM   2098  C   TYR A 269      12.328  14.334  22.801  1.00 30.39           C  
ATOM   2099  O   TYR A 269      13.304  15.070  22.907  1.00 32.49           O  
ATOM   2100  CB  TYR A 269      11.214  13.151  24.677  1.00 25.17           C  
ATOM   2101  CG  TYR A 269      10.670  13.384  26.063  1.00 26.76           C  
ATOM   2102  CD1 TYR A 269      11.209  14.381  26.872  1.00 22.92           C  
ATOM   2103  CD2 TYR A 269       9.624  12.601  26.576  1.00 22.66           C  
ATOM   2104  CE1 TYR A 269      10.732  14.596  28.149  1.00 22.91           C  
ATOM   2105  CE2 TYR A 269       9.138  12.814  27.855  1.00 20.81           C  
ATOM   2106  CZ  TYR A 269       9.698  13.818  28.637  1.00 22.98           C  
ATOM   2107  OH  TYR A 269       9.220  14.076  29.903  1.00 24.64           O  
ATOM   2108  N   ASP A 270      12.194  13.453  21.820  1.00 31.02           N  
ATOM   2109  CA  ASP A 270      13.229  13.271  20.819  1.00 29.86           C  
ATOM   2110  C   ASP A 270      13.330  14.496  19.935  1.00 30.86           C  
ATOM   2111  O   ASP A 270      12.418  14.785  19.157  1.00 32.22           O  
ATOM   2112  CB  ASP A 270      12.910  12.050  19.963  1.00 30.62           C  
ATOM   2113  CG  ASP A 270      14.076  11.625  19.112  1.00 33.85           C  
ATOM   2114  OD1 ASP A 270      14.903  12.492  18.767  1.00 35.76           O  
ATOM   2115  OD2 ASP A 270      14.162  10.427  18.778  1.00 34.62           O  
ATOM   2116  N   PRO A 271      14.443  15.238  20.032  1.00 31.18           N  
ATOM   2117  CA  PRO A 271      14.601  16.431  19.206  1.00 32.50           C  
ATOM   2118  C   PRO A 271      14.413  16.105  17.732  1.00 35.41           C  
ATOM   2119  O   PRO A 271      13.835  16.889  16.978  1.00 36.65           O  
ATOM   2120  CB  PRO A 271      16.025  16.876  19.520  1.00 28.57           C  
ATOM   2121  CG  PRO A 271      16.192  16.460  20.921  1.00 28.55           C  
ATOM   2122  CD  PRO A 271      15.603  15.074  20.923  1.00 31.03           C  
ATOM   2123  N   ASN A 272      14.894  14.938  17.323  1.00 38.17           N  
ATOM   2124  CA  ASN A 272      14.778  14.546  15.934  1.00 41.24           C  
ATOM   2125  C   ASN A 272      13.338  14.267  15.529  1.00 43.21           C  
ATOM   2126  O   ASN A 272      13.004  14.369  14.351  1.00 46.61           O  
ATOM   2127  CB  ASN A 272      15.637  13.322  15.641  1.00 44.68           C  
ATOM   2128  CG  ASN A 272      16.022  13.229  14.174  1.00 49.51           C  
ATOM   2129  OD1 ASN A 272      16.216  12.140  13.638  1.00 52.86           O  
ATOM   2130  ND2 ASN A 272      16.148  14.380  13.521  1.00 51.56           N  
ATOM   2131  N   LYS A 273      12.488  13.914  16.494  1.00 42.99           N  
ATOM   2132  CA  LYS A 273      11.079  13.639  16.206  1.00 42.22           C  
ATOM   2133  C   LYS A 273      10.262  14.914  16.329  1.00 39.71           C  
ATOM   2134  O   LYS A 273       9.168  15.010  15.781  1.00 38.47           O  
ATOM   2135  CB  LYS A 273      10.496  12.604  17.180  1.00 45.86           C  
ATOM   2136  CG  LYS A 273      11.016  11.187  17.041  1.00 50.60           C  
ATOM   2137  CD  LYS A 273      10.665  10.567  15.698  1.00 53.46           C  
ATOM   2138  CE  LYS A 273      11.620  11.014  14.596  1.00 56.46           C  
