CNRS Nantes University UFIP UFIP
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***  1yci  ***

elNémo ID: 21051400304796140

Job options:

ID        	=	 21051400304796140
JOBID     	=	 1yci
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1yci

HEADER    TRANSCRIPTION REGULATOR, OXIDOREDUCTASE 22-DEC-04   1YCI              
TITLE     FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH N-(CARBOXYCARBONYL)-D-  
TITLE    2 PHENYLALANINE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA INHIBITOR;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HYPOXIA- INDUCIBLE FACTOR ASPARAGINE HYDROXYLASE, FACTOR    
COMPND   5 INHIBITING HIF-1, FIH-1;                                             
COMPND   6 EC: 1.14.11.16;                                                      
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: HIF1AN;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    FIH, HIF, DSBH, OXYGENASE, TRANSCRIPTION, HYPOXIA, INHIBITOR 2-       
KEYWDS   2 OXOGLUTARATE, ASPARAGINYL HYDROXYLASE, HYDROXYLASE N-                
KEYWDS   3 (CARBOXYCARBONYL)-D-PHENYLALANINE, NOFD, NDF, TRANSCRIPTION          
KEYWDS   4 REGULATOR, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.MCDONOUGH,C.J.SCHOFIELD                                           
REVDAT   3   13-JUL-11 1YCI    1       VERSN                                    
REVDAT   2   24-FEB-09 1YCI    1       VERSN                                    
REVDAT   1   31-MAY-05 1YCI    0                                                
JRNL        AUTH   M.A.MCDONOUGH,L.A.MCNEILL,M.TILLIET,C.A.PAPAMICAEL,Q.Y.CHEN, 
JRNL        AUTH 2 B.BANERJI,K.S.HEWITSON,C.J.SCHOFIELD                         
JRNL        TITL   SELECTIVE INHIBITION OF FACTOR INHIBITING HYPOXIA-INDUCIBLE  
JRNL        TITL 2 FACTOR                                                       
JRNL        REF    J.AM.CHEM.SOC.                V. 127  7680 2005              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   15913349                                                     
JRNL        DOI    10.1021/JA050841B                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,              
REMARK   1  AUTH 2 I.SCHLEMMINGER,C.W.PUGH,P.J.RATCLIFFE,C.J.SCHOFIELD          
REMARK   1  TITL   STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR      
REMARK   1  TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF HIF-1   
REMARK   1  TITL 3 ALPHA                                                        
REMARK   1  REF    J.BIOL.CHEM.                  V. 278  1802 2003              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   12446723                                                     
REMARK   1  DOI    10.1074/JBC.C200644200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15709                          
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) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1589                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.80                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1263                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 137                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2715                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 90                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.89000                                             
REMARK   3    B22 (A**2) : -6.89000                                             
REMARK   3    B33 (A**2) : 13.79000                                             
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
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) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.880 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.070 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 58.91                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DOP.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : DOP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1YCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB031376.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(III)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16510                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS WITH 1H2N        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1H2N                                                 
REMARK 200                                                                      
REMARK 200 REMARK: REJECTION CRITERIA AS REJECTION PROBABILITY, REJECTION       
REMARK 200  CRITERIA (PROBABILITY)) : 0.0001                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE, 4% PEG400,       
REMARK 280  0.1M HEPES PH7.5 ARGON ATMOSPHERE, 28MG/ML PROTEIN WITH 1MM         
REMARK 280  FE(II), 10MM N-(CARBOXYCARBONYL)-D-PHENYLALANINE, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.25950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.42650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.62975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.42650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.88925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.42650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.62975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.42650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      112.88925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.25950            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
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 350   BIOMT1   2  0.000000 -1.000000  0.000000       86.85300            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       86.85300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       75.25950            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 119    CG   OD1                                            
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 304    CB   CG   CD   CE   NZ                              
REMARK 470     ARG A 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 306    CG1  CG2  CD1                                       
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
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    SER A  30       -8.88    -56.61                                   
REMARK 500    ASP A  66       43.41   -140.18                                   
REMARK 500    ILE A  85        6.03    -61.20                                   
REMARK 500    TYR A 145      119.21   -163.83                                   
REMARK 500    ASN A 151     -144.72    -85.94                                   
REMARK 500    THR A 153       17.16    -68.79                                   
REMARK 500    PRO A 197      152.77    -44.96                                   
REMARK 500    TYR A 228       70.49     33.21                                   
REMARK 500    ARG A 238        0.42     82.14                                   
REMARK 500    PHE A 252       65.11   -113.33                                   
REMARK 500    LEU A 284      138.83    -38.26                                   
REMARK 500    PRO A 303      -18.05    -43.87                                   
REMARK 500    ILE A 306      116.04    -33.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A1350  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 101.0                                              
REMARK 620 3 HIS A 279   NE2  85.1  83.5                                        
REMARK 620 4 NDF A 400   O2'  95.2 162.3 105.1                                  
REMARK 620 5 NDF A 400   O2  170.0  88.7  98.5  74.9                            
REMARK 620 6 HOH A1045   O    75.2  77.4 149.2 100.2 104.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDF A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDF A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H2K   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
REMARK 900 RELATED ID: 1H2L   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
REMARK 900 RELATED ID: 1H2N   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH AKG                    
REMARK 900 RELATED ID: 1H2M   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
DBREF  1YCI A    1   349  UNP    Q9NWT6   HIF1N_HUMAN      1    349             
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG          
SEQRES  13 A  349  LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN                  
HET    FE2  A1350       1                                                       
HET    SO4  A1352       5                                                       
HET    SO4  A1353       5                                                       
HET    SO4  A1354       5                                                       
HET    NDF  A 400      17                                                       
HET    NDF  A 401      17                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NDF N-(CARBOXYCARBONYL)-D-PHENYLALANINE                              
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  NDF    2(C11 H11 N O5)                                              
FORMUL   7  HOH   *90(H2 O)                                                     
HELIX    1   1 GLU A   19  LEU A   23  5                                   5    
HELIX    2   2 ASP A   28  LEU A   32  5                                   5    
HELIX    3   3 ASP A   49  ASN A   58  1                                  10    
HELIX    4   4 VAL A   70  TRP A   76  5                                   7    
HELIX    5   5 ASP A   77  ILE A   85  1                                   9    
HELIX    6   6 ASP A  104  MET A  108  5                                   5    
HELIX    7   7 LYS A  124  GLN A  137  1                                  14    
HELIX    8   8 GLY A  155  PHE A  165  1                                  11    
HELIX    9   9 ASN A  166  ARG A  177  1                                  12    
HELIX   10  10 PRO A  220  ASP A  222  5                                   3    
HELIX   11  11 GLN A  223  TYR A  228  1                                   6    
HELIX   12  12 PHE A  252  ASN A  257  5                                   6    
HELIX   13  13 LYS A  311  LEU A  330  1                                  20    
HELIX   14  14 ASN A  332  GLN A  334  5                                   3    
HELIX   15  15 GLU A  335  LYS A  345  1                                  11    
SHEET    1   A 5 THR A  39  PRO A  41  0                                        
SHEET    2   A 5 GLY A 260  VAL A 265  1  O  GLY A 260   N  ARG A  40           
SHEET    3   A 5 LYS A 214  PHE A 219 -1  N  LEU A 218   O  TYR A 261           
SHEET    4   A 5 TRP A 278  SER A 283 -1  O  GLU A 282   N  ARG A 215           
SHEET    5   A 5 VAL A 195  HIS A 199 -1  N  THR A 196   O  ILE A 281           
SHEET    1   B 9 ARG A  44  LEU A  45  0                                        
SHEET    2   B 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3   B 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4   B 9 GLN A 203  LYS A 211 -1  N  PHE A 207   O  LEU A 271           
SHEET    5   B 9 THR A 290  LYS A 298 -1  O  ILE A 291   N  LYS A 211           
SHEET    6   B 9 LEU A 182  GLY A 190 -1  N  LEU A 188   O  THR A 292           
SHEET    7   B 9 ARG A 143  THR A 149 -1  N  LEU A 146   O  ILE A 189           
SHEET    8   B 9 PHE A  90  ALA A  95 -1  N  TYR A  93   O  TYR A 145           
SHEET    9   B 9 GLU A 122  MET A 123 -1  O  MET A 123   N  PHE A  90           
LINK        FE   FE2 A1350                 NE2 HIS A 199     1555   1555  2.32  
LINK        FE   FE2 A1350                 OD2 ASP A 201     1555   1555  2.22  
LINK        FE   FE2 A1350                 NE2 HIS A 279     1555   1555  2.36  
LINK        FE   FE2 A1350                 O2' NDF A 400     1555   1555  2.25  
LINK        FE   FE2 A1350                 O2  NDF A 400     1555   1555  2.24  
LINK        FE   FE2 A1350                 O   HOH A1045     1555   1555  2.01  
CISPEP   1 TYR A  308    PRO A  309          0         0.01                     
SITE     1 AC1  5 HIS A 199  ASP A 201  HIS A 279  NDF A 400                    
SITE     2 AC1  5 HOH A1045                                                     
SITE     1 AC2  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC3  5 ARG A 143  GLU A 192  GLY A 193  LEU A 285                    
SITE     2 AC3  5 ASN A 286                                                     
SITE     1 AC4  4 LYS A 107  ARG A 320  LYS A 324  HOH A1006                    
SITE     1 AC5 13 TYR A 145  LEU A 188  THR A 196  HIS A 199                    
SITE     2 AC5 13 ASP A 201  ASN A 205  PHE A 207  LYS A 214                    
SITE     3 AC5 13 HIS A 279  ILE A 281  ASN A 294  TRP A 296                    
SITE     4 AC5 13 FE2 A1350                                                     
SITE     1 AC6  6 PRO A 221  ASP A 222  PHE A 224  GLU A 225                    
SITE     2 AC6  6 LYS A 315  HOH A1085                                          
CRYST1   86.853   86.853  150.519  90.00  90.00  90.00 P 41 21 2     8          
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      0.011514  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006644        0.00000                         
ATOM      1  N   GLY A  14      11.516  34.414  12.463  1.00 98.47           N  
ATOM      2  CA  GLY A  14      10.786  34.075  11.200  1.00 98.16           C  
ATOM      3  C   GLY A  14       9.368  33.579  11.435  1.00 97.95           C  
ATOM      4  O   GLY A  14       8.896  33.568  12.574  1.00 98.33           O  
ATOM      5  N   GLU A  15       8.687  33.169  10.365  1.00 96.67           N  
ATOM      6  CA  GLU A  15       7.315  32.667  10.458  1.00 95.28           C  
ATOM      7  C   GLU A  15       7.276  31.178  10.838  1.00 94.06           C  
ATOM      8  O   GLU A  15       8.160  30.405  10.463  1.00 93.74           O  
ATOM      9  CB  GLU A  15       6.592  32.896   9.130  1.00 94.77           C  
ATOM     10  N   PRO A  16       6.244  30.759  11.594  1.00 92.65           N  
ATOM     11  CA  PRO A  16       6.098  29.363  12.026  1.00 91.64           C  
ATOM     12  C   PRO A  16       6.266  28.375  10.885  1.00 90.97           C  
ATOM     13  O   PRO A  16       5.539  28.429   9.890  1.00 91.31           O  
ATOM     14  CB  PRO A  16       4.692  29.327  12.608  1.00 91.51           C  
ATOM     15  CG  PRO A  16       4.536  30.694  13.170  1.00 90.98           C  
ATOM     16  CD  PRO A  16       5.129  31.579  12.097  1.00 91.69           C  
ATOM     17  N   ARG A  17       7.225  27.468  11.024  1.00 89.80           N  
ATOM     18  CA  ARG A  17       7.462  26.475   9.987  1.00 88.38           C  
ATOM     19  C   ARG A  17       6.283  25.510   9.896  1.00 87.28           C  
ATOM     20  O   ARG A  17       5.530  25.325  10.860  1.00 86.32           O  
ATOM     21  CB  ARG A  17       8.737  25.682  10.278  1.00 88.90           C  
ATOM     22  CG  ARG A  17      10.006  26.517  10.350  1.00 90.29           C  
ATOM     23  CD  ARG A  17      11.232  25.636  10.574  1.00 90.93           C  
ATOM     24  NE  ARG A  17      11.229  24.928  11.859  1.00 91.39           N  
ATOM     25  CZ  ARG A  17      11.363  25.504  13.056  1.00 91.65           C  
ATOM     26  NH1 ARG A  17      11.516  26.822  13.175  1.00 91.19           N  
ATOM     27  NH2 ARG A  17      11.354  24.749  14.147  1.00 90.73           N  
ATOM     28  N   GLU A  18       6.135  24.896   8.726  1.00 86.53           N  
ATOM     29  CA  GLU A  18       5.065  23.937   8.468  1.00 85.64           C  
ATOM     30  C   GLU A  18       5.527  22.498   8.629  1.00 83.89           C  
ATOM     31  O   GLU A  18       6.586  22.123   8.123  1.00 83.50           O  
ATOM     32  CB  GLU A  18       4.528  24.121   7.051  1.00 87.39           C  
ATOM     33  CG  GLU A  18       3.733  25.392   6.864  1.00 90.04           C  
ATOM     34  CD  GLU A  18       2.467  25.408   7.702  1.00 91.69           C  
ATOM     35  OE1 GLU A  18       1.865  26.495   7.836  1.00 92.04           O  
ATOM     36  OE2 GLU A  18       2.063  24.338   8.215  1.00 93.28           O  
ATOM     37  N   GLU A  19       4.730  21.692   9.324  1.00 81.94           N  
ATOM     38  CA  GLU A  19       5.066  20.288   9.523  1.00 80.36           C  
ATOM     39  C   GLU A  19       4.662  19.433   8.325  1.00 78.24           C  
ATOM     40  O   GLU A  19       3.625  19.678   7.694  1.00 77.73           O  
ATOM     41  CB  GLU A  19       4.392  19.747  10.775  1.00 81.90           C  
ATOM     42  CG  GLU A  19       5.089  20.107  12.056  1.00 84.95           C  
ATOM     43  CD  GLU A  19       4.558  19.292  13.194  1.00 88.17           C  
ATOM     44  OE1 GLU A  19       4.660  18.046  13.120  1.00 89.39           O  
ATOM     45  OE2 GLU A  19       4.027  19.889  14.155  1.00 89.70           O  
ATOM     46  N   ALA A  20       5.490  18.431   8.022  1.00 75.91           N  
ATOM     47  CA  ALA A  20       5.259  17.532   6.899  1.00 73.38           C  
ATOM     48  C   ALA A  20       3.925  16.851   7.084  1.00 72.56           C  
ATOM     49  O   ALA A  20       3.376  16.840   8.190  1.00 72.71           O  
ATOM     50  CB  ALA A  20       6.374  16.485   6.803  1.00 71.69           C  
ATOM     51  N   GLY A  21       3.407  16.286   5.996  1.00 71.14           N  
ATOM     52  CA  GLY A  21       2.129  15.609   6.055  1.00 69.26           C  
ATOM     53  C   GLY A  21       1.004  16.571   6.368  1.00 68.81           C  
ATOM     54  O   GLY A  21      -0.072  16.150   6.782  1.00 67.92           O  
ATOM     55  N   ALA A  22       1.264  17.865   6.176  1.00 69.19           N  
ATOM     56  CA  ALA A  22       0.288  18.925   6.421  1.00 69.04           C  
ATOM     57  C   ALA A  22      -0.370  18.828   7.800  1.00 69.25           C  
ATOM     58  O   ALA A  22      -1.594  18.900   7.922  1.00 69.72           O  
ATOM     59  CB  ALA A  22      -0.778  18.899   5.335  1.00 68.40           C  
ATOM     60  N   LEU A  23       0.442  18.677   8.841  1.00 69.21           N  
ATOM     61  CA  LEU A  23      -0.092  18.567  10.194  1.00 69.13           C  
ATOM     62  C   LEU A  23      -0.284  19.953  10.814  1.00 69.42           C  
ATOM     63  O   LEU A  23      -0.577  20.089  12.005  1.00 68.95           O  
ATOM     64  CB  LEU A  23       0.837  17.703  11.056  1.00 68.49           C  
ATOM     65  CG  LEU A  23       0.949  16.202  10.736  1.00 67.23           C  
ATOM     66  CD1 LEU A  23       2.105  15.602  11.548  1.00 66.85           C  
ATOM     67  CD2 LEU A  23      -0.377  15.490  11.041  1.00 63.10           C  
ATOM     68  N   GLY A  24      -0.131  20.977   9.982  1.00 70.34           N  
ATOM     69  CA  GLY A  24      -0.305  22.336  10.446  1.00 71.95           C  
ATOM     70  C   GLY A  24       0.979  22.947  10.965  1.00 73.02           C  
ATOM     71  O   GLY A  24       2.024  22.296  10.970  1.00 73.85           O  
ATOM     72  N   PRO A  25       0.927  24.214  11.409  1.00 73.44           N  
ATOM     73  CA  PRO A  25       2.110  24.899  11.931  1.00 72.76           C  
ATOM     74  C   PRO A  25       2.601  24.294  13.232  1.00 71.74           C  
ATOM     75  O   PRO A  25       1.808  23.910  14.096  1.00 70.30           O  
ATOM     76  CB  PRO A  25       1.623  26.334  12.111  1.00 73.32           C  
ATOM     77  CG  PRO A  25       0.179  26.140  12.475  1.00 73.04           C  
ATOM     78  CD  PRO A  25      -0.253  25.096  11.468  1.00 73.49           C  
ATOM     79  N   ALA A  26       3.917  24.216  13.367  1.00 70.76           N  
ATOM     80  CA  ALA A  26       4.515  23.667  14.559  1.00 71.02           C  
ATOM     81  C   ALA A  26       4.124  24.467  15.821  1.00 71.42           C  
ATOM     82  O   ALA A  26       3.936  23.894  16.901  1.00 72.10           O  
ATOM     83  CB  ALA A  26       6.021  23.632  14.382  1.00 70.00           C  
ATOM     84  N   TRP A  27       3.985  25.783  15.674  1.00 71.02           N  
ATOM     85  CA  TRP A  27       3.631  26.680  16.775  1.00 68.57           C  
ATOM     86  C   TRP A  27       3.094  27.978  16.184  1.00 68.60           C  
ATOM     87  O   TRP A  27       3.094  28.154  14.959  1.00 69.08           O  
ATOM     88  CB  TRP A  27       4.872  26.998  17.610  1.00 66.99           C  
ATOM     89  CG  TRP A  27       6.077  27.281  16.763  1.00 67.00           C  
ATOM     90  CD1 TRP A  27       6.873  26.361  16.132  1.00 67.98           C  
ATOM     91  CD2 TRP A  27       6.571  28.561  16.376  1.00 66.35           C  
ATOM     92  NE1 TRP A  27       7.836  26.997  15.367  1.00 67.58           N  
ATOM     93  CE2 TRP A  27       7.669  28.349  15.503  1.00 66.96           C  
ATOM     94  CE3 TRP A  27       6.192  29.873  16.679  1.00 65.38           C  
ATOM     95  CZ2 TRP A  27       8.385  29.400  14.938  1.00 67.08           C  
ATOM     96  CZ3 TRP A  27       6.905  30.914  16.115  1.00 65.86           C  
ATOM     97  CH2 TRP A  27       7.987  30.674  15.256  1.00 67.84           C  
ATOM     98  N   ASP A  28       2.638  28.886  17.041  1.00 68.37           N  
ATOM     99  CA  ASP A  28       2.129  30.166  16.564  1.00 67.81           C  
ATOM    100  C   ASP A  28       2.571  31.264  17.516  1.00 65.36           C  
ATOM    101  O   ASP A  28       2.750  31.029  18.709  1.00 64.17           O  
ATOM    102  CB  ASP A  28       0.601  30.130  16.453  1.00 71.12           C  
ATOM    103  CG  ASP A  28      -0.088  30.276  17.791  1.00 74.24           C  
ATOM    104  OD1 ASP A  28      -0.334  31.430  18.206  1.00 77.36           O  
ATOM    105  OD2 ASP A  28      -0.389  29.244  18.434  1.00 75.67           O  
ATOM    106  N   GLU A  29       2.747  32.461  16.977  1.00 63.25           N  
ATOM    107  CA  GLU A  29       3.203  33.595  17.764  1.00 62.05           C  
ATOM    108  C   GLU A  29       2.633  33.701  19.182  1.00 61.77           C  
ATOM    109  O   GLU A  29       3.368  34.029  20.110  1.00 62.84           O  
ATOM    110  CB  GLU A  29       2.941  34.884  17.006  1.00 60.88           C  
ATOM    111  N   SER A  30       1.347  33.415  19.361  1.00 61.00           N  
ATOM    112  CA  SER A  30       0.715  33.526  20.681  1.00 60.32           C  
ATOM    113  C   SER A  30       1.373  32.703  21.790  1.00 59.88           C  
ATOM    114  O   SER A  30       1.038  32.850  22.970  1.00 60.20           O  
ATOM    115  CB  SER A  30      -0.770  33.150  20.583  1.00 60.44           C  
ATOM    116  OG  SER A  30      -0.979  31.790  20.927  1.00 60.80           O  
ATOM    117  N   GLN A  31       2.315  31.847  21.414  1.00 59.55           N  
ATOM    118  CA  GLN A  31       3.013  30.994  22.373  1.00 59.49           C  
ATOM    119  C   GLN A  31       4.343  31.597  22.835  1.00 59.40           C  
ATOM    120  O   GLN A  31       4.965  31.114  23.788  1.00 59.85           O  
ATOM    121  CB  GLN A  31       3.269  29.624  21.745  1.00 58.72           C  
ATOM    122  CG  GLN A  31       2.018  28.812  21.456  1.00 57.20           C  
ATOM    123  CD  GLN A  31       2.342  27.457  20.857  1.00 56.28           C  
ATOM    124  OE1 GLN A  31       2.624  27.342  19.661  1.00 56.35           O  
ATOM    125  NE2 GLN A  31       2.325  26.425  21.691  1.00 56.08           N  
ATOM    126  N   LEU A  32       4.779  32.650  22.152  1.00 58.63           N  
ATOM    127  CA  LEU A  32       6.028  33.316  22.483  1.00 56.88           C  
ATOM    128  C   LEU A  32       5.750  34.506  23.408  1.00 56.77           C  
ATOM    129  O   LEU A  32       4.687  35.116  23.332  1.00 57.46           O  
ATOM    130  CB  LEU A  32       6.696  33.815  21.202  1.00 55.67           C  
ATOM    131  CG  LEU A  32       6.806  32.841  20.028  1.00 54.61           C  
ATOM    132  CD1 LEU A  32       7.268  33.600  18.824  1.00 54.03           C  
ATOM    133  CD2 LEU A  32       7.786  31.731  20.320  1.00 55.10           C  
ATOM    134  N   ARG A  33       6.700  34.817  24.288  1.00 56.48           N  
ATOM    135  CA  ARG A  33       6.574  35.953  25.197  1.00 55.93           C  
ATOM    136  C   ARG A  33       7.001  37.214  24.458  1.00 56.33           C  
ATOM    137  O   ARG A  33       7.795  37.149  23.518  1.00 56.68           O  
ATOM    138  CB  ARG A  33       7.443  35.744  26.434  1.00 55.26           C  
ATOM    139  CG  ARG A  33       6.809  34.767  27.395  1.00 56.00           C  
ATOM    140  CD  ARG A  33       7.817  33.952  28.160  1.00 56.19           C  
ATOM    141  NE  ARG A  33       7.171  32.941  28.995  1.00 57.94           N  
ATOM    142  CZ  ARG A  33       6.400  33.218  30.045  1.00 58.14           C  
ATOM    143  NH1 ARG A  33       6.163  34.480  30.383  1.00 58.23           N  
ATOM    144  NH2 ARG A  33       5.869  32.236  30.763  1.00 57.85           N  
ATOM    145  N   SER A  34       6.468  38.355  24.873  1.00 56.52           N  
ATOM    146  CA  SER A  34       6.781  39.620  24.215  1.00 56.56           C  
ATOM    147  C   SER A  34       7.802  40.473  24.976  1.00 55.90           C  
ATOM    148  O   SER A  34       7.723  40.662  26.198  1.00 54.49           O  
ATOM    149  CB  SER A  34       5.479  40.391  23.999  1.00 57.45           C  
ATOM    150  OG  SER A  34       4.592  40.131  25.080  1.00 60.58           O  
ATOM    151  N   TYR A  35       8.775  40.977  24.229  1.00 55.23           N  
ATOM    152  CA  TYR A  35       9.843  41.767  24.804  1.00 54.33           C  
ATOM    153  C   TYR A  35      10.077  43.060  24.058  1.00 54.44           C  
ATOM    154  O   TYR A  35       9.724  43.197  22.891  1.00 54.42           O  
ATOM    155  CB  TYR A  35      11.122  40.937  24.824  1.00 53.58           C  
ATOM    156  CG  TYR A  35      10.982  39.694  25.667  1.00 52.07           C  
ATOM    157  CD1 TYR A  35      10.738  39.789  27.035  1.00 52.62           C  
ATOM    158  CD2 TYR A  35      11.083  38.425  25.100  1.00 52.18           C  
ATOM    159  CE1 TYR A  35      10.601  38.646  27.829  1.00 53.69           C  
ATOM    160  CE2 TYR A  35      10.942  37.271  25.881  1.00 52.53           C  
ATOM    161  CZ  TYR A  35      10.704  37.390  27.246  1.00 53.63           C  
ATOM    162  OH  TYR A  35      10.583  36.263  28.032  1.00 53.42           O  
ATOM    163  N   SER A  36      10.704  44.001  24.743  1.00 55.07           N  
ATOM    164  CA  SER A  36      10.977  45.317  24.193  1.00 54.57           C  
ATOM    165  C   SER A  36      12.057  45.433  23.125  1.00 53.87           C  
ATOM    166  O   SER A  36      12.100  46.423  22.397  1.00 56.01           O  
ATOM    167  CB  SER A  36      11.323  46.268  25.342  1.00 54.45           C  
ATOM    168  OG  SER A  36      12.450  45.788  26.066  1.00 51.84           O  
ATOM    169  N   PHE A  37      12.922  44.441  22.999  1.00 51.58           N  
ATOM    170  CA  PHE A  37      13.994  44.566  22.015  1.00 49.53           C  
ATOM    171  C   PHE A  37      13.727  43.861  20.702  1.00 48.20           C  
ATOM    172  O   PHE A  37      12.879  42.980  20.610  1.00 48.08           O  
ATOM    173  CB  PHE A  37      15.310  44.081  22.649  1.00 48.69           C  
ATOM    174  CG  PHE A  37      15.209  42.710  23.232  1.00 48.25           C  
ATOM    175  CD1 PHE A  37      15.349  41.595  22.415  1.00 47.44           C  
ATOM    176  CD2 PHE A  37      14.868  42.529  24.572  1.00 47.83           C  
ATOM    177  CE1 PHE A  37      15.145  40.321  22.913  1.00 46.32           C  
ATOM    178  CE2 PHE A  37      14.660  41.250  25.083  1.00 46.92           C  
ATOM    179  CZ  PHE A  37      14.797  40.145  24.252  1.00 47.04           C  
ATOM    180  N   PRO A  38      14.432  44.275  19.650  1.00 47.96           N  
ATOM    181  CA  PRO A  38      14.295  43.694  18.321  1.00 48.49           C  
ATOM    182  C   PRO A  38      15.207  42.490  18.202  1.00 51.04           C  
ATOM    183  O   PRO A  38      16.189  42.370  18.946  1.00 51.24           O  
ATOM    184  CB  PRO A  38      14.726  44.826  17.417  1.00 48.79           C  
ATOM    185  CG  PRO A  38      15.839  45.407  18.207  1.00 48.50           C  
ATOM    186  CD  PRO A  38      15.240  45.504  19.582  1.00 47.42           C  
ATOM    187  N   THR A  39      14.875  41.617  17.248  1.00 53.66           N  
ATOM    188  CA  THR A  39      15.604  40.366  16.999  1.00 53.63           C  
ATOM    189  C   THR A  39      15.554  39.922  15.542  1.00 53.38           C  
ATOM    190  O   THR A  39      14.591  40.174  14.817  1.00 53.42           O  
ATOM    191  CB  THR A  39      15.019  39.180  17.841  1.00 54.60           C  
ATOM    192  OG1 THR A  39      13.630  38.999  17.521  1.00 54.63           O  
ATOM    193  CG2 THR A  39      15.185  39.450  19.334  1.00 54.82           C  
ATOM    194  N   ARG A  40      16.608  39.239  15.137  1.00 54.74           N  
ATOM    195  CA  ARG A  40      16.687  38.738  13.791  1.00 57.18           C  
ATOM    196  C   ARG A  40      16.876  37.262  13.904  1.00 57.34           C  
ATOM    197  O   ARG A  40      17.527  36.776  14.822  1.00 57.17           O  
ATOM    198  CB  ARG A  40      17.867  39.341  13.064  1.00 59.98           C  
ATOM    199  CG  ARG A  40      17.912  40.841  13.207  1.00 66.81           C  
ATOM    200  CD  ARG A  40      16.520  41.522  13.082  1.00 72.17           C  
ATOM    201  NE  ARG A  40      15.911  41.449  11.748  1.00 74.55           N  
ATOM    202  CZ  ARG A  40      14.712  41.949  11.443  1.00 75.45           C  
ATOM    203  NH1 ARG A  40      13.971  42.563  12.370  1.00 74.37           N  
ATOM    204  NH2 ARG A  40      14.238  41.827  10.212  1.00 76.77           N  
ATOM    205  N   PRO A  41      16.296  36.517  12.968  1.00 57.78           N  
ATOM    206  CA  PRO A  41      16.378  35.056  12.938  1.00 56.95           C  
ATOM    207  C   PRO A  41      17.783  34.445  12.852  1.00 54.85           C  
ATOM    208  O   PRO A  41      18.687  35.011  12.242  1.00 54.27           O  
ATOM    209  CB  PRO A  41      15.531  34.704  11.714  1.00 57.56           C  
ATOM    210  CG  PRO A  41      14.497  35.801  11.695  1.00 59.46           C  
ATOM    211  CD  PRO A  41      15.349  37.013  11.950  1.00 59.03           C  
ATOM    212  N   ILE A  42      17.956  33.278  13.470  1.00 51.80           N  
ATOM    213  CA  ILE A  42      19.220  32.565  13.410  1.00 48.16           C  
ATOM    214  C   ILE A  42      19.112  31.569  12.240  1.00 47.57           C  
ATOM    215  O   ILE A  42      18.089  30.902  12.077  1.00 47.58           O  
ATOM    216  CB  ILE A  42      19.464  31.788  14.706  1.00 47.40           C  
ATOM    217  CG1 ILE A  42      19.483  32.743  15.882  1.00 45.88           C  
ATOM    218  CG2 ILE A  42      20.783  31.055  14.636  1.00 45.99           C  
ATOM    219  CD1 ILE A  42      19.813  32.056  17.161  1.00 42.82           C  
ATOM    220  N   PRO A  43      20.160  31.465  11.404  1.00 46.39           N  
ATOM    221  CA  PRO A  43      20.194  30.564  10.249  1.00 46.30           C  
ATOM    222  C   PRO A  43      19.833  29.114  10.548  1.00 48.08           C  
ATOM    223  O   PRO A  43      20.402  28.520  11.462  1.00 48.13           O  
ATOM    224  CB  PRO A  43      21.643  30.657   9.776  1.00 45.10           C  
ATOM    225  CG  PRO A  43      22.012  32.011  10.113  1.00 43.88           C  
ATOM    226  CD  PRO A  43      21.428  32.207  11.497  1.00 44.59           C  
ATOM    227  N   ARG A  44      18.895  28.552   9.783  1.00 48.14           N  
ATOM    228  CA  ARG A  44      18.537  27.138   9.930  1.00 47.40           C  
ATOM    229  C   ARG A  44      19.104  26.483   8.682  1.00 47.09           C  
ATOM    230  O   ARG A  44      18.556  26.665   7.600  1.00 46.70           O  
ATOM    231  CB  ARG A  44      17.028  26.936   9.944  1.00 47.51           C  
ATOM    232  CG  ARG A  44      16.397  27.063  11.308  1.00 51.52           C  
ATOM    233  CD  ARG A  44      14.893  26.911  11.222  1.00 55.74           C  
ATOM    234  NE  ARG A  44      14.470  25.631  10.653  1.00 56.96           N  
ATOM    235  CZ  ARG A  44      14.318  24.518  11.367  1.00 59.32           C  
ATOM    236  NH1 ARG A  44      14.563  24.533  12.677  1.00 59.27           N  
ATOM    237  NH2 ARG A  44      13.899  23.397  10.792  1.00 59.86           N  
ATOM    238  N   LEU A  45      20.201  25.738   8.839  1.00 47.41           N  
ATOM    239  CA  LEU A  45      20.862  25.079   7.708  1.00 48.47           C  
ATOM    240  C   LEU A  45      21.142  23.576   7.863  1.00 48.76           C  
ATOM    241  O   LEU A  45      20.875  22.960   8.888  1.00 49.25           O  
ATOM    242  CB  LEU A  45      22.191  25.779   7.402  1.00 48.21           C  
ATOM    243  CG  LEU A  45      22.254  27.289   7.602  1.00 50.25           C  
ATOM    244  CD1 LEU A  45      23.678  27.769   7.341  1.00 48.87           C  
ATOM    245  CD2 LEU A  45      21.253  27.982   6.689  1.00 50.06           C  
ATOM    246  N   SER A  46      21.704  22.995   6.819  1.00 48.26           N  
ATOM    247  CA  SER A  46      22.017  21.596   6.851  1.00 48.57           C  
ATOM    248  C   SER A  46      23.449  21.409   7.284  1.00 49.80           C  
ATOM    249  O   SER A  46      24.307  22.219   6.979  1.00 49.62           O  
ATOM    250  CB  SER A  46      21.843  20.996   5.473  1.00 49.25           C  
ATOM    251  OG  SER A  46      22.848  20.020   5.252  1.00 51.28           O  
ATOM    252  N   GLN A  47      23.699  20.320   7.996  1.00 51.46           N  
ATOM    253  CA  GLN A  47      25.038  19.984   8.450  1.00 52.90           C  
ATOM    254  C   GLN A  47      26.030  19.894   7.274  1.00 54.11           C  
ATOM    255  O   GLN A  47      27.222  20.132   7.447  1.00 54.64           O  
ATOM    256  CB  GLN A  47      24.972  18.658   9.222  1.00 52.97           C  
ATOM    257  CG  GLN A  47      26.158  17.726   9.058  1.00 56.10           C  
ATOM    258  CD  GLN A  47      26.064  16.923   7.782  1.00 56.76           C  
ATOM    259  OE1 GLN A  47      24.965  16.598   7.339  1.00 57.52           O  
ATOM    260  NE2 GLN A  47      27.207  16.586   7.190  1.00 59.09           N  
ATOM    261  N   SER A  48      25.534  19.566   6.082  1.00 55.46           N  
ATOM    262  CA  SER A  48      26.390  19.440   4.901  1.00 56.67           C  
ATOM    263  C   SER A  48      26.559  20.785   4.178  1.00 58.59           C  
ATOM    264  O   SER A  48      27.312  20.890   3.195  1.00 59.21           O  
ATOM    265  CB  SER A  48      25.782  18.433   3.942  1.00 55.85           C  
ATOM    266  OG  SER A  48      24.528  18.909   3.510  1.00 55.20           O  
ATOM    267  N   ASP A  49      25.854  21.806   4.666  1.00 59.28           N  
ATOM    268  CA  ASP A  49      25.930  23.150   4.090  1.00 58.73           C  
ATOM    269  C   ASP A  49      27.213  23.845   4.549  1.00 58.38           C  
ATOM    270  O   ASP A  49      27.432  24.038   5.748  1.00 58.69           O  
ATOM    271  CB  ASP A  49      24.733  23.987   4.536  1.00 60.59           C  
ATOM    272  CG  ASP A  49      24.635  25.318   3.797  1.00 61.41           C  
ATOM    273  OD1 ASP A  49      25.685  25.898   3.438  1.00 61.64           O  
ATOM    274  OD2 ASP A  49      23.498  25.795   3.584  1.00 62.30           O  
ATOM    275  N   PRO A  50      28.069  24.237   3.598  1.00 56.78           N  
ATOM    276  CA  PRO A  50      29.338  24.916   3.872  1.00 56.16           C  
ATOM    277  C   PRO A  50      29.181  26.177   4.711  1.00 56.25           C  
ATOM    278  O   PRO A  50      30.028  26.487   5.537  1.00 55.93           O  
ATOM    279  CB  PRO A  50      29.864  25.226   2.477  1.00 55.01           C  
ATOM    280  CG  PRO A  50      29.346  24.106   1.680  1.00 55.03           C  
ATOM    281  CD  PRO A  50      27.925  23.978   2.156  1.00 55.35           C  
ATOM    282  N   ARG A  51      28.099  26.913   4.490  1.00 56.97           N  
ATOM    283  CA  ARG A  51      27.869  28.137   5.236  1.00 57.34           C  
ATOM    284  C   ARG A  51      27.716  27.860   6.726  1.00 56.44           C  
ATOM    285  O   ARG A  51      28.081  28.684   7.565  1.00 56.83           O  
ATOM    286  CB  ARG A  51      26.617  28.837   4.717  1.00 60.45           C  
ATOM    287  CG  ARG A  51      26.278  30.127   5.461  1.00 66.39           C  
ATOM    288  CD  ARG A  51      24.840  30.596   5.117  1.00 72.09           C  
ATOM    289  NE  ARG A  51      24.397  31.738   5.928  1.00 76.53           N  
ATOM    290  CZ  ARG A  51      23.117  32.133   6.066  1.00 78.84           C  
ATOM    291  NH1 ARG A  51      22.108  31.484   5.457  1.00 78.14           N  
ATOM    292  NH2 ARG A  51      22.828  33.192   6.820  1.00 80.13           N  
ATOM    293  N   ALA A  52      27.168  26.699   7.057  1.00 56.54           N  
ATOM    294  CA  ALA A  52      26.982  26.339   8.453  1.00 56.09           C  
ATOM    295  C   ALA A  52      28.323  25.990   9.086  1.00 56.42           C  
ATOM    296  O   ALA A  52      28.586  26.318  10.234  1.00 57.22           O  
ATOM    297  CB  ALA A  52      26.032  25.172   8.560  1.00 54.21           C  
ATOM    298  N   GLU A  53      29.173  25.323   8.325  1.00 58.01           N  
ATOM    299  CA  GLU A  53      30.489  24.941   8.819  1.00 59.00           C  
ATOM    300  C   GLU A  53      31.286  26.205   9.018  1.00 58.95           C  
ATOM    301  O   GLU A  53      32.278  26.233   9.729  1.00 59.02           O  
ATOM    302  CB  GLU A  53      31.206  24.084   7.781  1.00 61.38           C  
ATOM    303  CG  GLU A  53      32.222  23.116   8.341  1.00 67.25           C  
ATOM    304  CD  GLU A  53      31.592  21.999   9.165  1.00 70.95           C  
ATOM    305  OE1 GLU A  53      30.444  21.588   8.872  1.00 73.43           O  
ATOM    306  OE2 GLU A  53      32.258  21.509  10.103  1.00 72.99           O  
ATOM    307  N   GLU A  54      30.838  27.251   8.348  1.00 60.21           N  
ATOM    308  CA  GLU A  54      31.494  28.548   8.390  1.00 59.94           C  
ATOM    309  C   GLU A  54      31.104  29.300   9.652  1.00 56.95           C  
ATOM    310  O   GLU A  54      31.946  29.862  10.342  1.00 55.72           O  
ATOM    311  CB  GLU A  54      31.103  29.343   7.131  1.00 65.43           C  
ATOM    312  CG  GLU A  54      31.384  30.839   7.197  1.00 74.22           C  
ATOM    313  CD  GLU A  54      30.783  31.627   6.023  1.00 79.25           C  
ATOM    314  OE1 GLU A  54      30.928  32.870   6.031  1.00 82.32           O  
ATOM    315  OE2 GLU A  54      30.178  31.028   5.096  1.00 80.90           O  
ATOM    316  N   LEU A  55      29.813  29.303   9.943  1.00 53.26           N  
ATOM    317  CA  LEU A  55      29.326  29.971  11.128  1.00 50.15           C  
ATOM    318  C   LEU A  55      29.945  29.405  12.397  1.00 49.64           C  
ATOM    319  O   LEU A  55      30.232  30.144  13.334  1.00 49.81           O  
ATOM    320  CB  LEU A  55      27.822  29.829  11.212  1.00 48.68           C  
ATOM    321  CG  LEU A  55      27.089  30.537  10.095  1.00 46.28           C  
ATOM    322  CD1 LEU A  55      25.610  30.252  10.124  1.00 45.88           C  
ATOM    323  CD2 LEU A  55      27.328  31.994  10.285  1.00 46.46           C  
ATOM    324  N   ILE A  56      30.132  28.092  12.438  1.00 48.04           N  
ATOM    325  CA  ILE A  56      30.711  27.452  13.615  1.00 47.25           C  
ATOM    326  C   ILE A  56      32.174  27.835  13.751  1.00 49.01           C  
ATOM    327  O   ILE A  56      32.669  28.137  14.840  1.00 49.48           O  
ATOM    328  CB  ILE A  56      30.613  25.921  13.501  1.00 45.01           C  
ATOM    329  CG1 ILE A  56      29.155  25.497  13.424  1.00 43.66           C  
ATOM    330  CG2 ILE A  56      31.251  25.262  14.704  1.00 44.56           C  
ATOM    331  CD1 ILE A  56      29.000  24.015  13.340  1.00 40.72           C  
ATOM    332  N   GLU A  57      32.859  27.822  12.621  1.00 51.42           N  
ATOM    333  CA  GLU A  57      34.269  28.156  12.587  1.00 54.01           C  
ATOM    334  C   GLU A  57      34.505  29.581  13.028  1.00 54.94           C  
ATOM    335  O   GLU A  57      35.609  29.930  13.425  1.00 55.79           O  
ATOM    336  CB  GLU A  57      34.831  27.972  11.177  1.00 56.71           C  
ATOM    337  CG  GLU A  57      36.350  28.126  11.068  1.00 62.39           C  
ATOM    338  CD  GLU A  57      37.132  27.261  12.061  1.00 66.91           C  
ATOM    339  OE1 GLU A  57      36.716  26.112  12.336  1.00 69.73           O  
ATOM    340  OE2 GLU A  57      38.186  27.720  12.558  1.00 68.52           O  
ATOM    341  N   ASN A  58      33.473  30.410  12.954  1.00 56.29           N  
ATOM    342  CA  ASN A  58      33.612  31.804  13.355  1.00 57.19           C  
ATOM    343  C   ASN A  58      32.835  32.068  14.624  1.00 55.76           C  
ATOM    344  O   ASN A  58      32.443  33.190  14.898  1.00 55.57           O  
ATOM    345  CB  ASN A  58      33.112  32.734  12.255  1.00 62.05           C  
ATOM    346  CG  ASN A  58      33.842  32.523  10.949  1.00 67.82           C  
ATOM    347  OD1 ASN A  58      35.070  32.482  10.917  1.00 70.64           O  
ATOM    348  ND2 ASN A  58      33.090  32.394   9.859  1.00 69.69           N  
ATOM    349  N   GLU A  59      32.606  31.019  15.394  1.00 54.56           N  
ATOM    350  CA  GLU A  59      31.887  31.141  16.652  1.00 54.14           C  
ATOM    351  C   GLU A  59      30.623  31.998  16.591  1.00 51.68           C  
ATOM    352  O   GLU A  59      30.427  32.939  17.376  1.00 50.29           O  
ATOM    353  CB  GLU A  59      32.840  31.652  17.741  1.00 56.59           C  
ATOM    354  CG  GLU A  59      33.641  30.530  18.438  1.00 61.08           C  
ATOM    355  CD  GLU A  59      34.850  31.040  19.217  1.00 63.78           C  
ATOM    356  OE1 GLU A  59      35.820  31.504  18.572  1.00 65.19           O  
ATOM    357  OE2 GLU A  59      34.846  30.984  20.472  1.00 66.30           O  
ATOM    358  N   GLU A  60      29.765  31.638  15.648  1.00 49.80           N  
ATOM    359  CA  GLU A  60      28.484  32.293  15.471  1.00 48.15           C  
ATOM    360  C   GLU A  60      27.401  31.229  15.518  1.00 46.20           C  
ATOM    361  O   GLU A  60      27.561  30.121  14.992  1.00 45.65           O  
ATOM    362  CB  GLU A  60      28.448  33.029  14.151  1.00 49.83           C  
ATOM    363  CG  GLU A  60      29.464  34.124  14.119  1.00 54.03           C  
ATOM    364  CD  GLU A  60      29.108  35.159  13.114  1.00 57.48           C  
ATOM    365  OE1 GLU A  60      29.752  35.187  12.044  1.00 59.24           O  
ATOM    366  OE2 GLU A  60      28.164  35.934  13.387  1.00 60.09           O  
ATOM    367  N   PRO A  61      26.273  31.538  16.173  1.00 42.96           N  
ATOM    368  CA  PRO A  61      25.162  30.593  16.291  1.00 42.02           C  
ATOM    369  C   PRO A  61      24.576  30.140  14.948  1.00 42.66           C  
ATOM    370  O   PRO A  61      24.683  30.840  13.943  1.00 44.15           O  
ATOM    371  CB  PRO A  61      24.163  31.371  17.148  1.00 40.20           C  
ATOM    372  CG  PRO A  61      24.428  32.787  16.779  1.00 40.29           C  
ATOM    373  CD  PRO A  61      25.929  32.842  16.761  1.00 41.89           C  
ATOM    374  N   VAL A  62      23.975  28.954  14.938  1.00 41.64           N  
ATOM    375  CA  VAL A  62      23.364  28.404  13.732  1.00 39.75           C  
ATOM    376  C   VAL A  62      22.567  27.193  14.174  1.00 41.03           C  
ATOM    377  O   VAL A  62      22.937  26.537  15.136  1.00 41.75           O  
ATOM    378  CB  VAL A  62      24.431  27.949  12.685  1.00 39.38           C  
ATOM    379  CG1 VAL A  62      25.384  26.931  13.283  1.00 37.41           C  
ATOM    380  CG2 VAL A  62      23.741  27.320  11.491  1.00 37.92           C  
ATOM    381  N   VAL A  63      21.462  26.910  13.492  1.00 41.24           N  
ATOM    382  CA  VAL A  63      20.646  25.743  13.822  1.00 40.46           C  
ATOM    383  C   VAL A  63      20.788  24.710  12.697  1.00 42.05           C  
ATOM    384  O   VAL A  63      20.469  25.002  11.543  1.00 43.42           O  
ATOM    385  CB  VAL A  63      19.152  26.122  13.985  1.00 39.26           C  
ATOM    386  CG1 VAL A  63      18.325  24.896  14.317  1.00 37.96           C  
ATOM    387  CG2 VAL A  63      18.997  27.167  15.085  1.00 39.03           C  
ATOM    388  N   LEU A  64      21.308  23.525  13.040  1.00 43.90           N  
ATOM    389  CA  LEU A  64      21.495  22.407  12.094  1.00 43.41           C  
ATOM    390  C   LEU A  64      20.253  21.510  12.186  1.00 43.81           C  
ATOM    391  O   LEU A  64      19.838  21.114  13.280  1.00 44.70           O  
ATOM    392  CB  LEU A  64      22.741  21.611  12.463  1.00 42.33           C  
ATOM    393  CG  LEU A  64      23.998  22.473  12.511  1.00 41.16           C  
ATOM    394  CD1 LEU A  64      25.111  21.673  13.114  1.00 40.59           C  
ATOM    395  CD2 LEU A  64      24.371  22.951  11.122  1.00 41.23           C  
ATOM    396  N   THR A  65      19.675  21.176  11.043  1.00 44.77           N  
ATOM    397  CA  THR A  65      18.440  20.411  11.028  1.00 46.62           C  
ATOM    398  C   THR A  65      18.517  18.940  10.653  1.00 47.88           C  
ATOM    399  O   THR A  65      17.508  18.220  10.746  1.00 46.16           O  
ATOM    400  CB  THR A  65      17.431  21.098  10.085  1.00 47.61           C  
ATOM    401  OG1 THR A  65      18.019  21.266   8.784  1.00 46.45           O  
ATOM    402  CG2 THR A  65      17.039  22.468  10.640  1.00 45.94           C  
ATOM    403  N   ASP A  66      19.702  18.478  10.270  1.00 48.91           N  
ATOM    404  CA  ASP A  66      19.842  17.101   9.843  1.00 49.85           C  
ATOM    405  C   ASP A  66      21.121  16.416  10.321  1.00 49.19           C  
ATOM    406  O   ASP A  66      21.777  15.683   9.566  1.00 49.93           O  
ATOM    407  CB  ASP A  66      19.752  17.077   8.327  1.00 52.05           C  
ATOM    408  CG  ASP A  66      20.806  17.933   7.676  1.00 53.75           C  
ATOM    409  OD1 ASP A  66      21.297  18.874   8.342  1.00 54.08           O  
ATOM    410  OD2 ASP A  66      21.135  17.680   6.495  1.00 54.62           O  
ATOM    411  N   THR A  67      21.466  16.629  11.584  1.00 47.97           N  
ATOM    412  CA  THR A  67      22.678  16.025  12.123  1.00 46.28           C  
ATOM    413  C   THR A  67      22.428  14.611  12.609  1.00 47.11           C  
ATOM    414  O   THR A  67      23.315  13.756  12.525  1.00 47.75           O  
ATOM    415  CB  THR A  67      23.238  16.833  13.309  1.00 43.77           C  
ATOM    416  OG1 THR A  67      22.275  16.869  14.375  1.00 41.57           O  
ATOM    417  CG2 THR A  67      23.540  18.239  12.869  1.00 42.70           C  
ATOM    418  N   ASN A  68      21.214  14.377  13.107  1.00 47.44           N  
ATOM    419  CA  ASN A  68      20.845  13.081  13.638  1.00 47.97           C  
ATOM    420  C   ASN A  68      21.648  12.842  14.905  1.00 48.47           C  
ATOM    421  O   ASN A  68      21.997  11.711  15.220  1.00 50.60           O  
ATOM    422  CB  ASN A  68      21.168  11.981  12.637  1.00 49.13           C  
ATOM    423  CG  ASN A  68      20.220  11.976  11.476  1.00 51.36           C  
ATOM    424  OD1 ASN A  68      19.021  11.783  11.661  1.00 52.58           O  
ATOM    425  ND2 ASN A  68      20.737  12.206  10.268  1.00 54.26           N  
ATOM    426  N   LEU A  69      21.926  13.906  15.647  1.00 47.58           N  
ATOM    427  CA  LEU A  69      22.717  13.778  16.863  1.00 44.93           C  
ATOM    428  C   LEU A  69      22.043  12.919  17.933  1.00 44.27           C  
ATOM    429  O   LEU A  69      22.646  11.977  18.464  1.00 43.58           O  
ATOM    430  CB  LEU A  69      23.006  15.169  17.410  1.00 42.65           C  
ATOM    431  CG  LEU A  69      23.991  15.278  18.560  1.00 41.86           C  
ATOM    432  CD1 LEU A  69      25.338  14.642  18.187  1.00 40.61           C  
ATOM    433  CD2 LEU A  69      24.132  16.753  18.904  1.00 39.71           C  
ATOM    434  N   VAL A  70      20.795  13.248  18.238  1.00 43.52           N  
ATOM    435  CA  VAL A  70      20.058  12.513  19.247  1.00 42.68           C  
ATOM    436  C   VAL A  70      18.910  11.724  18.657  1.00 43.34           C  
ATOM    437  O   VAL A  70      17.826  11.656  19.233  1.00 44.09           O  
ATOM    438  CB  VAL A  70      19.520  13.459  20.342  1.00 42.79           C  
ATOM    439  CG1 VAL A  70      20.701  14.087  21.085  1.00 40.27           C  
ATOM    440  CG2 VAL A  70      18.583  14.526  19.735  1.00 41.03           C  
ATOM    441  N   TYR A  71      19.155  11.114  17.511  1.00 42.57           N  
ATOM    442  CA  TYR A  71      18.132  10.332  16.845  1.00 43.63           C  
ATOM    443  C   TYR A  71      17.442   9.290  17.742  1.00 44.37           C  
ATOM    444  O   TYR A  71      16.208   9.238  17.795  1.00 45.01           O  
ATOM    445  CB  TYR A  71      18.751   9.647  15.634  1.00 45.92           C  
ATOM    446  CG  TYR A  71      17.829   8.684  14.929  1.00 48.65           C  
ATOM    447  CD1 TYR A  71      16.667   9.129  14.315  1.00 48.84           C  
ATOM    448  CD2 TYR A  71      18.110   7.315  14.897  1.00 49.14           C  
ATOM    449  CE1 TYR A  71      15.787   8.232  13.680  1.00 50.35           C  
ATOM    450  CE2 TYR A  71      17.241   6.406  14.269  1.00 48.95           C  
ATOM    451  CZ  TYR A  71      16.075   6.873  13.665  1.00 50.63           C  
ATOM    452  OH  TYR A  71      15.169   6.000  13.093  1.00 51.37           O  
ATOM    453  N   PRO A  72      18.227   8.454  18.461  1.00 44.32           N  
ATOM    454  CA  PRO A  72      17.661   7.425  19.342  1.00 44.28           C  
ATOM    455  C   PRO A  72      16.816   7.970  20.484  1.00 45.88           C  
ATOM    456  O   PRO A  72      15.941   7.283  20.999  1.00 46.68           O  
ATOM    457  CB  PRO A  72      18.904   6.708  19.875  1.00 41.78           C  
ATOM    458  CG  PRO A  72      19.891   6.880  18.791  1.00 43.32           C  
ATOM    459  CD  PRO A  72      19.690   8.330  18.406  1.00 43.55           C  
ATOM    460  N   ALA A  73      17.081   9.216  20.866  1.00 47.28           N  
ATOM    461  CA  ALA A  73      16.371   9.852  21.966  1.00 47.42           C  
ATOM    462  C   ALA A  73      15.080  10.541  21.542  1.00 48.52           C  
ATOM    463  O   ALA A  73      14.274  10.938  22.388  1.00 49.46           O  
ATOM    464  CB  ALA A  73      17.286  10.854  22.647  1.00 45.86           C  
ATOM    465  N   LEU A  74      14.873  10.684  20.239  1.00 48.70           N  
ATOM    466  CA  LEU A  74      13.670  11.357  19.775  1.00 48.03           C  
ATOM    467  C   LEU A  74      12.391  10.653  20.186  1.00 49.02           C  
ATOM    468  O   LEU A  74      11.319  11.247  20.142  1.00 49.94           O  
ATOM    469  CB  LEU A  74      13.723  11.526  18.260  1.00 44.81           C  
ATOM    470  CG  LEU A  74      14.740  12.580  17.815  1.00 44.75           C  
ATOM    471  CD1 LEU A  74      14.957  12.436  16.346  1.00 44.33           C  
ATOM    472  CD2 LEU A  74      14.259  13.979  18.147  1.00 42.66           C  
ATOM    473  N   LYS A  75      12.515   9.398  20.609  1.00 50.86           N  
ATOM    474  CA  LYS A  75      11.362   8.602  21.040  1.00 51.53           C  
ATOM    475  C   LYS A  75      11.112   8.710  22.545  1.00 52.03           C  
ATOM    476  O   LYS A  75      10.176   8.121  23.081  1.00 52.09           O  
ATOM    477  CB  LYS A  75      11.570   7.136  20.662  1.00 51.64           C  
ATOM    478  CG  LYS A  75      12.806   6.506  21.265  1.00 52.00           C  
ATOM    479  CD  LYS A  75      12.991   5.102  20.728  1.00 52.64           C  
ATOM    480  CE  LYS A  75      14.384   4.599  21.006  1.00 52.63           C  
ATOM    481  NZ  LYS A  75      14.677   4.714  22.452  1.00 54.66           N  
ATOM    482  N   TRP A  76      11.954   9.480  23.216  1.00 52.93           N  
ATOM    483  CA  TRP A  76      11.832   9.678  24.647  1.00 52.96           C  
ATOM    484  C   TRP A  76      10.595  10.471  25.027  1.00 55.05           C  
ATOM    485  O   TRP A  76      10.072  11.277  24.254  1.00 55.58           O  
ATOM    486  CB  TRP A  76      13.064  10.392  25.197  1.00 50.91           C  
ATOM    487  CG  TRP A  76      14.321   9.572  25.154  1.00 49.10           C  
ATOM    488  CD1 TRP A  76      14.485   8.313  24.629  1.00 49.16           C  
ATOM    489  CD2 TRP A  76      15.605   9.970  25.642  1.00 47.55           C  
ATOM    490  NE1 TRP A  76      15.792   7.905  24.763  1.00 47.77           N  
ATOM    491  CE2 TRP A  76      16.503   8.904  25.380  1.00 46.97           C  
ATOM    492  CE3 TRP A  76      16.091  11.120  26.273  1.00 45.39           C  
ATOM    493  CZ2 TRP A  76      17.861   8.963  25.732  1.00 46.21           C  
ATOM    494  CZ3 TRP A  76      17.438  11.180  26.618  1.00 44.74           C  
ATOM    495  CH2 TRP A  76      18.305  10.108  26.348  1.00 45.22           C  
ATOM    496  N   ASP A  77      10.149  10.214  26.246  1.00 57.77           N  
ATOM    497  CA  ASP A  77       8.982  10.855  26.830  1.00 60.94           C  
ATOM    498  C   ASP A  77       8.958  10.425  28.295  1.00 62.23           C  
ATOM    499  O   ASP A  77       9.668   9.491  28.682  1.00 62.20           O  
ATOM    500  CB  ASP A  77       7.698  10.441  26.080  1.00 62.70           C  
ATOM    501  CG  ASP A  77       7.324   8.964  26.269  1.00 66.24           C  
ATOM    502  OD1 ASP A  77       8.184   8.141  26.650  1.00 67.73           O  
ATOM    503  OD2 ASP A  77       6.151   8.614  26.001  1.00 66.49           O  
ATOM    504  N   LEU A  78       8.177  11.125  29.112  1.00 63.21           N  
ATOM    505  CA  LEU A  78       8.097  10.820  30.535  1.00 64.07           C  
ATOM    506  C   LEU A  78       7.922   9.319  30.821  1.00 65.49           C  
ATOM    507  O   LEU A  78       8.621   8.743  31.666  1.00 64.88           O  
ATOM    508  CB  LEU A  78       6.948  11.615  31.143  1.00 63.48           C  
ATOM    509  CG  LEU A  78       7.097  13.137  31.065  1.00 63.90           C  
ATOM    510  CD1 LEU A  78       5.805  13.829  31.500  1.00 64.37           C  
ATOM    511  CD2 LEU A  78       8.272  13.563  31.939  1.00 62.23           C  
ATOM    512  N   GLU A  79       6.996   8.688  30.104  1.00 66.68           N  
ATOM    513  CA  GLU A  79       6.718   7.267  30.271  1.00 67.46           C  
ATOM    514  C   GLU A  79       7.955   6.407  30.011  1.00 66.04           C  
ATOM    515  O   GLU A  79       8.498   5.780  30.925  1.00 64.58           O  
ATOM    516  CB  GLU A  79       5.611   6.869  29.308  1.00 71.23           C  
ATOM    517  CG  GLU A  79       5.171   5.436  29.445  1.00 77.19           C  
ATOM    518  CD  GLU A  79       4.180   5.049  28.377  1.00 80.78           C  
ATOM    519  OE1 GLU A  79       4.567   4.967  27.188  1.00 82.93           O  
ATOM    520  OE2 GLU A  79       3.002   4.839  28.733  1.00 82.77           O  
ATOM    521  N   TYR A  80       8.383   6.378  28.751  1.00 64.84           N  
ATOM    522  CA  TYR A  80       9.546   5.596  28.361  1.00 65.00           C  
ATOM    523  C   TYR A  80      10.741   5.865  29.256  1.00 65.37           C  
ATOM    524  O   TYR A  80      11.457   4.948  29.633  1.00 65.33           O  
ATOM    525  CB  TYR A  80       9.949   5.909  26.923  1.00 63.63           C  
ATOM    526  CG  TYR A  80      11.236   5.229  26.490  1.00 63.23           C  
ATOM    527  CD1 TYR A  80      11.227   3.948  25.934  1.00 64.22           C  
ATOM    528  CD2 TYR A  80      12.463   5.878  26.620  1.00 62.07           C  
ATOM    529  CE1 TYR A  80      12.414   3.334  25.507  1.00 62.54           C  
ATOM    530  CE2 TYR A  80      13.653   5.272  26.204  1.00 62.64           C  
ATOM    531  CZ  TYR A  80      13.622   4.003  25.644  1.00 62.63           C  
ATOM    532  OH  TYR A  80      14.795   3.425  25.201  1.00 61.92           O  
ATOM    533  N   LEU A  81      10.966   7.131  29.575  1.00 66.18           N  
ATOM    534  CA  LEU A  81      12.091   7.496  30.416  1.00 67.28           C  
ATOM    535  C   LEU A  81      12.003   6.913  31.819  1.00 68.59           C  
ATOM    536  O   LEU A  81      12.924   6.232  32.280  1.00 67.95           O  
ATOM    537  CB  LEU A  81      12.203   9.014  30.507  1.00 66.83           C  
ATOM    538  CG  LEU A  81      12.805   9.721  29.303  1.00 66.23           C  
ATOM    539  CD1 LEU A  81      12.849  11.206  29.588  1.00 65.90           C  
ATOM    540  CD2 LEU A  81      14.203   9.191  29.035  1.00 65.06           C  
ATOM    541  N   GLN A  82      10.898   7.185  32.505  1.00 70.21           N  
ATOM    542  CA  GLN A  82      10.706   6.682  33.864  1.00 72.10           C  
ATOM    543  C   GLN A  82      10.953   5.185  33.961  1.00 73.53           C  
ATOM    544  O   GLN A  82      11.429   4.688  34.977  1.00 74.04           O  
ATOM    545  CB  GLN A  82       9.291   6.996  34.338  1.00 72.34           C  
ATOM    546  CG  GLN A  82       8.825   6.164  35.523  1.00 73.27           C  
ATOM    547  CD  GLN A  82       7.537   6.695  36.112  1.00 73.88           C  
ATOM    548  OE1 GLN A  82       6.688   7.218  35.396  1.00 76.21           O  
ATOM    549  NE2 GLN A  82       7.377   6.551  37.422  1.00 73.22           N  
ATOM    550  N   GLU A  83      10.637   4.476  32.889  1.00 75.20           N  
ATOM    551  CA  GLU A  83      10.811   3.035  32.845  1.00 75.49           C  
ATOM    552  C   GLU A  83      12.243   2.526  32.662  1.00 74.86           C  
ATOM    553  O   GLU A  83      12.622   1.509  33.239  1.00 74.75           O  
ATOM    554  CB  GLU A  83       9.956   2.466  31.716  1.00 77.18           C  
ATOM    555  CG  GLU A  83       9.944   0.966  31.698  1.00 82.93           C  
ATOM    556  CD  GLU A  83       8.635   0.414  32.205  1.00 87.12           C  
ATOM    557  OE1 GLU A  83       7.608   0.620  31.524  1.00 89.09           O  
ATOM    558  OE2 GLU A  83       8.622  -0.221  33.284  1.00 89.62           O  
ATOM    559  N   ASN A  84      13.034   3.232  31.863  1.00 74.85           N  
ATOM    560  CA  ASN A  84      14.400   2.819  31.558  1.00 74.66           C  
ATOM    561  C   ASN A  84      15.498   3.718  32.118  1.00 74.48           C  
ATOM    562  O   ASN A  84      16.670   3.335  32.153  1.00 73.54           O  
ATOM    563  CB  ASN A  84      14.556   2.745  30.036  1.00 74.74           C  
ATOM    564  CG  ASN A  84      13.442   1.953  29.378  1.00 74.86           C  
ATOM    565  OD1 ASN A  84      13.425   0.728  29.446  1.00 76.78           O  
ATOM    566  ND2 ASN A  84      12.496   2.650  28.751  1.00 73.05           N  
ATOM    567  N   ILE A  85      15.116   4.909  32.564  1.00 74.87           N  
ATOM    568  CA  ILE A  85      16.074   5.879  33.083  1.00 75.10           C  
ATOM    569  C   ILE A  85      16.835   5.384  34.304  1.00 76.15           C  
ATOM    570  O   ILE A  85      17.603   6.127  34.915  1.00 76.06           O  
ATOM    571  CB  ILE A  85      15.367   7.212  33.425  1.00 74.10           C  
ATOM    572  CG1 ILE A  85      16.394   8.328  33.586  1.00 73.46           C  
ATOM    573  CG2 ILE A  85      14.553   7.063  34.687  1.00 74.04           C  
ATOM    574  CD1 ILE A  85      17.145   8.625  32.321  1.00 73.29           C  
ATOM    575  N   GLY A  86      16.631   4.123  34.658  1.00 77.16           N  
ATOM    576  CA  GLY A  86      17.311   3.595  35.821  1.00 78.21           C  
ATOM    577  C   GLY A  86      16.689   4.100  37.112  1.00 78.70           C  
ATOM    578  O   GLY A  86      15.530   4.517  37.141  1.00 79.41           O  
ATOM    579  N   ASN A  87      17.453   4.076  38.190  1.00 78.65           N  
ATOM    580  CA  ASN A  87      16.907   4.521  39.455  1.00 79.08           C  
ATOM    581  C   ASN A  87      17.956   5.273  40.238  1.00 78.38           C  
ATOM    582  O   ASN A  87      18.553   4.748  41.177  1.00 78.16           O  
ATOM    583  CB  ASN A  87      16.398   3.319  40.247  1.00 80.78           C  
ATOM    584  CG  ASN A  87      15.688   3.717  41.520  1.00 82.30           C  
ATOM    585  OD1 ASN A  87      16.314   3.874  42.569  1.00 82.49           O  
ATOM    586  ND2 ASN A  87      14.376   3.899  41.430  1.00 81.88           N  
ATOM    587  N   GLY A  88      18.178   6.515  39.832  1.00 77.65           N  
ATOM    588  CA  GLY A  88      19.165   7.336  40.492  1.00 76.07           C  
ATOM    589  C   GLY A  88      18.537   8.633  40.931  1.00 75.36           C  
ATOM    590  O   GLY A  88      17.324   8.797  40.831  1.00 74.96           O  
ATOM    591  N   ASP A  89      19.373   9.550  41.409  1.00 75.53           N  
ATOM    592  CA  ASP A  89      18.931  10.861  41.887  1.00 75.45           C  
ATOM    593  C   ASP A  89      19.062  11.927  40.812  1.00 73.49           C  
ATOM    594  O   ASP A  89      20.128  12.091  40.213  1.00 73.23           O  
ATOM    595  CB  ASP A  89      19.760  11.286  43.107  1.00 78.64           C  
ATOM    596  CG  ASP A  89      19.010  11.116  44.417  1.00 80.85           C  
ATOM    597  OD1 ASP A  89      18.158  10.207  44.509  1.00 81.40           O  
ATOM    598  OD2 ASP A  89      19.286  11.887  45.363  1.00 81.82           O  
ATOM    599  N   PHE A  90      17.974  12.652  40.585  1.00 71.61           N  
ATOM    600  CA  PHE A  90      17.946  13.711  39.587  1.00 70.05           C  
ATOM    601  C   PHE A  90      17.648  15.049  40.262  1.00 68.41           C  
ATOM    602  O   PHE A  90      16.713  15.154  41.054  1.00 67.86           O  
ATOM    603  CB  PHE A  90      16.860  13.436  38.531  1.00 69.90           C  
ATOM    604  CG  PHE A  90      16.995  12.104  37.827  1.00 70.55           C  
ATOM    605  CD1 PHE A  90      16.663  10.917  38.472  1.00 71.55           C  
ATOM    606  CD2 PHE A  90      17.471  12.039  36.521  1.00 70.72           C  
ATOM    607  CE1 PHE A  90      16.803   9.678  37.831  1.00 71.61           C  
ATOM    608  CE2 PHE A  90      17.616  10.807  35.875  1.00 70.46           C  
ATOM    609  CZ  PHE A  90      17.281   9.628  36.532  1.00 71.14           C  
ATOM    610  N   SER A  91      18.436  16.071  39.947  1.00 66.59           N  
ATOM    611  CA  SER A  91      18.218  17.394  40.521  1.00 65.20           C  
ATOM    612  C   SER A  91      16.977  18.023  39.878  1.00 64.72           C  
ATOM    613  O   SER A  91      16.882  18.089  38.655  1.00 65.68           O  
ATOM    614  CB  SER A  91      19.424  18.290  40.255  1.00 65.16           C  
ATOM    615  OG  SER A  91      20.633  17.632  40.597  1.00 65.81           O  
ATOM    616  N   VAL A  92      16.038  18.487  40.701  1.00 63.10           N  
ATOM    617  CA  VAL A  92      14.815  19.107  40.195  1.00 61.73           C  
ATOM    618  C   VAL A  92      14.605  20.487  40.803  1.00 62.08           C  
ATOM    619  O   VAL A  92      14.430  20.629  42.009  1.00 62.89           O  
ATOM    620  CB  VAL A  92      13.590  18.250  40.517  1.00 60.96           C  
ATOM    621  CG1 VAL A  92      12.339  18.906  39.973  1.00 59.83           C  
ATOM    622  CG2 VAL A  92      13.769  16.865  39.931  1.00 61.10           C  
ATOM    623  N   TYR A  93      14.610  21.501  39.954  1.00 62.89           N  
ATOM    624  CA  TYR A  93      14.442  22.872  40.419  1.00 63.72           C  
ATOM    625  C   TYR A  93      12.986  23.315  40.435  1.00 65.18           C  
ATOM    626  O   TYR A  93      12.204  22.950  39.561  1.00 64.82           O  
ATOM    627  CB  TYR A  93      15.268  23.813  39.539  1.00 62.07           C  
ATOM    628  CG  TYR A  93      16.760  23.563  39.631  1.00 61.42           C  
ATOM    629  CD1 TYR A  93      17.553  24.263  40.542  1.00 61.11           C  
ATOM    630  CD2 TYR A  93      17.369  22.577  38.854  1.00 60.94           C  
ATOM    631  CE1 TYR A  93      18.918  23.983  40.681  1.00 61.87           C  
ATOM    632  CE2 TYR A  93      18.731  22.286  38.988  1.00 62.56           C  
ATOM    633  CZ  TYR A  93      19.500  22.989  39.905  1.00 62.57           C  
ATOM    634  OH  TYR A  93      20.832  22.667  40.073  1.00 63.85           O  
ATOM    635  N   SER A  94      12.632  24.111  41.436  1.00 67.38           N  
ATOM    636  CA  SER A  94      11.273  24.616  41.579  1.00 69.29           C  
ATOM    637  C   SER A  94      11.238  26.137  41.394  1.00 70.87           C  
ATOM    638  O   SER A  94      12.277  26.802  41.444  1.00 72.24           O  
ATOM    639  CB  SER A  94      10.752  24.265  42.964  1.00 69.56           C  
ATOM    640  OG  SER A  94      11.653  24.738  43.941  1.00 69.79           O  
ATOM    641  N   ALA A  95      10.047  26.687  41.173  1.00 70.92           N  
ATOM    642  CA  ALA A  95       9.904  28.126  40.996  1.00 70.75           C  
ATOM    643  C   ALA A  95       8.450  28.530  41.116  1.00 70.89           C  
ATOM    644  O   ALA A  95       7.548  27.867  40.607  1.00 70.77           O  
ATOM    645  CB  ALA A  95      10.457  28.558  39.647  1.00 70.36           C  
ATOM    646  N   SER A  96       8.226  29.631  41.806  1.00 71.40           N  
ATOM    647  CA  SER A  96       6.880  30.114  42.003  1.00 72.00           C  
ATOM    648  C   SER A  96       6.452  30.896  40.775  1.00 71.87           C  
ATOM    649  O   SER A  96       5.270  31.169  40.573  1.00 72.82           O  
ATOM    650  CB  SER A  96       6.842  30.978  43.262  1.00 72.74           C  
ATOM    651  OG  SER A  96       7.986  31.817  43.321  1.00 74.77           O  
ATOM    652  N   THR A  97       7.426  31.223  39.941  1.00 71.45           N  
ATOM    653  CA  THR A  97       7.169  31.978  38.728  1.00 71.61           C  
ATOM    654  C   THR A  97       7.745  31.254  37.519  1.00 71.11           C  
ATOM    655  O   THR A  97       8.427  30.242  37.665  1.00 71.57           O  
ATOM    656  CB  THR A  97       7.825  33.346  38.812  1.00 72.64           C  
ATOM    657  OG1 THR A  97       7.702  34.012  37.550  1.00 74.94           O  
ATOM    658  CG2 THR A  97       9.305  33.189  39.194  1.00 72.74           C  
ATOM    659  N   HIS A  98       7.481  31.770  36.324  1.00 69.77           N  
ATOM    660  CA  HIS A  98       8.013  31.134  35.137  1.00 69.60           C  
ATOM    661  C   HIS A  98       9.525  31.317  35.004  1.00 69.47           C  
ATOM    662  O   HIS A  98      10.175  30.571  34.269  1.00 69.96           O  
ATOM    663  CB  HIS A  98       7.330  31.679  33.890  1.00 70.90           C  
ATOM    664  CG  HIS A  98       7.437  33.159  33.738  1.00 71.70           C  
ATOM    665  ND1 HIS A  98       6.647  34.035  34.454  1.00 72.22           N  
ATOM    666  CD2 HIS A  98       8.227  33.925  32.951  1.00 71.48           C  
ATOM    667  CE1 HIS A  98       6.949  35.279  34.112  1.00 72.00           C  
ATOM    668  NE2 HIS A  98       7.904  35.237  33.203  1.00 70.81           N  
ATOM    669  N   LYS A  99      10.080  32.314  35.695  1.00 68.68           N  
ATOM    670  CA  LYS A  99      11.522  32.574  35.644  1.00 67.06           C  
ATOM    671  C   LYS A  99      12.262  31.765  36.677  1.00 66.13           C  
ATOM    672  O   LYS A  99      11.953  31.832  37.863  1.00 65.38           O  
ATOM    673  CB  LYS A  99      11.848  34.053  35.884  1.00 66.80           C  
ATOM    674  CG  LYS A  99      11.820  34.902  34.632  1.00 68.59           C  
ATOM    675  CD  LYS A  99      12.736  36.118  34.730  1.00 69.73           C  
ATOM    676  CE  LYS A  99      12.191  37.202  35.655  1.00 70.79           C  
ATOM    677  NZ  LYS A  99      11.002  37.922  35.109  1.00 70.36           N  
ATOM    678  N   PHE A 100      13.242  31.007  36.206  1.00 66.52           N  
ATOM    679  CA  PHE A 100      14.046  30.191  37.092  1.00 68.34           C  
ATOM    680  C   PHE A 100      15.362  30.858  37.459  1.00 71.94           C  
ATOM    681  O   PHE A 100      16.184  31.205  36.592  1.00 71.33           O  
ATOM    682  CB  PHE A 100      14.330  28.825  36.473  1.00 65.88           C  
ATOM    683  CG  PHE A 100      13.205  27.845  36.627  1.00 63.53           C  
ATOM    684  CD1 PHE A 100      12.054  27.957  35.855  1.00 62.86           C  
ATOM    685  CD2 PHE A 100      13.302  26.794  37.533  1.00 62.19           C  
ATOM    686  CE1 PHE A 100      11.019  27.033  35.980  1.00 61.76           C  
ATOM    687  CE2 PHE A 100      12.274  25.869  37.667  1.00 60.96           C  
ATOM    688  CZ  PHE A 100      11.131  25.987  36.887  1.00 61.18           C  
ATOM    689  N   LEU A 101      15.541  31.026  38.770  1.00 76.19           N  
ATOM    690  CA  LEU A 101      16.735  31.638  39.347  1.00 79.90           C  
ATOM    691  C   LEU A 101      17.865  30.632  39.537  1.00 81.68           C  
ATOM    692  O   LEU A 101      17.855  29.847  40.491  1.00 81.84           O  
ATOM    693  CB  LEU A 101      16.415  32.271  40.716  1.00 81.59           C  
ATOM    694  CG  LEU A 101      17.632  32.794  41.516  1.00 83.87           C  
ATOM    695  CD1 LEU A 101      18.265  33.986  40.773  1.00 84.58           C  
ATOM    696  CD2 LEU A 101      17.223  33.189  42.948  1.00 82.86           C  
ATOM    697  N   TYR A 102      18.840  30.653  38.634  1.00 83.84           N  
ATOM    698  CA  TYR A 102      19.985  29.758  38.754  1.00 85.56           C  
ATOM    699  C   TYR A 102      21.016  30.397  39.704  1.00 84.76           C  
ATOM    700  O   TYR A 102      21.611  31.423  39.387  1.00 84.39           O  
ATOM    701  CB  TYR A 102      20.623  29.518  37.376  1.00 89.67           C  
ATOM    702  CG  TYR A 102      21.977  28.824  37.437  1.00 93.63           C  
ATOM    703  CD1 TYR A 102      22.085  27.489  37.831  1.00 94.75           C  
ATOM    704  CD2 TYR A 102      23.159  29.521  37.159  1.00 94.45           C  
ATOM    705  CE1 TYR A 102      23.329  26.870  37.953  1.00 94.00           C  
ATOM    706  CE2 TYR A 102      24.409  28.911  37.282  1.00 94.10           C  
ATOM    707  CZ  TYR A 102      24.485  27.584  37.682  1.00 94.13           C  
ATOM    708  OH  TYR A 102      25.709  26.969  37.838  1.00 93.29           O  
ATOM    709  N   TYR A 103      21.222  29.806  40.874  1.00 83.49           N  
ATOM    710  CA  TYR A 103      22.195  30.363  41.800  1.00 83.03           C  
ATOM    711  C   TYR A 103      23.267  29.331  42.154  1.00 81.44           C  
ATOM    712  O   TYR A 103      22.989  28.139  42.220  1.00 81.16           O  
ATOM    713  CB  TYR A 103      21.490  30.889  43.068  1.00 86.20           C  
ATOM    714  CG  TYR A 103      20.642  29.864  43.807  1.00 90.87           C  
ATOM    715  CD1 TYR A 103      19.415  29.434  43.296  1.00 92.85           C  
ATOM    716  CD2 TYR A 103      21.095  29.283  44.991  1.00 93.15           C  
ATOM    717  CE1 TYR A 103      18.657  28.433  43.951  1.00 95.27           C  
ATOM    718  CE2 TYR A 103      20.345  28.285  45.654  1.00 95.75           C  
ATOM    719  CZ  TYR A 103      19.129  27.864  45.130  1.00 96.29           C  
ATOM    720  OH  TYR A 103      18.397  26.885  45.783  1.00 96.99           O  
ATOM    721  N   ASP A 104      24.498  29.796  42.351  1.00 79.83           N  
ATOM    722  CA  ASP A 104      25.610  28.914  42.713  1.00 79.26           C  
ATOM    723  C   ASP A 104      25.686  28.831  44.232  1.00 80.07           C  
ATOM    724  O   ASP A 104      25.950  29.836  44.896  1.00 80.34           O  
ATOM    725  CB  ASP A 104      26.925  29.475  42.190  1.00 77.47           C  
ATOM    726  CG  ASP A 104      28.054  28.473  42.273  1.00 76.25           C  
ATOM    727  OD1 ASP A 104      28.232  27.829  43.328  1.00 75.67           O  
ATOM    728  OD2 ASP A 104      28.776  28.347  41.267  1.00 76.01           O  
ATOM    729  N   GLU A 105      25.472  27.636  44.776  1.00 80.09           N  
ATOM    730  CA  GLU A 105      25.490  27.447  46.224  1.00 79.03           C  
ATOM    731  C   GLU A 105      26.889  27.603  46.810  1.00 77.26           C  
ATOM    732  O   GLU A 105      27.046  27.902  47.991  1.00 77.54           O  
ATOM    733  CB  GLU A 105      24.920  26.071  46.558  1.00 81.52           C  
ATOM    734  CG  GLU A 105      23.730  25.712  45.671  1.00 86.01           C  
ATOM    735  CD  GLU A 105      22.805  24.687  46.295  1.00 88.14           C  
ATOM    736  OE1 GLU A 105      22.218  24.984  47.357  1.00 89.32           O  
ATOM    737  OE2 GLU A 105      22.653  23.590  45.717  1.00 88.43           O  
ATOM    738  N   LYS A 106      27.902  27.421  45.968  1.00 75.12           N  
ATOM    739  CA  LYS A 106      29.291  27.552  46.398  1.00 72.89           C  
ATOM    740  C   LYS A 106      29.766  29.015  46.509  1.00 72.32           C  
ATOM    741  O   LYS A 106      30.943  29.261  46.746  1.00 73.00           O  
ATOM    742  CB  LYS A 106      30.196  26.769  45.444  1.00 71.17           C  
ATOM    743  N   LYS A 107      28.855  29.974  46.340  1.00 71.78           N  
ATOM    744  CA  LYS A 107      29.190  31.397  46.442  1.00 70.47           C  
ATOM    745  C   LYS A 107      28.257  32.137  47.377  1.00 72.60           C  
ATOM    746  O   LYS A 107      28.410  33.335  47.587  1.00 73.15           O  
ATOM    747  CB  LYS A 107      29.107  32.078  45.076  1.00 67.29           C  
ATOM    748  CG  LYS A 107      30.259  31.790  44.170  1.00 62.67           C  
ATOM    749  CD  LYS A 107      30.089  32.485  42.837  1.00 60.72           C  
ATOM    750  CE  LYS A 107      31.225  32.131  41.885  1.00 60.65           C  
ATOM    751  NZ  LYS A 107      31.049  32.639  40.490  1.00 60.71           N  
ATOM    752  N   MET A 108      27.282  31.426  47.926  1.00 75.58           N  
ATOM    753  CA  MET A 108      26.308  32.048  48.818  1.00 79.14           C  
ATOM    754  C   MET A 108      26.921  32.588  50.094  1.00 80.24           C  
ATOM    755  O   MET A 108      26.318  33.390  50.811  1.00 80.47           O  
ATOM    756  CB  MET A 108      25.215  31.050  49.166  1.00 81.03           C  
ATOM    757  CG  MET A 108      24.438  30.590  47.955  1.00 84.40           C  
ATOM    758  SD  MET A 108      22.911  29.772  48.417  1.00 88.43           S  
ATOM    759  CE  MET A 108      22.109  31.123  49.441  1.00 87.66           C  
ATOM    760  N   ALA A 109      28.133  32.130  50.363  1.00 80.85           N  
ATOM    761  CA  ALA A 109      28.862  32.550  51.534  1.00 80.86           C  
ATOM    762  C   ALA A 109      29.134  34.056  51.476  1.00 81.64           C  
ATOM    763  O   ALA A 109      28.734  34.803  52.372  1.00 81.48           O  
ATOM    764  CB  ALA A 109      30.156  31.783  51.604  1.00 79.79           C  
ATOM    765  N   ASN A 110      29.806  34.488  50.413  1.00 82.77           N  
ATOM    766  CA  ASN A 110      30.159  35.896  50.230  1.00 83.21           C  
ATOM    767  C   ASN A 110      28.952  36.795  50.425  1.00 83.34           C  
ATOM    768  O   ASN A 110      28.957  37.687  51.274  1.00 84.52           O  
ATOM    769  CB  ASN A 110      30.728  36.139  48.826  1.00 83.93           C  
ATOM    770  CG  ASN A 110      31.744  35.094  48.417  1.00 84.61           C  
ATOM    771  OD1 ASN A 110      32.559  34.656  49.228  1.00 86.33           O  
ATOM    772  ND2 ASN A 110      31.704  34.691  47.150  1.00 82.88           N  
ATOM    773  N   PHE A 111      27.914  36.562  49.635  1.00 82.46           N  
ATOM    774  CA  PHE A 111      26.728  37.381  49.751  1.00 81.55           C  
ATOM    775  C   PHE A 111      25.689  36.704  50.620  1.00 82.99           C  
ATOM    776  O   PHE A 111      24.736  36.103  50.128  1.00 82.88           O  
ATOM    777  CB  PHE A 111      26.166  37.664  48.374  1.00 76.89           C  
ATOM    778  CG  PHE A 111      27.113  38.403  47.486  1.00 73.17           C  
ATOM    779  CD1 PHE A 111      28.320  37.831  47.094  1.00 71.84           C  
ATOM    780  CD2 PHE A 111      26.788  39.664  47.015  1.00 71.84           C  
ATOM    781  CE1 PHE A 111      29.185  38.503  46.236  1.00 70.91           C  
ATOM    782  CE2 PHE A 111      27.643  40.342  46.160  1.00 71.78           C  
ATOM    783  CZ  PHE A 111      28.846  39.760  45.766  1.00 70.80           C  
ATOM    784  N   GLN A 112      25.885  36.813  51.929  1.00 85.29           N  
ATOM    785  CA  GLN A 112      24.974  36.218  52.895  1.00 87.14           C  
ATOM    786  C   GLN A 112      23.642  36.960  52.838  1.00 87.57           C  
ATOM    787  O   GLN A 112      22.632  36.469  53.332  1.00 86.69           O  
ATOM    788  CB  GLN A 112      25.577  36.321  54.297  1.00 87.60           C  
ATOM    789  CG  GLN A 112      24.916  35.449  55.357  1.00 90.57           C  
ATOM    790  CD  GLN A 112      25.577  35.622  56.715  1.00 92.38           C  
ATOM    791  OE1 GLN A 112      26.801  35.521  56.835  1.00 92.98           O  
ATOM    792  NE2 GLN A 112      24.775  35.886  57.744  1.00 92.48           N  
ATOM    793  N   ASN A 113      23.657  38.145  52.228  1.00 89.50           N  
ATOM    794  CA  ASN A 113      22.459  38.968  52.096  1.00 91.49           C  
ATOM    795  C   ASN A 113      21.585  38.474  50.955  1.00 93.06           C  
ATOM    796  O   ASN A 113      20.586  39.113  50.594  1.00 92.32           O  
ATOM    797  CB  ASN A 113      22.842  40.424  51.828  1.00 91.66           C  
ATOM    798  CG  ASN A 113      22.238  41.371  52.838  1.00 93.46           C  
ATOM    799  OD1 ASN A 113      22.236  42.588  52.651  1.00 92.82           O  
ATOM    800  ND2 ASN A 113      21.730  40.813  53.933  1.00 93.84           N  
ATOM    801  N   PHE A 114      21.968  37.331  50.389  1.00 95.08           N  
ATOM    802  CA  PHE A 114      21.254  36.720  49.271  1.00 96.25           C  
ATOM    803  C   PHE A 114      20.398  35.523  49.673  1.00 96.70           C  
ATOM    804  O   PHE A 114      20.878  34.573  50.293  1.00 96.89           O  
ATOM    805  CB  PHE A 114      22.261  36.281  48.203  1.00 96.81           C  
ATOM    806  CG  PHE A 114      21.657  35.462  47.088  1.00 98.12           C  
ATOM    807  CD1 PHE A 114      20.600  35.955  46.330  1.00 98.41           C  
ATOM    808  CD2 PHE A 114      22.156  34.195  46.791  1.00 98.67           C  
ATOM    809  CE1 PHE A 114      20.046  35.201  45.286  1.00 98.34           C  
ATOM    810  CE2 PHE A 114      21.609  33.433  45.750  1.00 98.96           C  
ATOM    811  CZ  PHE A 114      20.553  33.937  44.997  1.00 98.43           C  
ATOM    812  N   LYS A 115      19.124  35.577  49.299  1.00 97.18           N  
ATOM    813  CA  LYS A 115      18.183  34.502  49.594  1.00 97.49           C  
ATOM    814  C   LYS A 115      17.607  33.965  48.275  1.00 98.13           C  
ATOM    815  O   LYS A 115      16.923  34.684  47.549  1.00 99.07           O  
ATOM    816  CB  LYS A 115      17.066  35.020  50.491  1.00 96.07           C  
ATOM    817  N   PRO A 116      17.887  32.691  47.952  1.00 99.57           N  
ATOM    818  CA  PRO A 116      17.429  32.009  46.734  1.00100.58           C  
ATOM    819  C   PRO A 116      15.922  32.054  46.488  1.00101.21           C  
ATOM    820  O   PRO A 116      15.128  31.895  47.420  1.00101.58           O  
ATOM    821  CB  PRO A 116      17.914  30.578  46.935  1.00101.45           C  
ATOM    822  CG  PRO A 116      19.146  30.757  47.734  1.00102.12           C  
ATOM    823  CD  PRO A 116      18.733  31.790  48.754  1.00101.43           C  
ATOM    824  N   ARG A 117      15.548  32.257  45.222  1.00101.94           N  
ATOM    825  CA  ARG A 117      14.145  32.309  44.797  1.00102.36           C  
ATOM    826  C   ARG A 117      13.764  31.015  44.050  1.00101.85           C  
ATOM    827  O   ARG A 117      12.737  30.962  43.358  1.00102.11           O  
ATOM    828  CB  ARG A 117      13.903  33.538  43.896  1.00102.32           C  
ATOM    829  N   SER A 118      14.606  29.986  44.206  1.00100.75           N  
ATOM    830  CA  SER A 118      14.417  28.658  43.605  1.00 99.21           C  
ATOM    831  C   SER A 118      14.995  27.572  44.532  1.00 97.84           C  
ATOM    832  O   SER A 118      16.091  27.708  45.082  1.00 98.58           O  
ATOM    833  CB  SER A 118      15.091  28.589  42.226  1.00 99.00           C  
ATOM    834  OG  SER A 118      14.436  29.441  41.298  1.00 98.32           O  
ATOM    835  N   ASN A 119      14.254  26.493  44.719  1.00 95.87           N  
ATOM    836  CA  ASN A 119      14.730  25.447  45.597  1.00 94.13           C  
ATOM    837  C   ASN A 119      15.017  24.185  44.818  1.00 92.82           C  
ATOM    838  O   ASN A 119      14.152  23.664  44.127  1.00 92.67           O  
ATOM    839  CB  ASN A 119      13.703  25.184  46.687  1.00 93.43           C  
ATOM    840  N   ARG A 120      16.247  23.706  44.923  1.00 91.52           N  
ATOM    841  CA  ARG A 120      16.645  22.483  44.242  1.00 91.16           C  
ATOM    842  C   ARG A 120      16.290  21.301  45.143  1.00 91.42           C  
ATOM    843  O   ARG A 120      16.110  21.476  46.347  1.00 92.82           O  
ATOM    844  CB  ARG A 120      18.150  22.499  43.974  1.00 91.49           C  
ATOM    845  CG  ARG A 120      18.680  21.225  43.334  1.00 92.67           C  
ATOM    846  CD  ARG A 120      20.112  21.391  42.844  1.00 93.41           C  
ATOM    847  NE  ARG A 120      21.047  21.496  43.951  1.00 94.49           N  
ATOM    848  CZ  ARG A 120      21.337  20.487  44.762  1.00 95.74           C  
ATOM    849  NH1 ARG A 120      20.764  19.307  44.571  1.00 96.14           N  
ATOM    850  NH2 ARG A 120      22.183  20.656  45.769  1.00 96.76           N  
ATOM    851  N   GLU A 121      16.181  20.103  44.568  1.00 90.37           N  
ATOM    852  CA  GLU A 121      15.862  18.904  45.349  1.00 88.57           C  
ATOM    853  C   GLU A 121      16.143  17.616  44.574  1.00 85.96           C  
ATOM    854  O   GLU A 121      15.678  17.454  43.458  1.00 85.88           O  
ATOM    855  CB  GLU A 121      14.388  18.910  45.762  1.00 90.41           C  
ATOM    856  CG  GLU A 121      14.056  17.848  46.802  1.00 94.71           C  
ATOM    857  CD  GLU A 121      12.570  17.725  47.070  1.00 96.65           C  
ATOM    858  OE1 GLU A 121      11.933  18.759  47.362  1.00 98.77           O  
ATOM    859  OE2 GLU A 121      12.038  16.596  46.994  1.00 97.13           O  
ATOM    860  N   GLU A 122      16.892  16.698  45.170  1.00 83.72           N  
ATOM    861  CA  GLU A 122      17.189  15.434  44.507  1.00 81.77           C  
ATOM    862  C   GLU A 122      16.005  14.501  44.654  1.00 79.72           C  
ATOM    863  O   GLU A 122      15.324  14.534  45.668  1.00 79.80           O  
ATOM    864  CB  GLU A 122      18.413  14.782  45.135  1.00 83.26           C  
ATOM    865  CG  GLU A 122      19.625  15.640  45.036  1.00 86.79           C  
ATOM    866  CD  GLU A 122      19.947  15.973  43.607  1.00 89.00           C  
ATOM    867  OE1 GLU A 122      20.312  15.046  42.852  1.00 90.20           O  
ATOM    868  OE2 GLU A 122      19.820  17.158  43.233  1.00 90.64           O  