ATOM   2139  NZ  LYS A 273      11.291  10.366  13.288  1.00 58.62           N  
ATOM   2140  N   ARG A 274      10.797  15.883  17.067  1.00 37.82           N  
ATOM   2141  CA  ARG A 274      10.120  17.160  17.284  1.00 34.91           C  
ATOM   2142  C   ARG A 274       9.877  17.843  15.945  1.00 34.05           C  
ATOM   2143  O   ARG A 274      10.754  17.877  15.085  1.00 36.86           O  
ATOM   2144  CB  ARG A 274      10.971  18.047  18.198  1.00 31.65           C  
ATOM   2145  CG  ARG A 274      10.178  19.040  19.035  1.00 29.75           C  
ATOM   2146  CD  ARG A 274      11.076  19.754  20.032  1.00 27.51           C  
ATOM   2147  NE  ARG A 274      11.621  18.837  21.027  1.00 25.65           N  
ATOM   2148  CZ  ARG A 274      12.770  19.016  21.673  1.00 26.63           C  
ATOM   2149  NH1 ARG A 274      13.520  20.084  21.434  1.00 24.11           N  
ATOM   2150  NH2 ARG A 274      13.168  18.121  22.569  1.00 27.27           N  
ATOM   2151  N   ILE A 275       8.676  18.383  15.783  1.00 33.04           N  
ATOM   2152  CA  ILE A 275       8.248  19.060  14.560  1.00 30.28           C  
ATOM   2153  C   ILE A 275       9.112  20.300  14.263  1.00 31.52           C  
ATOM   2154  O   ILE A 275       9.533  21.016  15.178  1.00 29.26           O  
ATOM   2155  CB  ILE A 275       6.723  19.427  14.697  1.00 30.65           C  
ATOM   2156  CG1 ILE A 275       6.032  19.457  13.335  1.00 30.96           C  
ATOM   2157  CG2 ILE A 275       6.556  20.738  15.425  1.00 29.57           C  
ATOM   2158  CD1 ILE A 275       6.363  20.637  12.514  1.00 37.02           C  
ATOM   2159  N   SER A 276       9.390  20.538  12.979  1.00 32.01           N  
ATOM   2160  CA  SER A 276      10.198  21.688  12.558  1.00 32.22           C  
ATOM   2161  C   SER A 276       9.311  22.928  12.327  1.00 33.15           C  
ATOM   2162  O   SER A 276       8.107  22.800  12.090  1.00 34.11           O  
ATOM   2163  CB  SER A 276      10.955  21.346  11.274  1.00 28.78           C  
ATOM   2164  OG  SER A 276      10.059  21.175  10.187  1.00 35.12           O  
ATOM   2165  N   ALA A 277       9.891  24.123  12.390  1.00 32.62           N  
ATOM   2166  CA  ALA A 277       9.091  25.340  12.187  1.00 34.29           C  
ATOM   2167  C   ALA A 277       8.403  25.358  10.830  1.00 34.96           C  
ATOM   2168  O   ALA A 277       7.227  25.724  10.719  1.00 34.13           O  
ATOM   2169  CB  ALA A 277       9.958  26.579  12.324  1.00 32.06           C  
ATOM   2170  N   LYS A 278       9.137  24.964   9.797  1.00 35.23           N  
ATOM   2171  CA  LYS A 278       8.588  24.962   8.453  1.00 38.34           C  
ATOM   2172  C   LYS A 278       7.420  24.003   8.325  1.00 38.57           C  
ATOM   2173  O   LYS A 278       6.415  24.316   7.697  1.00 40.44           O  
ATOM   2174  CB  LYS A 278       9.674  24.600   7.436  1.00 41.95           C  
ATOM   2175  CG  LYS A 278       9.223  24.728   5.999  1.00 47.02           C  
ATOM   2176  CD  LYS A 278       8.626  26.114   5.740  1.00 50.78           C  
ATOM   2177  CE  LYS A 278       8.110  26.249   4.309  1.00 52.52           C  
ATOM   2178  NZ  LYS A 278       7.432  27.556   4.079  1.00 54.64           N  
ATOM   2179  N   ALA A 279       7.550  22.831   8.930  1.00 39.19           N  