ATOM    869  N   MET A 123      15.761  13.674  43.644  1.00 77.35           N  
ATOM    870  CA  MET A 123      14.649  12.731  43.701  1.00 75.20           C  
ATOM    871  C   MET A 123      14.694  11.694  42.585  1.00 74.85           C  
ATOM    872  O   MET A 123      15.404  11.864  41.595  1.00 74.36           O  
ATOM    873  CB  MET A 123      13.308  13.485  43.669  1.00 73.18           C  
ATOM    874  CG  MET A 123      13.055  14.339  42.430  1.00 70.92           C  
ATOM    875  SD  MET A 123      11.421  15.130  42.412  1.00 68.22           S  
ATOM    876  CE  MET A 123      11.700  16.497  43.461  1.00 66.01           C  
ATOM    877  N   LYS A 124      13.945  10.607  42.766  1.00 74.57           N  
ATOM    878  CA  LYS A 124      13.884   9.548  41.771  1.00 73.40           C  
ATOM    879  C   LYS A 124      12.965  10.002  40.660  1.00 72.93           C  
ATOM    880  O   LYS A 124      12.038  10.789  40.880  1.00 71.18           O  
ATOM    881  CB  LYS A 124      13.364   8.245  42.381  1.00 73.69           C  
ATOM    882  CG  LYS A 124      14.223   7.726  43.511  1.00 72.21           C  
ATOM    883  CD  LYS A 124      15.615   7.384  43.020  1.00 73.07           C  
ATOM    884  CE  LYS A 124      16.549   7.064  44.173  1.00 72.80           C  
ATOM    885  NZ  LYS A 124      17.915   6.726  43.687  1.00 73.40           N  
ATOM    886  N   PHE A 125      13.220   9.492  39.464  1.00 73.35           N  
ATOM    887  CA  PHE A 125      12.439   9.891  38.315  1.00 74.26           C  
ATOM    888  C   PHE A 125      10.964   9.699  38.558  1.00 75.29           C  
ATOM    889  O   PHE A 125      10.173  10.631  38.399  1.00 74.30           O  
ATOM    890  CB  PHE A 125      12.859   9.112  37.071  1.00 72.75           C  
ATOM    891  CG  PHE A 125      12.672   9.881  35.798  1.00 71.08           C  
ATOM    892  CD1 PHE A 125      13.729  10.576  35.230  1.00 69.87           C  
ATOM    893  CD2 PHE A 125      11.425   9.942  35.189  1.00 70.36           C  
ATOM    894  CE1 PHE A 125      13.546  11.322  34.072  1.00 68.61           C  
ATOM    895  CE2 PHE A 125      11.232  10.689  34.030  1.00 68.84           C  
ATOM    896  CZ  PHE A 125      12.292  11.378  33.472  1.00 68.41           C  
ATOM    897  N   HIS A 126      10.603   8.486  38.954  1.00 77.25           N  
ATOM    898  CA  HIS A 126       9.211   8.170  39.199  1.00 79.59           C  
ATOM    899  C   HIS A 126       8.589   9.221  40.110  1.00 79.84           C  
ATOM    900  O   HIS A 126       7.416   9.568  39.962  1.00 79.71           O  
ATOM    901  CB  HIS A 126       9.090   6.756  39.809  1.00 81.14           C  
ATOM    902  CG  HIS A 126       9.342   6.690  41.284  1.00 82.81           C  
ATOM    903  ND1 HIS A 126       8.340   6.846  42.217  1.00 82.42           N  
ATOM    904  CD2 HIS A 126      10.482   6.495  41.990  1.00 83.16           C  
ATOM    905  CE1 HIS A 126       8.850   6.753  43.434  1.00 83.34           C  
ATOM    906  NE2 HIS A 126      10.151   6.539  43.324  1.00 83.18           N  
ATOM    907  N   GLU A 127       9.390   9.762  41.023  1.00 79.86           N  
ATOM    908  CA  GLU A 127       8.891  10.763  41.953  1.00 79.92           C  
ATOM    909  C   GLU A 127       8.642  12.049  41.208  1.00 79.41           C  
ATOM    910  O   GLU A 127       7.581  12.673  41.342  1.00 78.46           O  
ATOM    911  CB  GLU A 127       9.907  10.998  43.058  1.00 80.92           C  
ATOM    912  CG  GLU A 127      10.441   9.718  43.661  1.00 83.51           C  
ATOM    913  CD  GLU A 127      11.354   9.969  44.835  1.00 85.10           C  
ATOM    914  OE1 GLU A 127      12.112   9.054  45.214  1.00 88.19           O  
ATOM    915  OE2 GLU A 127      11.297  11.083  45.401  1.00 85.59           O  
ATOM    916  N   PHE A 128       9.634  12.444  40.421  1.00 78.91           N  
ATOM    917  CA  PHE A 128       9.533  13.650  39.630  1.00 78.06           C  
ATOM    918  C   PHE A 128       8.246  13.620  38.818  1.00 78.32           C  
ATOM    919  O   PHE A 128       7.480  14.579  38.832  1.00 77.54           O  
ATOM    920  CB  PHE A 128      10.742  13.758  38.701  1.00 76.61           C  
ATOM    921  CG  PHE A 128      10.574  14.767  37.595  1.00 74.63           C  
ATOM    922  CD1 PHE A 128      10.237  16.089  37.876  1.00 73.99           C  
ATOM    923  CD2 PHE A 128      10.760  14.394  36.269  1.00 72.06           C  
ATOM    924  CE1 PHE A 128      10.088  17.027  36.846  1.00 72.23           C  
ATOM    925  CE2 PHE A 128      10.615  15.319  35.241  1.00 70.95           C  
ATOM    926  CZ  PHE A 128      10.280  16.635  35.527  1.00 70.90           C  
ATOM    927  N   VAL A 129       8.007  12.511  38.123  1.00 79.27           N  
ATOM    928  CA  VAL A 129       6.822  12.348  37.279  1.00 80.16           C  
ATOM    929  C   VAL A 129       5.538  12.507  38.088  1.00 80.58           C  
ATOM    930  O   VAL A 129       4.556  13.116  37.645  1.00 78.86           O  
ATOM    931  CB  VAL A 129       6.824  10.956  36.606  1.00 79.70           C  
ATOM    932  CG1 VAL A 129       5.679  10.851  35.619  1.00 79.16           C  
ATOM    933  CG2 VAL A 129       8.163  10.715  35.908  1.00 78.30           C  
ATOM    934  N   GLU A 130       5.553  11.942  39.284  1.00 81.90           N  
ATOM    935  CA  GLU A 130       4.408  12.014  40.158  1.00 83.83           C  
ATOM    936  C   GLU A 130       4.170  13.446  40.593  1.00 83.97           C  
ATOM    937  O   GLU A 130       3.043  13.941  40.520  1.00 83.83           O  
ATOM    938  CB  GLU A 130       4.637  11.125  41.371  1.00 85.97           C  
ATOM    939  CG  GLU A 130       4.442   9.647  41.085  1.00 90.28           C  
ATOM    940  CD  GLU A 130       5.357   8.757  41.910  1.00 93.48           C  
ATOM    941  OE1 GLU A 130       5.556   9.033  43.113  1.00 94.98           O  
ATOM    942  OE2 GLU A 130       5.873   7.762  41.356  1.00 95.52           O  
ATOM    943  N   LYS A 131       5.239  14.105  41.043  1.00 84.51           N  
ATOM    944  CA  LYS A 131       5.170  15.486  41.514  1.00 84.68           C  
ATOM    945  C   LYS A 131       4.699  16.395  40.401  1.00 85.11           C  
ATOM    946  O   LYS A 131       4.116  17.446  40.634  1.00 84.30           O  
ATOM    947  CB  LYS A 131       6.546  15.944  42.021  1.00 83.37           C  
ATOM    948  N   LEU A 132       4.956  15.967  39.178  1.00 87.38           N  
ATOM    949  CA  LEU A 132       4.574  16.738  38.015  1.00 89.56           C  
ATOM    950  C   LEU A 132       3.118  16.498  37.650  1.00 91.06           C  
ATOM    951  O   LEU A 132       2.342  17.445  37.484  1.00 91.01           O  
ATOM    952  CB  LEU A 132       5.473  16.360  36.845  1.00 90.02           C  
ATOM    953  CG  LEU A 132       5.353  17.224  35.599  1.00 89.73           C  
ATOM    954  CD1 LEU A 132       5.709  18.660  35.931  1.00 89.78           C  
ATOM    955  CD2 LEU A 132       6.286  16.678  34.541  1.00 90.08           C  
ATOM    956  N   GLN A 133       2.755  15.221  37.523  1.00 93.19           N  
ATOM    957  CA  GLN A 133       1.394  14.831  37.175  1.00 94.49           C  
ATOM    958  C   GLN A 133       0.460  15.318  38.267  1.00 95.66           C  
ATOM    959  O   GLN A 133      -0.728  15.518  38.033  1.00 95.11           O  
ATOM    960  CB  GLN A 133       1.302  13.307  37.034  1.00 94.61           C  
ATOM    961  N   ASP A 134       1.017  15.515  39.458  1.00 97.67           N  
ATOM    962  CA  ASP A 134       0.261  15.985  40.608  1.00 99.65           C  
ATOM    963  C   ASP A 134      -0.194  17.431  40.401  1.00100.72           C  
ATOM    964  O   ASP A 134      -1.385  17.744  40.497  1.00100.02           O  
ATOM    965  CB  ASP A 134       1.128  15.864  41.864  1.00100.01           C  
ATOM    966  CG  ASP A 134       0.355  16.141  43.131  1.00102.17           C  
ATOM    967  OD1 ASP A 134       0.674  15.524  44.175  1.00102.49           O  
ATOM    968  OD2 ASP A 134      -0.569  16.981  43.087  1.00103.03           O  
ATOM    969  N   ILE A 135       0.762  18.307  40.113  1.00102.69           N  
ATOM    970  CA  ILE A 135       0.480  19.714  39.867  1.00104.52           C  
ATOM    971  C   ILE A 135      -0.589  19.832  38.784  1.00105.87           C  
ATOM    972  O   ILE A 135      -1.656  20.403  39.000  1.00106.46           O  
ATOM    973  CB  ILE A 135       1.736  20.449  39.375  1.00104.24           C  
ATOM    974  CG1 ILE A 135       2.879  20.270  40.371  1.00104.09           C  
ATOM    975  CG2 ILE A 135       1.436  21.919  39.194  1.00105.14           C  
ATOM    976  CD1 ILE A 135       4.192  20.825  39.876  1.00103.37           C  
ATOM    977  N   GLN A 136      -0.286  19.284  37.615  1.00107.52           N  
ATOM    978  CA  GLN A 136      -1.208  19.328  36.491  1.00109.11           C  
ATOM    979  C   GLN A 136      -2.591  18.816  36.867  1.00109.69           C  
ATOM    980  O   GLN A 136      -3.603  19.390  36.469  1.00109.54           O  
ATOM    981  CB  GLN A 136      -0.654  18.501  35.329  1.00110.07           C  
ATOM    982  CG  GLN A 136       0.732  18.941  34.884  1.00111.25           C  
ATOM    983  CD  GLN A 136       1.223  18.197  33.657  1.00111.72           C  
ATOM    984  OE1 GLN A 136       1.369  16.976  33.671  1.00112.24           O  
ATOM    985  NE2 GLN A 136       1.484  18.938  32.583  1.00111.91           N  
ATOM    986  N   GLN A 137      -2.624  17.739  37.644  1.00110.70           N  
ATOM    987  CA  GLN A 137      -3.884  17.135  38.063  1.00111.53           C  
ATOM    988  C   GLN A 137      -4.521  17.822  39.267  1.00111.46           C  
ATOM    989  O   GLN A 137      -5.512  17.336  39.807  1.00112.11           O  
ATOM    990  CB  GLN A 137      -3.679  15.648  38.359  1.00111.53           C  
ATOM    991  N   ARG A 138      -3.964  18.949  39.692  1.00110.81           N  
ATOM    992  CA  ARG A 138      -4.548  19.658  40.821  1.00109.88           C  
ATOM    993  C   ARG A 138      -4.677  21.143  40.533  1.00109.23           C  
ATOM    994  O   ARG A 138      -4.889  21.938  41.450  1.00108.39           O  
ATOM    995  CB  ARG A 138      -3.705  19.460  42.076  1.00110.14           C  
ATOM    996  CG  ARG A 138      -2.413  20.233  42.062  1.00111.09           C  
ATOM    997  CD  ARG A 138      -1.734  20.147  43.405  1.00111.84           C  
ATOM    998  NE  ARG A 138      -0.516  20.946  43.450  1.00112.64           N  
ATOM    999  CZ  ARG A 138       0.294  21.003  44.501  1.00113.33           C  
ATOM   1000  NH1 ARG A 138       0.016  20.303  45.594  1.00113.67           N  
ATOM   1001  NH2 ARG A 138       1.384  21.758  44.463  1.00113.12           N  
ATOM   1002  N   GLY A 139      -4.547  21.514  39.260  1.00108.88           N  
ATOM   1003  CA  GLY A 139      -4.666  22.907  38.863  1.00108.31           C  
ATOM   1004  C   GLY A 139      -3.739  23.849  39.609  1.00107.78           C  
ATOM   1005  O   GLY A 139      -4.114  24.980  39.935  1.00108.46           O  
ATOM   1006  N   GLY A 140      -2.525  23.385  39.886  1.00106.59           N  
ATOM   1007  CA  GLY A 140      -1.566  24.214  40.592  1.00104.22           C  
ATOM   1008  C   GLY A 140      -1.009  25.333  39.724  1.00102.53           C  
ATOM   1009  O   GLY A 140      -1.488  25.559  38.603  1.00102.53           O  
ATOM   1010  N   GLU A 141       0.003  26.034  40.241  1.00100.03           N  
ATOM   1011  CA  GLU A 141       0.644  27.143  39.528  1.00 97.08           C  
ATOM   1012  C   GLU A 141       2.177  27.008  39.557  1.00 94.24           C  
ATOM   1013  O   GLU A 141       2.896  27.621  38.760  1.00 94.07           O  
ATOM   1014  CB  GLU A 141       0.243  28.477  40.159  1.00 97.47           C  
ATOM   1015  CG  GLU A 141       0.652  29.677  39.332  1.00 99.23           C  
ATOM   1016  CD  GLU A 141       0.834  30.920  40.172  1.00100.58           C  
ATOM   1017  OE1 GLU A 141       1.829  31.001  40.934  1.00 99.52           O  
ATOM   1018  OE2 GLU A 141      -0.024  31.822  40.073  1.00101.48           O  
ATOM   1019  N   GLU A 142       2.670  26.203  40.491  1.00 90.74           N  
ATOM   1020  CA  GLU A 142       4.096  25.969  40.613  1.00 87.22           C  
ATOM   1021  C   GLU A 142       4.669  25.378  39.320  1.00 84.61           C  
ATOM   1022  O   GLU A 142       3.949  24.764  38.524  1.00 85.08           O  
ATOM   1023  CB  GLU A 142       4.359  25.016  41.771  1.00 88.22           C  
ATOM   1024  CG  GLU A 142       5.812  24.610  41.904  1.00 89.78           C  
ATOM   1025  CD  GLU A 142       6.037  23.633  43.033  1.00 91.22           C  
ATOM   1026  OE1 GLU A 142       5.251  22.666  43.146  1.00 92.16           O  
ATOM   1027  OE2 GLU A 142       7.009  23.820  43.797  1.00 91.57           O  
ATOM   1028  N   ARG A 143       5.973  25.561  39.128  1.00 80.47           N  
ATOM   1029  CA  ARG A 143       6.677  25.059  37.954  1.00 76.05           C  
ATOM   1030  C   ARG A 143       7.918  24.272  38.372  1.00 73.14           C  
ATOM   1031  O   ARG A 143       8.492  24.524  39.424  1.00 72.79           O  
ATOM   1032  CB  ARG A 143       7.078  26.231  37.069  1.00 75.40           C  
ATOM   1033  CG  ARG A 143       5.905  27.006  36.536  1.00 75.21           C  
ATOM   1034  CD  ARG A 143       6.329  28.414  36.243  1.00 77.00           C  
ATOM   1035  NE  ARG A 143       5.342  29.144  35.460  1.00 79.61           N  
ATOM   1036  CZ  ARG A 143       5.063  28.864  34.193  1.00 80.46           C  
ATOM   1037  NH1 ARG A 143       5.701  27.868  33.586  1.00 80.63           N  
ATOM   1038  NH2 ARG A 143       4.173  29.587  33.526  1.00 80.93           N  
ATOM   1039  N   LEU A 144       8.327  23.322  37.540  1.00 70.46           N  
ATOM   1040  CA  LEU A 144       9.501  22.501  37.830  1.00 68.38           C  
ATOM   1041  C   LEU A 144      10.440  22.451  36.627  1.00 66.83           C  
ATOM   1042  O   LEU A 144      10.074  22.896  35.550  1.00 67.66           O  
ATOM   1043  CB  LEU A 144       9.066  21.085  38.186  1.00 68.06           C  
ATOM   1044  CG  LEU A 144       8.234  20.943  39.448  1.00 68.97           C  
ATOM   1045  CD1 LEU A 144       7.758  19.510  39.580  1.00 69.06           C  
ATOM   1046  CD2 LEU A 144       9.079  21.341  40.639  1.00 68.38           C  
ATOM   1047  N   TYR A 145      11.643  21.910  36.805  1.00 64.50           N  
ATOM   1048  CA  TYR A 145      12.611  21.806  35.712  1.00 62.67           C  
ATOM   1049  C   TYR A 145      13.674  20.808  36.135  1.00 61.91           C  
ATOM   1050  O   TYR A 145      14.356  21.024  37.128  1.00 61.75           O  
ATOM   1051  CB  TYR A 145      13.278  23.160  35.441  1.00 62.26           C  
ATOM   1052  CG  TYR A 145      13.687  23.385  34.000  1.00 61.59           C  
ATOM   1053  CD1 TYR A 145      14.346  22.396  33.272  1.00 61.58           C  
ATOM   1054  CD2 TYR A 145      13.403  24.592  33.363  1.00 61.84           C  
ATOM   1055  CE1 TYR A 145      14.708  22.603  31.938  1.00 62.86           C  
ATOM   1056  CE2 TYR A 145      13.761  24.813  32.039  1.00 63.10           C  
ATOM   1057  CZ  TYR A 145      14.412  23.816  31.331  1.00 63.68           C  
ATOM   1058  OH  TYR A 145      14.769  24.045  30.024  1.00 64.77           O  
ATOM   1059  N   LEU A 146      13.815  19.724  35.383  1.00 61.14           N  
ATOM   1060  CA  LEU A 146      14.799  18.711  35.727  1.00 60.37           C  
ATOM   1061  C   LEU A 146      16.068  18.923  34.942  1.00 60.19           C  
ATOM   1062  O   LEU A 146      16.053  18.966  33.716  1.00 61.59           O  
ATOM   1063  CB  LEU A 146      14.253  17.316  35.440  1.00 60.38           C  
ATOM   1064  CG  LEU A 146      15.143  16.107  35.752  1.00 61.24           C  
ATOM   1065  CD1 LEU A 146      14.251  14.927  36.051  1.00 62.38           C  
ATOM   1066  CD2 LEU A 146      16.073  15.784  34.593  1.00 60.19           C  
ATOM   1067  N   GLN A 147      17.169  19.042  35.660  1.00 58.79           N  
ATOM   1068  CA  GLN A 147      18.450  19.260  35.026  1.00 57.42           C  
ATOM   1069  C   GLN A 147      19.413  18.293  35.678  1.00 56.96           C  
ATOM   1070  O   GLN A 147      19.819  18.516  36.801  1.00 57.95           O  
ATOM   1071  CB  GLN A 147      18.890  20.699  35.281  1.00 56.71           C  
ATOM   1072  CG  GLN A 147      17.871  21.734  34.822  1.00 57.41           C  
ATOM   1073  CD  GLN A 147      18.251  23.158  35.194  1.00 58.67           C  
ATOM   1074  OE1 GLN A 147      17.551  24.112  34.839  1.00 57.16           O  
ATOM   1075  NE2 GLN A 147      19.353  23.310  35.921  1.00 58.67           N  
ATOM   1076  N   GLN A 148      19.777  17.225  34.986  1.00 56.81           N  
ATOM   1077  CA  GLN A 148      20.692  16.255  35.571  1.00 57.53           C  
ATOM   1078  C   GLN A 148      21.699  15.698  34.572  1.00 58.22           C  
ATOM   1079  O   GLN A 148      21.355  15.390  33.436  1.00 58.06           O  
ATOM   1080  CB  GLN A 148      19.886  15.116  36.214  1.00 59.14           C  
ATOM   1081  CG  GLN A 148      20.721  13.968  36.788  1.00 60.29           C  
ATOM   1082  CD  GLN A 148      21.674  14.416  37.879  1.00 61.84           C  
ATOM   1083  OE1 GLN A 148      21.274  15.083  38.837  1.00 63.08           O  
ATOM   1084  NE2 GLN A 148      22.944  14.040  37.748  1.00 62.49           N  
ATOM   1085  N   THR A 149      22.950  15.571  35.006  1.00 59.08           N  
ATOM   1086  CA  THR A 149      23.999  15.038  34.152  1.00 61.40           C  
ATOM   1087  C   THR A 149      23.744  13.562  33.852  1.00 64.52           C  
ATOM   1088  O   THR A 149      23.143  12.849  34.652  1.00 65.46           O  
ATOM   1089  CB  THR A 149      25.354  15.166  34.831  1.00 60.31           C  
ATOM   1090  OG1 THR A 149      25.499  16.499  35.328  1.00 58.42           O  
ATOM   1091  CG2 THR A 149      26.473  14.869  33.851  1.00 60.53           C  
ATOM   1092  N   LEU A 150      24.209  13.096  32.703  1.00 67.70           N  
ATOM   1093  CA  LEU A 150      24.009  11.703  32.343  1.00 71.47           C  
ATOM   1094  C   LEU A 150      25.194  10.870  32.773  1.00 75.17           C  
ATOM   1095  O   LEU A 150      26.121  10.659  31.991  1.00 75.66           O  
ATOM   1096  CB  LEU A 150      23.827  11.561  30.841  1.00 70.77           C  
ATOM   1097  CG  LEU A 150      22.626  12.272  30.241  1.00 71.35           C  
ATOM   1098  CD1 LEU A 150      22.538  11.957  28.757  1.00 70.35           C  
ATOM   1099  CD2 LEU A 150      21.374  11.814  30.965  1.00 71.84           C  
ATOM   1100  N   ASN A 151      25.153  10.385  34.011  1.00 79.24           N  
ATOM   1101  CA  ASN A 151      26.222   9.570  34.579  1.00 82.13           C  
ATOM   1102  C   ASN A 151      26.069   8.093  34.246  1.00 83.29           C  
ATOM   1103  O   ASN A 151      25.605   7.737  33.164  1.00 82.85           O  
ATOM   1104  CB  ASN A 151      26.260   9.769  36.093  1.00 83.72           C  
ATOM   1105  CG  ASN A 151      24.872   9.837  36.700  1.00 85.62           C  
ATOM   1106  OD1 ASN A 151      24.088   8.892  36.590  1.00 85.58           O  
ATOM   1107  ND2 ASN A 151      24.559  10.960  37.337  1.00 86.01           N  
ATOM   1108  N   ASP A 152      26.449   7.235  35.186  1.00 85.27           N  
ATOM   1109  CA  ASP A 152      26.385   5.796  34.971  1.00 86.79           C  
ATOM   1110  C   ASP A 152      25.146   5.166  35.581  1.00 85.81           C  
ATOM   1111  O   ASP A 152      24.780   4.050  35.233  1.00 84.83           O  
ATOM   1112  CB  ASP A 152      27.621   5.128  35.560  1.00 90.20           C  
ATOM   1113  CG  ASP A 152      28.877   5.933  35.331  1.00 94.40           C  
ATOM   1114  OD1 ASP A 152      29.185   6.253  34.156  1.00 95.74           O  
ATOM   1115  OD2 ASP A 152      29.559   6.251  36.330  1.00 96.59           O  
ATOM   1116  N   THR A 153      24.504   5.888  36.491  1.00 85.56           N  
ATOM   1117  CA  THR A 153      23.300   5.406  37.170  1.00 86.49           C  
ATOM   1118  C   THR A 153      22.120   5.322  36.190  1.00 86.10           C  
ATOM   1119  O   THR A 153      20.956   5.240  36.604  1.00 86.77           O  
ATOM   1120  CB  THR A 153      22.914   6.361  38.334  1.00 86.94           C  
ATOM   1121  OG1 THR A 153      24.109   6.890  38.924  1.00 86.88           O  
ATOM   1122  CG2 THR A 153      22.104   5.622  39.407  1.00 87.94           C  
ATOM   1123  N   VAL A 154      22.428   5.336  34.894  1.00 84.99           N  
ATOM   1124  CA  VAL A 154      21.403   5.305  33.858  1.00 82.78           C  
ATOM   1125  C   VAL A 154      21.032   3.890  33.445  1.00 81.78           C  
ATOM   1126  O   VAL A 154      21.887   3.011  33.369  1.00 81.17           O  
ATOM   1127  CB  VAL A 154      21.876   6.080  32.615  1.00 81.90           C  
ATOM   1128  CG1 VAL A 154      20.746   6.208  31.629  1.00 81.99           C  
ATOM   1129  CG2 VAL A 154      22.374   7.459  33.024  1.00 81.17           C  
ATOM   1130  N   GLY A 155      19.746   3.681  33.180  1.00 81.29           N  
ATOM   1131  CA  GLY A 155      19.267   2.375  32.780  1.00 80.89           C  
ATOM   1132  C   GLY A 155      20.010   1.812  31.585  1.00 81.09           C  
ATOM   1133  O   GLY A 155      20.650   2.543  30.836  1.00 81.58           O  
ATOM   1134  N   ARG A 156      19.903   0.501  31.405  1.00 81.40           N  
ATOM   1135  CA  ARG A 156      20.576  -0.195  30.309  1.00 80.61           C  
ATOM   1136  C   ARG A 156      20.053   0.259  28.946  1.00 78.04           C  
ATOM   1137  O   ARG A 156      20.821   0.637  28.061  1.00 76.90           O  
ATOM   1138  CB  ARG A 156      20.374  -1.718  30.451  1.00 83.56           C  
ATOM   1139  CG  ARG A 156      20.683  -2.296  31.858  1.00 87.45           C  
ATOM   1140  CD  ARG A 156      19.482  -3.066  32.475  1.00 89.29           C  
ATOM   1141  NE  ARG A 156      18.322  -2.209  32.741  1.00 89.54           N  
ATOM   1142  CZ  ARG A 156      18.245  -1.349  33.750  1.00 89.31           C  
ATOM   1143  NH1 ARG A 156      19.256  -1.246  34.596  1.00 89.31           N  
ATOM   1144  NH2 ARG A 156      17.176  -0.578  33.900  1.00 89.18           N  
ATOM   1145  N   LYS A 157      18.734   0.227  28.795  1.00 75.97           N  
ATOM   1146  CA  LYS A 157      18.091   0.588  27.541  1.00 73.80           C  
ATOM   1147  C   LYS A 157      18.420   2.001  27.100  1.00 72.08           C  
ATOM   1148  O   LYS A 157      18.565   2.275  25.903  1.00 71.88           O  
ATOM   1149  CB  LYS A 157      16.585   0.428  27.676  1.00 74.35           C  
ATOM   1150  CG  LYS A 157      15.896   0.154  26.361  1.00 76.37           C  
ATOM   1151  CD  LYS A 157      14.411  -0.082  26.596  1.00 79.65           C  
ATOM   1152  CE  LYS A 157      13.619  -0.246  25.297  1.00 81.81           C  
ATOM   1153  NZ  LYS A 157      12.136  -0.109  25.501  1.00 82.38           N  
ATOM   1154  N   ILE A 158      18.530   2.888  28.086  1.00 69.67           N  
ATOM   1155  CA  ILE A 158      18.853   4.277  27.825  1.00 65.90           C  
ATOM   1156  C   ILE A 158      20.294   4.382  27.371  1.00 65.43           C  
ATOM   1157  O   ILE A 158      20.633   5.243  26.585  1.00 65.29           O  
ATOM   1158  CB  ILE A 158      18.675   5.132  29.069  1.00 63.27           C  
ATOM   1159  CG1 ILE A 158      17.217   5.099  29.534  1.00 62.81           C  
ATOM   1160  CG2 ILE A 158      19.049   6.541  28.751  1.00 61.71           C  
ATOM   1161  CD1 ILE A 158      16.216   5.640  28.518  1.00 61.93           C  
ATOM   1162  N   VAL A 159      21.148   3.506  27.879  1.00 65.30           N  
ATOM   1163  CA  VAL A 159      22.544   3.509  27.468  1.00 65.16           C  
ATOM   1164  C   VAL A 159      22.641   3.158  25.981  1.00 65.56           C  
ATOM   1165  O   VAL A 159      23.566   3.577  25.283  1.00 65.31           O  
ATOM   1166  CB  VAL A 159      23.337   2.485  28.266  1.00 64.93           C  
ATOM   1167  CG1 VAL A 159      24.743   2.434  27.781  1.00 65.42           C  
ATOM   1168  CG2 VAL A 159      23.323   2.860  29.705  1.00 65.30           C  
ATOM   1169  N   MET A 160      21.677   2.371  25.509  1.00 66.22           N  
ATOM   1170  CA  MET A 160      21.629   1.967  24.110  1.00 66.09           C  
ATOM   1171  C   MET A 160      21.327   3.175  23.241  1.00 64.52           C  
ATOM   1172  O   MET A 160      21.888   3.336  22.156  1.00 65.07           O  
ATOM   1173  CB  MET A 160      20.553   0.899  23.904  1.00 69.29           C  
ATOM   1174  CG  MET A 160      20.959  -0.473  24.400  1.00 72.51           C  
ATOM   1175  SD  MET A 160      22.587  -0.976  23.757  1.00 78.69           S  
ATOM   1176  CE  MET A 160      22.160  -2.184  22.408  1.00 76.18           C  
ATOM   1177  N   ASP A 161      20.425   4.020  23.723  1.00 61.68           N  
ATOM   1178  CA  ASP A 161      20.061   5.220  22.994  1.00 58.81           C  
ATOM   1179  C   ASP A 161      21.280   6.158  22.953  1.00 57.16           C  
ATOM   1180  O   ASP A 161      21.638   6.702  21.906  1.00 58.05           O  
ATOM   1181  CB  ASP A 161      18.874   5.898  23.689  1.00 56.91           C  
ATOM   1182  CG  ASP A 161      17.657   4.978  23.818  1.00 56.11           C  
ATOM   1183  OD1 ASP A 161      17.557   3.996  23.056  1.00 56.12           O  
ATOM   1184  OD2 ASP A 161      16.788   5.254  24.672  1.00 54.35           O  
ATOM   1185  N   PHE A 162      21.921   6.321  24.102  1.00 55.25           N  
ATOM   1186  CA  PHE A 162      23.085   7.182  24.224  1.00 53.03           C  
ATOM   1187  C   PHE A 162      24.138   6.776  23.216  1.00 51.50           C  
ATOM   1188  O   PHE A 162      24.706   7.608  22.510  1.00 50.44           O  
ATOM   1189  CB  PHE A 162      23.673   7.072  25.629  1.00 55.10           C  
ATOM   1190  CG  PHE A 162      24.754   8.082  25.923  1.00 56.92           C  
ATOM   1191  CD1 PHE A 162      24.428   9.398  26.244  1.00 58.09           C  
ATOM   1192  CD2 PHE A 162      26.099   7.714  25.904  1.00 58.81           C  
ATOM   1193  CE1 PHE A 162      25.437  10.336  26.553  1.00 58.73           C  
ATOM   1194  CE2 PHE A 162      27.117   8.645  26.208  1.00 58.59           C  
ATOM   1195  CZ  PHE A 162      26.781   9.954  26.534  1.00 59.14           C  
ATOM   1196  N   LEU A 163      24.410   5.481  23.167  1.00 50.56           N  
ATOM   1197  CA  LEU A 163      25.406   4.978  22.244  1.00 49.91           C  
ATOM   1198  C   LEU A 163      24.949   5.225  20.815  1.00 50.42           C  
ATOM   1199  O   LEU A 163      25.764   5.225  19.882  1.00 50.58           O  
ATOM   1200  CB  LEU A 163      25.601   3.487  22.453  1.00 48.67           C  
ATOM   1201  CG  LEU A 163      26.370   3.054  23.688  1.00 47.83           C  
ATOM   1202  CD1 LEU A 163      26.472   1.534  23.696  1.00 45.81           C  
ATOM   1203  CD2 LEU A 163      27.750   3.698  23.670  1.00 46.77           C  
ATOM   1204  N   GLY A 164      23.639   5.432  20.662  1.00 50.05           N  
ATOM   1205  CA  GLY A 164      23.061   5.675  19.353  1.00 48.96           C  
ATOM   1206  C   GLY A 164      23.319   7.065  18.810  1.00 46.93           C  
ATOM   1207  O   GLY A 164      23.187   7.299  17.613  1.00 47.33           O  
ATOM   1208  N   PHE A 165      23.691   7.995  19.677  1.00 44.85           N  
ATOM   1209  CA  PHE A 165      23.953   9.352  19.219  1.00 43.22           C  
ATOM   1210  C   PHE A 165      24.993   9.376  18.104  1.00 42.90           C  
ATOM   1211  O   PHE A 165      25.803   8.463  17.973  1.00 42.15           O  
ATOM   1212  CB  PHE A 165      24.403  10.223  20.389  1.00 41.28           C  
ATOM   1213  CG  PHE A 165      23.334  10.432  21.428  1.00 39.89           C  
ATOM   1214  CD1 PHE A 165      22.054   9.886  21.263  1.00 37.93           C  
ATOM   1215  CD2 PHE A 165      23.602  11.174  22.570  1.00 37.76           C  
ATOM   1216  CE1 PHE A 165      21.060  10.080  22.232  1.00 35.93           C  
ATOM   1217  CE2 PHE A 165      22.613  11.369  23.543  1.00 35.57           C  
ATOM   1218  CZ  PHE A 165      21.342  10.817  23.367  1.00 36.08           C  
ATOM   1219  N   ASN A 166      24.958  10.427  17.295  1.00 43.08           N  
ATOM   1220  CA  ASN A 166      25.890  10.579  16.175  1.00 43.95           C  
ATOM   1221  C   ASN A 166      27.247  11.098  16.667  1.00 43.95           C  
ATOM   1222  O   ASN A 166      27.562  12.286  16.543  1.00 44.21           O  
ATOM   1223  CB  ASN A 166      25.297  11.533  15.111  1.00 45.73           C  
ATOM   1224  CG  ASN A 166      26.116  11.561  13.826  1.00 47.88           C  
ATOM   1225  OD1 ASN A 166      27.230  11.041  13.784  1.00 49.72           O  
ATOM   1226  ND2 ASN A 166      25.569  12.178  12.774  1.00 49.08           N  
ATOM   1227  N   TRP A 167      28.059  10.205  17.218  1.00 43.05           N  
ATOM   1228  CA  TRP A 167      29.361  10.607  17.737  1.00 42.20           C  
ATOM   1229  C   TRP A 167      30.366  10.809  16.611  1.00 42.87           C  
ATOM   1230  O   TRP A 167      31.387  11.477  16.767  1.00 42.09           O  
ATOM   1231  CB  TRP A 167      29.862   9.553  18.733  1.00 39.67           C  
ATOM   1232  CG  TRP A 167      28.932   9.391  19.922  1.00 38.64           C  
ATOM   1233  CD1 TRP A 167      28.010   8.393  20.133  1.00 37.72           C  
ATOM   1234  CD2 TRP A 167      28.777  10.301  20.995  1.00 37.68           C  
ATOM   1235  NE1 TRP A 167      27.291   8.645  21.270  1.00 36.75           N  
ATOM   1236  CE2 TRP A 167      27.738   9.813  21.822  1.00 38.46           C  
ATOM   1237  CE3 TRP A 167      29.411  11.500  21.341  1.00 37.66           C  
ATOM   1238  CZ2 TRP A 167      27.326  10.486  22.974  1.00 40.34           C  
ATOM   1239  CZ3 TRP A 167      29.004  12.169  22.479  1.00 40.12           C  
ATOM   1240  CH2 TRP A 167      27.969  11.658  23.287  1.00 40.56           C  
ATOM   1241  N   ASN A 168      30.063  10.242  15.458  1.00 43.82           N  
ATOM   1242  CA  ASN A 168      30.976  10.371  14.343  1.00 45.51           C  
ATOM   1243  C   ASN A 168      31.046  11.818  13.909  1.00 45.57           C  
ATOM   1244  O   ASN A 168      32.124  12.349  13.654  1.00 46.15           O  
ATOM   1245  CB  ASN A 168      30.531   9.470  13.185  1.00 46.67           C  
ATOM   1246  CG  ASN A 168      31.350   9.683  11.920  1.00 47.52           C  
ATOM   1247  OD1 ASN A 168      32.583   9.718  11.953  1.00 50.77           O  
ATOM   1248  ND2 ASN A 168      30.661   9.813  10.791  1.00 46.84           N  
ATOM   1249  N   TRP A 169      29.882  12.454  13.866  1.00 46.40           N  
ATOM   1250  CA  TRP A 169      29.756  13.838  13.421  1.00 47.15           C  
ATOM   1251  C   TRP A 169      30.250  14.835  14.455  1.00 47.00           C  
ATOM   1252  O   TRP A 169      31.084  15.705  14.167  1.00 45.91           O  
ATOM   1253  CB  TRP A 169      28.283  14.144  13.072  1.00 46.76           C  
ATOM   1254  CG  TRP A 169      28.034  15.584  12.743  1.00 47.61           C  
ATOM   1255  CD1 TRP A 169      28.284  16.227  11.554  1.00 48.50           C  
ATOM   1256  CD2 TRP A 169      27.619  16.604  13.660  1.00 46.47           C  
ATOM   1257  NE1 TRP A 169      28.061  17.584  11.685  1.00 47.50           N  
ATOM   1258  CE2 TRP A 169      27.651  17.838  12.970  1.00 47.06           C  
ATOM   1259  CE3 TRP A 169      27.229  16.591  15.009  1.00 44.50           C  
ATOM   1260  CZ2 TRP A 169      27.311  19.051  13.587  1.00 45.14           C  
ATOM   1261  CZ3 TRP A 169      26.894  17.791  15.616  1.00 44.65           C  
ATOM   1262  CH2 TRP A 169      26.939  19.005  14.909  1.00 44.92           C  
ATOM   1263  N   ILE A 170      29.732  14.691  15.666  1.00 47.18           N  
ATOM   1264  CA  ILE A 170      30.102  15.592  16.719  1.00 46.98           C  
ATOM   1265  C   ILE A 170      31.580  15.468  17.070  1.00 48.79           C  
ATOM   1266  O   ILE A 170      32.191  16.462  17.441  1.00 50.12           O  
ATOM   1267  CB  ILE A 170      29.235  15.357  17.953  1.00 45.76           C  
ATOM   1268  CG1 ILE A 170      29.319  16.577  18.866  1.00 43.76           C  
ATOM   1269  CG2 ILE A 170      29.670  14.091  18.663  1.00 43.76           C  
ATOM   1270  CD1 ILE A 170      28.130  16.758  19.780  1.00 40.92           C  
ATOM   1271  N   ASN A 171      32.161  14.273  16.940  1.00 49.51           N  
ATOM   1272  CA  ASN A 171      33.586  14.110  17.267  1.00 49.96           C  
ATOM   1273  C   ASN A 171      34.476  14.803  16.252  1.00 50.69           C  
ATOM   1274  O   ASN A 171      35.629  15.123  16.539  1.00 51.21           O  
ATOM   1275  CB  ASN A 171      33.979  12.628  17.364  1.00 49.51           C  
ATOM   1276  CG  ASN A 171      33.525  11.978  18.669  1.00 50.19           C  
ATOM   1277  OD1 ASN A 171      33.454  12.623  19.718  1.00 51.50           O  
ATOM   1278  ND2 ASN A 171      33.254  10.681  18.617  1.00 53.02           N  
ATOM   1279  N   LYS A 172      33.949  15.021  15.055  1.00 52.35           N  
ATOM   1280  CA  LYS A 172      34.722  15.697  14.030  1.00 54.36           C  
ATOM   1281  C   LYS A 172      34.629  17.199  14.244  1.00 54.86           C  
ATOM   1282  O   LYS A 172      35.547  17.929  13.890  1.00 55.19           O  
ATOM   1283  CB  LYS A 172      34.216  15.335  12.635  1.00 56.06           C  
ATOM   1284  CG  LYS A 172      34.502  13.907  12.227  1.00 58.93           C  
ATOM   1285  CD  LYS A 172      34.246  13.691  10.735  1.00 61.76           C  
ATOM   1286  CE  LYS A 172      32.773  13.866  10.364  1.00 63.63           C  
ATOM   1287  NZ  LYS A 172      32.526  13.573   8.919  1.00 64.17           N  
ATOM   1288  N   GLN A 173      33.521  17.665  14.814  1.00 55.82           N  
ATOM   1289  CA  GLN A 173      33.364  19.096  15.078  1.00 56.82           C  
ATOM   1290  C   GLN A 173      34.365  19.459  16.163  1.00 57.22           C  
ATOM   1291  O   GLN A 173      35.081  20.456  16.074  1.00 57.49           O  
ATOM   1292  CB  GLN A 173      31.949  19.418  15.572  1.00 56.65           C  
ATOM   1293  CG  GLN A 173      30.890  19.327  14.506  1.00 58.02           C  
ATOM   1294  CD  GLN A 173      31.203  20.210  13.328  1.00 59.14           C  
ATOM   1295  OE1 GLN A 173      31.351  21.423  13.473  1.00 58.30           O  
ATOM   1296  NE2 GLN A 173      31.327  19.608  12.153  1.00 60.90           N  
ATOM   1297  N   GLN A 174      34.401  18.630  17.195  1.00 57.18           N  
ATOM   1298  CA  GLN A 174      35.319  18.834  18.295  1.00 57.50           C  
ATOM   1299  C   GLN A 174      36.754  18.875  17.774  1.00 57.79           C  
ATOM   1300  O   GLN A 174      37.555  19.699  18.208  1.00 58.77           O  
ATOM   1301  CB  GLN A 174      35.162  17.695  19.293  1.00 57.64           C  
ATOM   1302  CG  GLN A 174      36.252  17.625  20.340  1.00 59.18           C  
ATOM   1303  CD  GLN A 174      36.133  16.390  21.207  1.00 60.28           C  
ATOM   1304  OE1 GLN A 174      36.195  15.260  20.716  1.00 60.49           O  
ATOM   1305  NE2 GLN A 174      35.955  16.598  22.505  1.00 61.39           N  
ATOM   1306  N   GLY A 175      37.061  17.973  16.842  1.00 57.38           N  
ATOM   1307  CA  GLY A 175      38.394  17.889  16.275  1.00 56.21           C  
ATOM   1308  C   GLY A 175      38.727  19.057  15.378  1.00 56.83           C  
ATOM   1309  O   GLY A 175      39.736  19.717  15.563  1.00 58.18           O  
ATOM   1310  N   LYS A 176      37.866  19.307  14.401  1.00 58.00           N  
ATOM   1311  CA  LYS A 176      38.072  20.412  13.469  1.00 58.76           C  
ATOM   1312  C   LYS A 176      38.203  21.765  14.160  1.00 58.94           C  
ATOM   1313  O   LYS A 176      38.983  22.613  13.744  1.00 59.77           O  
ATOM   1314  CB  LYS A 176      36.923  20.477  12.455  1.00 59.14           C  
ATOM   1315  CG  LYS A 176      37.167  19.649  11.208  1.00 61.98           C  
ATOM   1316  CD  LYS A 176      36.035  19.763  10.188  1.00 63.00           C  
ATOM   1317  CE  LYS A 176      34.746  19.135  10.689  1.00 62.18           C  
ATOM   1318  NZ  LYS A 176      33.781  18.946   9.571  1.00 62.19           N  
ATOM   1319  N   ARG A 177      37.437  21.962  15.219  1.00 58.69           N  
ATOM   1320  CA  ARG A 177      37.465  23.222  15.934  1.00 58.11           C  
ATOM   1321  C   ARG A 177      38.571  23.247  16.977  1.00 57.08           C  
ATOM   1322  O   ARG A 177      38.854  24.283  17.569  1.00 56.97           O  
ATOM   1323  CB  ARG A 177      36.113  23.446  16.596  1.00 59.76           C  
ATOM   1324  CG  ARG A 177      34.958  23.347  15.629  1.00 62.16           C  
ATOM   1325  CD  ARG A 177      34.928  24.552  14.728  1.00 65.31           C  
ATOM   1326  NE  ARG A 177      34.050  24.354  13.587  1.00 68.72           N  
ATOM   1327  CZ  ARG A 177      34.387  23.645  12.520  1.00 71.20           C  
ATOM   1328  NH1 ARG A 177      35.582  23.080  12.462  1.00 73.05           N  
ATOM   1329  NH2 ARG A 177      33.543  23.515  11.507  1.00 73.10           N  
ATOM   1330  N   GLY A 178      39.192  22.100  17.206  1.00 56.29           N  
ATOM   1331  CA  GLY A 178      40.254  22.033  18.199  1.00 54.95           C  
ATOM   1332  C   GLY A 178      39.798  22.269  19.634  1.00 54.40           C  
ATOM   1333  O   GLY A 178      40.592  22.672  20.491  1.00 54.05           O  
ATOM   1334  N   TRP A 179      38.518  22.018  19.898  1.00 54.33           N  
ATOM   1335  CA  TRP A 179      37.962  22.201  21.233  1.00 53.75           C  
ATOM   1336  C   TRP A 179      38.543  21.202  22.207  1.00 55.30           C  
ATOM   1337  O   TRP A 179      39.291  20.303  21.829  1.00 55.66           O  
ATOM   1338  CB  TRP A 179      36.449  22.019  21.222  1.00 51.76           C  
ATOM   1339  CG  TRP A 179      35.726  23.012  20.417  1.00 50.05           C  
ATOM   1340  CD1 TRP A 179      36.238  24.147  19.860  1.00 49.88           C  
ATOM   1341  CD2 TRP A 179      34.334  22.998  20.110  1.00 49.84           C  
ATOM   1342  NE1 TRP A 179      35.244  24.848  19.221  1.00 50.59           N  
ATOM   1343  CE2 TRP A 179      34.062  24.167  19.361  1.00 49.88           C  
ATOM   1344  CE3 TRP A 179      33.283  22.118  20.390  1.00 48.70           C  
ATOM   1345  CZ2 TRP A 179      32.780  24.475  18.895  1.00 50.87           C  
ATOM   1346  CZ3 TRP A 179      32.006  22.424  19.926  1.00 48.91           C  
ATOM   1347  CH2 TRP A 179      31.768  23.595  19.189  1.00 49.26           C  
ATOM   1348  N   GLY A 180      38.167  21.360  23.469  1.00 56.42           N  
ATOM   1349  CA  GLY A 180      38.652  20.474  24.505  1.00 56.95           C  
ATOM   1350  C   GLY A 180      37.783  19.253  24.560  1.00 57.85           C  
ATOM   1351  O   GLY A 180      37.114  18.922  23.588  1.00 57.69           O  
ATOM   1352  N   GLN A 181      37.778  18.601  25.714  1.00 59.60           N  
ATOM   1353  CA  GLN A 181      37.004  17.387  25.904  1.00 61.56           C  
ATOM   1354  C   GLN A 181      35.579  17.645  26.368  1.00 59.66           C  
ATOM   1355  O   GLN A 181      35.312  18.574  27.132  1.00 59.57           O  
ATOM   1356  CB  GLN A 181      37.709  16.467  26.913  1.00 65.75           C  
ATOM   1357  CG  GLN A 181      37.979  17.122  28.273  1.00 72.05           C  
ATOM   1358  CD  GLN A 181      37.768  16.165  29.447  1.00 75.85           C  
ATOM   1359  OE1 GLN A 181      38.330  15.066  29.481  1.00 77.64           O  
ATOM   1360  NE2 GLN A 181      36.963  16.588  30.419  1.00 76.62           N  
ATOM   1361  N   LEU A 182      34.665  16.810  25.894  1.00 57.55           N  
ATOM   1362  CA  LEU A 182      33.274  16.941  26.277  1.00 56.91           C  
ATOM   1363  C   LEU A 182      33.245  16.927  27.782  1.00 56.64           C  
ATOM   1364  O   LEU A 182      33.602  15.923  28.386  1.00 56.86           O  
ATOM   1365  CB  LEU A 182      32.457  15.766  25.751  1.00 56.13           C  
ATOM   1366  CG  LEU A 182      30.986  15.668  26.167  1.00 56.49           C  
ATOM   1367  CD1 LEU A 182      30.177  16.800  25.565  1.00 56.27           C  
ATOM   1368  CD2 LEU A 182      30.442  14.348  25.684  1.00 55.56           C  
ATOM   1369  N   THR A 183      32.829  18.032  28.388  1.00 56.37           N  
ATOM   1370  CA  THR A 183      32.754  18.098  29.838  1.00 56.91           C  
ATOM   1371  C   THR A 183      31.498  17.433  30.405  1.00 56.62           C  
ATOM   1372  O   THR A 183      31.562  16.802  31.446  1.00 58.84           O  
ATOM   1373  CB  THR A 183      32.796  19.538  30.346  1.00 57.43           C  
ATOM   1374  OG1 THR A 183      31.471  20.086  30.326  1.00 58.13           O  
ATOM   1375  CG2 THR A 183      33.718  20.368  29.473  1.00 57.42           C  
ATOM   1376  N   SER A 184      30.348  17.565  29.757  1.00 55.23           N  
ATOM   1377  CA  SER A 184      29.160  16.918  30.301  1.00 53.00           C  
ATOM   1378  C   SER A 184      27.985  17.002  29.354  1.00 52.57           C  
ATOM   1379  O   SER A 184      28.042  17.698  28.344  1.00 53.12           O  
ATOM   1380  CB  SER A 184      28.760  17.562  31.625  1.00 52.13           C  
ATOM   1381  OG  SER A 184      28.178  18.830  31.397  1.00 50.33           O  
ATOM   1382  N   ASN A 185      26.920  16.285  29.693  1.00 52.31           N  
ATOM   1383  CA  ASN A 185      25.694  16.245  28.912  1.00 51.11           C  
ATOM   1384  C   ASN A 185      24.556  16.356  29.902  1.00 50.98           C  
ATOM   1385  O   ASN A 185      24.410  15.500  30.767  1.00 52.59           O  
ATOM   1386  CB  ASN A 185      25.536  14.907  28.190  1.00 52.65           C  
ATOM   1387  CG  ASN A 185      26.594  14.674  27.141  1.00 54.11           C  
ATOM   1388  OD1 ASN A 185      27.723  14.284  27.445  1.00 56.73           O  
ATOM   1389  ND2 ASN A 185      26.228  14.895  25.883  1.00 54.90           N  
ATOM   1390  N   LEU A 186      23.744  17.392  29.787  1.00 50.85           N  
ATOM   1391  CA  LEU A 186      22.631  17.532  30.716  1.00 50.53           C  
ATOM   1392  C   LEU A 186      21.300  17.183  30.089  1.00 50.62           C  
ATOM   1393  O   LEU A 186      21.027  17.549  28.943  1.00 51.34           O  
ATOM   1394  CB  LEU A 186      22.535  18.955  31.243  1.00 50.13           C  
ATOM   1395  CG  LEU A 186      23.287  19.296  32.512  1.00 50.81           C  
ATOM   1396  CD1 LEU A 186      24.782  19.061  32.330  1.00 51.48           C  
ATOM   1397  CD2 LEU A 186      22.970  20.746  32.853  1.00 51.32           C  
ATOM   1398  N   LEU A 187      20.477  16.476  30.849  1.00 49.13           N  
ATOM   1399  CA  LEU A 187      19.149  16.115  30.394  1.00 47.33           C  
ATOM   1400  C   LEU A 187      18.231  17.213  30.932  1.00 46.60           C  
ATOM   1401  O   LEU A 187      18.132  17.413  32.139  1.00 45.13           O  
ATOM   1402  CB  LEU A 187      18.746  14.759  30.969  1.00 46.75           C  
ATOM   1403  CG  LEU A 187      17.265  14.404  30.820  1.00 47.20           C  
ATOM   1404  CD1 LEU A 187      16.889  14.295  29.347  1.00 46.07           C  
ATOM   1405  CD2 LEU A 187      16.998  13.102  31.547  1.00 46.88           C  
ATOM   1406  N   LEU A 188      17.567  17.936  30.044  1.00 45.70           N  
ATOM   1407  CA  LEU A 188      16.705  19.007  30.495  1.00 45.19           C  
ATOM   1408  C   LEU A 188      15.266  18.741  30.133  1.00 45.53           C  
ATOM   1409  O   LEU A 188      14.921  18.678  28.959  1.00 45.48           O  
ATOM   1410  CB  LEU A 188      17.145  20.326  29.877  1.00 45.54           C  
ATOM   1411  CG  LEU A 188      18.633  20.629  29.993  1.00 44.96           C  
ATOM   1412  CD1 LEU A 188      18.988  21.805  29.112  1.00 44.49           C  
ATOM   1413  CD2 LEU A 188      18.970  20.920  31.437  1.00 46.42           C  
ATOM   1414  N   ILE A 189      14.433  18.582  31.151  1.00 45.51           N  
ATOM   1415  CA  ILE A 189      13.012  18.347  30.951  1.00 46.65           C  
ATOM   1416  C   ILE A 189      12.296  19.464  31.673  1.00 48.20           C  
ATOM   1417  O   ILE A 189      12.401  19.561  32.894  1.00 47.85           O  
ATOM   1418  CB  ILE A 189      12.577  17.032  31.573  1.00 45.34           C  
ATOM   1419  CG1 ILE A 189      13.445  15.914  31.018  1.00 45.44           C  
ATOM   1420  CG2 ILE A 189      11.115  16.772  31.277  1.00 44.16           C  
ATOM   1421  CD1 ILE A 189      13.194  14.615  31.650  1.00 44.59           C  
ATOM   1422  N   GLY A 190      11.582  20.310  30.931  1.00 50.14           N  
ATOM   1423  CA  GLY A 190      10.878  21.418  31.555  1.00 51.18           C  
ATOM   1424  C   GLY A 190       9.409  21.541  31.177  1.00 52.30           C  
ATOM   1425  O   GLY A 190       8.979  20.992  30.167  1.00 53.06           O  
ATOM   1426  N   MET A 191       8.643  22.266  31.992  1.00 53.27           N  
ATOM   1427  CA  MET A 191       7.209  22.478  31.766  1.00 54.65           C  
ATOM   1428  C   MET A 191       6.980  23.658  30.813  1.00 55.58           C  
ATOM   1429  O   MET A 191       7.815  24.553  30.714  1.00 56.13           O  
ATOM   1430  CB  MET A 191       6.501  22.774  33.098  1.00 55.39           C  
ATOM   1431  CG  MET A 191       6.501  21.624  34.115  1.00 56.62           C  
ATOM   1432  SD  MET A 191       5.762  22.034  35.737  1.00 60.44           S  
ATOM   1433  CE  MET A 191       4.194  22.871  35.267  1.00 57.74           C  
ATOM   1434  N   GLU A 192       5.857  23.665  30.108  1.00 56.23           N  
ATOM   1435  CA  GLU A 192       5.582  24.774  29.198  1.00 57.94           C  
ATOM   1436  C   GLU A 192       5.600  26.086  29.970  1.00 57.40           C  
ATOM   1437  O   GLU A 192       5.250  26.115  31.148  1.00 58.00           O  
ATOM   1438  CB  GLU A 192       4.214  24.597  28.558  1.00 61.06           C  
ATOM   1439  CG  GLU A 192       3.160  24.092  29.534  1.00 64.26           C  
ATOM   1440  CD  GLU A 192       1.814  23.892  28.871  1.00 67.12           C  
ATOM   1441  OE1 GLU A 192       1.788  23.505  27.680  1.00 67.36           O  
ATOM   1442  OE2 GLU A 192       0.781  24.098  29.541  1.00 67.19           O  
ATOM   1443  N   GLY A 193       6.005  27.167  29.310  1.00 56.26           N  
ATOM   1444  CA  GLY A 193       6.035  28.461  29.970  1.00 55.39           C  
ATOM   1445  C   GLY A 193       7.273  28.734  30.804  1.00 55.37           C  
ATOM   1446  O   GLY A 193       7.537  29.871  31.179  1.00 55.16           O  
ATOM   1447  N   ASN A 194       8.020  27.678  31.106  1.00 55.32           N  
ATOM   1448  CA  ASN A 194       9.257  27.781  31.873  1.00 54.24           C  
ATOM   1449  C   ASN A 194      10.261  28.670  31.167  1.00 54.16           C  
ATOM   1450  O   ASN A 194      10.401  28.598  29.940  1.00 55.48           O  
ATOM   1451  CB  ASN A 194       9.890  26.412  32.035  1.00 54.17           C  
ATOM   1452  CG  ASN A 194       9.368  25.693  33.227  1.00 55.86           C  
ATOM   1453  OD1 ASN A 194       8.365  26.097  33.818  1.00 56.27           O  
ATOM   1454  ND2 ASN A 194      10.041  24.620  33.606  1.00 55.52           N  
ATOM   1455  N   VAL A 195      10.990  29.477  31.938  1.00 52.61           N  
ATOM   1456  CA  VAL A 195      11.986  30.381  31.365  1.00 49.52           C  
ATOM   1457  C   VAL A 195      13.340  30.320  32.095  1.00 47.22           C  
ATOM   1458  O   VAL A 195      13.400  30.201  33.318  1.00 46.55           O  
ATOM   1459  CB  VAL A 195      11.455  31.848  31.364  1.00 49.28           C  
ATOM   1460  CG1 VAL A 195      12.476  32.782  30.761  1.00 47.37           C  
ATOM   1461  CG2 VAL A 195      10.180  31.934  30.549  1.00 47.73           C  
ATOM   1462  N   THR A 196      14.418  30.382  31.316  1.00 45.30           N  
ATOM   1463  CA  THR A 196      15.795  30.383  31.825  1.00 43.72           C  
ATOM   1464  C   THR A 196      16.363  31.758  31.441  1.00 43.35           C  
ATOM   1465  O   THR A 196      16.767  31.963  30.292  1.00 42.91           O  
ATOM   1466  CB  THR A 196      16.665  29.264  31.168  1.00 43.14           C  
ATOM   1467  OG1 THR A 196      16.310  27.997  31.723  1.00 44.24           O  
ATOM   1468  CG2 THR A 196      18.133  29.496  31.425  1.00 40.01           C  
ATOM   1469  N   PRO A 197      16.390  32.721  32.393  1.00 42.70           N  
ATOM   1470  CA  PRO A 197      16.887  34.092  32.217  1.00 42.01           C  
ATOM   1471  C   PRO A 197      18.216  34.181  31.471  1.00 41.44           C  
ATOM   1472  O   PRO A 197      19.015  33.249  31.504  1.00 42.22           O  
ATOM   1473  CB  PRO A 197      16.982  34.607  33.645  1.00 41.61           C  
ATOM   1474  CG  PRO A 197      15.807  33.958  34.290  1.00 41.35           C  
ATOM   1475  CD  PRO A 197      15.960  32.525  33.795  1.00 41.95           C  
ATOM   1476  N   ALA A 198      18.448  35.304  30.800  1.00 39.95           N  
ATOM   1477  CA  ALA A 198      19.671  35.505  30.036  1.00 38.37           C  
ATOM   1478  C   ALA A 198      20.961  35.310  30.845  1.00 38.32           C  
ATOM   1479  O   ALA A 198      21.069  35.738  32.006  1.00 37.38           O  
ATOM   1480  CB  ALA A 198      19.662  36.875  29.427  1.00 37.05           C  
ATOM   1481  N   HIS A 199      21.940  34.672  30.206  1.00 37.61           N  
ATOM   1482  CA  HIS A 199      23.234  34.396  30.826  1.00 37.73           C  
ATOM   1483  C   HIS A 199      24.176  33.823  29.774  1.00 38.52           C  
ATOM   1484  O   HIS A 199      23.792  33.624  28.628  1.00 39.95           O  
ATOM   1485  CB  HIS A 199      23.077  33.339  31.905  1.00 37.39           C  
ATOM   1486  CG  HIS A 199      22.818  31.971  31.369  1.00 37.89           C  
ATOM   1487  ND1 HIS A 199      21.559  31.540  30.988  1.00 37.68           N  
ATOM   1488  CD2 HIS A 199      23.647  30.918  31.156  1.00 38.59           C  
ATOM   1489  CE1 HIS A 199      21.630  30.281  30.570  1.00 38.61           C  
ATOM   1490  NE2 HIS A 199      22.884  29.882  30.666  1.00 38.73           N  
ATOM   1491  N   TYR A 200      25.409  33.539  30.151  1.00 37.97           N  
ATOM   1492  CA  TYR A 200      26.305  32.993  29.162  1.00 37.39           C  
ATOM   1493  C   TYR A 200      27.108  31.925  29.845  1.00 37.78           C  
ATOM   1494  O   TYR A 200      27.185  31.898  31.070  1.00 36.12           O  
ATOM   1495  CB  TYR A 200      27.203  34.097  28.610  1.00 37.78           C  
ATOM   1496  CG  TYR A 200      28.146  34.702  29.623  1.00 38.82           C  
ATOM   1497  CD1 TYR A 200      29.391  34.129  29.864  1.00 37.73           C  
ATOM   1498  CD2 TYR A 200      27.807  35.862  30.335  1.00 38.05           C  
ATOM   1499  CE1 TYR A 200      30.296  34.697  30.785  1.00 38.62           C  
ATOM   1500  CE2 TYR A 200      28.705  36.438  31.266  1.00 36.61           C  
ATOM   1501  CZ  TYR A 200      29.951  35.850  31.478  1.00 37.42           C  
ATOM   1502  OH  TYR A 200      30.880  36.412  32.339  1.00 38.09           O  
ATOM   1503  N   ASP A 201      27.690  31.028  29.059  1.00 39.41           N  
ATOM   1504  CA  ASP A 201      28.492  29.941  29.607  1.00 42.01           C  
ATOM   1505  C   ASP A 201      29.899  30.000  29.017  1.00 44.28           C  
ATOM   1506  O   ASP A 201      30.101  30.458  27.889  1.00 46.02           O  
ATOM   1507  CB  ASP A 201      27.853  28.573  29.301  1.00 41.71           C  
ATOM   1508  CG  ASP A 201      26.462  28.396  29.929  1.00 41.84           C  
ATOM   1509  OD1 ASP A 201      26.318  28.540  31.169  1.00 42.38           O  
ATOM   1510  OD2 ASP A 201      25.508  28.096  29.176  1.00 43.13           O  
ATOM   1511  N   GLU A 202      30.874  29.530  29.781  1.00 46.09           N  
ATOM   1512  CA  GLU A 202      32.260  29.556  29.340  1.00 47.30           C  
ATOM   1513  C   GLU A 202      32.661  28.338  28.474  1.00 46.99           C  
ATOM   1514  O   GLU A 202      33.842  28.092  28.234  1.00 49.27           O  
ATOM   1515  CB  GLU A 202      33.162  29.690  30.585  1.00 48.65           C  
ATOM   1516  CG  GLU A 202      33.096  31.069  31.283  1.00 52.22           C  
ATOM   1517  CD  GLU A 202      33.917  31.129  32.567  1.00 55.57           C  
ATOM   1518  OE1 GLU A 202      33.395  30.743  33.641  1.00 57.29           O  
ATOM   1519  OE2 GLU A 202      35.098  31.547  32.506  1.00 57.76           O  
ATOM   1520  N   GLN A 203      31.678  27.600  27.978  1.00 44.99           N  
ATOM   1521  CA  GLN A 203      31.998  26.439  27.169  1.00 42.88           C  
ATOM   1522  C   GLN A 203      31.221  26.447  25.878  1.00 41.07           C  
ATOM   1523  O   GLN A 203      30.231  27.164  25.763  1.00 41.42           O  
ATOM   1524  CB  GLN A 203      31.677  25.184  27.953  1.00 45.43           C  
ATOM   1525  CG  GLN A 203      32.339  25.179  29.300  1.00 52.47           C  
ATOM   1526  CD  GLN A 203      32.658  23.791  29.778  1.00 57.52           C  
ATOM   1527  OE1 GLN A 203      31.787  22.924  29.813  1.00 60.56           O  
ATOM   1528  NE2 GLN A 203      33.914  23.562  30.150  1.00 59.82           N  
ATOM   1529  N   GLN A 204      31.678  25.669  24.899  1.00 38.96           N  
ATOM   1530  CA  GLN A 204      30.981  25.592  23.622  1.00 36.85           C  
ATOM   1531  C   GLN A 204      29.784  24.669  23.849  1.00 36.27           C  
ATOM   1532  O   GLN A 204      29.897  23.691  24.578  1.00 37.86           O  
ATOM   1533  CB  GLN A 204      31.915  25.020  22.560  1.00 35.32           C  
ATOM   1534  CG  GLN A 204      33.176  25.834  22.371  1.00 33.95           C  
ATOM   1535  CD  GLN A 204      32.960  27.168  21.659  1.00 35.13           C  
ATOM   1536  OE1 GLN A 204      31.835  27.578  21.377  1.00 34.94           O  
ATOM   1537  NE2 GLN A 204      34.058  27.845  21.352  1.00 34.93           N  
ATOM   1538  N   ASN A 205      28.639  24.972  23.246  1.00 36.30           N  
ATOM   1539  CA  ASN A 205      27.446  24.157  23.471  1.00 36.17           C  
ATOM   1540  C   ASN A 205      26.670  23.764  22.213  1.00 36.88           C  
ATOM   1541  O   ASN A 205      26.527  24.554  21.273  1.00 37.82           O  
ATOM   1542  CB  ASN A 205      26.531  24.895  24.472  1.00 35.11           C  
ATOM   1543  CG  ASN A 205      25.194  24.190  24.721  1.00 35.62           C  
ATOM   1544  OD1 ASN A 205      25.027  22.998  24.451  1.00 38.31           O  
ATOM   1545  ND2 ASN A 205      24.237  24.927  25.283  1.00 35.21           N  
ATOM   1546  N   PHE A 206      26.208  22.517  22.205  1.00 37.27           N  
ATOM   1547  CA  PHE A 206      25.388  21.963  21.135  1.00 36.50           C  
ATOM   1548  C   PHE A 206      24.070  21.580  21.805  1.00 36.48           C  
ATOM   1549  O   PHE A 206      23.995  20.581  22.505  1.00 36.58           O  
ATOM   1550  CB  PHE A 206      26.050  20.724  20.535  1.00 37.02           C  
ATOM   1551  CG  PHE A 206      26.969  21.030  19.386  1.00 37.79           C  
ATOM   1552  CD1 PHE A 206      26.497  21.743  18.290  1.00 37.15           C  
ATOM   1553  CD2 PHE A 206      28.305  20.633  19.405  1.00 38.37           C  
ATOM   1554  CE1 PHE A 206      27.336  22.069  17.219  1.00 37.24           C  
ATOM   1555  CE2 PHE A 206      29.170  20.954  18.326  1.00 36.51           C  
ATOM   1556  CZ  PHE A 206      28.678  21.673  17.236  1.00 36.39           C  
ATOM   1557  N   PHE A 207      23.052  22.404  21.594  1.00 36.45           N  
ATOM   1558  CA  PHE A 207      21.720  22.253  22.185  1.00 36.46           C  
ATOM   1559  C   PHE A 207      20.903  21.313  21.298  1.00 37.51           C  
ATOM   1560  O   PHE A 207      20.460  21.721  20.229  1.00 39.08           O  
ATOM   1561  CB  PHE A 207      21.081  23.643  22.216  1.00 36.59           C  
ATOM   1562  CG  PHE A 207      19.954  23.808  23.201  1.00 35.31           C  
ATOM   1563  CD1 PHE A 207      18.621  23.825  22.777  1.00 35.17           C  
ATOM   1564  CD2 PHE A 207      20.228  24.055  24.538  1.00 35.85           C  
ATOM   1565  CE1 PHE A 207      17.575  24.098  23.677  1.00 37.60           C  
ATOM   1566  CE2 PHE A 207      19.199  24.333  25.452  1.00 35.93           C  
ATOM   1567  CZ  PHE A 207      17.870  24.357  25.023  1.00 38.17           C  
ATOM   1568  N   ALA A 208      20.688  20.072  21.735  1.00 37.42           N  
ATOM   1569  CA  ALA A 208      19.936  19.090  20.948  1.00 36.90           C  
ATOM   1570  C   ALA A 208      18.491  18.950  21.402  1.00 37.30           C  
ATOM   1571  O   ALA A 208      18.232  18.310  22.426  1.00 37.45           O  
ATOM   1572  CB  ALA A 208      20.632  17.756  21.027  1.00 35.20           C  
ATOM   1573  N   GLN A 209      17.559  19.538  20.639  1.00 37.94           N  
ATOM   1574  CA  GLN A 209      16.142  19.493  21.006  1.00 38.52           C  
ATOM   1575  C   GLN A 209      15.560  18.108  20.731  1.00 40.79           C  
ATOM   1576  O   GLN A 209      15.836  17.501  19.684  1.00 40.38           O  
ATOM   1577  CB  GLN A 209      15.350  20.570  20.256  1.00 36.17           C  
ATOM   1578  CG  GLN A 209      13.895  20.813  20.771  1.00 33.49           C  
ATOM   1579  CD  GLN A 209      13.809  21.156  22.271  1.00 33.28           C  
ATOM   1580  OE1 GLN A 209      14.824  21.344  22.944  1.00 32.97           O  
ATOM   1581  NE2 GLN A 209      12.583  21.245  22.789  1.00 31.12           N  
ATOM   1582  N   ILE A 210      14.762  17.609  21.680  1.00 41.97           N  
ATOM   1583  CA  ILE A 210      14.165  16.280  21.593  1.00 43.05           C  
ATOM   1584  C   ILE A 210      12.635  16.262  21.605  1.00 45.49           C  
ATOM   1585  O   ILE A 210      12.018  15.678  20.717  1.00 46.60           O  
ATOM   1586  CB  ILE A 210      14.692  15.373  22.754  1.00 41.75           C  
ATOM   1587  CG1 ILE A 210      16.141  15.003  22.482  1.00 39.38           C  
ATOM   1588  CG2 ILE A 210      13.849  14.087  22.907  1.00 40.09           C  
ATOM   1589  CD1 ILE A 210      16.792  14.369  23.659  1.00 39.06           C  
ATOM   1590  N   LYS A 211      12.019  16.876  22.605  1.00 45.94           N  
ATOM   1591  CA  LYS A 211      10.570  16.865  22.680  1.00 45.71           C  
ATOM   1592  C   LYS A 211      10.099  18.257  22.997  1.00 47.24           C  
ATOM   1593  O   LYS A 211      10.645  18.894  23.881  1.00 49.25           O  
ATOM   1594  CB  LYS A 211      10.108  15.937  23.790  1.00 45.98           C  
ATOM   1595  CG  LYS A 211       8.609  15.933  23.955  1.00 46.94           C  
ATOM   1596  CD  LYS A 211       8.182  15.049  25.104  1.00 49.58           C  
ATOM   1597  CE  LYS A 211       6.671  14.966  25.178  1.00 51.07           C  
ATOM   1598  NZ  LYS A 211       6.116  14.403  23.918  1.00 53.57           N  
ATOM   1599  N   GLY A 212       9.078  18.731  22.295  1.00 47.67           N  
ATOM   1600  CA  GLY A 212       8.588  20.075  22.553  1.00 47.13           C  
ATOM   1601  C   GLY A 212       9.360  21.136  21.787  1.00 46.99           C  
ATOM   1602  O   GLY A 212      10.266  20.813  21.012  1.00 46.36           O  
ATOM   1603  N   TYR A 213       8.990  22.402  21.972  1.00 47.51           N  
ATOM   1604  CA  TYR A 213       9.676  23.508  21.289  1.00 47.37           C  
ATOM   1605  C   TYR A 213      10.200  24.552  22.282  1.00 45.52           C  
ATOM   1606  O   TYR A 213       9.531  24.888  23.269  1.00 43.64           O  
ATOM   1607  CB  TYR A 213       8.753  24.205  20.261  1.00 49.23           C  
ATOM   1608  CG  TYR A 213       8.327  23.324  19.089  1.00 50.98           C  
ATOM   1609  CD1 TYR A 213       7.291  22.396  19.223  1.00 51.01           C  
ATOM   1610  CD2 TYR A 213       9.005  23.376  17.870  1.00 51.99           C  
ATOM   1611  CE1 TYR A 213       6.944  21.538  18.178  1.00 50.95           C  
ATOM   1612  CE2 TYR A 213       8.663  22.512  16.810  1.00 52.25           C  
ATOM   1613  CZ  TYR A 213       7.632  21.598  16.976  1.00 53.39           C  
ATOM   1614  OH  TYR A 213       7.298  20.743  15.945  1.00 55.31           O  
ATOM   1615  N   LYS A 214      11.407  25.047  22.005  1.00 44.64           N  
ATOM   1616  CA  LYS A 214      12.073  26.060  22.823  1.00 43.16           C  
ATOM   1617  C   LYS A 214      12.518  27.273  22.000  1.00 43.25           C  
ATOM   1618  O   LYS A 214      13.156  27.142  20.945  1.00 41.96           O  
ATOM   1619  CB  LYS A 214      13.297  25.470  23.521  1.00 41.23           C  
ATOM   1620  CG  LYS A 214      13.012  24.794  24.840  1.00 39.70           C  
ATOM   1621  CD  LYS A 214      14.309  24.298  25.398  1.00 38.06           C  
ATOM   1622  CE  LYS A 214      14.149  23.866  26.812  1.00 37.89           C  
ATOM   1623  NZ  LYS A 214      15.421  23.255  27.234  1.00 41.16           N  
ATOM   1624  N   ARG A 215      12.159  28.459  22.481  1.00 43.78           N  
ATOM   1625  CA  ARG A 215      12.534  29.692  21.810  1.00 43.71           C  
ATOM   1626  C   ARG A 215      13.815  30.128  22.469  1.00 43.21           C  
ATOM   1627  O   ARG A 215      13.871  30.245  23.701  1.00 44.71           O  
ATOM   1628  CB  ARG A 215      11.495  30.766  22.043  1.00 44.36           C  
ATOM   1629  CG  ARG A 215      11.829  32.082  21.391  1.00 44.24           C  
ATOM   1630  CD  ARG A 215      11.137  33.179  22.160  1.00 44.88           C  
ATOM   1631  NE  ARG A 215      11.038  34.398  21.382  1.00 46.15           N  
ATOM   1632  CZ  ARG A 215      10.407  35.492  21.796  1.00 46.80           C  
ATOM   1633  NH1 ARG A 215       9.815  35.527  22.989  1.00 44.74           N  
ATOM   1634  NH2 ARG A 215      10.356  36.552  21.007  1.00 47.99           N  
ATOM   1635  N   CYS A 216      14.838  30.369  21.655  1.00 41.78           N  
ATOM   1636  CA  CYS A 216      16.135  30.782  22.157  1.00 39.87           C  
ATOM   1637  C   CYS A 216      16.543  32.121  21.602  1.00 39.01           C  
ATOM   1638  O   CYS A 216      16.646  32.287  20.389  1.00 39.77           O  
ATOM   1639  CB  CYS A 216      17.200  29.790  21.741  1.00 40.90           C  
ATOM   1640  SG  CYS A 216      16.733  28.094  22.058  1.00 44.19           S  
ATOM   1641  N   ILE A 217      16.808  33.063  22.495  1.00 39.63           N  
ATOM   1642  CA  ILE A 217      17.251  34.389  22.090  1.00 39.31           C  
ATOM   1643  C   ILE A 217      18.698  34.594  22.559  1.00 38.64           C  
ATOM   1644  O   ILE A 217      18.950  34.587  23.762  1.00 40.62           O  
ATOM   1645  CB  ILE A 217      16.384  35.468  22.727  1.00 37.40           C  
ATOM   1646  CG1 ILE A 217      14.907  35.156  22.491  1.00 36.14           C  
ATOM   1647  CG2 ILE A 217      16.705  36.794  22.107  1.00 37.16           C  
ATOM   1648  CD1 ILE A 217      13.963  36.058  23.226  1.00 34.60           C  
ATOM   1649  N   LEU A 218      19.622  34.780  21.614  1.00 38.10           N  
ATOM   1650  CA  LEU A 218      21.060  34.962  21.886  1.00 37.44           C  
ATOM   1651  C   LEU A 218      21.582  36.385  21.634  1.00 38.70           C  
ATOM   1652  O   LEU A 218      21.041  37.122  20.804  1.00 38.83           O  
ATOM   1653  CB  LEU A 218      21.894  34.009  21.019  1.00 35.79           C  
ATOM   1654  CG  LEU A 218      21.995  32.519  21.361  1.00 33.84           C  
ATOM   1655  CD1 LEU A 218      20.608  31.911  21.544  1.00 31.77           C  
ATOM   1656  CD2 LEU A 218      22.770  31.807  20.253  1.00 30.12           C  
ATOM   1657  N   PHE A 219      22.657  36.748  22.334  1.00 38.99           N  
ATOM   1658  CA  PHE A 219      23.275  38.061  22.196  1.00 38.12           C  
ATOM   1659  C   PHE A 219      24.777  37.859  22.145  1.00 37.56           C  
ATOM   1660  O   PHE A 219      25.332  37.065  22.906  1.00 37.67           O  
ATOM   1661  CB  PHE A 219      22.912  38.945  23.376  1.00 38.62           C  
ATOM   1662  CG  PHE A 219      21.431  39.118  23.572  1.00 39.45           C  
ATOM   1663  CD1 PHE A 219      20.724  38.292  24.443  1.00 40.05           C  
ATOM   1664  CD2 PHE A 219      20.754  40.142  22.917  1.00 40.06           C  
ATOM   1665  CE1 PHE A 219      19.357  38.489  24.672  1.00 39.47           C  
ATOM   1666  CE2 PHE A 219      19.394  40.351  23.135  1.00 39.76           C  
ATOM   1667  CZ  PHE A 219      18.694  39.523  24.017  1.00 41.28           C  
ATOM   1668  N   PRO A 220      25.446  38.554  21.245  1.00 37.10           N  
ATOM   1669  CA  PRO A 220      26.896  38.439  21.097  1.00 38.30           C  
ATOM   1670  C   PRO A 220      27.613  38.905  22.338  1.00 39.16           C  
ATOM   1671  O   PRO A 220      27.097  39.714  23.102  1.00 37.79           O  
ATOM   1672  CB  PRO A 220      27.199  39.306  19.903  1.00 37.03           C  
ATOM   1673  CG  PRO A 220      25.933  39.236  19.116  1.00 38.57           C  
ATOM   1674  CD  PRO A 220      24.882  39.379  20.163  1.00 39.35           C  
ATOM   1675  N   PRO A 221      28.835  38.408  22.550  1.00 40.81           N  
ATOM   1676  CA  PRO A 221      29.633  38.795  23.713  1.00 43.62           C  
ATOM   1677  C   PRO A 221      29.846  40.311  23.868  1.00 45.26           C  
ATOM   1678  O   PRO A 221      29.906  40.831  24.996  1.00 44.86           O  
ATOM   1679  CB  PRO A 221      30.936  38.027  23.483  1.00 41.96           C  
ATOM   1680  CG  PRO A 221      30.435  36.761  22.827  1.00 39.86           C  
ATOM   1681  CD  PRO A 221      29.468  37.303  21.812  1.00 40.25           C  
ATOM   1682  N   ASP A 222      29.940  41.019  22.742  1.00 46.06           N  
ATOM   1683  CA  ASP A 222      30.159  42.456  22.788  1.00 47.33           C  
ATOM   1684  C   ASP A 222      28.969  43.254  23.342  1.00 48.10           C  
ATOM   1685  O   ASP A 222      29.073  44.467  23.537  1.00 50.25           O  
ATOM   1686  CB  ASP A 222      30.571  42.987  21.404  1.00 47.65           C  
ATOM   1687  CG  ASP A 222      29.487  42.832  20.352  1.00 49.40           C  
ATOM   1688  OD1 ASP A 222      28.301  42.727  20.723  1.00 50.74           O  
ATOM   1689  OD2 ASP A 222      29.819  42.848  19.141  1.00 48.05           O  
ATOM   1690  N   GLN A 223      27.855  42.583  23.615  1.00 47.31           N  
ATOM   1691  CA  GLN A 223      26.671  43.257  24.157  1.00 46.52           C  
ATOM   1692  C   GLN A 223      26.810  43.337  25.674  1.00 44.82           C  
ATOM   1693  O   GLN A 223      25.851  43.628  26.393  1.00 44.23           O  
ATOM   1694  CB  GLN A 223      25.413  42.463  23.802  1.00 47.90           C  
ATOM   1695  CG  GLN A 223      25.174  42.314  22.309  1.00 53.96           C  
ATOM   1696  CD  GLN A 223      24.467  43.508  21.705  1.00 56.93           C  
ATOM   1697  OE1 GLN A 223      23.277  43.727  21.945  1.00 58.55           O  
ATOM   1698  NE2 GLN A 223      25.198  44.298  20.930  1.00 58.61           N  
ATOM   1699  N   PHE A 224      28.020  43.091  26.156  1.00 43.16           N  
ATOM   1700  CA  PHE A 224      28.289  43.096  27.583  1.00 42.05           C  
ATOM   1701  C   PHE A 224      27.706  44.300  28.318  1.00 42.02           C  
ATOM   1702  O   PHE A 224      27.063  44.153  29.372  1.00 39.64           O  
ATOM   1703  CB  PHE A 224      29.795  43.004  27.810  1.00 41.40           C  
ATOM   1704  CG  PHE A 224      30.177  42.784  29.250  1.00 41.83           C  
ATOM   1705  CD1 PHE A 224      30.242  43.853  30.137  1.00 41.40           C  
ATOM   1706  CD2 PHE A 224      30.440  41.505  29.729  1.00 42.08           C  
ATOM   1707  CE1 PHE A 224      30.561  43.650  31.478  1.00 39.78           C  
ATOM   1708  CE2 PHE A 224      30.760  41.293  31.072  1.00 40.79           C  
ATOM   1709  CZ  PHE A 224      30.819  42.372  31.946  1.00 39.97           C  
ATOM   1710  N   GLU A 225      27.930  45.488  27.750  1.00 43.22           N  
ATOM   1711  CA  GLU A 225      27.479  46.740  28.340  1.00 42.89           C  
ATOM   1712  C   GLU A 225      25.970  46.859  28.423  1.00 41.28           C  
ATOM   1713  O   GLU A 225      25.457  47.659  29.188  1.00 42.14           O  
ATOM   1714  CB  GLU A 225      28.029  47.955  27.558  1.00 45.33           C  
ATOM   1715  CG  GLU A 225      29.571  48.078  27.483  1.00 51.65           C  
ATOM   1716  CD  GLU A 225      30.075  49.529  27.290  1.00 55.39           C  
ATOM   1717  OE1 GLU A 225      30.309  50.238  28.296  1.00 55.91           O  
ATOM   1718  OE2 GLU A 225      30.249  49.969  26.131  1.00 57.83           O  
ATOM   1719  N   CYS A 226      25.258  46.064  27.636  1.00 41.89           N  
ATOM   1720  CA  CYS A 226      23.799  46.122  27.637  1.00 41.76           C  
ATOM   1721  C   CYS A 226      23.102  45.134  28.553  1.00 42.24           C  
ATOM   1722  O   CYS A 226      21.921  45.311  28.856  1.00 42.10           O  
ATOM   1723  CB  CYS A 226      23.253  45.879  26.237  1.00 40.74           C  
ATOM   1724  SG  CYS A 226      23.979  46.945  25.009  1.00 42.41           S  
ATOM   1725  N   LEU A 227      23.812  44.094  28.985  1.00 42.72           N  
ATOM   1726  CA  LEU A 227      23.182  43.080  29.813  1.00 41.94           C  
ATOM   1727  C   LEU A 227      23.545  43.046  31.292  1.00 40.42           C  
ATOM   1728  O   LEU A 227      23.032  42.219  32.040  1.00 40.86           O  
ATOM   1729  CB  LEU A 227      23.404  41.722  29.168  1.00 43.67           C  
ATOM   1730  CG  LEU A 227      22.788  41.727  27.766  1.00 44.08           C  
ATOM   1731  CD1 LEU A 227      23.387  40.621  26.919  1.00 44.02           C  
ATOM   1732  CD2 LEU A 227      21.268  41.609  27.883  1.00 43.55           C  
ATOM   1733  N   TYR A 228      24.434  43.937  31.696  1.00 39.40           N  
ATOM   1734  CA  TYR A 228      24.821  44.068  33.100  1.00 38.58           C  
ATOM   1735  C   TYR A 228      24.835  42.789  33.938  1.00 37.55           C  
ATOM   1736  O   TYR A 228      23.997  42.612  34.826  1.00 36.83           O  
ATOM   1737  CB  TYR A 228      23.888  45.074  33.779  1.00 36.79           C  
ATOM   1738  CG  TYR A 228      23.786  46.392  33.053  1.00 37.90           C  
ATOM   1739  CD1 TYR A 228      24.649  47.455  33.350  1.00 38.10           C  
ATOM   1740  CD2 TYR A 228      22.822  46.582  32.067  1.00 37.66           C  
ATOM   1741  CE1 TYR A 228      24.539  48.673  32.687  1.00 38.83           C  
ATOM   1742  CE2 TYR A 228      22.715  47.792  31.395  1.00 39.01           C  
ATOM   1743  CZ  TYR A 228      23.569  48.830  31.714  1.00 39.61           C  
ATOM   1744  OH  TYR A 228      23.436  50.033  31.071  1.00 41.39           O  
ATOM   1745  N   PRO A 229      25.793  41.889  33.685  1.00 37.00           N  
ATOM   1746  CA  PRO A 229      25.854  40.651  34.471  1.00 39.15           C  
ATOM   1747  C   PRO A 229      26.205  40.906  35.946  1.00 39.51           C  
ATOM   1748  O   PRO A 229      26.848  41.902  36.273  1.00 40.66           O  
ATOM   1749  CB  PRO A 229      26.952  39.863  33.765  1.00 36.78           C  
ATOM   1750  CG  PRO A 229      27.855  40.939  33.208  1.00 34.83           C  
ATOM   1751  CD  PRO A 229      26.837  41.910  32.647  1.00 35.70           C  
ATOM   1752  N   TYR A 230      25.785  40.017  36.838  1.00 38.32           N  
ATOM   1753  CA  TYR A 230      26.123  40.163  38.253  1.00 39.18           C  
ATOM   1754  C   TYR A 230      27.646  40.151  38.493  1.00 39.03           C  
ATOM   1755  O   TYR A 230      28.419  39.766  37.617  1.00 38.62           O  
ATOM   1756  CB  TYR A 230      25.547  39.007  39.044  1.00 37.86           C  
ATOM   1757  CG  TYR A 230      24.072  39.082  39.287  1.00 37.94           C  
ATOM   1758  CD1 TYR A 230      23.162  38.722  38.299  1.00 38.47           C  
ATOM   1759  CD2 TYR A 230      23.587  39.492  40.519  1.00 38.41           C  
ATOM   1760  CE1 TYR A 230      21.797  38.766  38.545  1.00 38.14           C  
ATOM   1761  CE2 TYR A 230      22.243  39.539  40.772  1.00 37.92           C  
ATOM   1762  CZ  TYR A 230      21.348  39.175  39.791  1.00 39.44           C  
ATOM   1763  OH  TYR A 230      20.004  39.207  40.079  1.00 42.82           O  
ATOM   1764  N   PRO A 231      28.094  40.553  39.703  1.00 37.86           N  
ATOM   1765  CA  PRO A 231      29.531  40.541  39.975  1.00 39.90           C  
ATOM   1766  C   PRO A 231      30.025  39.099  39.957  1.00 40.39           C  
ATOM   1767  O   PRO A 231      29.279  38.178  40.321  1.00 39.19           O  
ATOM   1768  CB  PRO A 231      29.616  41.150  41.373  1.00 38.71           C  
ATOM   1769  CG  PRO A 231      28.470  42.095  41.378  1.00 37.70           C  
ATOM   1770  CD  PRO A 231      27.383  41.223  40.804  1.00 38.03           C  
ATOM   1771  N   VAL A 232      31.273  38.905  39.537  1.00 41.03           N  
ATOM   1772  CA  VAL A 232      31.856  37.573  39.470  1.00 40.70           C  
ATOM   1773  C   VAL A 232      31.718  36.753  40.754  1.00 42.51           C  
ATOM   1774  O   VAL A 232      31.417  35.572  40.681  1.00 43.71           O  
ATOM   1775  CB  VAL A 232      33.339  37.644  39.091  1.00 39.56           C  
ATOM   1776  CG1 VAL A 232      33.992  36.306  39.292  1.00 38.06           C  
ATOM   1777  CG2 VAL A 232      33.477  38.031  37.642  1.00 37.44           C  
ATOM   1778  N   HIS A 233      31.932  37.355  41.922  1.00 43.88           N  
ATOM   1779  CA  HIS A 233      31.806  36.606  43.182  1.00 43.84           C  
ATOM   1780  C   HIS A 233      30.373  36.407  43.669  1.00 43.87           C  
ATOM   1781  O   HIS A 233      30.139  35.760  44.694  1.00 44.25           O  
ATOM   1782  CB  HIS A 233      32.612  37.284  44.287  1.00 43.56           C  
ATOM   1783  CG  HIS A 233      34.081  37.264  44.055  1.00 45.73           C  
ATOM   1784  ND1 HIS A 233      34.753  38.304  43.447  1.00 46.36           N  
ATOM   1785  CD2 HIS A 233      35.013  36.326  44.338  1.00 46.49           C  
ATOM   1786  CE1 HIS A 233      36.045  38.009  43.369  1.00 47.89           C  
ATOM   1787  NE2 HIS A 233      36.228  36.811  43.906  1.00 49.26           N  
ATOM   1788  N   HIS A 234      29.414  36.956  42.941  1.00 44.54           N  
ATOM   1789  CA  HIS A 234      28.019  36.819  43.324  1.00 45.62           C  
ATOM   1790  C   HIS A 234      27.463  35.465  42.876  1.00 46.57           C  
ATOM   1791  O   HIS A 234      27.823  34.956  41.815  1.00 47.05           O  
ATOM   1792  CB  HIS A 234      27.196  37.961  42.717  1.00 46.35           C  
ATOM   1793  CG  HIS A 234      25.782  38.009  43.206  1.00 47.87           C  
ATOM   1794  ND1 HIS A 234      24.854  37.034  42.907  1.00 48.72           N  
ATOM   1795  CD2 HIS A 234      25.149  38.894  44.018  1.00 48.81           C  
ATOM   1796  CE1 HIS A 234      23.715  37.308  43.512  1.00 48.64           C  
ATOM   1797  NE2 HIS A 234      23.864  38.429  44.193  1.00 48.24           N  
ATOM   1798  N   PRO A 235      26.590  34.850  43.693  1.00 46.75           N  
ATOM   1799  CA  PRO A 235      25.964  33.558  43.402  1.00 46.93           C  
ATOM   1800  C   PRO A 235      25.361  33.477  41.990  1.00 47.46           C  
ATOM   1801  O   PRO A 235      25.286  32.404  41.398  1.00 47.85           O  
ATOM   1802  CB  PRO A 235      24.890  33.451  44.479  1.00 46.13           C  
ATOM   1803  CG  PRO A 235      25.552  34.089  45.647  1.00 47.51           C  
ATOM   1804  CD  PRO A 235      26.206  35.316  45.040  1.00 48.26           C  
ATOM   1805  N   CYS A 236      24.936  34.618  41.456  1.00 47.05           N  
ATOM   1806  CA  CYS A 236      24.336  34.630  40.131  1.00 45.72           C  
ATOM   1807  C   CYS A 236      25.297  35.078  39.050  1.00 47.00           C  
ATOM   1808  O   CYS A 236      24.874  35.535  37.981  1.00 47.78           O  
ATOM   1809  CB  CYS A 236      23.105  35.521  40.125  1.00 45.18           C  
ATOM   1810  SG  CYS A 236      21.829  34.844  41.181  1.00 45.08           S  
ATOM   1811  N   ASP A 237      26.588  34.942  39.333  1.00 47.53           N  
ATOM   1812  CA  ASP A 237      27.624  35.318  38.378  1.00 47.99           C  
ATOM   1813  C   ASP A 237      27.280  34.753  36.993  1.00 48.49           C  
ATOM   1814  O   ASP A 237      26.751  33.645  36.884  1.00 49.86           O  
ATOM   1815  CB  ASP A 237      28.981  34.784  38.871  1.00 49.27           C  
ATOM   1816  CG  ASP A 237      30.052  34.747  37.776  1.00 51.69           C  
ATOM   1817  OD1 ASP A 237      30.230  35.756  37.054  1.00 52.76           O  
ATOM   1818  OD2 ASP A 237      30.736  33.704  37.634  1.00 52.28           O  
ATOM   1819  N   ARG A 238      27.557  35.532  35.948  1.00 46.63           N  
ATOM   1820  CA  ARG A 238      27.300  35.130  34.563  1.00 45.15           C  
ATOM   1821  C   ARG A 238      25.862  35.336  34.095  1.00 45.21           C  
ATOM   1822  O   ARG A 238      25.528  35.064  32.934  1.00 43.58           O  
ATOM   1823  CB  ARG A 238      27.735  33.678  34.331  1.00 43.96           C  
ATOM   1824  CG  ARG A 238      29.235  33.526  34.174  1.00 44.92           C  
ATOM   1825  CD  ARG A 238      29.568  32.300  33.382  1.00 47.43           C  
ATOM   1826  NE  ARG A 238      29.178  31.081  34.078  1.00 54.00           N  
ATOM   1827  CZ  ARG A 238      27.941  30.569  34.106  1.00 57.77           C  
ATOM   1828  NH1 ARG A 238      26.907  31.151  33.476  1.00 60.82           N  
ATOM   1829  NH2 ARG A 238      27.737  29.440  34.773  1.00 56.91           N  
ATOM   1830  N   GLN A 239      25.033  35.858  34.993  1.00 45.49           N  
ATOM   1831  CA  GLN A 239      23.640  36.128  34.677  1.00 46.71           C  
ATOM   1832  C   GLN A 239      23.337  37.617  34.595  1.00 45.77           C  
ATOM   1833  O   GLN A 239      23.960  38.433  35.281  1.00 45.74           O  
ATOM   1834  CB  GLN A 239      22.754  35.497  35.730  1.00 50.03           C  
ATOM   1835  CG  GLN A 239      22.796  34.000  35.648  1.00 59.12           C  
ATOM   1836  CD  GLN A 239      22.211  33.331  36.863  1.00 64.37           C  
ATOM   1837  OE1 GLN A 239      21.067  33.590  37.249  1.00 66.33           O  
ATOM   1838  NE2 GLN A 239      22.997  32.452  37.479  1.00 68.32           N  
ATOM   1839  N   SER A 240      22.370  37.969  33.755  1.00 43.97           N  
ATOM   1840  CA  SER A 240      22.001  39.361  33.583  1.00 41.43           C  
ATOM   1841  C   SER A 240      21.125  39.843  34.715  1.00 41.09           C  
ATOM   1842  O   SER A 240      20.215  39.158  35.158  1.00 41.00           O  
ATOM   1843  CB  SER A 240      21.258  39.559  32.275  1.00 39.39           C  
ATOM   1844  OG  SER A 240      20.798  40.888  32.179  1.00 40.00           O  
ATOM   1845  N   GLN A 241      21.396  41.049  35.171  1.00 41.53           N  
ATOM   1846  CA  GLN A 241      20.623  41.606  36.260  1.00 42.89           C  
ATOM   1847  C   GLN A 241      19.331  42.213  35.752  1.00 43.54           C  
ATOM   1848  O   GLN A 241      18.393  42.425  36.518  1.00 44.41           O  
ATOM   1849  CB  GLN A 241      21.431  42.674  36.963  1.00 42.54           C  
ATOM   1850  CG  GLN A 241      22.812  42.241  37.371  1.00 42.96           C  
ATOM   1851  CD  GLN A 241      23.570  43.371  38.014  1.00 42.97           C  
ATOM   1852  OE1 GLN A 241      23.285  43.749  39.151  1.00 41.76           O  
ATOM   1853  NE2 GLN A 241      24.522  43.941  37.285  1.00 43.04           N  
ATOM   1854  N   VAL A 242      19.301  42.494  34.458  1.00 44.16           N  
ATOM   1855  CA  VAL A 242      18.145  43.112  33.834  1.00 46.72           C  
ATOM   1856  C   VAL A 242      16.941  42.186  33.744  1.00 47.96           C  
ATOM   1857  O   VAL A 242      17.046  41.122  33.161  1.00 50.66           O  
ATOM   1858  CB  VAL A 242      18.490  43.556  32.413  1.00 46.72           C  
ATOM   1859  CG1 VAL A 242      17.311  44.283  31.799  1.00 46.60           C  
ATOM   1860  CG2 VAL A 242      19.730  44.431  32.435  1.00 47.19           C  
ATOM   1861  N   ASP A 243      15.810  42.601  34.317  1.00 49.27           N  
ATOM   1862  CA  ASP A 243      14.572  41.808  34.267  1.00 49.19           C  
ATOM   1863  C   ASP A 243      13.930  42.047  32.904  1.00 49.74           C  
ATOM   1864  O   ASP A 243      13.412  43.134  32.654  1.00 49.85           O  
ATOM   1865  CB  ASP A 243      13.592  42.266  35.346  1.00 49.24           C  
ATOM   1866  CG  ASP A 243      12.313  41.431  35.385  1.00 49.95           C  
ATOM   1867  OD1 ASP A 243      11.732  41.133  34.313  1.00 49.85           O  
ATOM   1868  OD2 ASP A 243      11.875  41.089  36.504  1.00 49.00           O  
ATOM   1869  N   PHE A 244      13.946  41.041  32.034  1.00 50.07           N  
ATOM   1870  CA  PHE A 244      13.380  41.167  30.693  1.00 49.85           C  
ATOM   1871  C   PHE A 244      11.897  41.460  30.634  1.00 51.91           C  
ATOM   1872  O   PHE A 244      11.407  42.033  29.653  1.00 51.04           O  
ATOM   1873  CB  PHE A 244      13.646  39.904  29.906  1.00 47.41           C  
ATOM   1874  CG  PHE A 244      15.010  39.852  29.312  1.00 46.07           C  
ATOM   1875  CD1 PHE A 244      16.121  40.238  30.054  1.00 45.28           C  
ATOM   1876  CD2 PHE A 244      15.187  39.396  28.016  1.00 45.18           C  
ATOM   1877  CE1 PHE A 244      17.406  40.165  29.508  1.00 44.78           C  
ATOM   1878  CE2 PHE A 244      16.452  39.317  27.459  1.00 45.13           C  
ATOM   1879  CZ  PHE A 244      17.569  39.703  28.211  1.00 45.68           C  
ATOM   1880  N   ASP A 245      11.181  41.053  31.678  1.00 53.65           N  
ATOM   1881  CA  ASP A 245       9.751  41.280  31.738  1.00 56.20           C  
ATOM   1882  C   ASP A 245       9.413  42.696  32.185  1.00 57.25           C  
ATOM   1883  O   ASP A 245       8.354  43.211  31.848  1.00 58.39           O  
ATOM   1884  CB  ASP A 245       9.090  40.286  32.677  1.00 59.00           C  
ATOM   1885  CG  ASP A 245       9.130  38.873  32.146  1.00 61.88           C  
ATOM   1886  OD1 ASP A 245       8.965  38.686  30.919  1.00 62.81           O  
ATOM   1887  OD2 ASP A 245       9.310  37.945  32.966  1.00 64.16           O  
ATOM   1888  N   ASN A 246      10.314  43.309  32.953  1.00 58.85           N  
ATOM   1889  CA  ASN A 246      10.147  44.688  33.442  1.00 58.66           C  
ATOM   1890  C   ASN A 246      11.518  45.371  33.586  1.00 55.72           C  
ATOM   1891  O   ASN A 246      12.043  45.557  34.685  1.00 56.14           O  
ATOM   1892  CB  ASN A 246       9.382  44.692  34.773  1.00 62.37           C  
ATOM   1893  CG  ASN A 246       9.052  46.097  35.257  1.00 67.47           C  
ATOM   1894  OD1 ASN A 246       8.696  46.976  34.464  1.00 69.53           O  
ATOM   1895  ND2 ASN A 246       9.161  46.314  36.564  1.00 69.21           N  
ATOM   1896  N   PRO A 247      12.118  45.754  32.448  1.00 53.03           N  
ATOM   1897  CA  PRO A 247      13.425  46.406  32.421  1.00 52.14           C  
ATOM   1898  C   PRO A 247      13.488  47.756  33.128  1.00 52.24           C  
ATOM   1899  O   PRO A 247      12.656  48.634  32.896  1.00 51.81           O  
ATOM   1900  CB  PRO A 247      13.717  46.507  30.926  1.00 51.22           C  