ATOM   2180  CA  ALA A 279       6.495  21.833   8.868  1.00 37.47           C  
ATOM   2181  C   ALA A 279       5.295  22.221   9.730  1.00 38.68           C  
ATOM   2182  O   ALA A 279       4.154  21.853   9.424  1.00 38.64           O  
ATOM   2183  CB  ALA A 279       7.039  20.481   9.302  1.00 34.29           C  
ATOM   2184  N   ALA A 280       5.545  22.962  10.806  1.00 38.06           N  
ATOM   2185  CA  ALA A 280       4.462  23.381  11.689  1.00 37.48           C  
ATOM   2186  C   ALA A 280       3.578  24.398  10.972  1.00 37.80           C  
ATOM   2187  O   ALA A 280       2.393  24.549  11.280  1.00 39.22           O  
ATOM   2188  CB  ALA A 280       5.031  23.980  12.971  1.00 36.88           C  
ATOM   2189  N   LEU A 281       4.156  25.096  10.007  1.00 36.66           N  
ATOM   2190  CA  LEU A 281       3.404  26.089   9.263  1.00 36.28           C  
ATOM   2191  C   LEU A 281       2.328  25.440   8.396  1.00 36.40           C  
ATOM   2192  O   LEU A 281       1.352  26.088   8.021  1.00 38.63           O  
ATOM   2193  CB  LEU A 281       4.352  26.923   8.401  1.00 33.49           C  
ATOM   2194  CG  LEU A 281       5.311  27.805   9.205  1.00 31.97           C  
ATOM   2195  CD1 LEU A 281       6.428  28.295   8.328  1.00 32.80           C  
ATOM   2196  CD2 LEU A 281       4.547  28.976   9.789  1.00 32.18           C  
ATOM   2197  N   ALA A 282       2.495  24.156   8.093  1.00 36.01           N  
ATOM   2198  CA  ALA A 282       1.527  23.443   7.254  1.00 35.55           C  
ATOM   2199  C   ALA A 282       0.570  22.573   8.064  1.00 34.54           C  
ATOM   2200  O   ALA A 282      -0.116  21.720   7.514  1.00 34.94           O  
ATOM   2201  CB  ALA A 282       2.265  22.583   6.231  1.00 33.88           C  
ATOM   2202  N   HIS A 283       0.521  22.792   9.370  1.00 34.20           N  
ATOM   2203  CA  HIS A 283      -0.345  21.999  10.221  1.00 34.33           C  
ATOM   2204  C   HIS A 283      -1.792  22.460  10.110  1.00 34.87           C  
ATOM   2205  O   HIS A 283      -2.066  23.654  10.055  1.00 36.33           O  
ATOM   2206  CB  HIS A 283       0.136  22.090  11.675  1.00 31.75           C  
ATOM   2207  CG  HIS A 283      -0.489  21.080  12.588  1.00 29.85           C  
ATOM   2208  ND1 HIS A 283      -1.761  21.220  13.096  1.00 28.79           N  
ATOM   2209  CD2 HIS A 283      -0.016  19.911  13.082  1.00 29.56           C  
ATOM   2210  CE1 HIS A 283      -2.044  20.185  13.865  1.00 26.48           C  
ATOM   2211  NE2 HIS A 283      -1.002  19.376  13.874  1.00 27.59           N  
ATOM   2212  N   PRO A 284      -2.740  21.510  10.069  1.00 36.87           N  
ATOM   2213  CA  PRO A 284      -4.167  21.833   9.965  1.00 37.13           C  
ATOM   2214  C   PRO A 284      -4.619  22.914  10.948  1.00 38.09           C  
ATOM   2215  O   PRO A 284      -5.568  23.646  10.675  1.00 40.32           O  
ATOM   2216  CB  PRO A 284      -4.841  20.494  10.241  1.00 36.51           C  
ATOM   2217  CG  PRO A 284      -3.882  19.526   9.665  1.00 35.22           C  
ATOM   2218  CD  PRO A 284      -2.540  20.051  10.117  1.00 35.59           C  
ATOM   2219  N   PHE A 285      -3.941  23.018  12.087  1.00 37.75           N  
ATOM   2220  CA  PHE A 285      -4.307  24.017  13.091  1.00 36.79           C  