ATOM   1901  CG  PRO A 247      12.374  46.671  30.345  1.00 51.22           C  
ATOM   1902  CD  PRO A 247      11.565  45.647  31.087  1.00 51.27           C  
ATOM   1903  N   ASP A 248      14.492  47.908  33.988  1.00 51.86           N  
ATOM   1904  CA  ASP A 248      14.718  49.138  34.742  1.00 51.84           C  
ATOM   1905  C   ASP A 248      15.730  49.995  33.987  1.00 51.51           C  
ATOM   1906  O   ASP A 248      16.924  49.960  34.291  1.00 51.18           O  
ATOM   1907  CB  ASP A 248      15.281  48.803  36.114  1.00 54.18           C  
ATOM   1908  CG  ASP A 248      15.404  50.018  37.002  1.00 56.05           C  
ATOM   1909  OD1 ASP A 248      15.456  51.145  36.465  1.00 58.59           O  
ATOM   1910  OD2 ASP A 248      15.452  49.843  38.239  1.00 56.40           O  
ATOM   1911  N   TYR A 249      15.260  50.776  33.020  1.00 51.67           N  
ATOM   1912  CA  TYR A 249      16.174  51.586  32.218  1.00 52.49           C  
ATOM   1913  C   TYR A 249      16.925  52.637  33.009  1.00 53.30           C  
ATOM   1914  O   TYR A 249      17.759  53.359  32.466  1.00 52.42           O  
ATOM   1915  CB  TYR A 249      15.427  52.255  31.062  1.00 51.84           C  
ATOM   1916  CG  TYR A 249      14.725  51.278  30.146  1.00 53.11           C  
ATOM   1917  CD1 TYR A 249      15.407  50.199  29.578  1.00 52.77           C  
ATOM   1918  CD2 TYR A 249      13.373  51.429  29.851  1.00 53.44           C  
ATOM   1919  CE1 TYR A 249      14.754  49.299  28.739  1.00 53.46           C  
ATOM   1920  CE2 TYR A 249      12.712  50.540  29.017  1.00 53.87           C  
ATOM   1921  CZ  TYR A 249      13.404  49.483  28.464  1.00 53.48           C  
ATOM   1922  OH  TYR A 249      12.731  48.635  27.621  1.00 54.44           O  
ATOM   1923  N   GLU A 250      16.633  52.707  34.299  1.00 55.32           N  
ATOM   1924  CA  GLU A 250      17.285  53.663  35.175  1.00 57.20           C  
ATOM   1925  C   GLU A 250      18.648  53.098  35.533  1.00 55.41           C  
ATOM   1926  O   GLU A 250      19.671  53.744  35.343  1.00 56.35           O  
ATOM   1927  CB  GLU A 250      16.477  53.855  36.456  1.00 63.36           C  
ATOM   1928  CG  GLU A 250      16.368  55.289  36.901  1.00 70.99           C  
ATOM   1929  CD  GLU A 250      15.451  56.084  36.006  1.00 76.61           C  
ATOM   1930  OE1 GLU A 250      14.237  55.773  35.986  1.00 79.29           O  
ATOM   1931  OE2 GLU A 250      15.934  57.016  35.323  1.00 79.04           O  
ATOM   1932  N   ARG A 251      18.654  51.877  36.048  1.00 52.41           N  
ATOM   1933  CA  ARG A 251      19.898  51.254  36.444  1.00 50.73           C  
ATOM   1934  C   ARG A 251      20.667  50.712  35.265  1.00 49.67           C  
ATOM   1935  O   ARG A 251      21.903  50.800  35.208  1.00 49.25           O  
ATOM   1936  CB  ARG A 251      19.608  50.103  37.378  1.00 51.61           C  
ATOM   1937  CG  ARG A 251      18.562  50.402  38.407  1.00 56.27           C  
ATOM   1938  CD  ARG A 251      18.384  49.198  39.291  1.00 59.07           C  
ATOM   1939  NE  ARG A 251      19.666  48.801  39.855  1.00 61.46           N  
ATOM   1940  CZ  ARG A 251      19.919  47.594  40.347  1.00 62.37           C  
ATOM   1941  NH1 ARG A 251      18.966  46.668  40.349  1.00 61.29           N  
ATOM   1942  NH2 ARG A 251      21.128  47.297  40.806  1.00 62.56           N  
ATOM   1943  N   PHE A 252      19.915  50.134  34.333  1.00 48.30           N  
ATOM   1944  CA  PHE A 252      20.469  49.494  33.150  1.00 45.96           C  
ATOM   1945  C   PHE A 252      20.104  50.235  31.856  1.00 45.63           C  
ATOM   1946  O   PHE A 252      19.426  49.700  30.976  1.00 47.19           O  
ATOM   1947  CB  PHE A 252      19.945  48.065  33.090  1.00 44.02           C  
ATOM   1948  CG  PHE A 252      19.945  47.366  34.424  1.00 41.85           C  
ATOM   1949  CD1 PHE A 252      21.141  47.027  35.064  1.00 40.64           C  
ATOM   1950  CD2 PHE A 252      18.741  47.036  35.038  1.00 40.27           C  
ATOM   1951  CE1 PHE A 252      21.131  46.363  36.293  1.00 39.09           C  
ATOM   1952  CE2 PHE A 252      18.720  46.378  36.262  1.00 39.37           C  
ATOM   1953  CZ  PHE A 252      19.914  46.038  36.891  1.00 38.94           C  
ATOM   1954  N   PRO A 253      20.601  51.462  31.717  1.00 45.01           N  
ATOM   1955  CA  PRO A 253      20.326  52.282  30.535  1.00 43.26           C  
ATOM   1956  C   PRO A 253      20.598  51.678  29.162  1.00 42.39           C  
ATOM   1957  O   PRO A 253      19.850  51.916  28.218  1.00 41.57           O  
ATOM   1958  CB  PRO A 253      21.178  53.516  30.772  1.00 41.95           C  
ATOM   1959  CG  PRO A 253      22.309  53.000  31.621  1.00 41.99           C  
ATOM   1960  CD  PRO A 253      21.610  52.095  32.581  1.00 43.32           C  
ATOM   1961  N   ASN A 254      21.676  50.913  29.052  1.00 42.94           N  
ATOM   1962  CA  ASN A 254      22.035  50.330  27.771  1.00 42.89           C  
ATOM   1963  C   ASN A 254      21.252  49.125  27.343  1.00 42.26           C  
ATOM   1964  O   ASN A 254      21.576  48.519  26.322  1.00 42.39           O  
ATOM   1965  CB  ASN A 254      23.510  49.992  27.734  1.00 43.38           C  
ATOM   1966  CG  ASN A 254      24.354  51.191  27.460  1.00 45.12           C  
ATOM   1967  OD1 ASN A 254      25.003  51.723  28.351  1.00 45.23           O  
ATOM   1968  ND2 ASN A 254      24.336  51.645  26.213  1.00 46.11           N  
ATOM   1969  N   PHE A 255      20.241  48.747  28.109  1.00 41.36           N  
ATOM   1970  CA  PHE A 255      19.453  47.604  27.693  1.00 41.69           C  
ATOM   1971  C   PHE A 255      18.523  48.062  26.567  1.00 42.55           C  
ATOM   1972  O   PHE A 255      17.833  47.267  25.950  1.00 44.28           O  
ATOM   1973  CB  PHE A 255      18.609  47.087  28.840  1.00 40.67           C  
ATOM   1974  CG  PHE A 255      17.866  45.819  28.513  1.00 40.35           C  
ATOM   1975  CD1 PHE A 255      18.559  44.639  28.248  1.00 39.77           C  
ATOM   1976  CD2 PHE A 255      16.470  45.802  28.468  1.00 40.60           C  
ATOM   1977  CE1 PHE A 255      17.875  43.455  27.946  1.00 39.14           C  
ATOM   1978  CE2 PHE A 255      15.773  44.617  28.164  1.00 41.46           C  
ATOM   1979  CZ  PHE A 255      16.483  43.442  27.904  1.00 39.09           C  
ATOM   1980  N   GLN A 256      18.511  49.358  26.312  1.00 43.38           N  
ATOM   1981  CA  GLN A 256      17.659  49.888  25.267  1.00 42.36           C  
ATOM   1982  C   GLN A 256      18.405  49.862  23.967  1.00 41.93           C  
ATOM   1983  O   GLN A 256      17.892  50.336  22.959  1.00 44.25           O  
ATOM   1984  CB  GLN A 256      17.257  51.318  25.576  1.00 45.07           C  
ATOM   1985  CG  GLN A 256      16.952  51.527  27.025  1.00 48.63           C  
ATOM   1986  CD  GLN A 256      16.545  52.936  27.323  1.00 50.85           C  
ATOM   1987  OE1 GLN A 256      15.416  53.342  27.044  1.00 52.64           O  
ATOM   1988  NE2 GLN A 256      17.467  53.707  27.883  1.00 52.83           N  
ATOM   1989  N   ASN A 257      19.620  49.331  23.985  1.00 41.35           N  
ATOM   1990  CA  ASN A 257      20.403  49.232  22.746  1.00 42.59           C  
ATOM   1991  C   ASN A 257      20.627  47.792  22.358  1.00 43.91           C  
ATOM   1992  O   ASN A 257      21.229  47.512  21.325  1.00 43.89           O  
ATOM   1993  CB  ASN A 257      21.772  49.878  22.886  1.00 41.17           C  
ATOM   1994  CG  ASN A 257      21.685  51.310  23.266  1.00 40.06           C  
ATOM   1995  OD1 ASN A 257      21.922  51.668  24.413  1.00 39.34           O  
ATOM   1996  ND2 ASN A 257      21.325  52.149  22.307  1.00 38.20           N  
ATOM   1997  N   VAL A 258      20.154  46.877  23.193  1.00 45.17           N  
ATOM   1998  CA  VAL A 258      20.332  45.472  22.930  1.00 46.90           C  
ATOM   1999  C   VAL A 258      19.588  44.992  21.678  1.00 47.98           C  
ATOM   2000  O   VAL A 258      18.467  45.423  21.394  1.00 47.77           O  
ATOM   2001  CB  VAL A 258      19.895  44.669  24.158  1.00 46.35           C  
ATOM   2002  CG1 VAL A 258      18.404  44.421  24.128  1.00 46.35           C  
ATOM   2003  CG2 VAL A 258      20.651  43.395  24.227  1.00 47.38           C  
ATOM   2004  N   VAL A 259      20.228  44.097  20.930  1.00 50.62           N  
ATOM   2005  CA  VAL A 259      19.651  43.518  19.723  1.00 50.80           C  
ATOM   2006  C   VAL A 259      20.045  42.044  19.712  1.00 52.92           C  
ATOM   2007  O   VAL A 259      21.240  41.731  19.750  1.00 53.86           O  
ATOM   2008  CB  VAL A 259      20.228  44.145  18.458  1.00 49.87           C  
ATOM   2009  CG1 VAL A 259      19.487  43.630  17.274  1.00 48.68           C  
ATOM   2010  CG2 VAL A 259      20.120  45.637  18.521  1.00 49.69           C  
ATOM   2011  N   GLY A 260      19.060  41.145  19.649  1.00 53.08           N  
ATOM   2012  CA  GLY A 260      19.377  39.726  19.652  1.00 52.89           C  
ATOM   2013  C   GLY A 260      19.036  38.908  18.410  1.00 53.09           C  
ATOM   2014  O   GLY A 260      18.468  39.403  17.438  1.00 52.39           O  
ATOM   2015  N   TYR A 261      19.413  37.632  18.464  1.00 52.79           N  
ATOM   2016  CA  TYR A 261      19.149  36.690  17.386  1.00 52.32           C  
ATOM   2017  C   TYR A 261      18.254  35.611  17.965  1.00 51.21           C  
ATOM   2018  O   TYR A 261      18.624  34.970  18.943  1.00 49.96           O  
ATOM   2019  CB  TYR A 261      20.448  36.041  16.912  1.00 54.66           C  
ATOM   2020  CG  TYR A 261      21.494  37.001  16.405  1.00 59.07           C  
ATOM   2021  CD1 TYR A 261      22.040  36.847  15.133  1.00 61.15           C  
ATOM   2022  CD2 TYR A 261      21.979  38.032  17.212  1.00 60.93           C  
ATOM   2023  CE1 TYR A 261      23.046  37.691  14.674  1.00 62.71           C  
ATOM   2024  CE2 TYR A 261      22.992  38.886  16.760  1.00 61.74           C  
ATOM   2025  CZ  TYR A 261      23.518  38.705  15.486  1.00 62.86           C  
ATOM   2026  OH  TYR A 261      24.505  39.533  14.995  1.00 64.63           O  
ATOM   2027  N   GLU A 262      17.066  35.406  17.404  1.00 50.43           N  
ATOM   2028  CA  GLU A 262      16.222  34.351  17.946  1.00 49.55           C  
ATOM   2029  C   GLU A 262      15.890  33.262  16.954  1.00 48.56           C  
ATOM   2030  O   GLU A 262      16.224  33.358  15.767  1.00 46.47           O  
ATOM   2031  CB  GLU A 262      14.934  34.908  18.534  1.00 50.44           C  
ATOM   2032  CG  GLU A 262      14.093  35.674  17.585  1.00 53.52           C  
ATOM   2033  CD  GLU A 262      12.730  35.921  18.161  1.00 57.28           C  
ATOM   2034  OE1 GLU A 262      12.080  36.876  17.707  1.00 62.83           O  
ATOM   2035  OE2 GLU A 262      12.294  35.149  19.055  1.00 56.16           O  
ATOM   2036  N   THR A 263      15.236  32.218  17.467  1.00 48.32           N  
ATOM   2037  CA  THR A 263      14.828  31.042  16.693  1.00 48.63           C  
ATOM   2038  C   THR A 263      14.071  30.070  17.608  1.00 47.54           C  
ATOM   2039  O   THR A 263      14.165  30.141  18.844  1.00 47.85           O  
ATOM   2040  CB  THR A 263      16.063  30.290  16.077  1.00 47.88           C  
ATOM   2041  OG1 THR A 263      15.622  29.328  15.112  1.00 50.01           O  
ATOM   2042  CG2 THR A 263      16.819  29.529  17.137  1.00 46.54           C  
ATOM   2043  N   VAL A 264      13.300  29.173  16.999  1.00 47.29           N  
ATOM   2044  CA  VAL A 264      12.558  28.181  17.765  1.00 45.76           C  
ATOM   2045  C   VAL A 264      13.027  26.811  17.325  1.00 46.14           C  
ATOM   2046  O   VAL A 264      12.862  26.429  16.159  1.00 46.49           O  
ATOM   2047  CB  VAL A 264      11.052  28.288  17.521  1.00 43.86           C  
ATOM   2048  CG1 VAL A 264      10.303  27.256  18.344  1.00 40.67           C  
ATOM   2049  CG2 VAL A 264      10.599  29.663  17.905  1.00 43.41           C  
ATOM   2050  N   VAL A 265      13.640  26.090  18.264  1.00 45.81           N  
ATOM   2051  CA  VAL A 265      14.138  24.738  17.999  1.00 45.07           C  
ATOM   2052  C   VAL A 265      13.068  23.707  18.344  1.00 45.15           C  
ATOM   2053  O   VAL A 265      12.353  23.830  19.352  1.00 43.78           O  
ATOM   2054  CB  VAL A 265      15.461  24.399  18.804  1.00 43.60           C  
ATOM   2055  CG1 VAL A 265      16.644  25.165  18.230  1.00 42.08           C  
ATOM   2056  CG2 VAL A 265      15.288  24.709  20.286  1.00 42.45           C  
ATOM   2057  N   GLY A 266      12.966  22.691  17.489  1.00 44.70           N  
ATOM   2058  CA  GLY A 266      12.003  21.633  17.693  1.00 44.17           C  
ATOM   2059  C   GLY A 266      12.707  20.297  17.642  1.00 43.54           C  
ATOM   2060  O   GLY A 266      13.927  20.241  17.466  1.00 43.03           O  
ATOM   2061  N   PRO A 267      11.961  19.194  17.793  1.00 42.51           N  
ATOM   2062  CA  PRO A 267      12.547  17.854  17.762  1.00 41.23           C  
ATOM   2063  C   PRO A 267      13.443  17.628  16.554  1.00 40.71           C  
ATOM   2064  O   PRO A 267      13.058  17.907  15.416  1.00 41.00           O  
ATOM   2065  CB  PRO A 267      11.311  16.959  17.773  1.00 40.74           C  
ATOM   2066  CG  PRO A 267      10.371  17.746  18.678  1.00 41.26           C  
ATOM   2067  CD  PRO A 267      10.523  19.138  18.113  1.00 41.76           C  
ATOM   2068  N   GLY A 268      14.654  17.151  16.815  1.00 40.93           N  
ATOM   2069  CA  GLY A 268      15.586  16.882  15.739  1.00 41.98           C  
ATOM   2070  C   GLY A 268      16.545  18.015  15.420  1.00 43.15           C  
ATOM   2071  O   GLY A 268      17.575  17.785  14.765  1.00 43.18           O  
ATOM   2072  N   ASP A 269      16.212  19.233  15.856  1.00 43.36           N  
ATOM   2073  CA  ASP A 269      17.062  20.398  15.609  1.00 41.87           C  
ATOM   2074  C   ASP A 269      18.200  20.453  16.622  1.00 41.31           C  
ATOM   2075  O   ASP A 269      18.062  19.988  17.767  1.00 41.08           O  
ATOM   2076  CB  ASP A 269      16.266  21.707  15.718  1.00 42.62           C  
ATOM   2077  CG  ASP A 269      15.177  21.828  14.671  1.00 43.85           C  
ATOM   2078  OD1 ASP A 269      15.445  21.485  13.499  1.00 44.23           O  
ATOM   2079  OD2 ASP A 269      14.059  22.280  15.013  1.00 44.61           O  
ATOM   2080  N   VAL A 270      19.321  21.029  16.190  1.00 39.35           N  
ATOM   2081  CA  VAL A 270      20.494  21.202  17.037  1.00 37.92           C  
ATOM   2082  C   VAL A 270      20.980  22.653  16.898  1.00 37.44           C  
ATOM   2083  O   VAL A 270      21.262  23.114  15.794  1.00 37.18           O  
ATOM   2084  CB  VAL A 270      21.613  20.247  16.621  1.00 38.23           C  
ATOM   2085  CG1 VAL A 270      22.859  20.497  17.465  1.00 35.89           C  
ATOM   2086  CG2 VAL A 270      21.128  18.815  16.782  1.00 39.05           C  
ATOM   2087  N   LEU A 271      21.062  23.361  18.026  1.00 36.08           N  
ATOM   2088  CA  LEU A 271      21.496  24.761  18.051  1.00 34.67           C  
ATOM   2089  C   LEU A 271      22.893  24.905  18.599  1.00 34.17           C  
ATOM   2090  O   LEU A 271      23.196  24.371  19.649  1.00 34.66           O  
ATOM   2091  CB  LEU A 271      20.569  25.603  18.933  1.00 33.36           C  
ATOM   2092  CG  LEU A 271      21.046  27.026  19.264  1.00 34.29           C  
ATOM   2093  CD1 LEU A 271      21.322  27.836  18.005  1.00 33.11           C  
ATOM   2094  CD2 LEU A 271      19.975  27.699  20.083  1.00 32.11           C  
ATOM   2095  N   TYR A 272      23.732  25.650  17.897  1.00 33.75           N  
ATOM   2096  CA  TYR A 272      25.083  25.862  18.357  1.00 33.39           C  
ATOM   2097  C   TYR A 272      25.135  27.188  19.064  1.00 34.98           C  
ATOM   2098  O   TYR A 272      24.880  28.211  18.449  1.00 36.07           O  
ATOM   2099  CB  TYR A 272      26.044  25.905  17.185  1.00 33.12           C  
ATOM   2100  CG  TYR A 272      27.422  26.402  17.568  1.00 34.76           C  
ATOM   2101  CD1 TYR A 272      28.162  25.777  18.578  1.00 33.77           C  
ATOM   2102  CD2 TYR A 272      27.993  27.490  16.911  1.00 35.81           C  
ATOM   2103  CE1 TYR A 272      29.435  26.229  18.919  1.00 35.34           C  
ATOM   2104  CE2 TYR A 272      29.262  27.948  17.247  1.00 35.20           C  
ATOM   2105  CZ  TYR A 272      29.976  27.321  18.253  1.00 36.80           C  
ATOM   2106  OH  TYR A 272      31.201  27.855  18.606  1.00 39.29           O  
ATOM   2107  N   ILE A 273      25.471  27.165  20.351  1.00 34.92           N  
ATOM   2108  CA  ILE A 273      25.585  28.376  21.183  1.00 33.58           C  
ATOM   2109  C   ILE A 273      27.074  28.610  21.452  1.00 35.21           C  
ATOM   2110  O   ILE A 273      27.651  27.955  22.309  1.00 36.03           O  
ATOM   2111  CB  ILE A 273      24.882  28.182  22.552  1.00 31.90           C  
ATOM   2112  CG1 ILE A 273      23.409  27.825  22.330  1.00 30.06           C  
ATOM   2113  CG2 ILE A 273      25.032  29.441  23.411  1.00 33.70           C  
ATOM   2114  CD1 ILE A 273      22.640  27.659  23.598  1.00 21.23           C  
ATOM   2115  N   PRO A 274      27.704  29.548  20.732  1.00 35.87           N  
ATOM   2116  CA  PRO A 274      29.137  29.807  20.941  1.00 36.67           C  
ATOM   2117  C   PRO A 274      29.435  30.191  22.397  1.00 40.21           C  
ATOM   2118  O   PRO A 274      28.619  30.847  23.052  1.00 41.89           O  
ATOM   2119  CB  PRO A 274      29.413  30.931  19.949  1.00 36.63           C  
ATOM   2120  CG  PRO A 274      28.378  30.699  18.877  1.00 36.29           C  
ATOM   2121  CD  PRO A 274      27.157  30.440  19.704  1.00 35.33           C  
ATOM   2122  N   MET A 275      30.594  29.774  22.913  1.00 41.81           N  
ATOM   2123  CA  MET A 275      30.944  30.084  24.297  1.00 41.93           C  
ATOM   2124  C   MET A 275      30.893  31.595  24.474  1.00 42.26           C  
ATOM   2125  O   MET A 275      31.195  32.342  23.549  1.00 42.90           O  
ATOM   2126  CB  MET A 275      32.351  29.579  24.634  1.00 43.07           C  
ATOM   2127  CG  MET A 275      33.476  30.346  23.954  1.00 47.67           C  
ATOM   2128  SD  MET A 275      35.139  29.672  24.210  1.00 54.70           S  
ATOM   2129  CE  MET A 275      35.139  29.345  25.987  1.00 49.96           C  
ATOM   2130  N   TYR A 276      30.492  32.022  25.663  1.00 43.01           N  
ATOM   2131  CA  TYR A 276      30.388  33.435  26.013  1.00 43.28           C  
ATOM   2132  C   TYR A 276      29.225  34.174  25.363  1.00 43.01           C  
ATOM   2133  O   TYR A 276      29.055  35.376  25.574  1.00 44.83           O  
ATOM   2134  CB  TYR A 276      31.701  34.145  25.700  1.00 44.31           C  
ATOM   2135  CG  TYR A 276      32.779  33.869  26.724  1.00 47.59           C  
ATOM   2136  CD1 TYR A 276      32.649  34.318  28.042  1.00 48.37           C  
ATOM   2137  CD2 TYR A 276      33.941  33.175  26.378  1.00 48.96           C  
ATOM   2138  CE1 TYR A 276      33.657  34.088  28.990  1.00 50.12           C  
ATOM   2139  CE2 TYR A 276      34.953  32.937  27.324  1.00 49.83           C  
ATOM   2140  CZ  TYR A 276      34.804  33.398  28.625  1.00 50.31           C  
ATOM   2141  OH  TYR A 276      35.799  33.175  29.559  1.00 50.08           O  
ATOM   2142  N   TRP A 277      28.418  33.475  24.576  1.00 41.74           N  
ATOM   2143  CA  TRP A 277      27.273  34.133  23.966  1.00 40.44           C  
ATOM   2144  C   TRP A 277      26.096  34.099  24.927  1.00 40.67           C  
ATOM   2145  O   TRP A 277      25.758  33.051  25.477  1.00 41.98           O  
ATOM   2146  CB  TRP A 277      26.865  33.437  22.675  1.00 38.37           C  
ATOM   2147  CG  TRP A 277      27.596  33.942  21.500  1.00 37.52           C  
ATOM   2148  CD1 TRP A 277      28.939  33.876  21.276  1.00 36.97           C  
ATOM   2149  CD2 TRP A 277      27.033  34.605  20.373  1.00 38.26           C  
ATOM   2150  NE1 TRP A 277      29.255  34.457  20.068  1.00 37.13           N  
ATOM   2151  CE2 TRP A 277      28.095  34.915  19.492  1.00 38.30           C  
ATOM   2152  CE3 TRP A 277      25.730  34.968  20.017  1.00 39.42           C  
ATOM   2153  CZ2 TRP A 277      27.891  35.578  18.277  1.00 36.71           C  
ATOM   2154  CZ3 TRP A 277      25.526  35.624  18.803  1.00 37.70           C  
ATOM   2155  CH2 TRP A 277      26.600  35.924  17.954  1.00 37.02           C  
ATOM   2156  N   TRP A 278      25.466  35.241  25.141  1.00 40.23           N  
ATOM   2157  CA  TRP A 278      24.314  35.276  26.026  1.00 39.93           C  
ATOM   2158  C   TRP A 278      23.139  34.497  25.427  1.00 39.69           C  
ATOM   2159  O   TRP A 278      22.959  34.470  24.213  1.00 39.76           O  
ATOM   2160  CB  TRP A 278      23.854  36.715  26.252  1.00 39.49           C  
ATOM   2161  CG  TRP A 278      24.846  37.592  26.912  1.00 38.29           C  
ATOM   2162  CD1 TRP A 278      25.860  38.291  26.316  1.00 37.79           C  
ATOM   2163  CD2 TRP A 278      24.926  37.879  28.312  1.00 37.39           C  
ATOM   2164  NE1 TRP A 278      26.567  39.001  27.259  1.00 37.98           N  
ATOM   2165  CE2 TRP A 278      26.013  38.763  28.494  1.00 38.58           C  
ATOM   2166  CE3 TRP A 278      24.184  37.474  29.425  1.00 35.76           C  
ATOM   2167  CZ2 TRP A 278      26.374  39.251  29.757  1.00 39.10           C  
ATOM   2168  CZ3 TRP A 278      24.542  37.952  30.676  1.00 35.87           C  
ATOM   2169  CH2 TRP A 278      25.625  38.829  30.832  1.00 38.53           C  
ATOM   2170  N   HIS A 279      22.338  33.877  26.290  1.00 40.22           N  
ATOM   2171  CA  HIS A 279      21.152  33.168  25.823  1.00 41.33           C  
ATOM   2172  C   HIS A 279      19.985  33.090  26.803  1.00 41.21           C  
ATOM   2173  O   HIS A 279      20.134  32.746  27.973  1.00 40.73           O  
ATOM   2174  CB  HIS A 279      21.488  31.754  25.312  1.00 42.80           C  
ATOM   2175  CG  HIS A 279      22.392  30.968  26.206  1.00 45.60           C  
ATOM   2176  ND1 HIS A 279      23.746  31.206  26.290  1.00 46.79           N  
ATOM   2177  CD2 HIS A 279      22.148  29.904  27.010  1.00 46.48           C  
ATOM   2178  CE1 HIS A 279      24.300  30.321  27.104  1.00 47.56           C  
ATOM   2179  NE2 HIS A 279      23.351  29.515  27.555  1.00 48.02           N  
ATOM   2180  N   HIS A 280      18.813  33.430  26.287  1.00 41.44           N  
ATOM   2181  CA  HIS A 280      17.581  33.394  27.045  1.00 43.27           C  
ATOM   2182  C   HIS A 280      16.792  32.228  26.429  1.00 45.48           C  
ATOM   2183  O   HIS A 280      16.576  32.220  25.214  1.00 47.57           O  
ATOM   2184  CB  HIS A 280      16.854  34.713  26.835  1.00 42.86           C  
ATOM   2185  CG  HIS A 280      15.406  34.673  27.193  1.00 44.55           C  
ATOM   2186  ND1 HIS A 280      14.936  34.986  28.447  1.00 45.72           N  
ATOM   2187  CD2 HIS A 280      14.319  34.339  26.454  1.00 44.82           C  
ATOM   2188  CE1 HIS A 280      13.623  34.851  28.470  1.00 46.42           C  
ATOM   2189  NE2 HIS A 280      13.221  34.460  27.275  1.00 46.20           N  
ATOM   2190  N   ILE A 281      16.395  31.241  27.234  1.00 45.42           N  
ATOM   2191  CA  ILE A 281      15.652  30.093  26.699  1.00 45.32           C  
ATOM   2192  C   ILE A 281      14.293  29.923  27.343  1.00 46.77           C  
ATOM   2193  O   ILE A 281      14.170  29.885  28.556  1.00 48.32           O  
ATOM   2194  CB  ILE A 281      16.423  28.799  26.908  1.00 43.50           C  
ATOM   2195  CG1 ILE A 281      17.669  28.827  26.031  1.00 42.21           C  
ATOM   2196  CG2 ILE A 281      15.547  27.600  26.581  1.00 42.74           C  
ATOM   2197  CD1 ILE A 281      18.590  27.711  26.288  1.00 42.61           C  
ATOM   2198  N   GLU A 282      13.263  29.804  26.526  1.00 49.00           N  
ATOM   2199  CA  GLU A 282      11.937  29.645  27.087  1.00 51.50           C  
ATOM   2200  C   GLU A 282      11.181  28.549  26.359  1.00 51.58           C  
ATOM   2201  O   GLU A 282      11.346  28.377  25.152  1.00 50.32           O  
ATOM   2202  CB  GLU A 282      11.172  30.971  27.006  1.00 53.22           C  
ATOM   2203  CG  GLU A 282      10.913  31.447  25.577  1.00 55.73           C  
ATOM   2204  CD  GLU A 282      10.225  32.807  25.505  1.00 57.59           C  
ATOM   2205  OE1 GLU A 282      10.834  33.813  25.924  1.00 59.52           O  
ATOM   2206  OE2 GLU A 282       9.071  32.869  25.031  1.00 58.54           O  
ATOM   2207  N   SER A 283      10.370  27.806  27.108  1.00 52.96           N  
ATOM   2208  CA  SER A 283       9.552  26.733  26.555  1.00 54.42           C  
ATOM   2209  C   SER A 283       8.195  27.313  26.145  1.00 55.80           C  
ATOM   2210  O   SER A 283       7.477  27.886  26.983  1.00 56.45           O  
ATOM   2211  CB  SER A 283       9.328  25.616  27.589  1.00 53.92           C  
ATOM   2212  OG  SER A 283      10.534  24.977  27.986  1.00 53.19           O  
ATOM   2213  N   LEU A 284       7.861  27.159  24.859  1.00 56.34           N  
ATOM   2214  CA  LEU A 284       6.612  27.650  24.278  1.00 56.13           C  
ATOM   2215  C   LEU A 284       5.412  27.500  25.206  1.00 56.35           C  
ATOM   2216  O   LEU A 284       5.249  26.494  25.910  1.00 56.54           O  
ATOM   2217  CB  LEU A 284       6.343  26.940  22.941  1.00 55.97           C  
ATOM   2218  CG  LEU A 284       7.046  27.429  21.663  1.00 55.74           C  
ATOM   2219  CD1 LEU A 284       6.311  28.618  21.120  1.00 56.72           C  
ATOM   2220  CD2 LEU A 284       8.486  27.805  21.934  1.00 57.40           C  
ATOM   2221  N   LEU A 285       4.587  28.538  25.209  1.00 57.29           N  
ATOM   2222  CA  LEU A 285       3.395  28.585  26.027  1.00 57.79           C  
ATOM   2223  C   LEU A 285       2.395  27.580  25.499  1.00 59.32           C  
ATOM   2224  O   LEU A 285       2.120  27.537  24.297  1.00 59.63           O  
ATOM   2225  CB  LEU A 285       2.788  29.981  25.975  1.00 57.21           C  
ATOM   2226  CG  LEU A 285       3.642  31.110  26.546  1.00 56.65           C  
ATOM   2227  CD1 LEU A 285       3.134  32.433  26.010  1.00 57.22           C  
ATOM   2228  CD2 LEU A 285       3.597  31.080  28.065  1.00 54.19           C  
ATOM   2229  N   ASN A 286       1.860  26.765  26.402  1.00 60.70           N  
ATOM   2230  CA  ASN A 286       0.872  25.757  26.039  1.00 62.22           C  
ATOM   2231  C   ASN A 286       1.410  24.780  24.992  1.00 61.82           C  
ATOM   2232  O   ASN A 286       0.702  24.441  24.042  1.00 62.28           O  
ATOM   2233  CB  ASN A 286      -0.396  26.434  25.493  1.00 64.08           C  
ATOM   2234  CG  ASN A 286      -1.014  27.413  26.480  1.00 66.32           C  
ATOM   2235  OD1 ASN A 286      -1.276  27.070  27.636  1.00 66.43           O  
ATOM   2236  ND2 ASN A 286      -1.264  28.636  26.021  1.00 68.33           N  
ATOM   2237  N   GLY A 287       2.653  24.334  25.171  1.00 60.58           N  
ATOM   2238  CA  GLY A 287       3.257  23.411  24.225  1.00 58.84           C  
ATOM   2239  C   GLY A 287       3.722  22.123  24.875  1.00 57.78           C  
ATOM   2240  O   GLY A 287       4.710  21.515  24.457  1.00 58.55           O  
ATOM   2241  N   GLY A 288       3.008  21.697  25.907  1.00 56.05           N  
ATOM   2242  CA  GLY A 288       3.396  20.475  26.581  1.00 55.12           C  
ATOM   2243  C   GLY A 288       4.783  20.610  27.175  1.00 54.11           C  
ATOM   2244  O   GLY A 288       5.342  21.700  27.228  1.00 54.15           O  
ATOM   2245  N   ILE A 289       5.342  19.497  27.631  1.00 52.90           N  
ATOM   2246  CA  ILE A 289       6.673  19.530  28.211  1.00 50.55           C  
ATOM   2247  C   ILE A 289       7.695  19.578  27.098  1.00 50.87           C  
ATOM   2248  O   ILE A 289       7.369  19.341  25.931  1.00 52.13           O  
ATOM   2249  CB  ILE A 289       6.953  18.302  29.061  1.00 49.48           C  
ATOM   2250  CG1 ILE A 289       7.038  17.070  28.171  1.00 49.85           C  
ATOM   2251  CG2 ILE A 289       5.868  18.141  30.101  1.00 47.33           C  
ATOM   2252  CD1 ILE A 289       7.829  15.950  28.783  1.00 50.94           C  
ATOM   2253  N   THR A 290       8.937  19.872  27.476  1.00 49.85           N  
ATOM   2254  CA  THR A 290      10.055  19.977  26.541  1.00 48.03           C  
ATOM   2255  C   THR A 290      11.242  19.181  27.077  1.00 46.07           C  
ATOM   2256  O   THR A 290      11.550  19.210  28.267  1.00 45.94           O  
ATOM   2257  CB  THR A 290      10.503  21.458  26.342  1.00 48.14           C  
ATOM   2258  OG1 THR A 290      11.047  21.962  27.567  1.00 49.33           O  
ATOM   2259  CG2 THR A 290       9.318  22.331  25.911  1.00 47.44           C  
ATOM   2260  N   ILE A 291      11.910  18.475  26.181  1.00 44.25           N  
ATOM   2261  CA  ILE A 291      13.050  17.671  26.564  1.00 43.98           C  
ATOM   2262  C   ILE A 291      14.215  18.045  25.675  1.00 43.40           C  
ATOM   2263  O   ILE A 291      14.075  18.131  24.454  1.00 43.53           O  
ATOM   2264  CB  ILE A 291      12.747  16.185  26.389  1.00 44.40           C  
ATOM   2265  CG1 ILE A 291      11.496  15.817  27.188  1.00 43.82           C  
ATOM   2266  CG2 ILE A 291      13.933  15.373  26.838  1.00 43.66           C  
ATOM   2267  CD1 ILE A 291      11.043  14.401  26.951  1.00 44.19           C  
ATOM   2268  N   THR A 292      15.373  18.260  26.282  1.00 43.02           N  
ATOM   2269  CA  THR A 292      16.549  18.635  25.514  1.00 42.83           C  
ATOM   2270  C   THR A 292      17.779  17.969  26.102  1.00 42.14           C  
ATOM   2271  O   THR A 292      17.744  17.508  27.238  1.00 42.55           O  
ATOM   2272  CB  THR A 292      16.787  20.149  25.575  1.00 42.93           C  
ATOM   2273  OG1 THR A 292      15.552  20.841  25.366  1.00 44.74           O  
ATOM   2274  CG2 THR A 292      17.768  20.562  24.519  1.00 41.23           C  
ATOM   2275  N   VAL A 293      18.862  17.927  25.335  1.00 42.07           N  
ATOM   2276  CA  VAL A 293      20.111  17.354  25.823  1.00 43.22           C  
ATOM   2277  C   VAL A 293      21.236  18.212  25.264  1.00 44.91           C  
ATOM   2278  O   VAL A 293      21.368  18.312  24.050  1.00 46.39           O  
ATOM   2279  CB  VAL A 293      20.306  15.903  25.336  1.00 42.13           C  
ATOM   2280  CG1 VAL A 293      21.741  15.420  25.617  1.00 38.27           C  
ATOM   2281  CG2 VAL A 293      19.300  15.010  26.023  1.00 40.09           C  
ATOM   2282  N   ASN A 294      22.024  18.845  26.133  1.00 46.28           N  
ATOM   2283  CA  ASN A 294      23.119  19.682  25.645  1.00 47.91           C  
ATOM   2284  C   ASN A 294      24.460  18.962  25.693  1.00 47.47           C  
ATOM   2285  O   ASN A 294      24.599  17.955  26.379  1.00 47.13           O  
ATOM   2286  CB  ASN A 294      23.205  21.012  26.426  1.00 50.62           C  
ATOM   2287  CG  ASN A 294      23.603  20.830  27.891  1.00 54.61           C  
ATOM   2288  OD1 ASN A 294      24.595  20.174  28.212  1.00 56.72           O  
ATOM   2289  ND2 ASN A 294      22.829  21.431  28.788  1.00 56.17           N  
ATOM   2290  N   PHE A 295      25.434  19.482  24.946  1.00 47.66           N  
ATOM   2291  CA  PHE A 295      26.775  18.912  24.889  1.00 48.20           C  
ATOM   2292  C   PHE A 295      27.764  20.031  25.169  1.00 49.05           C  
ATOM   2293  O   PHE A 295      27.975  20.889  24.324  1.00 49.08           O  
ATOM   2294  CB  PHE A 295      27.062  18.338  23.499  1.00 48.43           C  
ATOM   2295  CG  PHE A 295      26.199  17.169  23.132  1.00 48.15           C  
ATOM   2296  CD1 PHE A 295      24.824  17.311  23.031  1.00 48.48           C  
ATOM   2297  CD2 PHE A 295      26.766  15.921  22.904  1.00 48.13           C  
ATOM   2298  CE1 PHE A 295      24.015  16.229  22.708  1.00 47.61           C  
ATOM   2299  CE2 PHE A 295      25.970  14.828  22.579  1.00 48.44           C  
ATOM   2300  CZ  PHE A 295      24.589  14.985  22.481  1.00 48.67           C  
ATOM   2301  N   TRP A 296      28.368  20.034  26.351  1.00 50.00           N  
ATOM   2302  CA  TRP A 296      29.316  21.090  26.680  1.00 50.92           C  
ATOM   2303  C   TRP A 296      30.763  20.679  26.491  1.00 50.38           C  
ATOM   2304  O   TRP A 296      31.208  19.701  27.077  1.00 50.68           O  
ATOM   2305  CB  TRP A 296      29.125  21.554  28.124  1.00 51.69           C  
ATOM   2306  CG  TRP A 296      28.070  22.592  28.303  1.00 55.02           C  
ATOM   2307  CD1 TRP A 296      27.630  23.469  27.369  1.00 56.61           C  
ATOM   2308  CD2 TRP A 296      27.400  22.924  29.526  1.00 57.86           C  
ATOM   2309  NE1 TRP A 296      26.728  24.344  27.923  1.00 56.50           N  
ATOM   2310  CE2 TRP A 296      26.568  24.032  29.248  1.00 57.50           C  
ATOM   2311  CE3 TRP A 296      27.425  22.403  30.821  1.00 61.35           C  
ATOM   2312  CZ2 TRP A 296      25.768  24.632  30.222  1.00 59.91           C  
ATOM   2313  CZ3 TRP A 296      26.624  23.001  31.802  1.00 62.97           C  
ATOM   2314  CH2 TRP A 296      25.808  24.106  31.491  1.00 62.41           C  
ATOM   2315  N   TYR A 297      31.489  21.443  25.677  1.00 50.69           N  
ATOM   2316  CA  TYR A 297      32.906  21.196  25.396  1.00 52.20           C  
ATOM   2317  C   TYR A 297      33.768  22.391  25.826  1.00 54.25           C  
ATOM   2318  O   TYR A 297      33.326  23.533  25.811  1.00 54.78           O  
ATOM   2319  CB  TYR A 297      33.144  20.962  23.894  1.00 51.18           C  
ATOM   2320  CG  TYR A 297      32.548  19.695  23.322  1.00 50.86           C  
ATOM   2321  CD1 TYR A 297      31.181  19.589  23.067  1.00 50.67           C  
ATOM   2322  CD2 TYR A 297      33.355  18.593  23.057  1.00 50.26           C  
ATOM   2323  CE1 TYR A 297      30.640  18.413  22.569  1.00 51.16           C  
ATOM   2324  CE2 TYR A 297      32.829  17.423  22.562  1.00 50.73           C  
ATOM   2325  CZ  TYR A 297      31.477  17.336  22.325  1.00 51.75           C  
ATOM   2326  OH  TYR A 297      30.976  16.143  21.882  1.00 54.36           O  
ATOM   2327  N   LYS A 298      35.007  22.128  26.202  1.00 57.11           N  
ATOM   2328  CA  LYS A 298      35.869  23.229  26.593  1.00 60.11           C  
ATOM   2329  C   LYS A 298      36.410  23.902  25.351  1.00 60.97           C  
ATOM   2330  O   LYS A 298      36.899  23.240  24.445  1.00 61.21           O  
ATOM   2331  CB  LYS A 298      37.021  22.740  27.461  1.00 62.27           C  
ATOM   2332  CG  LYS A 298      36.592  22.438  28.880  1.00 67.63           C  
ATOM   2333  CD  LYS A 298      37.766  22.066  29.771  1.00 71.11           C  
ATOM   2334  CE  LYS A 298      37.324  21.942  31.230  1.00 73.23           C  
ATOM   2335  NZ  LYS A 298      38.410  21.415  32.110  1.00 75.87           N  
ATOM   2336  N   GLY A 299      36.324  25.222  25.307  1.00 62.27           N  
ATOM   2337  CA  GLY A 299      36.824  25.936  24.151  1.00 64.60           C  
ATOM   2338  C   GLY A 299      38.251  25.569  23.792  1.00 66.47           C  
ATOM   2339  O   GLY A 299      38.973  24.935  24.569  1.00 65.68           O  
ATOM   2340  N   ALA A 300      38.659  25.964  22.592  1.00 69.01           N  
ATOM   2341  CA  ALA A 300      40.014  25.704  22.134  1.00 71.25           C  
ATOM   2342  C   ALA A 300      40.975  26.421  23.088  1.00 73.61           C  
ATOM   2343  O   ALA A 300      40.647  27.472  23.635  1.00 74.18           O  
ATOM   2344  CB  ALA A 300      40.190  26.227  20.707  1.00 70.14           C  
ATOM   2345  N   PRO A 301      42.169  25.856  23.304  1.00 76.07           N  
ATOM   2346  CA  PRO A 301      43.162  26.460  24.201  1.00 78.07           C  
ATOM   2347  C   PRO A 301      43.620  27.847  23.734  1.00 79.80           C  
ATOM   2348  O   PRO A 301      43.367  28.245  22.593  1.00 78.78           O  
ATOM   2349  CB  PRO A 301      44.288  25.433  24.189  1.00 77.59           C  
ATOM   2350  CG  PRO A 301      44.200  24.879  22.788  1.00 77.59           C  
ATOM   2351  CD  PRO A 301      42.719  24.669  22.629  1.00 77.22           C  
ATOM   2352  N   THR A 302      44.293  28.581  24.620  1.00 82.92           N  
ATOM   2353  CA  THR A 302      44.789  29.931  24.316  1.00 85.72           C  
ATOM   2354  C   THR A 302      46.041  29.890  23.425  1.00 86.57           C  
ATOM   2355  O   THR A 302      47.010  29.201  23.747  1.00 86.36           O  
ATOM   2356  CB  THR A 302      45.143  30.668  25.606  1.00 86.85           C  
ATOM   2357  OG1 THR A 302      44.087  30.504  26.564  1.00 87.22           O  
ATOM   2358  CG2 THR A 302      45.348  32.139  25.315  1.00 87.84           C  
ATOM   2359  N   PRO A 303      46.044  30.653  22.315  1.00 87.12           N  
ATOM   2360  CA  PRO A 303      47.140  30.734  21.340  1.00 88.46           C  
ATOM   2361  C   PRO A 303      48.552  30.838  21.896  1.00 90.54           C  
ATOM   2362  O   PRO A 303      49.529  30.579  21.175  1.00 91.77           O  
ATOM   2363  CB  PRO A 303      46.769  31.954  20.515  1.00 87.75           C  
ATOM   2364  CG  PRO A 303      45.300  31.884  20.497  1.00 87.34           C  
ATOM   2365  CD  PRO A 303      44.969  31.589  21.945  1.00 86.95           C  
ATOM   2366  N   LYS A 304      48.670  31.216  23.168  1.00 91.17           N  
ATOM   2367  CA  LYS A 304      49.983  31.349  23.780  1.00 91.09           C  
ATOM   2368  C   LYS A 304      50.782  32.478  23.154  1.00 90.88           C  
ATOM   2369  O   LYS A 304      51.933  32.702  23.520  1.00 90.90           O  
ATOM   2370  N   ARG A 305      50.165  33.178  22.203  1.00 90.19           N  
ATOM   2371  CA  ARG A 305      50.775  34.301  21.500  1.00 88.32           C  
ATOM   2372  C   ARG A 305      49.661  35.284  21.143  1.00 87.25           C  
ATOM   2373  O   ARG A 305      49.344  35.486  19.968  1.00 88.17           O  
ATOM   2374  CB  ARG A 305      51.473  33.807  20.235  1.00 87.83           C  
ATOM   2375  N   ILE A 306      49.067  35.889  22.174  1.00 84.99           N  
ATOM   2376  CA  ILE A 306      47.966  36.834  22.003  1.00 81.97           C  
ATOM   2377  C   ILE A 306      48.058  37.662  20.718  1.00 80.07           C  
ATOM   2378  O   ILE A 306      48.982  38.450  20.515  1.00 80.06           O  
ATOM   2379  CB  ILE A 306      47.870  37.752  23.230  1.00 80.41           C  
ATOM   2380  N   GLU A 307      47.090  37.472  19.840  1.00 77.84           N  
ATOM   2381  CA  GLU A 307      47.103  38.204  18.596  1.00 76.75           C  
ATOM   2382  C   GLU A 307      45.983  39.222  18.590  1.00 74.02           C  
ATOM   2383  O   GLU A 307      44.809  38.887  18.743  1.00 73.49           O  
ATOM   2384  CB  GLU A 307      46.976  37.238  17.422  1.00 79.88           C  
ATOM   2385  CG  GLU A 307      45.760  36.322  17.527  1.00 85.13           C  
ATOM   2386  CD  GLU A 307      45.600  35.414  16.319  1.00 88.35           C  
ATOM   2387  OE1 GLU A 307      44.583  34.688  16.232  1.00 88.63           O  
ATOM   2388  OE2 GLU A 307      46.497  35.424  15.447  1.00 90.01           O  
ATOM   2389  N   TYR A 308      46.363  40.477  18.420  1.00 71.38           N  
ATOM   2390  CA  TYR A 308      45.415  41.572  18.406  1.00 68.99           C  
ATOM   2391  C   TYR A 308      44.916  41.817  17.000  1.00 67.30           C  
ATOM   2392  O   TYR A 308      45.567  41.437  16.027  1.00 68.75           O  
ATOM   2393  CB  TYR A 308      46.092  42.818  18.957  1.00 68.93           C  
ATOM   2394  CG  TYR A 308      46.586  42.619  20.366  1.00 69.33           C  
ATOM   2395  CD1 TYR A 308      45.843  43.070  21.455  1.00 69.07           C  
ATOM   2396  CD2 TYR A 308      47.785  41.952  20.618  1.00 68.52           C  
ATOM   2397  CE1 TYR A 308      46.284  42.867  22.764  1.00 68.74           C  
ATOM   2398  CE2 TYR A 308      48.230  41.740  21.921  1.00 67.89           C  
ATOM   2399  CZ  TYR A 308      47.480  42.201  22.988  1.00 68.60           C  
ATOM   2400  OH  TYR A 308      47.930  42.011  24.277  1.00 68.29           O  
ATOM   2401  N   PRO A 309      43.747  42.454  16.868  1.00 65.36           N  
ATOM   2402  CA  PRO A 309      42.884  42.948  17.948  1.00 62.78           C  
ATOM   2403  C   PRO A 309      42.177  41.818  18.684  1.00 60.59           C  
ATOM   2404  O   PRO A 309      41.903  40.764  18.117  1.00 61.75           O  
ATOM   2405  CB  PRO A 309      41.903  43.841  17.216  1.00 63.26           C  
ATOM   2406  CG  PRO A 309      41.753  43.134  15.903  1.00 63.46           C  
ATOM   2407  CD  PRO A 309      43.179  42.791  15.554  1.00 64.61           C  
ATOM   2408  N   LEU A 310      41.872  42.049  19.950  1.00 56.63           N  
ATOM   2409  CA  LEU A 310      41.199  41.040  20.751  1.00 52.63           C  
ATOM   2410  C   LEU A 310      39.728  40.911  20.399  1.00 51.38           C  
ATOM   2411  O   LEU A 310      39.087  41.875  19.983  1.00 52.14           O  
ATOM   2412  CB  LEU A 310      41.309  41.383  22.228  1.00 51.03           C  
ATOM   2413  CG  LEU A 310      42.511  40.892  23.031  1.00 49.99           C  
ATOM   2414  CD1 LEU A 310      43.733  40.728  22.140  1.00 49.23           C  
ATOM   2415  CD2 LEU A 310      42.751  41.873  24.180  1.00 48.20           C  
ATOM   2416  N   LYS A 311      39.197  39.709  20.575  1.00 48.75           N  
ATOM   2417  CA  LYS A 311      37.789  39.486  20.304  1.00 47.63           C  
ATOM   2418  C   LYS A 311      37.008  39.820  21.583  1.00 48.04           C  
ATOM   2419  O   LYS A 311      37.539  39.742  22.693  1.00 48.51           O  
ATOM   2420  CB  LYS A 311      37.551  38.030  19.873  1.00 45.60           C  
ATOM   2421  N   ALA A 312      35.755  40.221  21.412  1.00 49.40           N  
ATOM   2422  CA  ALA A 312      34.897  40.588  22.535  1.00 49.52           C  
ATOM   2423  C   ALA A 312      34.971  39.625  23.715  1.00 50.27           C  
ATOM   2424  O   ALA A 312      35.253  40.041  24.830  1.00 51.93           O  
ATOM   2425  CB  ALA A 312      33.440  40.718  22.067  1.00 49.80           C  
ATOM   2426  N   HIS A 313      34.731  38.337  23.474  1.00 50.62           N  
ATOM   2427  CA  HIS A 313      34.751  37.368  24.573  1.00 49.42           C  
ATOM   2428  C   HIS A 313      36.087  37.298  25.294  1.00 47.34           C  
ATOM   2429  O   HIS A 313      36.155  36.931  26.463  1.00 47.41           O  
ATOM   2430  CB  HIS A 313      34.351  35.971  24.079  1.00 51.78           C  
ATOM   2431  CG  HIS A 313      35.443  35.238  23.368  1.00 54.58           C  
ATOM   2432  ND1 HIS A 313      35.893  35.589  22.117  1.00 56.77           N  
ATOM   2433  CD2 HIS A 313      36.172  34.156  23.743  1.00 55.62           C  
ATOM   2434  CE1 HIS A 313      36.847  34.759  21.744  1.00 56.47           C  
ATOM   2435  NE2 HIS A 313      37.038  33.875  22.708  1.00 56.95           N  
ATOM   2436  N   GLN A 314      37.152  37.651  24.600  1.00 45.21           N  
ATOM   2437  CA  GLN A 314      38.447  37.634  25.244  1.00 44.70           C  
ATOM   2438  C   GLN A 314      38.544  38.721  26.306  1.00 43.92           C  
ATOM   2439  O   GLN A 314      39.150  38.507  27.359  1.00 44.11           O  
ATOM   2440  CB  GLN A 314      39.551  37.815  24.222  1.00 46.01           C  
ATOM   2441  CG  GLN A 314      39.792  36.571  23.408  1.00 50.68           C  
ATOM   2442  CD  GLN A 314      40.925  36.732  22.426  1.00 52.75           C  
ATOM   2443  OE1 GLN A 314      40.826  37.492  21.458  1.00 56.05           O  
ATOM   2444  NE2 GLN A 314      42.023  36.024  22.674  1.00 52.51           N  
ATOM   2445  N   LYS A 315      37.955  39.886  26.037  1.00 42.58           N  
ATOM   2446  CA  LYS A 315      37.976  40.993  26.994  1.00 40.81           C  
ATOM   2447  C   LYS A 315      37.144  40.636  28.220  1.00 39.91           C  
ATOM   2448  O   LYS A 315      37.508  40.971  29.340  1.00 40.29           O  
ATOM   2449  CB  LYS A 315      37.416  42.264  26.355  1.00 41.09           C  
ATOM   2450  CG  LYS A 315      38.265  42.772  25.213  1.00 42.44           C  
ATOM   2451  CD  LYS A 315      37.694  44.031  24.600  1.00 42.07           C  
ATOM   2452  CE  LYS A 315      38.616  44.543  23.508  1.00 42.61           C  
ATOM   2453  NZ  LYS A 315      38.099  45.772  22.847  1.00 45.74           N  
ATOM   2454  N   VAL A 316      36.028  39.951  27.999  1.00 38.71           N  
ATOM   2455  CA  VAL A 316      35.171  39.550  29.097  1.00 37.60           C  
ATOM   2456  C   VAL A 316      35.947  38.598  29.998  1.00 38.22           C  
ATOM   2457  O   VAL A 316      35.706  38.516  31.208  1.00 37.30           O  
ATOM   2458  CB  VAL A 316      33.941  38.835  28.572  1.00 37.62           C  
ATOM   2459  CG1 VAL A 316      32.914  38.717  29.667  1.00 37.33           C  
ATOM   2460  CG2 VAL A 316      33.383  39.584  27.376  1.00 36.60           C  
ATOM   2461  N   ALA A 317      36.875  37.868  29.393  1.00 38.52           N  
ATOM   2462  CA  ALA A 317      37.689  36.927  30.141  1.00 38.37           C  
ATOM   2463  C   ALA A 317      38.635  37.714  31.033  1.00 38.92           C  
ATOM   2464  O   ALA A 317      38.934  37.304  32.157  1.00 39.97           O  
ATOM   2465  CB  ALA A 317      38.475  36.073  29.189  1.00 36.33           C  
ATOM   2466  N   ILE A 318      39.105  38.845  30.507  1.00 39.84           N  
ATOM   2467  CA  ILE A 318      40.016  39.721  31.228  1.00 39.18           C  
ATOM   2468  C   ILE A 318      39.292  40.373  32.408  1.00 40.26           C  
ATOM   2469  O   ILE A 318      39.834  40.430  33.513  1.00 42.25           O  
ATOM   2470  CB  ILE A 318      40.546  40.834  30.324  1.00 38.89           C  
ATOM   2471  CG1 ILE A 318      41.423  40.240  29.214  1.00 37.70           C  
ATOM   2472  CG2 ILE A 318      41.304  41.850  31.159  1.00 39.98           C  
ATOM   2473  CD1 ILE A 318      41.978  41.258  28.229  1.00 36.70           C  
ATOM   2474  N   MET A 319      38.081  40.876  32.171  1.00 39.23           N  
ATOM   2475  CA  MET A 319      37.320  41.490  33.238  1.00 38.67           C  
ATOM   2476  C   MET A 319      37.095  40.482  34.349  1.00 40.46           C  
ATOM   2477  O   MET A 319      37.362  40.769  35.522  1.00 40.81           O  
ATOM   2478  CB  MET A 319      35.991  41.972  32.709  1.00 37.94           C  
ATOM   2479  CG  MET A 319      36.153  42.990  31.622  1.00 38.32           C  
ATOM   2480  SD  MET A 319      34.676  43.978  31.472  1.00 41.79           S  
ATOM   2481  CE  MET A 319      33.883  43.183  30.166  1.00 39.84           C  
ATOM   2482  N   ARG A 320      36.604  39.299  33.988  1.00 41.55           N  
ATOM   2483  CA  ARG A 320      36.360  38.250  34.971  1.00 41.58           C  
ATOM   2484  C   ARG A 320      37.601  37.996  35.817  1.00 42.28           C  
ATOM   2485  O   ARG A 320      37.505  37.825  37.027  1.00 42.32           O  
ATOM   2486  CB  ARG A 320      35.972  36.948  34.283  1.00 40.12           C  
ATOM   2487  CG  ARG A 320      34.626  36.981  33.608  1.00 39.81           C  
ATOM   2488  CD  ARG A 320      34.231  35.582  33.158  1.00 38.05           C  
ATOM   2489  NE  ARG A 320      34.145  34.602  34.249  1.00 37.42           N  
ATOM   2490  CZ  ARG A 320      33.126  34.501  35.105  1.00 37.92           C  
ATOM   2491  NH1 ARG A 320      32.085  35.325  35.025  1.00 37.98           N  
ATOM   2492  NH2 ARG A 320      33.142  33.563  36.043  1.00 39.05           N  
ATOM   2493  N   ASN A 321      38.759  37.966  35.155  1.00 44.82           N  
ATOM   2494  CA  ASN A 321      40.031  37.740  35.832  1.00 46.12           C  
ATOM   2495  C   ASN A 321      40.366  38.806  36.845  1.00 44.99           C  
ATOM   2496  O   ASN A 321      40.791  38.501  37.964  1.00 44.56           O  
ATOM   2497  CB  ASN A 321      41.177  37.699  34.848  1.00 50.67           C  
ATOM   2498  CG  ASN A 321      41.901  36.399  34.900  1.00 57.14           C  
ATOM   2499  OD1 ASN A 321      41.436  35.409  34.340  1.00 61.29           O  
ATOM   2500  ND2 ASN A 321      43.026  36.365  35.615  1.00 59.33           N  
ATOM   2501  N   ILE A 322      40.205  40.061  36.437  1.00 43.96           N  
ATOM   2502  CA  ILE A 322      40.483  41.179  37.315  1.00 43.15           C  
ATOM   2503  C   ILE A 322      39.660  41.062  38.595  1.00 43.13           C  
ATOM   2504  O   ILE A 322      40.203  41.174  39.694  1.00 43.84           O  
ATOM   2505  CB  ILE A 322      40.143  42.502  36.647  1.00 42.39           C  
ATOM   2506  CG1 ILE A 322      40.915  42.649  35.335  1.00 42.41           C  
ATOM   2507  CG2 ILE A 322      40.514  43.633  37.572  1.00 41.14           C  
ATOM   2508  CD1 ILE A 322      42.423  42.743  35.519  1.00 43.23           C  
ATOM   2509  N   GLU A 323      38.354  40.852  38.445  1.00 42.65           N  
ATOM   2510  CA  GLU A 323      37.455  40.707  39.586  1.00 43.11           C  
ATOM   2511  C   GLU A 323      37.897  39.558  40.510  1.00 43.75           C  
ATOM   2512  O   GLU A 323      37.893  39.685  41.736  1.00 43.71           O  
ATOM   2513  CB  GLU A 323      36.013  40.450  39.096  1.00 42.85           C  
ATOM   2514  CG  GLU A 323      35.363  41.626  38.318  1.00 43.95           C  
ATOM   2515  CD  GLU A 323      33.936  41.352  37.780  1.00 44.30           C  
ATOM   2516  OE1 GLU A 323      32.986  41.114  38.566  1.00 44.09           O  
ATOM   2517  OE2 GLU A 323      33.762  41.393  36.546  1.00 44.37           O  
ATOM   2518  N   LYS A 324      38.270  38.430  39.909  1.00 45.97           N  
ATOM   2519  CA  LYS A 324      38.705  37.257  40.662  1.00 46.36           C  
ATOM   2520  C   LYS A 324      39.948  37.524  41.463  1.00 47.18           C  
ATOM   2521  O   LYS A 324      39.984  37.264  42.658  1.00 47.47           O  
ATOM   2522  CB  LYS A 324      38.950  36.070  39.724  1.00 46.47           C  
ATOM   2523  CG  LYS A 324      37.817  35.069  39.773  1.00 49.40           C  
ATOM   2524  CD  LYS A 324      37.323  34.616  38.390  1.00 51.22           C  
ATOM   2525  CE  LYS A 324      38.236  33.590  37.713  1.00 53.37           C  
ATOM   2526  NZ  LYS A 324      37.599  32.957  36.505  1.00 52.95           N  
ATOM   2527  N   MET A 325      40.963  38.052  40.797  1.00 48.52           N  
ATOM   2528  CA  MET A 325      42.222  38.344  41.461  1.00 52.33           C  
ATOM   2529  C   MET A 325      42.143  39.475  42.471  1.00 51.59           C  
ATOM   2530  O   MET A 325      42.844  39.472  43.477  1.00 51.75           O  
ATOM   2531  CB  MET A 325      43.297  38.640  40.429  1.00 56.53           C  
ATOM   2532  CG  MET A 325      43.652  37.418  39.606  1.00 64.53           C  
ATOM   2533  SD  MET A 325      45.076  37.689  38.537  1.00 74.82           S  
ATOM   2534  CE  MET A 325      45.353  35.925  37.771  1.00 72.82           C  
ATOM   2535  N   LEU A 326      41.301  40.452  42.200  1.00 50.94           N  
ATOM   2536  CA  LEU A 326      41.141  41.550  43.130  1.00 49.74           C  
ATOM   2537  C   LEU A 326      40.471  41.043  44.422  1.00 49.42           C  
ATOM   2538  O   LEU A 326      40.773  41.507  45.508  1.00 50.16           O  
ATOM   2539  CB  LEU A 326      40.297  42.633  42.478  1.00 49.80           C  
ATOM   2540  CG  LEU A 326      40.295  43.996  43.150  1.00 50.04           C  
ATOM   2541  CD1 LEU A 326      41.731  44.462  43.311  1.00 51.00           C  
ATOM   2542  CD2 LEU A 326      39.486  44.972  42.306  1.00 48.68           C  
ATOM   2543  N   GLY A 327      39.556  40.090  44.301  1.00 49.29           N  
ATOM   2544  CA  GLY A 327      38.910  39.573  45.492  1.00 48.30           C  
ATOM   2545  C   GLY A 327      39.881  38.724  46.298  1.00 49.34           C  
ATOM   2546  O   GLY A 327      39.654  38.467  47.481  1.00 50.09           O  
ATOM   2547  N   GLU A 328      40.959  38.277  45.652  1.00 50.70           N  
ATOM   2548  CA  GLU A 328      41.973  37.441  46.315  1.00 51.63           C  
ATOM   2549  C   GLU A 328      42.893  38.326  47.112  1.00 49.93           C  
ATOM   2550  O   GLU A 328      43.151  38.085  48.287  1.00 49.56           O  
ATOM   2551  CB  GLU A 328      42.831  36.681  45.297  1.00 56.81           C  
ATOM   2552  CG  GLU A 328      42.137  35.529  44.578  1.00 65.92           C  
ATOM   2553  CD  GLU A 328      41.747  34.394  45.512  1.00 70.83           C  
ATOM   2554  OE1 GLU A 328      42.111  34.447  46.712  1.00 74.48           O  
ATOM   2555  OE2 GLU A 328      41.088  33.433  45.045  1.00 73.43           O  
ATOM   2556  N   ALA A 329      43.395  39.346  46.428  1.00 47.95           N  
ATOM   2557  CA  ALA A 329      44.290  40.310  47.022  1.00 47.05           C  
ATOM   2558  C   ALA A 329      43.666  40.960  48.249  1.00 47.32           C  
ATOM   2559  O   ALA A 329      44.292  41.011  49.301  1.00 48.10           O  
ATOM   2560  CB  ALA A 329      44.639  41.357  46.011  1.00 45.17           C  
ATOM   2561  N   LEU A 330      42.441  41.461  48.116  1.00 46.66           N  
ATOM   2562  CA  LEU A 330      41.762  42.110  49.236  1.00 46.56           C  
ATOM   2563  C   LEU A 330      41.310  41.121  50.308  1.00 47.84           C  
ATOM   2564  O   LEU A 330      40.918  41.514  51.410  1.00 47.71           O  
ATOM   2565  CB  LEU A 330      40.544  42.881  48.732  1.00 45.25           C  
ATOM   2566  CG  LEU A 330      40.801  43.936  47.661  1.00 45.89           C  
ATOM   2567  CD1 LEU A 330      39.480  44.584  47.275  1.00 45.70           C  
ATOM   2568  CD2 LEU A 330      41.788  44.974  48.186  1.00 45.28           C  
ATOM   2569  N   GLY A 331      41.361  39.836  49.971  1.00 49.99           N  
ATOM   2570  CA  GLY A 331      40.947  38.802  50.907  1.00 52.87           C  
ATOM   2571  C   GLY A 331      39.466  38.884  51.237  1.00 54.48           C  
ATOM   2572  O   GLY A 331      38.973  38.243  52.170  1.00 56.05           O  
ATOM   2573  N   ASN A 332      38.750  39.674  50.452  1.00 55.82           N  
ATOM   2574  CA  ASN A 332      37.338  39.850  50.680  1.00 56.67           C  
ATOM   2575  C   ASN A 332      36.648  40.332  49.426  1.00 55.80           C  
ATOM   2576  O   ASN A 332      36.881  41.441  48.952  1.00 57.08           O  
ATOM   2577  CB  ASN A 332      37.120  40.858  51.799  1.00 59.50           C  
ATOM   2578  CG  ASN A 332      35.665  41.196  51.989  1.00 62.86           C  
ATOM   2579  OD1 ASN A 332      34.812  40.306  52.090  1.00 64.47           O  
ATOM   2580  ND2 ASN A 332      35.365  42.486  52.053  1.00 63.84           N  
ATOM   2581  N   PRO A 333      35.771  39.496  48.876  1.00 54.01           N  
ATOM   2582  CA  PRO A 333      35.037  39.839  47.660  1.00 53.78           C  
ATOM   2583  C   PRO A 333      34.103  41.028  47.821  1.00 53.63           C  
ATOM   2584  O   PRO A 333      33.677  41.641  46.845  1.00 53.40           O  
ATOM   2585  CB  PRO A 333      34.293  38.552  47.355  1.00 52.96           C  
ATOM   2586  CG  PRO A 333      34.028  38.007  48.711  1.00 52.16           C  
ATOM   2587  CD  PRO A 333      35.344  38.190  49.396  1.00 53.14           C  
ATOM   2588  N   GLN A 334      33.787  41.362  49.058  1.00 55.26           N  
ATOM   2589  CA  GLN A 334      32.881  42.465  49.325  1.00 56.66           C  
ATOM   2590  C   GLN A 334      33.509  43.827  49.012  1.00 55.79           C  
ATOM   2591  O   GLN A 334      32.802  44.762  48.635  1.00 56.48           O  
ATOM   2592  CB  GLN A 334      32.436  42.425  50.793  1.00 61.06           C  
ATOM   2593  CG  GLN A 334      32.052  41.025  51.322  1.00 68.21           C  
ATOM   2594  CD  GLN A 334      30.937  40.345  50.523  1.00 73.35           C  
ATOM   2595  OE1 GLN A 334      29.816  40.856  50.421  1.00 75.49           O  
ATOM   2596  NE2 GLN A 334      31.236  39.169  49.977  1.00 75.00           N  
ATOM   2597  N   GLU A 335      34.832  43.927  49.151  1.00 54.63           N  
ATOM   2598  CA  GLU A 335      35.539  45.184  48.910  1.00 53.09           C  
ATOM   2599  C   GLU A 335      35.928  45.400  47.452  1.00 51.01           C  
ATOM   2600  O   GLU A 335      36.430  46.461  47.081  1.00 50.14           O  
ATOM   2601  CB  GLU A 335      36.791  45.256  49.790  1.00 55.76           C  
ATOM   2602  CG  GLU A 335      37.532  46.586  49.669  1.00 59.16           C  
ATOM   2603  CD  GLU A 335      38.632  46.750  50.695  1.00 62.05           C  
ATOM   2604  OE1 GLU A 335      39.318  47.793  50.640  1.00 62.53           O  
ATOM   2605  OE2 GLU A 335      38.805  45.853  51.554  1.00 61.49           O  
ATOM   2606  N   VAL A 336      35.697  44.382  46.636  1.00 48.97           N  
ATOM   2607  CA  VAL A 336      36.005  44.467  45.222  1.00 46.51           C  
ATOM   2608  C   VAL A 336      35.357  45.712  44.616  1.00 45.00           C  
ATOM   2609  O   VAL A 336      35.997  46.475  43.898  1.00 43.59           O  
ATOM   2610  CB  VAL A 336      35.504  43.202  44.502  1.00 46.54           C  
ATOM   2611  CG1 VAL A 336      35.658  43.346  43.006  1.00 46.13           C  
ATOM   2612  CG2 VAL A 336      36.286  41.996  44.991  1.00 46.51           C  
ATOM   2613  N   GLY A 337      34.088  45.934  44.921  1.00 43.69           N  
ATOM   2614  CA  GLY A 337      33.429  47.100  44.365  1.00 43.12           C  
ATOM   2615  C   GLY A 337      34.032  48.427  44.786  1.00 42.86           C  
ATOM   2616  O   GLY A 337      34.367  49.269  43.953  1.00 44.23           O  
ATOM   2617  N   PRO A 338      34.177  48.659  46.092  1.00 42.08           N  
ATOM   2618  CA  PRO A 338      34.743  49.912  46.588  1.00 41.35           C  
ATOM   2619  C   PRO A 338      36.072  50.270  45.957  1.00 41.96           C  
ATOM   2620  O   PRO A 338      36.321  51.424  45.618  1.00 43.07           O  
ATOM   2621  CB  PRO A 338      34.880  49.654  48.074  1.00 41.26           C  
ATOM   2622  CG  PRO A 338      33.708  48.778  48.346  1.00 40.82           C  
ATOM   2623  CD  PRO A 338      33.744  47.803  47.208  1.00 40.89           C  
ATOM   2624  N   LEU A 339      36.932  49.275  45.798  1.00 41.66           N  
ATOM   2625  CA  LEU A 339      38.235  49.534  45.228  1.00 41.95           C  
ATOM   2626  C   LEU A 339      38.179  49.920  43.756  1.00 40.45           C  
ATOM   2627  O   LEU A 339      38.958  50.744  43.290  1.00 40.93           O  
ATOM   2628  CB  LEU A 339      39.126  48.318  45.410  1.00 43.44           C  
ATOM   2629  CG  LEU A 339      40.601  48.641  45.192  1.00 45.09           C  
ATOM   2630  CD1 LEU A 339      41.069  49.641  46.245  1.00 45.40           C  
ATOM   2631  CD2 LEU A 339      41.408  47.373  45.274  1.00 46.45           C  
ATOM   2632  N   LEU A 340      37.255  49.316  43.025  1.00 39.47           N  
ATOM   2633  CA  LEU A 340      37.111  49.622  41.616  1.00 37.48           C  
ATOM   2634  C   LEU A 340      36.624  51.044  41.445  1.00 37.63           C  
ATOM   2635  O   LEU A 340      37.102  51.766  40.578  1.00 38.18           O  
ATOM   2636  CB  LEU A 340      36.139  48.647  40.951  1.00 36.70           C  
ATOM   2637  CG  LEU A 340      36.633  47.210  40.782  1.00 35.33           C  
ATOM   2638  CD1 LEU A 340      35.522  46.364  40.224  1.00 32.15           C  
ATOM   2639  CD2 LEU A 340      37.814  47.182  39.843  1.00 32.56           C  
ATOM   2640  N   ASN A 341      35.671  51.458  42.268  1.00 38.94           N  
ATOM   2641  CA  ASN A 341      35.177  52.829  42.159  1.00 40.46           C  
ATOM   2642  C   ASN A 341      36.268  53.820  42.537  1.00 40.50           C  
ATOM   2643  O   ASN A 341      36.407  54.871  41.912  1.00 41.31           O  
ATOM   2644  CB  ASN A 341      33.958  53.047  43.049  1.00 42.44           C  
ATOM   2645  CG  ASN A 341      32.702  52.409  42.493  1.00 45.21           C  
ATOM   2646  OD1 ASN A 341      32.191  52.826  41.448  1.00 45.73           O  
ATOM   2647  ND2 ASN A 341      32.204  51.388  43.176  1.00 46.50           N  
ATOM   2648  N   THR A 342      37.046  53.476  43.564  1.00 40.82           N  
ATOM   2649  CA  THR A 342      38.143  54.315  44.038  1.00 40.02           C  
ATOM   2650  C   THR A 342      39.152  54.512  42.911  1.00 40.53           C  
ATOM   2651  O   THR A 342      39.769  55.571  42.781  1.00 42.61           O  
ATOM   2652  CB  THR A 342      38.873  53.660  45.227  1.00 40.51           C  
ATOM   2653  OG1 THR A 342      37.992  53.591  46.349  1.00 41.30           O  
ATOM   2654  CG2 THR A 342      40.098  54.454  45.611  1.00 38.73           C  
ATOM   2655  N   MET A 343      39.300  53.476  42.093  1.00 40.05           N  
ATOM   2656  CA  MET A 343      40.229  53.470  40.984  1.00 38.91           C  
ATOM   2657  C   MET A 343      39.799  54.337  39.808  1.00 38.86           C  
ATOM   2658  O   MET A 343      40.631  54.955  39.141  1.00 38.64           O  
ATOM   2659  CB  MET A 343      40.389  52.042  40.497  1.00 39.81           C  
ATOM   2660  CG  MET A 343      41.807  51.542  40.484  1.00 42.41           C  
ATOM   2661  SD  MET A 343      41.915  50.051  39.499  1.00 42.91           S  
ATOM   2662  CE  MET A 343      40.897  48.981  40.456  1.00 44.57           C  
ATOM   2663  N   ILE A 344      38.491  54.377  39.565  1.00 38.94           N  
ATOM   2664  CA  ILE A 344      37.917  55.100  38.435  1.00 39.83           C  
ATOM   2665  C   ILE A 344      37.411  56.526  38.644  1.00 38.66           C  
ATOM   2666  O   ILE A 344      37.555  57.374  37.754  1.00 36.86           O  
ATOM   2667  CB  ILE A 344      36.782  54.276  37.853  1.00 41.82           C  
ATOM   2668  CG1 ILE A 344      37.373  52.991  37.293  1.00 44.88           C  
ATOM   2669  CG2 ILE A 344      36.063  55.020  36.751  1.00 43.38           C  
ATOM   2670  CD1 ILE A 344      36.363  51.920  37.003  1.00 48.11           C  
ATOM   2671  N   LYS A 345      36.796  56.778  39.793  1.00 39.06           N  
ATOM   2672  CA  LYS A 345      36.243  58.095  40.074  1.00 39.97           C  
ATOM   2673  C   LYS A 345      37.236  59.221  39.888  1.00 39.59           C  
ATOM   2674  O   LYS A 345      38.269  59.269  40.552  1.00 39.40           O  
ATOM   2675  CB  LYS A 345      35.688  58.157  41.494  1.00 41.43           C  
ATOM   2676  CG  LYS A 345      34.429  57.361  41.717  1.00 42.26           C  
ATOM   2677  CD  LYS A 345      33.952  57.440  43.176  1.00 46.23           C  
ATOM   2678  CE  LYS A 345      34.937  56.777  44.161  1.00 50.45           C  
ATOM   2679  NZ  LYS A 345      34.445  56.612  45.583  1.00 52.06           N  
ATOM   2680  N   GLY A 346      36.884  60.132  38.988  1.00 41.22           N  
ATOM   2681  CA  GLY A 346      37.705  61.291  38.700  1.00 42.11           C  
ATOM   2682  C   GLY A 346      39.019  60.988  38.002  1.00 43.26           C  
ATOM   2683  O   GLY A 346      39.869  61.874  37.881  1.00 45.15           O  
ATOM   2684  N   ARG A 347      39.198  59.752  37.541  1.00 42.43           N  
ATOM   2685  CA  ARG A 347      40.431  59.378  36.872  1.00 40.13           C  
ATOM   2686  C   ARG A 347      40.160  58.703  35.543  1.00 41.06           C  
ATOM   2687  O   ARG A 347      40.843  58.973  34.562  1.00 43.17           O  
ATOM   2688  CB  ARG A 347      41.253  58.424  37.733  1.00 38.23           C  
ATOM   2689  CG  ARG A 347      41.492  58.877  39.160  1.00 36.93           C  
ATOM   2690  CD  ARG A 347      42.795  58.278  39.693  1.00 37.37           C  
ATOM   2691  NE  ARG A 347      42.859  56.819  39.594  1.00 40.78           N  
ATOM   2692  CZ  ARG A 347      43.935  56.126  39.210  1.00 38.70           C  
ATOM   2693  NH1 ARG A 347      43.881  54.809  39.165  1.00 40.31           N  
ATOM   2694  NH2 ARG A 347      45.053  56.742  38.851  1.00 38.01           N  
ATOM   2695  N   TYR A 348      39.167  57.824  35.499  1.00 41.35           N  
ATOM   2696  CA  TYR A 348      38.892  57.146  34.243  1.00 41.72           C  
ATOM   2697  C   TYR A 348      37.502  57.381  33.682  1.00 43.41           C  
ATOM   2698  O   TYR A 348      37.160  56.856  32.633  1.00 44.19           O  
ATOM   2699  CB  TYR A 348      39.133  55.644  34.398  1.00 39.60           C  
ATOM   2700  CG  TYR A 348      40.595  55.247  34.423  1.00 38.07           C  
ATOM   2701  CD1 TYR A 348      41.374  55.301  33.265  1.00 37.26           C  
ATOM   2702  CD2 TYR A 348      41.210  54.833  35.605  1.00 37.30           C  
ATOM   2703  CE1 TYR A 348      42.728  54.952  33.285  1.00 35.74           C  
ATOM   2704  CE2 TYR A 348      42.565  54.485  35.634  1.00 36.81           C  
ATOM   2705  CZ  TYR A 348      43.317  54.548  34.468  1.00 36.08           C  
ATOM   2706  OH  TYR A 348      44.656  54.213  34.470  1.00 36.20           O  
ATOM   2707  N   ASN A 349      36.706  58.183  34.363  1.00 45.87           N  
ATOM   2708  CA  ASN A 349      35.362  58.421  33.871  1.00 48.72           C  
ATOM   2709  C   ASN A 349      35.143  59.878  33.487  1.00 49.94           C  
ATOM   2710  O   ASN A 349      35.867  60.762  33.941  1.00 52.03           O  
ATOM   2711  CB  ASN A 349      34.356  58.002  34.934  1.00 49.06           C  
ATOM   2712  CG  ASN A 349      34.571  58.725  36.239  1.00 51.13           C  
ATOM   2713  OD1 ASN A 349      35.377  59.650  36.323  1.00 51.71           O  
ATOM   2714  ND2 ASN A 349      33.852  58.306  37.271  1.00 52.24           N  
ATOM   2715  OXT ASN A 349      34.228  60.155  32.713  1.00 53.85           O  
TER    2716      ASN A 349                                                      
HETATM 2767  O   HOH A1001      30.969  28.512  42.237  1.00 61.06           O  
HETATM 2768  O   HOH A1002      26.825   8.521  30.108  1.00 52.29           O  
HETATM 2769  O   HOH A1003      27.257  30.854  26.286  1.00 39.94           O  
HETATM 2770  O   HOH A1004      17.540  39.159  37.404  1.00 38.55           O  
HETATM 2771  O   HOH A1005      26.040  15.234  39.636  1.00 43.38           O  
HETATM 2772  O   HOH A1006      38.228  30.181  39.285  1.00 62.10           O  
HETATM 2773  O   HOH A1007      28.980  37.804  36.104  1.00 32.38           O  
HETATM 2774  O   HOH A1008      18.919  56.736  28.428  1.00 41.39           O  
HETATM 2775  O   HOH A1009      31.049  39.640  19.727  1.00 37.99           O  
HETATM 2776  O   HOH A1010      27.304  38.654  15.248  1.00 60.98           O  
HETATM 2777  O   HOH A1011      16.408  47.202  22.341  1.00 38.01           O  
HETATM 2778  O   HOH A1012      31.820  35.893  16.981  1.00 53.79           O  
HETATM 2779  O   HOH A1013      32.919  39.860  34.290  1.00 32.52           O  
HETATM 2780  O   HOH A1014      15.662  43.062   7.973  1.00 73.41           O  
HETATM 2781  O   HOH A1015      15.316  38.296  35.982  1.00 54.20           O  
HETATM 2782  O   HOH A1016      36.362  11.690  21.493  1.00 48.73           O  
HETATM 2783  O   HOH A1017      17.130  38.707  33.167  1.00 56.37           O  
HETATM 2784  O   HOH A1018      34.725  16.377   8.183  1.00 67.57           O  
HETATM 2785  O   HOH A1019       7.390  36.257   9.590  1.00 70.25           O  
HETATM 2786  O   HOH A1020      15.870  52.289  40.004  1.00 47.63           O  
HETATM 2787  O   HOH A1021       5.489  12.633  28.071  1.00 35.37           O  
HETATM 2788  O   HOH A1022      30.084  37.090  27.837  1.00 50.13           O  
HETATM 2789  O   HOH A1023      13.993  24.179   7.476  1.00 51.95           O  
HETATM 2790  O   HOH A1024       3.990  32.724  35.626  1.00 52.82           O  
HETATM 2791  O   HOH A1025      11.068  19.546  14.440  1.00 57.18           O  
HETATM 2792  O   HOH A1026      28.973  47.531  20.022  1.00 35.31           O  
HETATM 2793  O   HOH A1027      12.037  33.352  14.763  1.00 68.30           O  
HETATM 2794  O   HOH A1028      17.590  30.424   7.714  1.00 60.56           O  
HETATM 2795  O   HOH A1029       7.276  16.965  20.543  1.00 49.30           O  
HETATM 2796  O   HOH A1030      31.616  41.170  44.785  1.00 40.66           O  
HETATM 2797  O   HOH A1031      15.120  51.491  22.443  1.00 43.41           O  
HETATM 2798  O   HOH A1032      15.574  30.848  12.942  1.00 52.26           O  
HETATM 2799  O   HOH A1033      38.486  61.225  34.048  1.00 61.16           O  
HETATM 2800  O   HOH A1034      29.010  39.529  27.212  1.00 37.78           O  
HETATM 2801  O   HOH A1035      20.053  18.264  13.766  1.00 40.84           O  
HETATM 2802  O   HOH A1036      17.941  17.218  18.182  1.00 33.63           O  
HETATM 2803  O   HOH A1037      32.820  40.054  42.783  1.00 33.35           O  
HETATM 2804  O   HOH A1038      27.973  28.376  25.176  1.00 34.06           O  
HETATM 2805  O   HOH A1039      33.312  37.748  20.831  1.00 40.10           O  
HETATM 2806  O   HOH A1040      26.291  31.763  38.918  1.00 38.76           O  
HETATM 2807  O   HOH A1041      25.732  51.572  31.366  1.00 55.25           O  
HETATM 2808  O   HOH A1042      15.325  18.898  12.231  1.00 54.88           O  
HETATM 2809  O   HOH A1043      26.382  13.461  38.008  1.00 54.89           O  
HETATM 2810  O   HOH A1044      38.084  49.024  54.061  1.00 45.94           O  
HETATM 2811  O   HOH A1045      23.914  27.497  31.205  1.00 41.96           O  
HETATM 2812  O   HOH A1046      12.847  36.075  14.321  1.00 45.82           O  
HETATM 2813  O   HOH A1047      11.408  21.770  13.714  1.00 49.47           O  
HETATM 2814  O   HOH A1048      28.829   8.807  31.620  1.00 57.41           O  
HETATM 2815  O   HOH A1049      28.397  16.800  37.561  1.00 66.42           O  
HETATM 2816  O   HOH A1050      28.703  14.161  37.568  1.00 76.91           O  
HETATM 2817  O   HOH A1051      38.388  50.293  49.301  1.00 58.80           O  
HETATM 2818  O   HOH A1052       7.289  12.450  22.312  1.00 56.08           O  
HETATM 2819  O   HOH A1053      42.866  35.577  49.786  1.00 45.09           O  
HETATM 2820  O   HOH A1054      13.524  41.578   7.576  1.00 61.83           O  
HETATM 2821  O   HOH A1055       8.134   5.928  24.219  1.00 60.13           O  
HETATM 2822  O   HOH A1056      18.583  26.917  37.235  1.00 36.72           O  
HETATM 2823  O   HOH A1057      19.815  32.077  34.590  1.00 34.48           O  
HETATM 2824  O   HOH A1058      28.235  27.281  33.000  1.00 45.83           O  
HETATM 2825  O   HOH A1059      11.221  48.758  36.849  1.00 64.13           O  
HETATM 2826  O   HOH A1060      35.794  49.749  51.792  1.00 48.50           O  
HETATM 2827  O   HOH A1061      36.187  14.946  24.610  1.00 63.87           O  
HETATM 2828  O   HOH A1062      10.948  13.732  19.466  1.00 41.46           O  
HETATM 2829  O   HOH A1063      49.054  40.581  16.581  1.00 61.06           O  
HETATM 2830  O   HOH A1064       3.653  33.461  32.839  1.00 60.11           O  
HETATM 2831  O   HOH A1065      12.681  39.853  12.150  1.00 63.71           O  
HETATM 2832  O   HOH A1066      14.534  26.606  14.257  1.00 49.23           O  
HETATM 2833  O   HOH A1067      19.312  14.950  16.800  1.00 40.90           O  
HETATM 2834  O   HOH A1068       4.750   5.905  24.076  1.00 72.39           O  
HETATM 2835  O   HOH A1069      15.479  27.373  48.474  1.00 57.64           O  
HETATM 2836  O   HOH A1070      38.230  13.715  25.290  1.00 52.59           O  
HETATM 2837  O   HOH A1071      17.532  27.975  35.440  1.00 50.67           O  
HETATM 2838  O   HOH A1072      16.254  36.438  30.274  1.00 43.97           O  
HETATM 2839  O   HOH A1073      30.403  38.803  33.974  1.00 40.43           O  
HETATM 2840  O   HOH A1074      26.069  27.244  26.433  1.00 35.57           O  
HETATM 2841  O   HOH A1075      23.533  46.839  20.727  1.00 50.38           O  
HETATM 2842  O   HOH A1076      18.859  53.948  39.930  1.00 79.11           O  
HETATM 2843  O   HOH A1077      38.596  29.999  23.733  1.00 57.51           O  
HETATM 2844  O   HOH A1078      34.177  39.767  18.480  1.00 39.54           O  
HETATM 2845  O   HOH A1079      41.536  43.961  52.009  1.00 45.29           O  
HETATM 2846  O   HOH A1080      13.192  26.554  29.282  1.00 54.88           O  
HETATM 2847  O   HOH A1081       6.618  24.003  25.807  1.00 45.03           O  
HETATM 2848  O   HOH A1082       7.487  31.069  26.103  1.00 59.00           O  
HETATM 2849  O   HOH A1083      14.445  37.997  32.699  1.00 53.38           O  
HETATM 2850  O   HOH A1084      29.437  30.842  36.299  1.00 46.18           O  
HETATM 2851  O   HOH A1085      31.422  46.831  19.629  1.00 49.79           O  
HETATM 2852  O   HOH A1086      27.341  45.056  31.654  1.00 41.69           O  
HETATM 2853  O   HOH A1087      13.742  21.168  28.509  1.00 41.80           O  
HETATM 2854  O   HOH A1088      19.004  15.544  13.155  1.00 47.93           O  
HETATM 2855  O   HOH A1089       3.467  13.592  26.226  1.00 62.95           O  
HETATM 2856  O   HOH A1090       5.221   9.901  28.641  1.00 51.58           O  
CONECT 1490 2717                                                                
CONECT 1510 2717                                                                
CONECT 2179 2717                                                                
CONECT 2717 1490 1510 2179 2746                                                 
CONECT 2717 2749 2811                                                           
CONECT 2718 2719 2720 2721 2722                                                 
CONECT 2719 2718                                                                
CONECT 2720 2718                                                                
CONECT 2721 2718                                                                
CONECT 2722 2718                                                                
CONECT 2723 2724 2725 2726 2727                                                 
CONECT 2724 2723                                                                
CONECT 2725 2723                                                                
CONECT 2726 2723                                                                
CONECT 2727 2723                                                                
CONECT 2728 2729 2730 2731 2732                                                 
CONECT 2729 2728                                                                
CONECT 2730 2728                                                                
CONECT 2731 2728                                                                
CONECT 2732 2728                                                                
CONECT 2733 2734 2738                                                           
CONECT 2734 2733 2735                                                           
CONECT 2735 2734 2736                                                           
CONECT 2736 2735 2737                                                           
CONECT 2737 2736 2738                                                           
CONECT 2738 2733 2737 2739                                                      
CONECT 2739 2738 2740                                                           
CONECT 2740 2739 2741 2744                                                      
CONECT 2741 2740 2742 2743                                                      
CONECT 2742 2741                                                                
CONECT 2743 2741                                                                
CONECT 2744 2740 2745                                                           
CONECT 2745 2744 2746 2747                                                      
CONECT 2746 2717 2745                                                           
CONECT 2747 2745 2748 2749                                                      
CONECT 2748 2747                                                                
CONECT 2749 2717 2747                                                           
CONECT 2750 2751 2755                                                           
CONECT 2751 2750 2752                                                           
CONECT 2752 2751 2753                                                           
CONECT 2753 2752 2754                                                           
CONECT 2754 2753 2755                                                           
CONECT 2755 2750 2754 2756                                                      
CONECT 2756 2755 2757                                                           
CONECT 2757 2756 2758 2761                                                      
CONECT 2758 2757 2759 2760                                                      
CONECT 2759 2758                                                                
CONECT 2760 2758                                                                
CONECT 2761 2757 2762                                                           
CONECT 2762 2761 2763 2764                                                      
CONECT 2763 2762                                                                
CONECT 2764 2762 2765 2766                                                      
CONECT 2765 2764                                                                
CONECT 2766 2764                                                                
CONECT 2811 2717                                                                
MASTER      376    0    6   15   14    0   12    6 2855    1   55   27          
END                                                                             


A second structure was input as follows:


HEADER    TRANSCRIPTION REGULATOR, OXIDOREDUCTASE 22-DEC-04   1YCI              
TITLE     FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH N-(CARBOXYCARBONYL)-D-  
TITLE    2 PHENYLALANINE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA INHIBITOR;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HYPOXIA- INDUCIBLE FACTOR ASPARAGINE HYDROXYLASE, FACTOR    
COMPND   5 INHIBITING HIF-1, FIH-1;                                             
COMPND   6 EC: 1.14.11.16;                                                      
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: HIF1AN;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    FIH, HIF, DSBH, OXYGENASE, TRANSCRIPTION, HYPOXIA, INHIBITOR 2-       
KEYWDS   2 OXOGLUTARATE, ASPARAGINYL HYDROXYLASE, HYDROXYLASE N-                
KEYWDS   3 (CARBOXYCARBONYL)-D-PHENYLALANINE, NOFD, NDF, TRANSCRIPTION          
KEYWDS   4 REGULATOR, OXIDOREDUCTASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.MCDONOUGH,C.J.SCHOFIELD                                           
REVDAT   3   13-JUL-11 1YCI    1       VERSN                                    
REVDAT   2   24-FEB-09 1YCI    1       VERSN                                    
REVDAT   1   31-MAY-05 1YCI    0                                                
JRNL        AUTH   M.A.MCDONOUGH,L.A.MCNEILL,M.TILLIET,C.A.PAPAMICAEL,Q.Y.CHEN, 
JRNL        AUTH 2 B.BANERJI,K.S.HEWITSON,C.J.SCHOFIELD                         
JRNL        TITL   SELECTIVE INHIBITION OF FACTOR INHIBITING HYPOXIA-INDUCIBLE  
JRNL        TITL 2 FACTOR                                                       
JRNL        REF    J.AM.CHEM.SOC.                V. 127  7680 2005              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   15913349                                                     
JRNL        DOI    10.1021/JA050841B                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.M.ELKINS,K.S.HEWITSON,L.A.MCNEILL,J.F.SEIBEL,              
REMARK   1  AUTH 2 I.SCHLEMMINGER,C.W.PUGH,P.J.RATCLIFFE,C.J.SCHOFIELD          
REMARK   1  TITL   STRUCTURE OF FACTOR-INHIBITING HYPOXIA-INDUCIBLE FACTOR      
REMARK   1  TITL 2 (HIF) REVEALS MECHANISM OF OXIDATIVE MODIFICATION OF HIF-1   
REMARK   1  TITL 3 ALPHA                                                        
REMARK   1  REF    J.BIOL.CHEM.                  V. 278  1802 2003              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   12446723                                                     
REMARK   1  DOI    10.1074/JBC.C200644200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 15709                          
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) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1589                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.80                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1263                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE                    : 0.4160                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 137                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2715                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 90                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 53.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.89000                                             
REMARK   3    B22 (A**2) : -6.89000                                             
REMARK   3    B33 (A**2) : 13.79000                                             
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
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) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
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) : 1.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.880 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.070 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 58.91                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DOP.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : DOP.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1YCI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB031376.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(III)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16510                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS WITH 1H2N        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1H2N                                                 
REMARK 200                                                                      
REMARK 200 REMARK: REJECTION CRITERIA AS REJECTION PROBABILITY, REJECTION       
REMARK 200  CRITERIA (PROBABILITY)) : 0.0001                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M AMMONIUM SULPHATE, 4% PEG400,       
REMARK 280  0.1M HEPES PH7.5 ARGON ATMOSPHERE, 28MG/ML PROTEIN WITH 1MM         
REMARK 280  FE(II), 10MM N-(CARBOXYCARBONYL)-D-PHENYLALANINE, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.25950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.42650            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       37.62975            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.42650            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      112.88925            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.42650            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       37.62975            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.42650            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.42650            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      112.88925            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.25950            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