ATOM   2221  C   PHE A 285      -4.338  25.442  12.524  1.00 36.98           C  
ATOM   2222  O   PHE A 285      -5.102  26.290  12.999  1.00 37.27           O  
ATOM   2223  CB  PHE A 285      -3.341  23.960  14.285  1.00 33.06           C  
ATOM   2224  CG  PHE A 285      -3.639  24.978  15.362  1.00 30.42           C  
ATOM   2225  CD1 PHE A 285      -4.818  24.906  16.102  1.00 29.40           C  
ATOM   2226  CD2 PHE A 285      -2.745  26.017  15.625  1.00 26.82           C  
ATOM   2227  CE1 PHE A 285      -5.107  25.849  17.090  1.00 26.47           C  
ATOM   2228  CE2 PHE A 285      -3.021  26.970  16.609  1.00 26.33           C  
ATOM   2229  CZ  PHE A 285      -4.207  26.886  17.345  1.00 28.06           C  
ATOM   2230  N   PHE A 286      -3.511  25.713  11.520  1.00 35.75           N  
ATOM   2231  CA  PHE A 286      -3.475  27.051  10.933  1.00 37.85           C  
ATOM   2232  C   PHE A 286      -4.307  27.106   9.671  1.00 40.26           C  
ATOM   2233  O   PHE A 286      -4.220  28.059   8.906  1.00 41.28           O  
ATOM   2234  CB  PHE A 286      -2.037  27.462  10.594  1.00 34.98           C  
ATOM   2235  CG  PHE A 286      -1.131  27.512  11.781  1.00 34.65           C  
ATOM   2236  CD1 PHE A 286      -1.385  28.395  12.825  1.00 30.35           C  
ATOM   2237  CD2 PHE A 286      -0.037  26.646  11.876  1.00 33.61           C  
ATOM   2238  CE1 PHE A 286      -0.568  28.415  13.946  1.00 31.63           C  
ATOM   2239  CE2 PHE A 286       0.785  26.660  12.998  1.00 33.64           C  
ATOM   2240  CZ  PHE A 286       0.520  27.545  14.036  1.00 31.36           C  
ATOM   2241  N   GLN A 287      -5.115  26.078   9.449  1.00 43.75           N  
ATOM   2242  CA  GLN A 287      -5.931  26.046   8.257  1.00 45.59           C  
ATOM   2243  C   GLN A 287      -6.815  27.277   8.163  1.00 44.65           C  
ATOM   2244  O   GLN A 287      -7.009  27.814   7.077  1.00 45.52           O  
ATOM   2245  CB  GLN A 287      -6.785  24.786   8.219  1.00 48.63           C  
ATOM   2246  CG  GLN A 287      -7.459  24.591   6.878  1.00 53.10           C  
ATOM   2247  CD  GLN A 287      -8.241  23.309   6.813  1.00 56.42           C  
ATOM   2248  OE1 GLN A 287      -7.679  22.218   6.943  1.00 60.20           O  
ATOM   2249  NE2 GLN A 287      -9.549  23.426   6.613  1.00 57.46           N  
ATOM   2250  N   ASP A 288      -7.343  27.736   9.290  1.00 42.87           N  
ATOM   2251  CA  ASP A 288      -8.191  28.925   9.264  1.00 44.45           C  
ATOM   2252  C   ASP A 288      -7.493  30.106   9.941  1.00 43.49           C  
ATOM   2253  O   ASP A 288      -8.117  30.880  10.669  1.00 44.64           O  
ATOM   2254  CB  ASP A 288      -9.535  28.649   9.954  1.00 44.97           C  
ATOM   2255  CG  ASP A 288      -9.385  28.356  11.438  1.00 47.96           C  
ATOM   2256  OD1 ASP A 288     -10.419  28.249  12.139  1.00 48.70           O  
ATOM   2257  OD2 ASP A 288      -8.234  28.226  11.904  1.00 49.98           O  
ATOM   2258  N   VAL A 289      -6.198  30.247   9.692  1.00 40.90           N  
ATOM   2259  CA  VAL A 289      -5.436  31.325  10.304  1.00 40.20           C  
ATOM   2260  C   VAL A 289      -5.703  32.714   9.721  1.00 40.38           C  
ATOM   2261  O   VAL A 289      -5.810  32.892   8.505  1.00 40.06           O  
ATOM   2262  CB  VAL A 289      -3.920  31.062  10.216  1.00 36.36           C  
ATOM   2263  CG1 VAL A 289      -3.483  31.023   8.771  1.00 34.66           C  
ATOM   2264  CG2 VAL A 289      -3.171  32.142  10.968  1.00 33.00           C  
ATOM   2265  N   THR A 290      -5.781  33.699  10.609  1.00 40.31           N  
ATOM   2266  CA  THR A 290      -6.025  35.073  10.204  1.00 42.23           C  
ATOM   2267  C   THR A 290      -5.084  35.993  10.963  1.00 42.39           C  
ATOM   2268  O   THR A 290      -4.219  35.531  11.706  1.00 45.49           O  
ATOM   2269  CB  THR A 290      -7.472  35.479  10.505  1.00 41.69           C  
ATOM   2270  OG1 THR A 290      -7.662  35.546  11.925  1.00 42.54           O  
ATOM   2271  CG2 THR A 290      -8.439  34.447   9.918  1.00 39.37           C  
ATOM   2272  N   LYS A 291      -5.253  37.295  10.778  1.00 42.14           N  
ATOM   2273  CA  LYS A 291      -4.409  38.267  11.458  1.00 40.46           C  
ATOM   2274  C   LYS A 291      -5.236  39.363  12.135  1.00 39.13           C  
ATOM   2275  O   LYS A 291      -5.438  40.441  11.579  1.00 40.31           O  
ATOM   2276  CB  LYS A 291      -3.427  38.893  10.465  1.00 40.62           C  
ATOM   2277  CG  LYS A 291      -2.375  39.772  11.107  1.00 42.64           C  
ATOM   2278  CD  LYS A 291      -1.293  40.144  10.104  1.00 45.87           C  
ATOM   2279  CE  LYS A 291      -0.088  40.769  10.799  1.00 46.50           C  
ATOM   2280  NZ  LYS A 291       1.039  41.020   9.856  1.00 48.82           N  
ATOM   2281  N   PRO A 292      -5.749  39.086  13.338  1.00 38.04           N  
ATOM   2282  CA  PRO A 292      -6.546  40.075  14.069  1.00 38.83           C  
ATOM   2283  C   PRO A 292      -5.643  41.113  14.736  1.00 40.76           C  
ATOM   2284  O   PRO A 292      -4.431  40.919  14.820  1.00 41.88           O  
ATOM   2285  CB  PRO A 292      -7.309  39.217  15.081  1.00 36.96           C  
ATOM   2286  CG  PRO A 292      -6.382  38.085  15.336  1.00 33.30           C  
ATOM   2287  CD  PRO A 292      -5.872  37.755  13.958  1.00 36.59           C  
ATOM   2288  N   VAL A 293      -6.222  42.218  15.194  1.00 43.77           N  
ATOM   2289  CA  VAL A 293      -5.436  43.257  15.853  1.00 47.56           C  
ATOM   2290  C   VAL A 293      -5.648  43.183  17.357  1.00 49.99           C  
ATOM   2291  O   VAL A 293      -6.771  42.997  17.825  1.00 51.94           O  
ATOM   2292  CB  VAL A 293      -5.833  44.662  15.369  1.00 49.06           C  
ATOM   2293  CG1 VAL A 293      -5.759  44.715  13.854  1.00 49.12           C  
ATOM   2294  CG2 VAL A 293      -7.229  45.020  15.864  1.00 46.68           C  
ATOM   2295  N   PRO A 294      -4.573  43.320  18.142  1.00 50.38           N  
ATOM   2296  CA  PRO A 294      -4.785  43.246  19.584  1.00 51.41           C  
ATOM   2297  C   PRO A 294      -5.275  44.588  20.096  1.00 53.53           C  
ATOM   2298  O   PRO A 294      -5.329  45.567  19.355  1.00 51.38           O  
ATOM   2299  CB  PRO A 294      -3.396  42.925  20.101  1.00 49.58           C  
ATOM   2300  CG  PRO A 294      -2.542  43.791  19.209  1.00 48.46           C  
ATOM   2301  CD  PRO A 294      -3.152  43.565  17.831  1.00 48.94           C  