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 350   BIOMT1   2  0.000000 -1.000000  0.000000       86.85300            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       86.85300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       75.25950            
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  29    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 106    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     ARG A 117    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 119    CG   OD1                                            
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     GLN A 133    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 137    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 304    CB   CG   CD   CE   NZ                              
REMARK 470     ARG A 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 306    CG1  CG2  CD1                                       
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
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    SER A  30       -8.88    -56.61                                   
REMARK 500    ASP A  66       43.41   -140.18                                   
REMARK 500    ILE A  85        6.03    -61.20                                   
REMARK 500    TYR A 145      119.21   -163.83                                   
REMARK 500    ASN A 151     -144.72    -85.94                                   
REMARK 500    THR A 153       17.16    -68.79                                   
REMARK 500    PRO A 197      152.77    -44.96                                   
REMARK 500    TYR A 228       70.49     33.21                                   
REMARK 500    ARG A 238        0.42     82.14                                   
REMARK 500    PHE A 252       65.11   -113.33                                   
REMARK 500    LEU A 284      138.83    -38.26                                   
REMARK 500    PRO A 303      -18.05    -43.87                                   
REMARK 500    ILE A 306      116.04    -33.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A1350  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 199   NE2                                                    
REMARK 620 2 ASP A 201   OD2 101.0                                              
REMARK 620 3 HIS A 279   NE2  85.1  83.5                                        
REMARK 620 4 NDF A 400   O2'  95.2 162.3 105.1                                  
REMARK 620 5 NDF A 400   O2  170.0  88.7  98.5  74.9                            
REMARK 620 6 HOH A1045   O    75.2  77.4 149.2 100.2 104.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDF A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDF A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H2K   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
REMARK 900 RELATED ID: 1H2L   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
REMARK 900 RELATED ID: 1H2N   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH AKG                    
REMARK 900 RELATED ID: 1H2M   RELATED DB: PDB                                   
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH HIF-1 ALPHA            
REMARK 900 FRAGMENT PEPTIDE                                                     
DBREF  1YCI A    1   349  UNP    Q9NWT6   HIF1N_HUMAN      1    349             
SEQRES   1 A  349  MET ALA ALA THR ALA ALA GLU ALA VAL ALA SER GLY SER          
SEQRES   2 A  349  GLY GLU PRO ARG GLU GLU ALA GLY ALA LEU GLY PRO ALA          
SEQRES   3 A  349  TRP ASP GLU SER GLN LEU ARG SER TYR SER PHE PRO THR          
SEQRES   4 A  349  ARG PRO ILE PRO ARG LEU SER GLN SER ASP PRO ARG ALA          
SEQRES   5 A  349  GLU GLU LEU ILE GLU ASN GLU GLU PRO VAL VAL LEU THR          
SEQRES   6 A  349  ASP THR ASN LEU VAL TYR PRO ALA LEU LYS TRP ASP LEU          
SEQRES   7 A  349  GLU TYR LEU GLN GLU ASN ILE GLY ASN GLY ASP PHE SER          
SEQRES   8 A  349  VAL TYR SER ALA SER THR HIS LYS PHE LEU TYR TYR ASP          
SEQRES   9 A  349  GLU LYS LYS MET ALA ASN PHE GLN ASN PHE LYS PRO ARG          
SEQRES  10 A  349  SER ASN ARG GLU GLU MET LYS PHE HIS GLU PHE VAL GLU          
SEQRES  11 A  349  LYS LEU GLN ASP ILE GLN GLN ARG GLY GLY GLU GLU ARG          
SEQRES  12 A  349  LEU TYR LEU GLN GLN THR LEU ASN ASP THR VAL GLY ARG          
SEQRES  13 A  349  LYS ILE VAL MET ASP PHE LEU GLY PHE ASN TRP ASN TRP          
SEQRES  14 A  349  ILE ASN LYS GLN GLN GLY LYS ARG GLY TRP GLY GLN LEU          
SEQRES  15 A  349  THR SER ASN LEU LEU LEU ILE GLY MET GLU GLY ASN VAL          
SEQRES  16 A  349  THR PRO ALA HIS TYR ASP GLU GLN GLN ASN PHE PHE ALA          
SEQRES  17 A  349  GLN ILE LYS GLY TYR LYS ARG CYS ILE LEU PHE PRO PRO          
SEQRES  18 A  349  ASP GLN PHE GLU CYS LEU TYR PRO TYR PRO VAL HIS HIS          
SEQRES  19 A  349  PRO CYS ASP ARG GLN SER GLN VAL ASP PHE ASP ASN PRO          
SEQRES  20 A  349  ASP TYR GLU ARG PHE PRO ASN PHE GLN ASN VAL VAL GLY          
SEQRES  21 A  349  TYR GLU THR VAL VAL GLY PRO GLY ASP VAL LEU TYR ILE          
SEQRES  22 A  349  PRO MET TYR TRP TRP HIS HIS ILE GLU SER LEU LEU ASN          
SEQRES  23 A  349  GLY GLY ILE THR ILE THR VAL ASN PHE TRP TYR LYS GLY          
SEQRES  24 A  349  ALA PRO THR PRO LYS ARG ILE GLU TYR PRO LEU LYS ALA          
SEQRES  25 A  349  HIS GLN LYS VAL ALA ILE MET ARG ASN ILE GLU LYS MET          
SEQRES  26 A  349  LEU GLY GLU ALA LEU GLY ASN PRO GLN GLU VAL GLY PRO          
SEQRES  27 A  349  LEU LEU ASN THR MET ILE LYS GLY ARG TYR ASN                  
HET    FE2  A1350       1                                                       
HET    SO4  A1352       5                                                       
HET    SO4  A1353       5                                                       
HET    SO4  A1354       5                                                       
HET    NDF  A 400      17                                                       
HET    NDF  A 401      17                                                       
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NDF N-(CARBOXYCARBONYL)-D-PHENYLALANINE                              
FORMUL   2  FE2    FE 2+                                                        
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  NDF    2(C11 H11 N O5)                                              
FORMUL   7  HOH   *90(H2 O)                                                     
HELIX    1   1 GLU A   19  LEU A   23  5                                   5    
HELIX    2   2 ASP A   28  LEU A   32  5                                   5    
HELIX    3   3 ASP A   49  ASN A   58  1                                  10    
HELIX    4   4 VAL A   70  TRP A   76  5                                   7    
HELIX    5   5 ASP A   77  ILE A   85  1                                   9    
HELIX    6   6 ASP A  104  MET A  108  5                                   5    
HELIX    7   7 LYS A  124  GLN A  137  1                                  14    
HELIX    8   8 GLY A  155  PHE A  165  1                                  11    
HELIX    9   9 ASN A  166  ARG A  177  1                                  12    
HELIX   10  10 PRO A  220  ASP A  222  5                                   3    
HELIX   11  11 GLN A  223  TYR A  228  1                                   6    
HELIX   12  12 PHE A  252  ASN A  257  5                                   6    
HELIX   13  13 LYS A  311  LEU A  330  1                                  20    
HELIX   14  14 ASN A  332  GLN A  334  5                                   3    
HELIX   15  15 GLU A  335  LYS A  345  1                                  11    
SHEET    1   A 5 THR A  39  PRO A  41  0                                        
SHEET    2   A 5 GLY A 260  VAL A 265  1  O  GLY A 260   N  ARG A  40           
SHEET    3   A 5 LYS A 214  PHE A 219 -1  N  LEU A 218   O  TYR A 261           
SHEET    4   A 5 TRP A 278  SER A 283 -1  O  GLU A 282   N  ARG A 215           
SHEET    5   A 5 VAL A 195  HIS A 199 -1  N  THR A 196   O  ILE A 281           
SHEET    1   B 9 ARG A  44  LEU A  45  0                                        
SHEET    2   B 9 VAL A  62  LEU A  64  1  O  VAL A  63   N  LEU A  45           
SHEET    3   B 9 VAL A 270  ILE A 273 -1  O  VAL A 270   N  LEU A  64           
SHEET    4   B 9 GLN A 203  LYS A 211 -1  N  PHE A 207   O  LEU A 271           
SHEET    5   B 9 THR A 290  LYS A 298 -1  O  ILE A 291   N  LYS A 211           
SHEET    6   B 9 LEU A 182  GLY A 190 -1  N  LEU A 188   O  THR A 292           
SHEET    7   B 9 ARG A 143  THR A 149 -1  N  LEU A 146   O  ILE A 189           
SHEET    8   B 9 PHE A  90  ALA A  95 -1  N  TYR A  93   O  TYR A 145           
SHEET    9   B 9 GLU A 122  MET A 123 -1  O  MET A 123   N  PHE A  90           
LINK        FE   FE2 A1350                 NE2 HIS A 199     1555   1555  2.32  
LINK        FE   FE2 A1350                 OD2 ASP A 201     1555   1555  2.22  
LINK        FE   FE2 A1350                 NE2 HIS A 279     1555   1555  2.36  
LINK        FE   FE2 A1350                 O2' NDF A 400     1555   1555  2.25  
LINK        FE   FE2 A1350                 O2  NDF A 400     1555   1555  2.24  
LINK        FE   FE2 A1350                 O   HOH A1045     1555   1555  2.01  
CISPEP   1 TYR A  308    PRO A  309          0         0.01                     
SITE     1 AC1  5 HIS A 199  ASP A 201  HIS A 279  NDF A 400                    
SITE     2 AC1  5 HOH A1045                                                     
SITE     1 AC2  4 ARG A 138  GLY A 140  GLU A 141  GLU A 142                    
SITE     1 AC3  5 ARG A 143  GLU A 192  GLY A 193  LEU A 285                    
SITE     2 AC3  5 ASN A 286                                                     
SITE     1 AC4  4 LYS A 107  ARG A 320  LYS A 324  HOH A1006                    
SITE     1 AC5 13 TYR A 145  LEU A 188  THR A 196  HIS A 199                    
SITE     2 AC5 13 ASP A 201  ASN A 205  PHE A 207  LYS A 214                    
SITE     3 AC5 13 HIS A 279  ILE A 281  ASN A 294  TRP A 296                    
SITE     4 AC5 13 FE2 A1350                                                     
SITE     1 AC6  6 PRO A 221  ASP A 222  PHE A 224  GLU A 225                    
SITE     2 AC6  6 LYS A 315  HOH A1085                                          
CRYST1   86.853   86.853  150.519  90.00  90.00  90.00 P 41 21 2     8          
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      0.011514  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011514  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006644        0.00000                         
ATOM      1  N   GLY A  14      11.516  34.414  12.463  1.00 98.47           N  
ATOM      2  CA  GLY A  14      10.786  34.075  11.200  1.00 98.16           C  
ATOM      3  C   GLY A  14       9.368  33.579  11.435  1.00 97.95           C  
ATOM      4  O   GLY A  14       8.896  33.568  12.574  1.00 98.33           O  
ATOM      5  N   GLU A  15       8.687  33.169  10.365  1.00 96.67           N  
ATOM      6  CA  GLU A  15       7.315  32.667  10.458  1.00 95.28           C  
ATOM      7  C   GLU A  15       7.276  31.178  10.838  1.00 94.06           C  
ATOM      8  O   GLU A  15       8.160  30.405  10.463  1.00 93.74           O  
ATOM      9  CB  GLU A  15       6.592  32.896   9.130  1.00 94.77           C  
ATOM     10  N   PRO A  16       6.244  30.759  11.594  1.00 92.65           N  
ATOM     11  CA  PRO A  16       6.098  29.363  12.026  1.00 91.64           C  
ATOM     12  C   PRO A  16       6.266  28.375  10.885  1.00 90.97           C  
ATOM     13  O   PRO A  16       5.539  28.429   9.890  1.00 91.31           O  
ATOM     14  CB  PRO A  16       4.692  29.327  12.608  1.00 91.51           C  
ATOM     15  CG  PRO A  16       4.536  30.694  13.170  1.00 90.98           C  
ATOM     16  CD  PRO A  16       5.129  31.579  12.097  1.00 91.69           C  
ATOM     17  N   ARG A  17       7.225  27.468  11.024  1.00 89.80           N  
ATOM     18  CA  ARG A  17       7.462  26.475   9.987  1.00 88.38           C  
ATOM     19  C   ARG A  17       6.283  25.510   9.896  1.00 87.28           C  
ATOM     20  O   ARG A  17       5.530  25.325  10.860  1.00 86.32           O  
ATOM     21  CB  ARG A  17       8.737  25.682  10.278  1.00 88.90           C  
ATOM     22  CG  ARG A  17      10.006  26.517  10.350  1.00 90.29           C  
ATOM     23  CD  ARG A  17      11.232  25.636  10.574  1.00 90.93           C  
ATOM     24  NE  ARG A  17      11.229  24.928  11.859  1.00 91.39           N  
ATOM     25  CZ  ARG A  17      11.363  25.504  13.056  1.00 91.65           C  
ATOM     26  NH1 ARG A  17      11.516  26.822  13.175  1.00 91.19           N  
ATOM     27  NH2 ARG A  17      11.354  24.749  14.147  1.00 90.73           N  
ATOM     28  N   GLU A  18       6.135  24.896   8.726  1.00 86.53           N  
ATOM     29  CA  GLU A  18       5.065  23.937   8.468  1.00 85.64           C  
ATOM     30  C   GLU A  18       5.527  22.498   8.629  1.00 83.89           C  
ATOM     31  O   GLU A  18       6.586  22.123   8.123  1.00 83.50           O  
ATOM     32  CB  GLU A  18       4.528  24.121   7.051  1.00 87.39           C  
ATOM     33  CG  GLU A  18       3.733  25.392   6.864  1.00 90.04           C  
ATOM     34  CD  GLU A  18       2.467  25.408   7.702  1.00 91.69           C  
ATOM     35  OE1 GLU A  18       1.865  26.495   7.836  1.00 92.04           O  
ATOM     36  OE2 GLU A  18       2.063  24.338   8.215  1.00 93.28           O  
ATOM     37  N   GLU A  19       4.730  21.692   9.324  1.00 81.94           N  
ATOM     38  CA  GLU A  19       5.066  20.288   9.523  1.00 80.36           C  
ATOM     39  C   GLU A  19       4.662  19.433   8.325  1.00 78.24           C  
ATOM     40  O   GLU A  19       3.625  19.678   7.694  1.00 77.73           O  
ATOM     41  CB  GLU A  19       4.392  19.747  10.775  1.00 81.90           C  
ATOM     42  CG  GLU A  19       5.089  20.107  12.056  1.00 84.95           C  
ATOM     43  CD  GLU A  19       4.558  19.292  13.194  1.00 88.17           C  
ATOM     44  OE1 GLU A  19       4.660  18.046  13.120  1.00 89.39           O  
ATOM     45  OE2 GLU A  19       4.027  19.889  14.155  1.00 89.70           O  
ATOM     46  N   ALA A  20       5.490  18.431   8.022  1.00 75.91           N  
ATOM     47  CA  ALA A  20       5.259  17.532   6.899  1.00 73.38           C  
ATOM     48  C   ALA A  20       3.925  16.851   7.084  1.00 72.56           C  
ATOM     49  O   ALA A  20       3.376  16.840   8.190  1.00 72.71           O  
ATOM     50  CB  ALA A  20       6.374  16.485   6.803  1.00 71.69           C  
ATOM     51  N   GLY A  21       3.407  16.286   5.996  1.00 71.14           N  
ATOM     52  CA  GLY A  21       2.129  15.609   6.055  1.00 69.26           C  
ATOM     53  C   GLY A  21       1.004  16.571   6.368  1.00 68.81           C  
ATOM     54  O   GLY A  21      -0.072  16.150   6.782  1.00 67.92           O  
ATOM     55  N   ALA A  22       1.264  17.865   6.176  1.00 69.19           N  
ATOM     56  CA  ALA A  22       0.288  18.925   6.421  1.00 69.04           C  
ATOM     57  C   ALA A  22      -0.370  18.828   7.800  1.00 69.25           C  
ATOM     58  O   ALA A  22      -1.594  18.900   7.922  1.00 69.72           O  
ATOM     59  CB  ALA A  22      -0.778  18.899   5.335  1.00 68.40           C  
ATOM     60  N   LEU A  23       0.442  18.677   8.841  1.00 69.21           N  
ATOM     61  CA  LEU A  23      -0.092  18.567  10.194  1.00 69.13           C  
ATOM     62  C   LEU A  23      -0.284  19.953  10.814  1.00 69.42           C  
ATOM     63  O   LEU A  23      -0.577  20.089  12.005  1.00 68.95           O  
ATOM     64  CB  LEU A  23       0.837  17.703  11.056  1.00 68.49           C  
ATOM     65  CG  LEU A  23       0.949  16.202  10.736  1.00 67.23           C  
ATOM     66  CD1 LEU A  23       2.105  15.602  11.548  1.00 66.85           C  
ATOM     67  CD2 LEU A  23      -0.377  15.490  11.041  1.00 63.10           C  
ATOM     68  N   GLY A  24      -0.131  20.977   9.982  1.00 70.34           N  
ATOM     69  CA  GLY A  24      -0.305  22.336  10.446  1.00 71.95           C  
ATOM     70  C   GLY A  24       0.979  22.947  10.965  1.00 73.02           C  
ATOM     71  O   GLY A  24       2.024  22.296  10.970  1.00 73.85           O  
ATOM     72  N   PRO A  25       0.927  24.214  11.409  1.00 73.44           N  
ATOM     73  CA  PRO A  25       2.110  24.899  11.931  1.00 72.76           C  
ATOM     74  C   PRO A  25       2.601  24.294  13.232  1.00 71.74           C  
ATOM     75  O   PRO A  25       1.808  23.910  14.096  1.00 70.30           O  
ATOM     76  CB  PRO A  25       1.623  26.334  12.111  1.00 73.32           C  
ATOM     77  CG  PRO A  25       0.179  26.140  12.475  1.00 73.04           C  
ATOM     78  CD  PRO A  25      -0.253  25.096  11.468  1.00 73.49           C  
ATOM     79  N   ALA A  26       3.917  24.216  13.367  1.00 70.76           N  
ATOM     80  CA  ALA A  26       4.515  23.667  14.559  1.00 71.02           C  
ATOM     81  C   ALA A  26       4.124  24.467  15.821  1.00 71.42           C  
ATOM     82  O   ALA A  26       3.936  23.894  16.901  1.00 72.10           O  
ATOM     83  CB  ALA A  26       6.021  23.632  14.382  1.00 70.00           C  
ATOM     84  N   TRP A  27       3.985  25.783  15.674  1.00 71.02           N  
ATOM     85  CA  TRP A  27       3.631  26.680  16.775  1.00 68.57           C  
ATOM     86  C   TRP A  27       3.094  27.978  16.184  1.00 68.60           C  
ATOM     87  O   TRP A  27       3.094  28.154  14.959  1.00 69.08           O  
ATOM     88  CB  TRP A  27       4.872  26.998  17.610  1.00 66.99           C  
ATOM     89  CG  TRP A  27       6.077  27.281  16.763  1.00 67.00           C  
ATOM     90  CD1 TRP A  27       6.873  26.361  16.132  1.00 67.98           C  
ATOM     91  CD2 TRP A  27       6.571  28.561  16.376  1.00 66.35           C  
ATOM     92  NE1 TRP A  27       7.836  26.997  15.367  1.00 67.58           N  
ATOM     93  CE2 TRP A  27       7.669  28.349  15.503  1.00 66.96           C  
ATOM     94  CE3 TRP A  27       6.192  29.873  16.679  1.00 65.38           C  
ATOM     95  CZ2 TRP A  27       8.385  29.400  14.938  1.00 67.08           C  
ATOM     96  CZ3 TRP A  27       6.905  30.914  16.115  1.00 65.86           C  
ATOM     97  CH2 TRP A  27       7.987  30.674  15.256  1.00 67.84           C  
ATOM     98  N   ASP A  28       2.638  28.886  17.041  1.00 68.37           N  
ATOM     99  CA  ASP A  28       2.129  30.166  16.564  1.00 67.81           C  
ATOM    100  C   ASP A  28       2.571  31.264  17.516  1.00 65.36           C  
ATOM    101  O   ASP A  28       2.750  31.029  18.709  1.00 64.17           O  
ATOM    102  CB  ASP A  28       0.601  30.130  16.453  1.00 71.12           C  
ATOM    103  CG  ASP A  28      -0.088  30.276  17.791  1.00 74.24           C  
ATOM    104  OD1 ASP A  28      -0.334  31.430  18.206  1.00 77.36           O  
ATOM    105  OD2 ASP A  28      -0.389  29.244  18.434  1.00 75.67           O  
ATOM    106  N   GLU A  29       2.747  32.461  16.977  1.00 63.25           N  
ATOM    107  CA  GLU A  29       3.203  33.595  17.764  1.00 62.05           C  
ATOM    108  C   GLU A  29       2.633  33.701  19.182  1.00 61.77           C  
ATOM    109  O   GLU A  29       3.368  34.029  20.110  1.00 62.84           O  
ATOM    110  CB  GLU A  29       2.941  34.884  17.006  1.00 60.88           C  
ATOM    111  N   SER A  30       1.347  33.415  19.361  1.00 61.00           N  
ATOM    112  CA  SER A  30       0.715  33.526  20.681  1.00 60.32           C  
ATOM    113  C   SER A  30       1.373  32.703  21.790  1.00 59.88           C  
ATOM    114  O   SER A  30       1.038  32.850  22.970  1.00 60.20           O  
ATOM    115  CB  SER A  30      -0.770  33.150  20.583  1.00 60.44           C  
ATOM    116  OG  SER A  30      -0.979  31.790  20.927  1.00 60.80           O  
ATOM    117  N   GLN A  31       2.315  31.847  21.414  1.00 59.55           N  
ATOM    118  CA  GLN A  31       3.013  30.994  22.373  1.00 59.49           C  
ATOM    119  C   GLN A  31       4.343  31.597  22.835  1.00 59.40           C  
ATOM    120  O   GLN A  31       4.965  31.114  23.788  1.00 59.85           O  
ATOM    121  CB  GLN A  31       3.269  29.624  21.745  1.00 58.72           C  
ATOM    122  CG  GLN A  31       2.018  28.812  21.456  1.00 57.20           C  
ATOM    123  CD  GLN A  31       2.342  27.457  20.857  1.00 56.28           C  
ATOM    124  OE1 GLN A  31       2.624  27.342  19.661  1.00 56.35           O  
ATOM    125  NE2 GLN A  31       2.325  26.425  21.691  1.00 56.08           N  
ATOM    126  N   LEU A  32       4.779  32.650  22.152  1.00 58.63           N  
ATOM    127  CA  LEU A  32       6.028  33.316  22.483  1.00 56.88           C  
ATOM    128  C   LEU A  32       5.750  34.506  23.408  1.00 56.77           C  
ATOM    129  O   LEU A  32       4.687  35.116  23.332  1.00 57.46           O  
ATOM    130  CB  LEU A  32       6.696  33.815  21.202  1.00 55.67           C  
ATOM    131  CG  LEU A  32       6.806  32.841  20.028  1.00 54.61           C  
ATOM    132  CD1 LEU A  32       7.268  33.600  18.824  1.00 54.03           C  
ATOM    133  CD2 LEU A  32       7.786  31.731  20.320  1.00 55.10           C  
ATOM    134  N   ARG A  33       6.700  34.817  24.288  1.00 56.48           N  
ATOM    135  CA  ARG A  33       6.574  35.953  25.197  1.00 55.93           C  
ATOM    136  C   ARG A  33       7.001  37.214  24.458  1.00 56.33           C  
ATOM    137  O   ARG A  33       7.795  37.149  23.518  1.00 56.68           O  
ATOM    138  CB  ARG A  33       7.443  35.744  26.434  1.00 55.26           C  
ATOM    139  CG  ARG A  33       6.809  34.767  27.395  1.00 56.00           C  
ATOM    140  CD  ARG A  33       7.817  33.952  28.160  1.00 56.19           C  
ATOM    141  NE  ARG A  33       7.171  32.941  28.995  1.00 57.94           N  
ATOM    142  CZ  ARG A  33       6.400  33.218  30.045  1.00 58.14           C  
ATOM    143  NH1 ARG A  33       6.163  34.480  30.383  1.00 58.23           N  
ATOM    144  NH2 ARG A  33       5.869  32.236  30.763  1.00 57.85           N  
ATOM    145  N   SER A  34       6.468  38.355  24.873  1.00 56.52           N  
ATOM    146  CA  SER A  34       6.781  39.620  24.215  1.00 56.56           C  
ATOM    147  C   SER A  34       7.802  40.473  24.976  1.00 55.90           C  
ATOM    148  O   SER A  34       7.723  40.662  26.198  1.00 54.49           O  
ATOM    149  CB  SER A  34       5.479  40.391  23.999  1.00 57.45           C  
ATOM    150  OG  SER A  34       4.592  40.131  25.080  1.00 60.58           O  
ATOM    151  N   TYR A  35       8.775  40.977  24.229  1.00 55.23           N  
ATOM    152  CA  TYR A  35       9.843  41.767  24.804  1.00 54.33           C  
ATOM    153  C   TYR A  35      10.077  43.060  24.058  1.00 54.44           C  
ATOM    154  O   TYR A  35       9.724  43.197  22.891  1.00 54.42           O  
ATOM    155  CB  TYR A  35      11.122  40.937  24.824  1.00 53.58           C  
ATOM    156  CG  TYR A  35      10.982  39.694  25.667  1.00 52.07           C  
ATOM    157  CD1 TYR A  35      10.738  39.789  27.035  1.00 52.62           C  
ATOM    158  CD2 TYR A  35      11.083  38.425  25.100  1.00 52.18           C  
ATOM    159  CE1 TYR A  35      10.601  38.646  27.829  1.00 53.69           C  
ATOM    160  CE2 TYR A  35      10.942  37.271  25.881  1.00 52.53           C  
ATOM    161  CZ  TYR A  35      10.704  37.390  27.246  1.00 53.63           C  
ATOM    162  OH  TYR A  35      10.583  36.263  28.032  1.00 53.42           O  
ATOM    163  N   SER A  36      10.704  44.001  24.743  1.00 55.07           N  
ATOM    164  CA  SER A  36      10.977  45.317  24.193  1.00 54.57           C  
ATOM    165  C   SER A  36      12.057  45.433  23.125  1.00 53.87           C  
ATOM    166  O   SER A  36      12.100  46.423  22.397  1.00 56.01           O  
ATOM    167  CB  SER A  36      11.323  46.268  25.342  1.00 54.45           C  
ATOM    168  OG  SER A  36      12.450  45.788  26.066  1.00 51.84           O  
ATOM    169  N   PHE A  37      12.922  44.441  22.999  1.00 51.58           N  
ATOM    170  CA  PHE A  37      13.994  44.566  22.015  1.00 49.53           C  
ATOM    171  C   PHE A  37      13.727  43.861  20.702  1.00 48.20           C  
ATOM    172  O   PHE A  37      12.879  42.980  20.610  1.00 48.08           O  
ATOM    173  CB  PHE A  37      15.310  44.081  22.649  1.00 48.69           C  
ATOM    174  CG  PHE A  37      15.209  42.710  23.232  1.00 48.25           C  
ATOM    175  CD1 PHE A  37      15.349  41.595  22.415  1.00 47.44           C  
ATOM    176  CD2 PHE A  37      14.868  42.529  24.572  1.00 47.83           C  
ATOM    177  CE1 PHE A  37      15.145  40.321  22.913  1.00 46.32           C  
ATOM    178  CE2 PHE A  37      14.660  41.250  25.083  1.00 46.92           C  
ATOM    179  CZ  PHE A  37      14.797  40.145  24.252  1.00 47.04           C  
ATOM    180  N   PRO A  38      14.432  44.275  19.650  1.00 47.96           N  
ATOM    181  CA  PRO A  38      14.295  43.694  18.321  1.00 48.49           C  
ATOM    182  C   PRO A  38      15.207  42.490  18.202  1.00 51.04           C  
ATOM    183  O   PRO A  38      16.189  42.370  18.946  1.00 51.24           O  
ATOM    184  CB  PRO A  38      14.726  44.826  17.417  1.00 48.79           C  
ATOM    185  CG  PRO A  38      15.839  45.407  18.207  1.00 48.50           C  
ATOM    186  CD  PRO A  38      15.240  45.504  19.582  1.00 47.42           C  
ATOM    187  N   THR A  39      14.875  41.617  17.248  1.00 53.66           N  
ATOM    188  CA  THR A  39      15.604  40.366  16.999  1.00 53.63           C  
ATOM    189  C   THR A  39      15.554  39.922  15.542  1.00 53.38           C  
ATOM    190  O   THR A  39      14.591  40.174  14.817  1.00 53.42           O  
ATOM    191  CB  THR A  39      15.019  39.180  17.841  1.00 54.60           C  
ATOM    192  OG1 THR A  39      13.630  38.999  17.521  1.00 54.63           O  
ATOM    193  CG2 THR A  39      15.185  39.450  19.334  1.00 54.82           C  
ATOM    194  N   ARG A  40      16.608  39.239  15.137  1.00 54.74           N  
ATOM    195  CA  ARG A  40      16.687  38.738  13.791  1.00 57.18           C  
ATOM    196  C   ARG A  40      16.876  37.262  13.904  1.00 57.34           C  
ATOM    197  O   ARG A  40      17.527  36.776  14.822  1.00 57.17           O  
ATOM    198  CB  ARG A  40      17.867  39.341  13.064  1.00 59.98           C  
ATOM    199  CG  ARG A  40      17.912  40.841  13.207  1.00 66.81           C  
ATOM    200  CD  ARG A  40      16.520  41.522  13.082  1.00 72.17           C  
ATOM    201  NE  ARG A  40      15.911  41.449  11.748  1.00 74.55           N  
ATOM    202  CZ  ARG A  40      14.712  41.949  11.443  1.00 75.45           C  
ATOM    203  NH1 ARG A  40      13.971  42.563  12.370  1.00 74.37           N  
ATOM    204  NH2 ARG A  40      14.238  41.827  10.212  1.00 76.77           N  
ATOM    205  N   PRO A  41      16.296  36.517  12.968  1.00 57.78           N  
ATOM    206  CA  PRO A  41      16.378  35.056  12.938  1.00 56.95           C  
ATOM    207  C   PRO A  41      17.783  34.445  12.852  1.00 54.85           C  
ATOM    208  O   PRO A  41      18.687  35.011  12.242  1.00 54.27           O  
ATOM    209  CB  PRO A  41      15.531  34.704  11.714  1.00 57.56           C  
ATOM    210  CG  PRO A  41      14.497  35.801  11.695  1.00 59.46           C  
ATOM    211  CD  PRO A  41      15.349  37.013  11.950  1.00 59.03           C  
ATOM    212  N   ILE A  42      17.956  33.278  13.470  1.00 51.80           N  
ATOM    213  CA  ILE A  42      19.220  32.565  13.410  1.00 48.16           C  
ATOM    214  C   ILE A  42      19.112  31.569  12.240  1.00 47.57           C  
ATOM    215  O   ILE A  42      18.089  30.902  12.077  1.00 47.58           O  
ATOM    216  CB  ILE A  42      19.464  31.788  14.706  1.00 47.40           C  
ATOM    217  CG1 ILE A  42      19.483  32.743  15.882  1.00 45.88           C  
ATOM    218  CG2 ILE A  42      20.783  31.055  14.636  1.00 45.99           C  
ATOM    219  CD1 ILE A  42      19.813  32.056  17.161  1.00 42.82           C  
ATOM    220  N   PRO A  43      20.160  31.465  11.404  1.00 46.39           N  
ATOM    221  CA  PRO A  43      20.194  30.564  10.249  1.00 46.30           C  
ATOM    222  C   PRO A  43      19.833  29.114  10.548  1.00 48.08           C  
ATOM    223  O   PRO A  43      20.402  28.520  11.462  1.00 48.13           O  
ATOM    224  CB  PRO A  43      21.643  30.657   9.776  1.00 45.10           C  
ATOM    225  CG  PRO A  43      22.012  32.011  10.113  1.00 43.88           C  
ATOM    226  CD  PRO A  43      21.428  32.207  11.497  1.00 44.59           C  
ATOM    227  N   ARG A  44      18.895  28.552   9.783  1.00 48.14           N  
ATOM    228  CA  ARG A  44      18.537  27.138   9.930  1.00 47.40           C  
ATOM    229  C   ARG A  44      19.104  26.483   8.682  1.00 47.09           C  
ATOM    230  O   ARG A  44      18.556  26.665   7.600  1.00 46.70           O  
ATOM    231  CB  ARG A  44      17.028  26.936   9.944  1.00 47.51           C  
ATOM    232  CG  ARG A  44      16.397  27.063  11.308  1.00 51.52           C  
ATOM    233  CD  ARG A  44      14.893  26.911  11.222  1.00 55.74           C  
ATOM    234  NE  ARG A  44      14.470  25.631  10.653  1.00 56.96           N  
ATOM    235  CZ  ARG A  44      14.318  24.518  11.367  1.00 59.32           C  
ATOM    236  NH1 ARG A  44      14.563  24.533  12.677  1.00 59.27           N  
ATOM    237  NH2 ARG A  44      13.899  23.397  10.792  1.00 59.86           N  
ATOM    238  N   LEU A  45      20.201  25.738   8.839  1.00 47.41           N  
ATOM    239  CA  LEU A  45      20.862  25.079   7.708  1.00 48.47           C  
ATOM    240  C   LEU A  45      21.142  23.576   7.863  1.00 48.76           C  
ATOM    241  O   LEU A  45      20.875  22.960   8.888  1.00 49.25           O  
ATOM    242  CB  LEU A  45      22.191  25.779   7.402  1.00 48.21           C  
ATOM    243  CG  LEU A  45      22.254  27.289   7.602  1.00 50.25           C  
ATOM    244  CD1 LEU A  45      23.678  27.769   7.341  1.00 48.87           C  
ATOM    245  CD2 LEU A  45      21.253  27.982   6.689  1.00 50.06           C  
ATOM    246  N   SER A  46      21.704  22.995   6.819  1.00 48.26           N  
ATOM    247  CA  SER A  46      22.017  21.596   6.851  1.00 48.57           C  
ATOM    248  C   SER A  46      23.449  21.409   7.284  1.00 49.80           C  
ATOM    249  O   SER A  46      24.307  22.219   6.979  1.00 49.62           O  
ATOM    250  CB  SER A  46      21.843  20.996   5.473  1.00 49.25           C  
ATOM    251  OG  SER A  46      22.848  20.020   5.252  1.00 51.28           O  
ATOM    252  N   GLN A  47      23.699  20.320   7.996  1.00 51.46           N  
ATOM    253  CA  GLN A  47      25.038  19.984   8.450  1.00 52.90           C  
ATOM    254  C   GLN A  47      26.030  19.894   7.274  1.00 54.11           C  
ATOM    255  O   GLN A  47      27.222  20.132   7.447  1.00 54.64           O  
ATOM    256  CB  GLN A  47      24.972  18.658   9.222  1.00 52.97           C  
ATOM    257  CG  GLN A  47      26.158  17.726   9.058  1.00 56.10           C  
ATOM    258  CD  GLN A  47      26.064  16.923   7.782  1.00 56.76           C  
ATOM    259  OE1 GLN A  47      24.965  16.598   7.339  1.00 57.52           O  
ATOM    260  NE2 GLN A  47      27.207  16.586   7.190  1.00 59.09           N  
ATOM    261  N   SER A  48      25.534  19.566   6.082  1.00 55.46           N  
ATOM    262  CA  SER A  48      26.390  19.440   4.901  1.00 56.67           C  
ATOM    263  C   SER A  48      26.559  20.785   4.178  1.00 58.59           C  
ATOM    264  O   SER A  48      27.312  20.890   3.195  1.00 59.21           O  
ATOM    265  CB  SER A  48      25.782  18.433   3.942  1.00 55.85           C  
ATOM    266  OG  SER A  48      24.528  18.909   3.510  1.00 55.20           O  
ATOM    267  N   ASP A  49      25.854  21.806   4.666  1.00 59.28           N  
ATOM    268  CA  ASP A  49      25.930  23.150   4.090  1.00 58.73           C  
ATOM    269  C   ASP A  49      27.213  23.845   4.549  1.00 58.38           C  
ATOM    270  O   ASP A  49      27.432  24.038   5.748  1.00 58.69           O  
ATOM    271  CB  ASP A  49      24.733  23.987   4.536  1.00 60.59           C  
ATOM    272  CG  ASP A  49      24.635  25.318   3.797  1.00 61.41           C  
ATOM    273  OD1 ASP A  49      25.685  25.898   3.438  1.00 61.64           O  
ATOM    274  OD2 ASP A  49      23.498  25.795   3.584  1.00 62.30           O  
ATOM    275  N   PRO A  50      28.069  24.237   3.598  1.00 56.78           N  
ATOM    276  CA  PRO A  50      29.338  24.916   3.872  1.00 56.16           C  
ATOM    277  C   PRO A  50      29.181  26.177   4.711  1.00 56.25           C  
ATOM    278  O   PRO A  50      30.028  26.487   5.537  1.00 55.93           O  
ATOM    279  CB  PRO A  50      29.864  25.226   2.477  1.00 55.01           C  
ATOM    280  CG  PRO A  50      29.346  24.106   1.680  1.00 55.03           C  
ATOM    281  CD  PRO A  50      27.925  23.978   2.156  1.00 55.35           C  
ATOM    282  N   ARG A  51      28.099  26.913   4.490  1.00 56.97           N  
ATOM    283  CA  ARG A  51      27.869  28.137   5.236  1.00 57.34           C  
ATOM    284  C   ARG A  51      27.716  27.860   6.726  1.00 56.44           C  
ATOM    285  O   ARG A  51      28.081  28.684   7.565  1.00 56.83           O  
ATOM    286  CB  ARG A  51      26.617  28.837   4.717  1.00 60.45           C  
ATOM    287  CG  ARG A  51      26.278  30.127   5.461  1.00 66.39           C  
ATOM    288  CD  ARG A  51      24.840  30.596   5.117  1.00 72.09           C  
ATOM    289  NE  ARG A  51      24.397  31.738   5.928  1.00 76.53           N  
ATOM    290  CZ  ARG A  51      23.117  32.133   6.066  1.00 78.84           C  
ATOM    291  NH1 ARG A  51      22.108  31.484   5.457  1.00 78.14           N  
ATOM    292  NH2 ARG A  51      22.828  33.192   6.820  1.00 80.13           N  
ATOM    293  N   ALA A  52      27.168  26.699   7.057  1.00 56.54           N  
ATOM    294  CA  ALA A  52      26.982  26.339   8.453  1.00 56.09           C  
ATOM    295  C   ALA A  52      28.323  25.990   9.086  1.00 56.42           C  
ATOM    296  O   ALA A  52      28.586  26.318  10.234  1.00 57.22           O  
ATOM    297  CB  ALA A  52      26.032  25.172   8.560  1.00 54.21           C  
ATOM    298  N   GLU A  53      29.173  25.323   8.325  1.00 58.01           N  
ATOM    299  CA  GLU A  53      30.489  24.941   8.819  1.00 59.00           C  
ATOM    300  C   GLU A  53      31.286  26.205   9.018  1.00 58.95           C  
ATOM    301  O   GLU A  53      32.278  26.233   9.729  1.00 59.02           O  
ATOM    302  CB  GLU A  53      31.206  24.084   7.781  1.00 61.38           C  
ATOM    303  CG  GLU A  53      32.222  23.116   8.341  1.00 67.25           C  
ATOM    304  CD  GLU A  53      31.592  21.999   9.165  1.00 70.95           C  
ATOM    305  OE1 GLU A  53      30.444  21.588   8.872  1.00 73.43           O  
ATOM    306  OE2 GLU A  53      32.258  21.509  10.103  1.00 72.99           O  
ATOM    307  N   GLU A  54      30.838  27.251   8.348  1.00 60.21           N  
ATOM    308  CA  GLU A  54      31.494  28.548   8.390  1.00 59.94           C  
ATOM    309  C   GLU A  54      31.104  29.300   9.652  1.00 56.95           C  
ATOM    310  O   GLU A  54      31.946  29.862  10.342  1.00 55.72           O  
ATOM    311  CB  GLU A  54      31.103  29.343   7.131  1.00 65.43           C  
ATOM    312  CG  GLU A  54      31.384  30.839   7.197  1.00 74.22           C  
ATOM    313  CD  GLU A  54      30.783  31.627   6.023  1.00 79.25           C  
ATOM    314  OE1 GLU A  54      30.928  32.870   6.031  1.00 82.32           O  
ATOM    315  OE2 GLU A  54      30.178  31.028   5.096  1.00 80.90           O  
ATOM    316  N   LEU A  55      29.813  29.303   9.943  1.00 53.26           N  
ATOM    317  CA  LEU A  55      29.326  29.971  11.128  1.00 50.15           C  
ATOM    318  C   LEU A  55      29.945  29.405  12.397  1.00 49.64           C  
ATOM    319  O   LEU A  55      30.232  30.144  13.334  1.00 49.81           O  
ATOM    320  CB  LEU A  55      27.822  29.829  11.212  1.00 48.68           C  
ATOM    321  CG  LEU A  55      27.089  30.537  10.095  1.00 46.28           C  
ATOM    322  CD1 LEU A  55      25.610  30.252  10.124  1.00 45.88           C  
ATOM    323  CD2 LEU A  55      27.328  31.994  10.285  1.00 46.46           C  
ATOM    324  N   ILE A  56      30.132  28.092  12.438  1.00 48.04           N  
ATOM    325  CA  ILE A  56      30.711  27.452  13.615  1.00 47.25           C  
ATOM    326  C   ILE A  56      32.174  27.835  13.751  1.00 49.01           C  
ATOM    327  O   ILE A  56      32.669  28.137  14.840  1.00 49.48           O  
ATOM    328  CB  ILE A  56      30.613  25.921  13.501  1.00 45.01           C  
ATOM    329  CG1 ILE A  56      29.155  25.497  13.424  1.00 43.66           C  
ATOM    330  CG2 ILE A  56      31.251  25.262  14.704  1.00 44.56           C  
ATOM    331  CD1 ILE A  56      29.000  24.015  13.340  1.00 40.72           C  
ATOM    332  N   GLU A  57      32.859  27.822  12.621  1.00 51.42           N  
ATOM    333  CA  GLU A  57      34.269  28.156  12.587  1.00 54.01           C  
ATOM    334  C   GLU A  57      34.505  29.581  13.028  1.00 54.94           C  
ATOM    335  O   GLU A  57      35.609  29.930  13.425  1.00 55.79           O  
ATOM    336  CB  GLU A  57      34.831  27.972  11.177  1.00 56.71           C  
ATOM    337  CG  GLU A  57      36.350  28.126  11.068  1.00 62.39           C  
ATOM    338  CD  GLU A  57      37.132  27.261  12.061  1.00 66.91           C  
ATOM    339  OE1 GLU A  57      36.716  26.112  12.336  1.00 69.73           O  
ATOM    340  OE2 GLU A  57      38.186  27.720  12.558  1.00 68.52           O  
ATOM    341  N   ASN A  58      33.473  30.410  12.954  1.00 56.29           N  
ATOM    342  CA  ASN A  58      33.612  31.804  13.355  1.00 57.19           C  
ATOM    343  C   ASN A  58      32.835  32.068  14.624  1.00 55.76           C  
ATOM    344  O   ASN A  58      32.443  33.190  14.898  1.00 55.57           O  
ATOM    345  CB  ASN A  58      33.112  32.734  12.255  1.00 62.05           C  
ATOM    346  CG  ASN A  58      33.842  32.523  10.949  1.00 67.82           C  
ATOM    347  OD1 ASN A  58      35.070  32.482  10.917  1.00 70.64           O  
ATOM    348  ND2 ASN A  58      33.090  32.394   9.859  1.00 69.69           N  
ATOM    349  N   GLU A  59      32.606  31.019  15.394  1.00 54.56           N  
ATOM    350  CA  GLU A  59      31.887  31.141  16.652  1.00 54.14           C  
ATOM    351  C   GLU A  59      30.623  31.998  16.591  1.00 51.68           C  
ATOM    352  O   GLU A  59      30.427  32.939  17.376  1.00 50.29           O  
ATOM    353  CB  GLU A  59      32.840  31.652  17.741  1.00 56.59           C  
ATOM    354  CG  GLU A  59      33.641  30.530  18.438  1.00 61.08           C  
ATOM    355  CD  GLU A  59      34.850  31.040  19.217  1.00 63.78           C  
ATOM    356  OE1 GLU A  59      35.820  31.504  18.572  1.00 65.19           O  
ATOM    357  OE2 GLU A  59      34.846  30.984  20.472  1.00 66.30           O  
ATOM    358  N   GLU A  60      29.765  31.638  15.648  1.00 49.80           N  
ATOM    359  CA  GLU A  60      28.484  32.293  15.471  1.00 48.15           C  
ATOM    360  C   GLU A  60      27.401  31.229  15.518  1.00 46.20           C  
ATOM    361  O   GLU A  60      27.561  30.121  14.992  1.00 45.65           O  
ATOM    362  CB  GLU A  60      28.448  33.029  14.151  1.00 49.83           C  
ATOM    363  CG  GLU A  60      29.464  34.124  14.119  1.00 54.03           C  
ATOM    364  CD  GLU A  60      29.108  35.159  13.114  1.00 57.48           C  
ATOM    365  OE1 GLU A  60      29.752  35.187  12.044  1.00 59.24           O  
ATOM    366  OE2 GLU A  60      28.164  35.934  13.387  1.00 60.09           O  
ATOM    367  N   PRO A  61      26.273  31.538  16.173  1.00 42.96           N  
ATOM    368  CA  PRO A  61      25.162  30.593  16.291  1.00 42.02           C  
ATOM    369  C   PRO A  61      24.576  30.140  14.948  1.00 42.66           C  
ATOM    370  O   PRO A  61      24.683  30.840  13.943  1.00 44.15           O  
ATOM    371  CB  PRO A  61      24.163  31.371  17.148  1.00 40.20           C  
ATOM    372  CG  PRO A  61      24.428  32.787  16.779  1.00 40.29           C  
ATOM    373  CD  PRO A  61      25.929  32.842  16.761  1.00 41.89           C  
ATOM    374  N   VAL A  62      23.975  28.954  14.938  1.00 41.64           N  
ATOM    375  CA  VAL A  62      23.364  28.404  13.732  1.00 39.75           C  
ATOM    376  C   VAL A  62      22.567  27.193  14.174  1.00 41.03           C  
ATOM    377  O   VAL A  62      22.937  26.537  15.136  1.00 41.75           O  
ATOM    378  CB  VAL A  62      24.431  27.949  12.685  1.00 39.38           C  
ATOM    379  CG1 VAL A  62      25.384  26.931  13.283  1.00 37.41           C  
ATOM    380  CG2 VAL A  62      23.741  27.320  11.491  1.00 37.92           C  
ATOM    381  N   VAL A  63      21.462  26.910  13.492  1.00 41.24           N  