ATOM   2302  N   HIS A 295      -5.643  44.622  21.368  1.00 57.28           N  
ATOM   2303  CA  HIS A 295      -6.061  45.865  21.983  1.00 59.99           C  
ATOM   2304  C   HIS A 295      -5.009  46.147  23.044  1.00 60.22           C  
ATOM   2305  O   HIS A 295      -5.061  45.600  24.145  1.00 59.24           O  
ATOM   2306  CB  HIS A 295      -7.433  45.736  22.633  1.00 62.48           C  
ATOM   2307  CG  HIS A 295      -7.924  47.016  23.226  1.00 66.70           C  
ATOM   2308  ND1 HIS A 295      -7.238  47.682  24.219  1.00 68.00           N  
ATOM   2309  CD2 HIS A 295      -9.007  47.775  22.941  1.00 67.24           C  
ATOM   2310  CE1 HIS A 295      -7.878  48.797  24.520  1.00 69.07           C  
ATOM   2311  NE2 HIS A 295      -8.955  48.877  23.760  1.00 70.32           N  
ATOM   2312  N   LEU A 296      -4.040  46.987  22.697  1.00 61.96           N  
ATOM   2313  CA  LEU A 296      -2.964  47.320  23.615  1.00 63.66           C  
ATOM   2314  C   LEU A 296      -3.192  48.635  24.325  1.00 64.92           C  
ATOM   2315  O   LEU A 296      -3.832  49.538  23.793  1.00 64.83           O  
ATOM   2316  CB  LEU A 296      -1.634  47.415  22.871  1.00 62.53           C  
ATOM   2317  CG  LEU A 296      -1.274  46.330  21.861  1.00 62.99           C  
ATOM   2318  CD1 LEU A 296       0.139  46.584  21.370  1.00 62.14           C  
ATOM   2319  CD2 LEU A 296      -1.385  44.950  22.491  1.00 63.83           C  
ATOM   2320  N   ARG A 297      -2.655  48.724  25.536  1.00 67.40           N  
ATOM   2321  CA  ARG A 297      -2.726  49.934  26.339  1.00 69.28           C  
ATOM   2322  C   ARG A 297      -1.276  50.386  26.447  1.00 69.82           C  
ATOM   2323  O   ARG A 297      -0.473  49.749  27.129  1.00 70.32           O  
ATOM   2324  CB  ARG A 297      -3.269  49.646  27.739  1.00 71.57           C  
ATOM   2325  CG  ARG A 297      -3.131  50.835  28.689  1.00 75.67           C  
ATOM   2326  CD  ARG A 297      -3.225  50.443  30.167  1.00 78.81           C  
ATOM   2327  NE  ARG A 297      -4.558  49.989  30.559  1.00 83.08           N  
ATOM   2328  CZ  ARG A 297      -4.914  49.705  31.810  1.00 85.31           C  
ATOM   2329  NH1 ARG A 297      -4.036  49.829  32.799  1.00 85.57           N  
ATOM   2330  NH2 ARG A 297      -6.150  49.296  32.075  1.00 85.86           N  
ATOM   2331  N   LEU A 298      -0.936  51.471  25.761  1.00 69.75           N  
ATOM   2332  CA  LEU A 298       0.427  51.982  25.786  1.00 68.37           C  
ATOM   2333  C   LEU A 298       0.525  53.272  26.594  1.00 68.66           C  
ATOM   2334  O   LEU A 298       1.403  53.415  27.448  1.00 69.82           O  
ATOM   2335  CB  LEU A 298       0.911  52.220  24.355  1.00 66.45           C  
ATOM   2336  CG  LEU A 298       0.801  51.004  23.437  1.00 64.38           C  
ATOM   2337  CD1 LEU A 298       1.262  51.388  22.052  1.00 64.03           C  
ATOM   2338  CD2 LEU A 298       1.637  49.853  23.980  1.00 63.46           C  
TER    2339      LEU A 298                                                      
HETATM 2340  F8BACK4 A 500       8.586  45.870  30.482  0.59 58.86           F  
HETATM 2341  C7BACK4 A 500       7.492  45.938  29.594  0.59 58.11           C  
HETATM 2342  F1BACK4 A 500       6.652  47.009  29.980  0.59 58.12           F  
HETATM 2343  F9BACK4 A 500       6.778  44.736  29.622  0.59 58.63           F  
HETATM 2344  C4BACK4 A 500       8.071  46.183  28.118  0.59 56.08           C  
HETATM 2345  C5BACK4 A 500       7.415  47.113  27.214  0.59 55.60           C  
HETATM 2346  C6BACK4 A 500       7.963  47.344  25.904  0.59 54.41           C  
HETATM 2347  C3BACK4 A 500       9.276  45.486  27.678  0.59 55.91           C  
HETATM 2348  C2BACK4 A 500       9.819  45.711  26.393  0.59 54.85           C  
HETATM 2349  C1BACK4 A 500       9.210  46.629  25.476  0.59 54.50           C  
HETATM 2350  N7 ACK4 A 500       9.805  46.881  24.140  0.59 55.20           N  
HETATM 2351  C2 ACK4 A 500      10.918  46.520  23.280  0.59 56.10           C  
HETATM 2352  N1 ACK4 A 500      10.968  47.099  22.093  0.59 55.70           N  
HETATM 2353  C6 ACK4 A 500      12.009  46.793  21.242  0.59 56.32           C  
HETATM 2354  C5 ACK4 A 500      13.055  45.881  21.546  0.59 57.28           C  
HETATM 2355  N3 ACK4 A 500      11.862  45.644  23.660  0.59 57.76           N  
HETATM 2356  C4 ACK4 A 500      12.953  45.271  22.857  0.59 58.34           C  
HETATM 2357  C5AACK4 A 500      13.862  44.309  23.428  0.59 59.50           C  
HETATM 2358  S4AACK4 A 500      13.440  43.741  25.086  0.59 59.56           S  
HETATM 2359  C1AACK4 A 500      15.056  43.645  23.036  0.59 60.03           C  
HETATM 2360  C6AACK4 A 500      15.807  43.799  21.686  0.59 59.42           C  
HETATM 2361  N2AACK4 A 500      15.595  42.759  23.994  0.59 60.30           N  
HETATM 2362  C3AACK4 A 500      14.803  42.754  25.098  0.59 60.18           C  
HETATM 2363  C7AACK4 A 500      14.989  41.964  26.362  0.59 60.57           C  
HETATM 2364  O  BHOH A 501      12.936  46.419  20.805  0.41 18.88           O  
HETATM 2365  O  BHOH A 502      11.538  47.726  22.484  0.41 27.42           O  
HETATM 2366  O  BHOH A 503      14.705  44.479  21.589  0.41 29.66           O  
HETATM 2367  O  BHOH A 504      16.225  42.604  20.392  0.41 10.98           O  
HETATM 2368  O  BHOH A 505       8.965  48.466  25.072  0.41109.41           O  
HETATM 2369  O  BHOH A 506      13.363  43.643  23.879  0.41 61.24           O  
HETATM 2370  O  BHOH A 507      11.926  45.557  25.138  0.41 75.71           O  
HETATM 2371  O  BHOH A 508      14.779  42.388  27.383  0.41 44.59           O  
HETATM 2372  O  BHOH A 509      12.928  41.711  25.411  0.41 31.11           O  
HETATM 2373  O   HOH A 510       4.831  28.072  29.529  1.00 24.22           O  
HETATM 2374  O   HOH A 511      11.558  54.969  15.098  1.00 33.73           O  
HETATM 2375  O   HOH A 512      15.122  25.401  24.657  1.00 23.60           O  
HETATM 2376  O   HOH A 513      12.494  24.631  12.808  1.00 28.15           O  
HETATM 2377  O   HOH A 514      10.875  23.618  29.519  1.00 20.22           O  
HETATM 2378  O   HOH A 515      18.029  20.164  19.915  1.00 31.64           O  
HETATM 2379  O   HOH A 516      -6.295  33.485  13.278  1.00 37.50           O  
HETATM 2380  O   HOH A 517      14.674  28.665  22.690  1.00 28.09           O  
HETATM 2381  O   HOH A 518      -2.290  39.398  14.558  1.00 33.80           O  
HETATM 2382  O   HOH A 519       2.225  31.528  35.587  1.00 36.23           O  
HETATM 2383  O   HOH A 520      -1.492  24.267  35.549  1.00 33.82           O  
HETATM 2384  O   HOH A 521      13.652  18.437  14.820  1.00 38.02           O  
HETATM 2385  O   HOH A 522      13.813  29.320  29.720  1.00 28.29           O  
HETATM 2386  O   HOH A 523       4.325  19.356  35.428  1.00 32.59           O  
HETATM 2387  O   HOH A 524      -8.443  24.125  14.417  1.00 30.73           O  
HETATM 2388  O   HOH A 525      22.914  30.454  16.850  1.00 40.79           O  
HETATM 2389  O   HOH A 526      12.358  21.055  15.352  1.00 39.26           O  
HETATM 2390  O   HOH A 527      11.770  24.798   9.832  1.00 45.65           O  
HETATM 2391  O   HOH A 528      12.423  51.576  15.863  1.00 43.68           O  
HETATM 2392  O   HOH A 529      15.567  27.684  25.882  1.00 41.54           O  
HETATM 2393  O   HOH A 530      14.259  29.859  26.958  1.00 29.63           O  
HETATM 2394  O   HOH A 531       7.148  53.375  26.146  1.00 37.98           O  
HETATM 2395  O   HOH A 532       3.542  48.422  27.066  1.00 43.26           O  
HETATM 2396  O   HOH A 533       4.784  21.612  36.675  1.00 42.62           O  
HETATM 2397  O   HOH A 534       7.080   9.963  27.675  1.00 42.57           O  
HETATM 2398  O   HOH A 535      11.207  18.389  42.099  1.00 43.17           O  
CONECT 2340 2341                                                                
CONECT 2341 2340 2342 2343 2344                                                 
CONECT 2342 2341                                                                
CONECT 2343 2341                                                                
CONECT 2344 2341 2345 2347                                                      
CONECT 2345 2344 2346                                                           
CONECT 2346 2345 2349                                                           
CONECT 2347 2344 2348                                                           
CONECT 2348 2347 2349                                                           
CONECT 2349 2346 2348 2350                                                      
CONECT 2350 2349 2351                                                           
CONECT 2351 2350 2352 2355                                                      
CONECT 2352 2351 2353                                                           
CONECT 2353 2352 2354                                                           
CONECT 2354 2353 2356                                                           
CONECT 2355 2351 2356                                                           
CONECT 2356 2354 2355 2357                                                      
CONECT 2357 2356 2358 2359                                                      
CONECT 2358 2357 2362                                                           
CONECT 2359 2357 2360 2361                                                      
CONECT 2360 2359                                                                
CONECT 2361 2359 2362                                                           
CONECT 2362 2358 2361 2363                                                      
CONECT 2363 2362                                                                
MASTER      346    0    1   13    8    0    6    6 2397    1   24   23          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.