ATOM    382  CA  VAL A  63      20.646  25.743  13.822  1.00 40.46           C  
ATOM    383  C   VAL A  63      20.788  24.710  12.697  1.00 42.05           C  
ATOM    384  O   VAL A  63      20.469  25.002  11.543  1.00 43.42           O  
ATOM    385  CB  VAL A  63      19.152  26.122  13.985  1.00 39.26           C  
ATOM    386  CG1 VAL A  63      18.325  24.896  14.317  1.00 37.96           C  
ATOM    387  CG2 VAL A  63      18.997  27.167  15.085  1.00 39.03           C  
ATOM    388  N   LEU A  64      21.308  23.525  13.040  1.00 43.90           N  
ATOM    389  CA  LEU A  64      21.495  22.407  12.094  1.00 43.41           C  
ATOM    390  C   LEU A  64      20.253  21.510  12.186  1.00 43.81           C  
ATOM    391  O   LEU A  64      19.838  21.114  13.280  1.00 44.70           O  
ATOM    392  CB  LEU A  64      22.741  21.611  12.463  1.00 42.33           C  
ATOM    393  CG  LEU A  64      23.998  22.473  12.511  1.00 41.16           C  
ATOM    394  CD1 LEU A  64      25.111  21.673  13.114  1.00 40.59           C  
ATOM    395  CD2 LEU A  64      24.371  22.951  11.122  1.00 41.23           C  
ATOM    396  N   THR A  65      19.675  21.176  11.043  1.00 44.77           N  
ATOM    397  CA  THR A  65      18.440  20.411  11.028  1.00 46.62           C  
ATOM    398  C   THR A  65      18.517  18.940  10.653  1.00 47.88           C  
ATOM    399  O   THR A  65      17.508  18.220  10.746  1.00 46.16           O  
ATOM    400  CB  THR A  65      17.431  21.098  10.085  1.00 47.61           C  
ATOM    401  OG1 THR A  65      18.019  21.266   8.784  1.00 46.45           O  
ATOM    402  CG2 THR A  65      17.039  22.468  10.640  1.00 45.94           C  
ATOM    403  N   ASP A  66      19.702  18.478  10.270  1.00 48.91           N  
ATOM    404  CA  ASP A  66      19.842  17.101   9.843  1.00 49.85           C  
ATOM    405  C   ASP A  66      21.121  16.416  10.321  1.00 49.19           C  
ATOM    406  O   ASP A  66      21.777  15.683   9.566  1.00 49.93           O  
ATOM    407  CB  ASP A  66      19.752  17.077   8.327  1.00 52.05           C  
ATOM    408  CG  ASP A  66      20.806  17.933   7.676  1.00 53.75           C  
ATOM    409  OD1 ASP A  66      21.297  18.874   8.342  1.00 54.08           O  
ATOM    410  OD2 ASP A  66      21.135  17.680   6.495  1.00 54.62           O  
ATOM    411  N   THR A  67      21.466  16.629  11.584  1.00 47.97           N  
ATOM    412  CA  THR A  67      22.678  16.025  12.123  1.00 46.28           C  
ATOM    413  C   THR A  67      22.428  14.611  12.609  1.00 47.11           C  
ATOM    414  O   THR A  67      23.315  13.756  12.525  1.00 47.75           O  
ATOM    415  CB  THR A  67      23.238  16.833  13.309  1.00 43.77           C  
ATOM    416  OG1 THR A  67      22.275  16.869  14.375  1.00 41.57           O  
ATOM    417  CG2 THR A  67      23.540  18.239  12.869  1.00 42.70           C  
ATOM    418  N   ASN A  68      21.214  14.377  13.107  1.00 47.44           N  
ATOM    419  CA  ASN A  68      20.845  13.081  13.638  1.00 47.97           C  
ATOM    420  C   ASN A  68      21.648  12.842  14.905  1.00 48.47           C  
ATOM    421  O   ASN A  68      21.997  11.711  15.220  1.00 50.60           O  
ATOM    422  CB  ASN A  68      21.168  11.981  12.637  1.00 49.13           C  
ATOM    423  CG  ASN A  68      20.220  11.976  11.476  1.00 51.36           C  
ATOM    424  OD1 ASN A  68      19.021  11.783  11.661  1.00 52.58           O  
ATOM    425  ND2 ASN A  68      20.737  12.206  10.268  1.00 54.26           N  
ATOM    426  N   LEU A  69      21.926  13.906  15.647  1.00 47.58           N  
ATOM    427  CA  LEU A  69      22.717  13.778  16.863  1.00 44.93           C  
ATOM    428  C   LEU A  69      22.043  12.919  17.933  1.00 44.27           C  
ATOM    429  O   LEU A  69      22.646  11.977  18.464  1.00 43.58           O  
ATOM    430  CB  LEU A  69      23.006  15.169  17.410  1.00 42.65           C  
ATOM    431  CG  LEU A  69      23.991  15.278  18.560  1.00 41.86           C  
ATOM    432  CD1 LEU A  69      25.338  14.642  18.187  1.00 40.61           C  
ATOM    433  CD2 LEU A  69      24.132  16.753  18.904  1.00 39.71           C  
ATOM    434  N   VAL A  70      20.795  13.248  18.238  1.00 43.52           N  
ATOM    435  CA  VAL A  70      20.058  12.513  19.247  1.00 42.68           C  
ATOM    436  C   VAL A  70      18.910  11.724  18.657  1.00 43.34           C  
ATOM    437  O   VAL A  70      17.826  11.656  19.233  1.00 44.09           O  
ATOM    438  CB  VAL A  70      19.520  13.459  20.342  1.00 42.79           C  
ATOM    439  CG1 VAL A  70      20.701  14.087  21.085  1.00 40.27           C  
ATOM    440  CG2 VAL A  70      18.583  14.526  19.735  1.00 41.03           C  
ATOM    441  N   TYR A  71      19.155  11.114  17.511  1.00 42.57           N  
ATOM    442  CA  TYR A  71      18.132  10.332  16.845  1.00 43.63           C  
ATOM    443  C   TYR A  71      17.442   9.290  17.742  1.00 44.37           C  
ATOM    444  O   TYR A  71      16.208   9.238  17.795  1.00 45.01           O  
ATOM    445  CB  TYR A  71      18.751   9.647  15.634  1.00 45.92           C  
ATOM    446  CG  TYR A  71      17.829   8.684  14.929  1.00 48.65           C  
ATOM    447  CD1 TYR A  71      16.667   9.129  14.315  1.00 48.84           C  
ATOM    448  CD2 TYR A  71      18.110   7.315  14.897  1.00 49.14           C  
ATOM    449  CE1 TYR A  71      15.787   8.232  13.680  1.00 50.35           C  
ATOM    450  CE2 TYR A  71      17.241   6.406  14.269  1.00 48.95           C  
ATOM    451  CZ  TYR A  71      16.075   6.873  13.665  1.00 50.63           C  
ATOM    452  OH  TYR A  71      15.169   6.000  13.093  1.00 51.37           O  
ATOM    453  N   PRO A  72      18.227   8.454  18.461  1.00 44.32           N  
ATOM    454  CA  PRO A  72      17.661   7.425  19.342  1.00 44.28           C  
ATOM    455  C   PRO A  72      16.816   7.970  20.484  1.00 45.88           C  
ATOM    456  O   PRO A  72      15.941   7.283  20.999  1.00 46.68           O  
ATOM    457  CB  PRO A  72      18.904   6.708  19.875  1.00 41.78           C  
ATOM    458  CG  PRO A  72      19.891   6.880  18.791  1.00 43.32           C  
ATOM    459  CD  PRO A  72      19.690   8.330  18.406  1.00 43.55           C  
ATOM    460  N   ALA A  73      17.081   9.216  20.866  1.00 47.28           N  
ATOM    461  CA  ALA A  73      16.371   9.852  21.966  1.00 47.42           C  
ATOM    462  C   ALA A  73      15.080  10.541  21.542  1.00 48.52           C  
ATOM    463  O   ALA A  73      14.274  10.938  22.388  1.00 49.46           O  
ATOM    464  CB  ALA A  73      17.286  10.854  22.647  1.00 45.86           C  
ATOM    465  N   LEU A  74      14.873  10.684  20.239  1.00 48.70           N  
ATOM    466  CA  LEU A  74      13.670  11.357  19.775  1.00 48.03           C  
ATOM    467  C   LEU A  74      12.391  10.653  20.186  1.00 49.02           C  
ATOM    468  O   LEU A  74      11.319  11.247  20.142  1.00 49.94           O  
ATOM    469  CB  LEU A  74      13.723  11.526  18.260  1.00 44.81           C  
ATOM    470  CG  LEU A  74      14.740  12.580  17.815  1.00 44.75           C  
ATOM    471  CD1 LEU A  74      14.957  12.436  16.346  1.00 44.33           C  
ATOM    472  CD2 LEU A  74      14.259  13.979  18.147  1.00 42.66           C  
ATOM    473  N   LYS A  75      12.515   9.398  20.609  1.00 50.86           N  
ATOM    474  CA  LYS A  75      11.362   8.602  21.040  1.00 51.53           C  
ATOM    475  C   LYS A  75      11.112   8.710  22.545  1.00 52.03           C  
ATOM    476  O   LYS A  75      10.176   8.121  23.081  1.00 52.09           O  
ATOM    477  CB  LYS A  75      11.570   7.136  20.662  1.00 51.64           C  
ATOM    478  CG  LYS A  75      12.806   6.506  21.265  1.00 52.00           C  
ATOM    479  CD  LYS A  75      12.991   5.102  20.728  1.00 52.64           C  
ATOM    480  CE  LYS A  75      14.384   4.599  21.006  1.00 52.63           C  
ATOM    481  NZ  LYS A  75      14.677   4.714  22.452  1.00 54.66           N  
ATOM    482  N   TRP A  76      11.954   9.480  23.216  1.00 52.93           N  
ATOM    483  CA  TRP A  76      11.832   9.678  24.647  1.00 52.96           C  
ATOM    484  C   TRP A  76      10.595  10.471  25.027  1.00 55.05           C  
ATOM    485  O   TRP A  76      10.072  11.277  24.254  1.00 55.58           O  
ATOM    486  CB  TRP A  76      13.064  10.392  25.197  1.00 50.91           C  
ATOM    487  CG  TRP A  76      14.321   9.572  25.154  1.00 49.10           C  
ATOM    488  CD1 TRP A  76      14.485   8.313  24.629  1.00 49.16           C  
ATOM    489  CD2 TRP A  76      15.605   9.970  25.642  1.00 47.55           C  
ATOM    490  NE1 TRP A  76      15.792   7.905  24.763  1.00 47.77           N  
ATOM    491  CE2 TRP A  76      16.503   8.904  25.380  1.00 46.97           C  
ATOM    492  CE3 TRP A  76      16.091  11.120  26.273  1.00 45.39           C  
ATOM    493  CZ2 TRP A  76      17.861   8.963  25.732  1.00 46.21           C  
ATOM    494  CZ3 TRP A  76      17.438  11.180  26.618  1.00 44.74           C  
ATOM    495  CH2 TRP A  76      18.305  10.108  26.348  1.00 45.22           C  
ATOM    496  N   ASP A  77      10.149  10.214  26.246  1.00 57.77           N  
ATOM    497  CA  ASP A  77       8.982  10.855  26.830  1.00 60.94           C  
ATOM    498  C   ASP A  77       8.958  10.425  28.295  1.00 62.23           C  
ATOM    499  O   ASP A  77       9.668   9.491  28.682  1.00 62.20           O  
ATOM    500  CB  ASP A  77       7.698  10.441  26.080  1.00 62.70           C  
ATOM    501  CG  ASP A  77       7.324   8.964  26.269  1.00 66.24           C  
ATOM    502  OD1 ASP A  77       8.184   8.141  26.650  1.00 67.73           O  
ATOM    503  OD2 ASP A  77       6.151   8.614  26.001  1.00 66.49           O  
ATOM    504  N   LEU A  78       8.177  11.125  29.112  1.00 63.21           N  
ATOM    505  CA  LEU A  78       8.097  10.820  30.535  1.00 64.07           C  
ATOM    506  C   LEU A  78       7.922   9.319  30.821  1.00 65.49           C  
ATOM    507  O   LEU A  78       8.621   8.743  31.666  1.00 64.88           O  
ATOM    508  CB  LEU A  78       6.948  11.615  31.143  1.00 63.48           C  
ATOM    509  CG  LEU A  78       7.097  13.137  31.065  1.00 63.90           C  
ATOM    510  CD1 LEU A  78       5.805  13.829  31.500  1.00 64.37           C  
ATOM    511  CD2 LEU A  78       8.272  13.563  31.939  1.00 62.23           C  
ATOM    512  N   GLU A  79       6.996   8.688  30.104  1.00 66.68           N  
ATOM    513  CA  GLU A  79       6.718   7.267  30.271  1.00 67.46           C  
ATOM    514  C   GLU A  79       7.955   6.407  30.011  1.00 66.04           C  
ATOM    515  O   GLU A  79       8.498   5.780  30.925  1.00 64.58           O  
ATOM    516  CB  GLU A  79       5.611   6.869  29.308  1.00 71.23           C  
ATOM    517  CG  GLU A  79       5.171   5.436  29.445  1.00 77.19           C  
ATOM    518  CD  GLU A  79       4.180   5.049  28.377  1.00 80.78           C  
ATOM    519  OE1 GLU A  79       4.567   4.967  27.188  1.00 82.93           O  
ATOM    520  OE2 GLU A  79       3.002   4.839  28.733  1.00 82.77           O  
ATOM    521  N   TYR A  80       8.383   6.378  28.751  1.00 64.84           N  
ATOM    522  CA  TYR A  80       9.546   5.596  28.361  1.00 65.00           C  
ATOM    523  C   TYR A  80      10.741   5.865  29.256  1.00 65.37           C  
ATOM    524  O   TYR A  80      11.457   4.948  29.633  1.00 65.33           O  
ATOM    525  CB  TYR A  80       9.949   5.909  26.923  1.00 63.63           C  
ATOM    526  CG  TYR A  80      11.236   5.229  26.490  1.00 63.23           C  
ATOM    527  CD1 TYR A  80      11.227   3.948  25.934  1.00 64.22           C  
ATOM    528  CD2 TYR A  80      12.463   5.878  26.620  1.00 62.07           C  
ATOM    529  CE1 TYR A  80      12.414   3.334  25.507  1.00 62.54           C  
ATOM    530  CE2 TYR A  80      13.653   5.272  26.204  1.00 62.64           C  
ATOM    531  CZ  TYR A  80      13.622   4.003  25.644  1.00 62.63           C  
ATOM    532  OH  TYR A  80      14.795   3.425  25.201  1.00 61.92           O  
ATOM    533  N   LEU A  81      10.966   7.131  29.575  1.00 66.18           N  
ATOM    534  CA  LEU A  81      12.091   7.496  30.416  1.00 67.28           C  
ATOM    535  C   LEU A  81      12.003   6.913  31.819  1.00 68.59           C  
ATOM    536  O   LEU A  81      12.924   6.232  32.280  1.00 67.95           O  
ATOM    537  CB  LEU A  81      12.203   9.014  30.507  1.00 66.83           C  
ATOM    538  CG  LEU A  81      12.805   9.721  29.303  1.00 66.23           C  
ATOM    539  CD1 LEU A  81      12.849  11.206  29.588  1.00 65.90           C  
ATOM    540  CD2 LEU A  81      14.203   9.191  29.035  1.00 65.06           C  
ATOM    541  N   GLN A  82      10.898   7.185  32.505  1.00 70.21           N  
ATOM    542  CA  GLN A  82      10.706   6.682  33.864  1.00 72.10           C  
ATOM    543  C   GLN A  82      10.953   5.185  33.961  1.00 73.53           C  
ATOM    544  O   GLN A  82      11.429   4.688  34.977  1.00 74.04           O  
ATOM    545  CB  GLN A  82       9.291   6.996  34.338  1.00 72.34           C  
ATOM    546  CG  GLN A  82       8.825   6.164  35.523  1.00 73.27           C  
ATOM    547  CD  GLN A  82       7.537   6.695  36.112  1.00 73.88           C  
ATOM    548  OE1 GLN A  82       6.688   7.218  35.396  1.00 76.21           O  
ATOM    549  NE2 GLN A  82       7.377   6.551  37.422  1.00 73.22           N  
ATOM    550  N   GLU A  83      10.637   4.476  32.889  1.00 75.20           N  
ATOM    551  CA  GLU A  83      10.811   3.035  32.845  1.00 75.49           C  
ATOM    552  C   GLU A  83      12.243   2.526  32.662  1.00 74.86           C  
ATOM    553  O   GLU A  83      12.622   1.509  33.239  1.00 74.75           O  
ATOM    554  CB  GLU A  83       9.956   2.466  31.716  1.00 77.18           C  
ATOM    555  CG  GLU A  83       9.944   0.966  31.698  1.00 82.93           C  
ATOM    556  CD  GLU A  83       8.635   0.414  32.205  1.00 87.12           C  
ATOM    557  OE1 GLU A  83       7.608   0.620  31.524  1.00 89.09           O  
ATOM    558  OE2 GLU A  83       8.622  -0.221  33.284  1.00 89.62           O  
ATOM    559  N   ASN A  84      13.034   3.232  31.863  1.00 74.85           N  
ATOM    560  CA  ASN A  84      14.400   2.819  31.558  1.00 74.66           C  
ATOM    561  C   ASN A  84      15.498   3.718  32.118  1.00 74.48           C  
ATOM    562  O   ASN A  84      16.670   3.335  32.153  1.00 73.54           O  
ATOM    563  CB  ASN A  84      14.556   2.745  30.036  1.00 74.74           C  
ATOM    564  CG  ASN A  84      13.442   1.953  29.378  1.00 74.86           C  
ATOM    565  OD1 ASN A  84      13.425   0.728  29.446  1.00 76.78           O  
ATOM    566  ND2 ASN A  84      12.496   2.650  28.751  1.00 73.05           N  
ATOM    567  N   ILE A  85      15.116   4.909  32.564  1.00 74.87           N  
ATOM    568  CA  ILE A  85      16.074   5.879  33.083  1.00 75.10           C  
ATOM    569  C   ILE A  85      16.835   5.384  34.304  1.00 76.15           C  
ATOM    570  O   ILE A  85      17.603   6.127  34.915  1.00 76.06           O  
ATOM    571  CB  ILE A  85      15.367   7.212  33.425  1.00 74.10           C  
ATOM    572  CG1 ILE A  85      16.394   8.328  33.586  1.00 73.46           C  
ATOM    573  CG2 ILE A  85      14.553   7.063  34.687  1.00 74.04           C  
ATOM    574  CD1 ILE A  85      17.145   8.625  32.321  1.00 73.29           C  
ATOM    575  N   GLY A  86      16.631   4.123  34.658  1.00 77.16           N  
ATOM    576  CA  GLY A  86      17.311   3.595  35.821  1.00 78.21           C  
ATOM    577  C   GLY A  86      16.689   4.100  37.112  1.00 78.70           C  
ATOM    578  O   GLY A  86      15.530   4.517  37.141  1.00 79.41           O  
ATOM    579  N   ASN A  87      17.453   4.076  38.190  1.00 78.65           N  
ATOM    580  CA  ASN A  87      16.907   4.521  39.455  1.00 79.08           C  
ATOM    581  C   ASN A  87      17.956   5.273  40.238  1.00 78.38           C  
ATOM    582  O   ASN A  87      18.553   4.748  41.177  1.00 78.16           O  
ATOM    583  CB  ASN A  87      16.398   3.319  40.247  1.00 80.78           C  
ATOM    584  CG  ASN A  87      15.688   3.717  41.520  1.00 82.30           C  
ATOM    585  OD1 ASN A  87      16.314   3.874  42.569  1.00 82.49           O  
ATOM    586  ND2 ASN A  87      14.376   3.899  41.430  1.00 81.88           N  
ATOM    587  N   GLY A  88      18.178   6.515  39.832  1.00 77.65           N  
ATOM    588  CA  GLY A  88      19.165   7.336  40.492  1.00 76.07           C  
ATOM    589  C   GLY A  88      18.537   8.633  40.931  1.00 75.36           C  
ATOM    590  O   GLY A  88      17.324   8.797  40.831  1.00 74.96           O  
ATOM    591  N   ASP A  89      19.373   9.550  41.409  1.00 75.53           N  
ATOM    592  CA  ASP A  89      18.931  10.861  41.887  1.00 75.45           C  
ATOM    593  C   ASP A  89      19.062  11.927  40.812  1.00 73.49           C  
ATOM    594  O   ASP A  89      20.128  12.091  40.213  1.00 73.23           O  
ATOM    595  CB  ASP A  89      19.760  11.286  43.107  1.00 78.64           C  
ATOM    596  CG  ASP A  89      19.010  11.116  44.417  1.00 80.85           C  
ATOM    597  OD1 ASP A  89      18.158  10.207  44.509  1.00 81.40           O  
ATOM    598  OD2 ASP A  89      19.286  11.887  45.363  1.00 81.82           O  
ATOM    599  N   PHE A  90      17.974  12.652  40.585  1.00 71.61           N  
ATOM    600  CA  PHE A  90      17.946  13.711  39.587  1.00 70.05           C  
ATOM    601  C   PHE A  90      17.648  15.049  40.262  1.00 68.41           C  
ATOM    602  O   PHE A  90      16.713  15.154  41.054  1.00 67.86           O  
ATOM    603  CB  PHE A  90      16.860  13.436  38.531  1.00 69.90           C  
ATOM    604  CG  PHE A  90      16.995  12.104  37.827  1.00 70.55           C  
ATOM    605  CD1 PHE A  90      16.663  10.917  38.472  1.00 71.55           C  
ATOM    606  CD2 PHE A  90      17.471  12.039  36.521  1.00 70.72           C  
ATOM    607  CE1 PHE A  90      16.803   9.678  37.831  1.00 71.61           C  
ATOM    608  CE2 PHE A  90      17.616  10.807  35.875  1.00 70.46           C  
ATOM    609  CZ  PHE A  90      17.281   9.628  36.532  1.00 71.14           C  
ATOM    610  N   SER A  91      18.436  16.071  39.947  1.00 66.59           N  
ATOM    611  CA  SER A  91      18.218  17.394  40.521  1.00 65.20           C  
ATOM    612  C   SER A  91      16.977  18.023  39.878  1.00 64.72           C  
ATOM    613  O   SER A  91      16.882  18.089  38.655  1.00 65.68           O  
ATOM    614  CB  SER A  91      19.424  18.290  40.255  1.00 65.16           C  
ATOM    615  OG  SER A  91      20.633  17.632  40.597  1.00 65.81           O  
ATOM    616  N   VAL A  92      16.038  18.487  40.701  1.00 63.10           N  
ATOM    617  CA  VAL A  92      14.815  19.107  40.195  1.00 61.73           C  
ATOM    618  C   VAL A  92      14.605  20.487  40.803  1.00 62.08           C  
ATOM    619  O   VAL A  92      14.430  20.629  42.009  1.00 62.89           O  
ATOM    620  CB  VAL A  92      13.590  18.250  40.517  1.00 60.96           C  
ATOM    621  CG1 VAL A  92      12.339  18.906  39.973  1.00 59.83           C  
ATOM    622  CG2 VAL A  92      13.769  16.865  39.931  1.00 61.10           C  
ATOM    623  N   TYR A  93      14.610  21.501  39.954  1.00 62.89           N  
ATOM    624  CA  TYR A  93      14.442  22.872  40.419  1.00 63.72           C  
ATOM    625  C   TYR A  93      12.986  23.315  40.435  1.00 65.18           C  
ATOM    626  O   TYR A  93      12.204  22.950  39.561  1.00 64.82           O  
ATOM    627  CB  TYR A  93      15.268  23.813  39.539  1.00 62.07           C  
ATOM    628  CG  TYR A  93      16.760  23.563  39.631  1.00 61.42           C  
ATOM    629  CD1 TYR A  93      17.553  24.263  40.542  1.00 61.11           C  
ATOM    630  CD2 TYR A  93      17.369  22.577  38.854  1.00 60.94           C  
ATOM    631  CE1 TYR A  93      18.918  23.983  40.681  1.00 61.87           C  
ATOM    632  CE2 TYR A  93      18.731  22.286  38.988  1.00 62.56           C  
ATOM    633  CZ  TYR A  93      19.500  22.989  39.905  1.00 62.57           C  
ATOM    634  OH  TYR A  93      20.832  22.667  40.073  1.00 63.85           O  
ATOM    635  N   SER A  94      12.632  24.111  41.436  1.00 67.38           N  
ATOM    636  CA  SER A  94      11.273  24.616  41.579  1.00 69.29           C  
ATOM    637  C   SER A  94      11.238  26.137  41.394  1.00 70.87           C  
ATOM    638  O   SER A  94      12.277  26.802  41.444  1.00 72.24           O  
ATOM    639  CB  SER A  94      10.752  24.265  42.964  1.00 69.56           C  
ATOM    640  OG  SER A  94      11.653  24.738  43.941  1.00 69.79           O  
ATOM    641  N   ALA A  95      10.047  26.687  41.173  1.00 70.92           N  
ATOM    642  CA  ALA A  95       9.904  28.126  40.996  1.00 70.75           C  
ATOM    643  C   ALA A  95       8.450  28.530  41.116  1.00 70.89           C  
ATOM    644  O   ALA A  95       7.548  27.867  40.607  1.00 70.77           O  
ATOM    645  CB  ALA A  95      10.457  28.558  39.647  1.00 70.36           C  
ATOM    646  N   SER A  96       8.226  29.631  41.806  1.00 71.40           N  
ATOM    647  CA  SER A  96       6.880  30.114  42.003  1.00 72.00           C  
ATOM    648  C   SER A  96       6.452  30.896  40.775  1.00 71.87           C  
ATOM    649  O   SER A  96       5.270  31.169  40.573  1.00 72.82           O  
ATOM    650  CB  SER A  96       6.842  30.978  43.262  1.00 72.74           C  
ATOM    651  OG  SER A  96       7.986  31.817  43.321  1.00 74.77           O  
ATOM    652  N   THR A  97       7.426  31.223  39.941  1.00 71.45           N  
ATOM    653  CA  THR A  97       7.169  31.978  38.728  1.00 71.61           C  
ATOM    654  C   THR A  97       7.745  31.254  37.519  1.00 71.11           C  
ATOM    655  O   THR A  97       8.427  30.242  37.665  1.00 71.57           O  
ATOM    656  CB  THR A  97       7.825  33.346  38.812  1.00 72.64           C  
ATOM    657  OG1 THR A  97       7.702  34.012  37.550  1.00 74.94           O  
ATOM    658  CG2 THR A  97       9.305  33.189  39.194  1.00 72.74           C  
ATOM    659  N   HIS A  98       7.481  31.770  36.324  1.00 69.77           N  
ATOM    660  CA  HIS A  98       8.013  31.134  35.137  1.00 69.60           C  
ATOM    661  C   HIS A  98       9.525  31.317  35.004  1.00 69.47           C  
ATOM    662  O   HIS A  98      10.175  30.571  34.269  1.00 69.96           O  
ATOM    663  CB  HIS A  98       7.330  31.679  33.890  1.00 70.90           C  
ATOM    664  CG  HIS A  98       7.437  33.159  33.738  1.00 71.70           C  
ATOM    665  ND1 HIS A  98       6.647  34.035  34.454  1.00 72.22           N  
ATOM    666  CD2 HIS A  98       8.227  33.925  32.951  1.00 71.48           C  
ATOM    667  CE1 HIS A  98       6.949  35.279  34.112  1.00 72.00           C  
ATOM    668  NE2 HIS A  98       7.904  35.237  33.203  1.00 70.81           N  
ATOM    669  N   LYS A  99      10.080  32.314  35.695  1.00 68.68           N  
ATOM    670  CA  LYS A  99      11.522  32.574  35.644  1.00 67.06           C  
ATOM    671  C   LYS A  99      12.262  31.765  36.677  1.00 66.13           C  
ATOM    672  O   LYS A  99      11.953  31.832  37.863  1.00 65.38           O  
ATOM    673  CB  LYS A  99      11.848  34.053  35.884  1.00 66.80           C  
ATOM    674  CG  LYS A  99      11.820  34.902  34.632  1.00 68.59           C  
ATOM    675  CD  LYS A  99      12.736  36.118  34.730  1.00 69.73           C  
ATOM    676  CE  LYS A  99      12.191  37.202  35.655  1.00 70.79           C  
ATOM    677  NZ  LYS A  99      11.002  37.922  35.109  1.00 70.36           N  
ATOM    678  N   PHE A 100      13.242  31.007  36.206  1.00 66.52           N  
ATOM    679  CA  PHE A 100      14.046  30.191  37.092  1.00 68.34           C  
ATOM    680  C   PHE A 100      15.362  30.858  37.459  1.00 71.94           C  
ATOM    681  O   PHE A 100      16.184  31.205  36.592  1.00 71.33           O  
ATOM    682  CB  PHE A 100      14.330  28.825  36.473  1.00 65.88           C  
ATOM    683  CG  PHE A 100      13.205  27.845  36.627  1.00 63.53           C  
ATOM    684  CD1 PHE A 100      12.054  27.957  35.855  1.00 62.86           C  
ATOM    685  CD2 PHE A 100      13.302  26.794  37.533  1.00 62.19           C  
ATOM    686  CE1 PHE A 100      11.019  27.033  35.980  1.00 61.76           C  
ATOM    687  CE2 PHE A 100      12.274  25.869  37.667  1.00 60.96           C  
ATOM    688  CZ  PHE A 100      11.131  25.987  36.887  1.00 61.18           C  
ATOM    689  N   LEU A 101      15.541  31.026  38.770  1.00 76.19           N  
ATOM    690  CA  LEU A 101      16.735  31.638  39.347  1.00 79.90           C  
ATOM    691  C   LEU A 101      17.865  30.632  39.537  1.00 81.68           C  
ATOM    692  O   LEU A 101      17.855  29.847  40.491  1.00 81.84           O  
ATOM    693  CB  LEU A 101      16.415  32.271  40.716  1.00 81.59           C  
ATOM    694  CG  LEU A 101      17.632  32.794  41.516  1.00 83.87           C  
ATOM    695  CD1 LEU A 101      18.265  33.986  40.773  1.00 84.58           C  
ATOM    696  CD2 LEU A 101      17.223  33.189  42.948  1.00 82.86           C  
ATOM    697  N   TYR A 102      18.840  30.653  38.634  1.00 83.84           N  
ATOM    698  CA  TYR A 102      19.985  29.758  38.754  1.00 85.56           C  
ATOM    699  C   TYR A 102      21.016  30.397  39.704  1.00 84.76           C  
ATOM    700  O   TYR A 102      21.611  31.423  39.387  1.00 84.39           O  
ATOM    701  CB  TYR A 102      20.623  29.518  37.376  1.00 89.67           C  
ATOM    702  CG  TYR A 102      21.977  28.824  37.437  1.00 93.63           C  
ATOM    703  CD1 TYR A 102      22.085  27.489  37.831  1.00 94.75           C  
ATOM    704  CD2 TYR A 102      23.159  29.521  37.159  1.00 94.45           C  
ATOM    705  CE1 TYR A 102      23.329  26.870  37.953  1.00 94.00           C  
ATOM    706  CE2 TYR A 102      24.409  28.911  37.282  1.00 94.10           C  
ATOM    707  CZ  TYR A 102      24.485  27.584  37.682  1.00 94.13           C  
ATOM    708  OH  TYR A 102      25.709  26.969  37.838  1.00 93.29           O  
ATOM    709  N   TYR A 103      21.222  29.806  40.874  1.00 83.49           N  
ATOM    710  CA  TYR A 103      22.195  30.363  41.800  1.00 83.03           C  
ATOM    711  C   TYR A 103      23.267  29.331  42.154  1.00 81.44           C  
ATOM    712  O   TYR A 103      22.989  28.139  42.220  1.00 81.16           O  
ATOM    713  CB  TYR A 103      21.490  30.889  43.068  1.00 86.20           C  
ATOM    714  CG  TYR A 103      20.642  29.864  43.807  1.00 90.87           C  
ATOM    715  CD1 TYR A 103      19.415  29.434  43.296  1.00 92.85           C  
ATOM    716  CD2 TYR A 103      21.095  29.283  44.991  1.00 93.15           C  
ATOM    717  CE1 TYR A 103      18.657  28.433  43.951  1.00 95.27           C  
ATOM    718  CE2 TYR A 103      20.345  28.285  45.654  1.00 95.75           C  
ATOM    719  CZ  TYR A 103      19.129  27.864  45.130  1.00 96.29           C  
ATOM    720  OH  TYR A 103      18.397  26.885  45.783  1.00 96.99           O  
ATOM    721  N   ASP A 104      24.498  29.796  42.351  1.00 79.83           N  
ATOM    722  CA  ASP A 104      25.610  28.914  42.713  1.00 79.26           C  
ATOM    723  C   ASP A 104      25.686  28.831  44.232  1.00 80.07           C  
ATOM    724  O   ASP A 104      25.950  29.836  44.896  1.00 80.34           O  
ATOM    725  CB  ASP A 104      26.925  29.475  42.190  1.00 77.47           C  
ATOM    726  CG  ASP A 104      28.054  28.473  42.273  1.00 76.25           C  
ATOM    727  OD1 ASP A 104      28.232  27.829  43.328  1.00 75.67           O  
ATOM    728  OD2 ASP A 104      28.776  28.347  41.267  1.00 76.01           O  
ATOM    729  N   GLU A 105      25.472  27.636  44.776  1.00 80.09           N  
ATOM    730  CA  GLU A 105      25.490  27.447  46.224  1.00 79.03           C  
ATOM    731  C   GLU A 105      26.889  27.603  46.810  1.00 77.26           C  
ATOM    732  O   GLU A 105      27.046  27.902  47.991  1.00 77.54           O  
ATOM    733  CB  GLU A 105      24.920  26.071  46.558  1.00 81.52           C  
ATOM    734  CG  GLU A 105      23.730  25.712  45.671  1.00 86.01           C  
ATOM    735  CD  GLU A 105      22.805  24.687  46.295  1.00 88.14           C  
ATOM    736  OE1 GLU A 105      22.218  24.984  47.357  1.00 89.32           O  
ATOM    737  OE2 GLU A 105      22.653  23.590  45.717  1.00 88.43           O  
ATOM    738  N   LYS A 106      27.902  27.421  45.968  1.00 75.12           N  
ATOM    739  CA  LYS A 106      29.291  27.552  46.398  1.00 72.89           C  
ATOM    740  C   LYS A 106      29.766  29.015  46.509  1.00 72.32           C  
ATOM    741  O   LYS A 106      30.943  29.261  46.746  1.00 73.00           O  
ATOM    742  CB  LYS A 106      30.196  26.769  45.444  1.00 71.17           C  
ATOM    743  N   LYS A 107      28.855  29.974  46.340  1.00 71.78           N  
ATOM    744  CA  LYS A 107      29.190  31.397  46.442  1.00 70.47           C  
ATOM    745  C   LYS A 107      28.257  32.137  47.377  1.00 72.60           C  
ATOM    746  O   LYS A 107      28.410  33.335  47.587  1.00 73.15           O  
ATOM    747  CB  LYS A 107      29.107  32.078  45.076  1.00 67.29           C  
ATOM    748  CG  LYS A 107      30.259  31.790  44.170  1.00 62.67           C  
ATOM    749  CD  LYS A 107      30.089  32.485  42.837  1.00 60.72           C  
ATOM    750  CE  LYS A 107      31.225  32.131  41.885  1.00 60.65           C  
ATOM    751  NZ  LYS A 107      31.049  32.639  40.490  1.00 60.71           N  
ATOM    752  N   MET A 108      27.282  31.426  47.926  1.00 75.58           N  
ATOM    753  CA  MET A 108      26.308  32.048  48.818  1.00 79.14           C  
ATOM    754  C   MET A 108      26.921  32.588  50.094  1.00 80.24           C  
ATOM    755  O   MET A 108      26.318  33.390  50.811  1.00 80.47           O  
ATOM    756  CB  MET A 108      25.215  31.050  49.166  1.00 81.03           C  
ATOM    757  CG  MET A 108      24.438  30.590  47.955  1.00 84.40           C  
ATOM    758  SD  MET A 108      22.911  29.772  48.417  1.00 88.43           S  
ATOM    759  CE  MET A 108      22.109  31.123  49.441  1.00 87.66           C  
ATOM    760  N   ALA A 109      28.133  32.130  50.363  1.00 80.85           N  
ATOM    761  CA  ALA A 109      28.862  32.550  51.534  1.00 80.86           C  
ATOM    762  C   ALA A 109      29.134  34.056  51.476  1.00 81.64           C  
ATOM    763  O   ALA A 109      28.734  34.803  52.372  1.00 81.48           O  
ATOM    764  CB  ALA A 109      30.156  31.783  51.604  1.00 79.79           C  
ATOM    765  N   ASN A 110      29.806  34.488  50.413  1.00 82.77           N  
ATOM    766  CA  ASN A 110      30.159  35.896  50.230  1.00 83.21           C  
ATOM    767  C   ASN A 110      28.952  36.795  50.425  1.00 83.34           C  
ATOM    768  O   ASN A 110      28.957  37.687  51.274  1.00 84.52           O  
ATOM    769  CB  ASN A 110      30.728  36.139  48.826  1.00 83.93           C  
ATOM    770  CG  ASN A 110      31.744  35.094  48.417  1.00 84.61           C  
ATOM    771  OD1 ASN A 110      32.559  34.656  49.228  1.00 86.33           O  
ATOM    772  ND2 ASN A 110      31.704  34.691  47.150  1.00 82.88           N  
ATOM    773  N   PHE A 111      27.914  36.562  49.635  1.00 82.46           N  
ATOM    774  CA  PHE A 111      26.728  37.381  49.751  1.00 81.55           C  
ATOM    775  C   PHE A 111      25.689  36.704  50.620  1.00 82.99           C  
ATOM    776  O   PHE A 111      24.736  36.103  50.128  1.00 82.88           O  
ATOM    777  CB  PHE A 111      26.166  37.664  48.374  1.00 76.89           C  
ATOM    778  CG  PHE A 111      27.113  38.403  47.486  1.00 73.17           C  
ATOM    779  CD1 PHE A 111      28.320  37.831  47.094  1.00 71.84           C  
ATOM    780  CD2 PHE A 111      26.788  39.664  47.015  1.00 71.84           C  
ATOM    781  CE1 PHE A 111      29.185  38.503  46.236  1.00 70.91           C  
ATOM    782  CE2 PHE A 111      27.643  40.342  46.160  1.00 71.78           C  
ATOM    783  CZ  PHE A 111      28.846  39.760  45.766  1.00 70.80           C  
ATOM    784  N   GLN A 112      25.885  36.813  51.929  1.00 85.29           N  
ATOM    785  CA  GLN A 112      24.974  36.218  52.895  1.00 87.14           C  
ATOM    786  C   GLN A 112      23.642  36.960  52.838  1.00 87.57           C  
ATOM    787  O   GLN A 112      22.632  36.469  53.332  1.00 86.69           O  
ATOM    788  CB  GLN A 112      25.577  36.321  54.297  1.00 87.60           C  
ATOM    789  CG  GLN A 112      24.916  35.449  55.357  1.00 90.57           C  
ATOM    790  CD  GLN A 112      25.577  35.622  56.715  1.00 92.38           C  
ATOM    791  OE1 GLN A 112      26.801  35.521  56.835  1.00 92.98           O  
ATOM    792  NE2 GLN A 112      24.775  35.886  57.744  1.00 92.48           N  
ATOM    793  N   ASN A 113      23.657  38.145  52.228  1.00 89.50           N  
ATOM    794  CA  ASN A 113      22.459  38.968  52.096  1.00 91.49           C  
ATOM    795  C   ASN A 113      21.585  38.474  50.955  1.00 93.06           C  
ATOM    796  O   ASN A 113      20.586  39.113  50.594  1.00 92.32           O  
ATOM    797  CB  ASN A 113      22.842  40.424  51.828  1.00 91.66           C  
ATOM    798  CG  ASN A 113      22.238  41.371  52.838  1.00 93.46           C  
ATOM    799  OD1 ASN A 113      22.236  42.588  52.651  1.00 92.82           O  
ATOM    800  ND2 ASN A 113      21.730  40.813  53.933  1.00 93.84           N  
ATOM    801  N   PHE A 114      21.968  37.331  50.389  1.00 95.08           N  
ATOM    802  CA  PHE A 114      21.254  36.720  49.271  1.00 96.25           C  
ATOM    803  C   PHE A 114      20.398  35.523  49.673  1.00 96.70           C  
ATOM    804  O   PHE A 114      20.878  34.573  50.293  1.00 96.89           O  
ATOM    805  CB  PHE A 114      22.261  36.281  48.203  1.00 96.81           C  
ATOM    806  CG  PHE A 114      21.657  35.462  47.088  1.00 98.12           C  
ATOM    807  CD1 PHE A 114      20.600  35.955  46.330  1.00 98.41           C  
ATOM    808  CD2 PHE A 114      22.156  34.195  46.791  1.00 98.67           C  
ATOM    809  CE1 PHE A 114      20.046  35.201  45.286  1.00 98.34           C  
ATOM    810  CE2 PHE A 114      21.609  33.433  45.750  1.00 98.96           C  
ATOM    811  CZ  PHE A 114      20.553  33.937  44.997  1.00 98.43           C  
ATOM    812  N   LYS A 115      19.124  35.577  49.299  1.00 97.18           N  
ATOM    813  CA  LYS A 115      18.183  34.502  49.594  1.00 97.49           C  
ATOM    814  C   LYS A 115      17.607  33.965  48.275  1.00 98.13           C  
ATOM    815  O   LYS A 115      16.923  34.684  47.549  1.00 99.07           O  
ATOM    816  CB  LYS A 115      17.066  35.020  50.491  1.00 96.07           C  
ATOM    817  N   PRO A 116      17.887  32.691  47.952  1.00 99.57           N  
ATOM    818  CA  PRO A 116      17.429  32.009  46.734  1.00100.58           C  
ATOM    819  C   PRO A 116      15.922  32.054  46.488  1.00101.21           C  
ATOM    820  O   PRO A 116      15.128  31.895  47.420  1.00101.58           O  
ATOM    821  CB  PRO A 116      17.914  30.578  46.935  1.00101.45           C  
ATOM    822  CG  PRO A 116      19.146  30.757  47.734  1.00102.12           C  
ATOM    823  CD  PRO A 116      18.733  31.790  48.754  1.00101.43           C  
ATOM    824  N   ARG A 117      15.548  32.257  45.222  1.00101.94           N  
ATOM    825  CA  ARG A 117      14.145  32.309  44.797  1.00102.36           C  
ATOM    826  C   ARG A 117      13.764  31.015  44.050  1.00101.85           C  
ATOM    827  O   ARG A 117      12.737  30.962  43.358  1.00102.11           O  
ATOM    828  CB  ARG A 117      13.903  33.538  43.896  1.00102.32           C  
ATOM    829  N   SER A 118      14.606  29.986  44.206  1.00100.75           N  
ATOM    830  CA  SER A 118      14.417  28.658  43.605  1.00 99.21           C  
ATOM    831  C   SER A 118      14.995  27.572  44.532  1.00 97.84           C  
ATOM    832  O   SER A 118      16.091  27.708  45.082  1.00 98.58           O  
ATOM    833  CB  SER A 118      15.091  28.589  42.226  1.00 99.00           C  
ATOM    834  OG  SER A 118      14.436  29.441  41.298  1.00 98.32           O  
ATOM    835  N   ASN A 119      14.254  26.493  44.719  1.00 95.87           N  
ATOM    836  CA  ASN A 119      14.730  25.447  45.597  1.00 94.13           C  
ATOM    837  C   ASN A 119      15.017  24.185  44.818  1.00 92.82           C  
ATOM    838  O   ASN A 119      14.152  23.664  44.127  1.00 92.67           O  
ATOM    839  CB  ASN A 119      13.703  25.184  46.687  1.00 93.43           C  
ATOM    840  N   ARG A 120      16.247  23.706  44.923  1.00 91.52           N  
ATOM    841  CA  ARG A 120      16.645  22.483  44.242  1.00 91.16           C  
ATOM    842  C   ARG A 120      16.290  21.301  45.143  1.00 91.42           C  
ATOM    843  O   ARG A 120      16.110  21.476  46.347  1.00 92.82           O  
ATOM    844  CB  ARG A 120      18.150  22.499  43.974  1.00 91.49           C  
ATOM    845  CG  ARG A 120      18.680  21.225  43.334  1.00 92.67           C  
ATOM    846  CD  ARG A 120      20.112  21.391  42.844  1.00 93.41           C  
ATOM    847  NE  ARG A 120      21.047  21.496  43.951  1.00 94.49           N  
ATOM    848  CZ  ARG A 120      21.337  20.487  44.762  1.00 95.74           C  
ATOM    849  NH1 ARG A 120      20.764  19.307  44.571  1.00 96.14           N  
ATOM    850  NH2 ARG A 120      22.183  20.656  45.769  1.00 96.76           N  
ATOM    851  N   GLU A 121      16.181  20.103  44.568  1.00 90.37           N  
ATOM    852  CA  GLU A 121      15.862  18.904  45.349  1.00 88.57           C  
ATOM    853  C   GLU A 121      16.143  17.616  44.574  1.00 85.96           C  
ATOM    854  O   GLU A 121      15.678  17.454  43.458  1.00 85.88           O  
ATOM    855  CB  GLU A 121      14.388  18.910  45.762  1.00 90.41           C  
ATOM    856  CG  GLU A 121      14.056  17.848  46.802  1.00 94.71           C  
ATOM    857  CD  GLU A 121      12.570  17.725  47.070  1.00 96.65           C  
ATOM    858  OE1 GLU A 121      11.933  18.759  47.362  1.00 98.77           O  
ATOM    859  OE2 GLU A 121      12.038  16.596  46.994  1.00 97.13           O  
ATOM    860  N   GLU A 122      16.892  16.698  45.170  1.00 83.72           N  
ATOM    861  CA  GLU A 122      17.189  15.434  44.507  1.00 81.77           C  
ATOM    862  C   GLU A 122      16.005  14.501  44.654  1.00 79.72           C  
ATOM    863  O   GLU A 122      15.324  14.534  45.668  1.00 79.80           O  
ATOM    864  CB  GLU A 122      18.413  14.782  45.135  1.00 83.26           C  
ATOM    865  CG  GLU A 122      19.625  15.640  45.036  1.00 86.79           C  
ATOM    866  CD  GLU A 122      19.947  15.973  43.607  1.00 89.00           C  
ATOM    867  OE1 GLU A 122      20.312  15.046  42.852  1.00 90.20           O  
ATOM    868  OE2 GLU A 122      19.820  17.158  43.233  1.00 90.64           O  
ATOM    869  N   MET A 123      15.761  13.674  43.644  1.00 77.35           N  
ATOM    870  CA  MET A 123      14.649  12.731  43.701  1.00 75.20           C  
ATOM    871  C   MET A 123      14.694  11.694  42.585  1.00 74.85           C  
ATOM    872  O   MET A 123      15.404  11.864  41.595  1.00 74.36           O  
ATOM    873  CB  MET A 123      13.308  13.485  43.669  1.00 73.18           C  
ATOM    874  CG  MET A 123      13.055  14.339  42.430  1.00 70.92           C  
ATOM    875  SD  MET A 123      11.421  15.130  42.412  1.00 68.22           S  
ATOM    876  CE  MET A 123      11.700  16.497  43.461  1.00 66.01           C  
ATOM    877  N   LYS A 124      13.945  10.607  42.766  1.00 74.57           N  
ATOM    878  CA  LYS A 124      13.884   9.548  41.771  1.00 73.40           C  
ATOM    879  C   LYS A 124      12.965  10.002  40.660  1.00 72.93           C  
ATOM    880  O   LYS A 124      12.038  10.789  40.880  1.00 71.18           O  
ATOM    881  CB  LYS A 124      13.364   8.245  42.381  1.00 73.69           C  
ATOM    882  CG  LYS A 124      14.223   7.726  43.511  1.00 72.21           C  
ATOM    883  CD  LYS A 124      15.615   7.384  43.020  1.00 73.07           C  
ATOM    884  CE  LYS A 124      16.549   7.064  44.173  1.00 72.80           C  
ATOM    885  NZ  LYS A 124      17.915   6.726  43.687  1.00 73.40           N  
ATOM    886  N   PHE A 125      13.220   9.492  39.464  1.00 73.35           N  
ATOM    887  CA  PHE A 125      12.439   9.891  38.315  1.00 74.26           C  
ATOM    888  C   PHE A 125      10.964   9.699  38.558  1.00 75.29           C  
ATOM    889  O   PHE A 125      10.173  10.631  38.399  1.00 74.30           O  
ATOM    890  CB  PHE A 125      12.859   9.112  37.071  1.00 72.75           C  
ATOM    891  CG  PHE A 125      12.672   9.881  35.798  1.00 71.08           C  
ATOM    892  CD1 PHE A 125      13.729  10.576  35.230  1.00 69.87           C  
ATOM    893  CD2 PHE A 125      11.425   9.942  35.189  1.00 70.36           C  
ATOM    894  CE1 PHE A 125      13.546  11.322  34.072  1.00 68.61           C  
ATOM    895  CE2 PHE A 125      11.232  10.689  34.030  1.00 68.84           C  
ATOM    896  CZ  PHE A 125      12.292  11.378  33.472  1.00 68.41           C  
ATOM    897  N   HIS A 126      10.603   8.486  38.954  1.00 77.25           N  
ATOM    898  CA  HIS A 126       9.211   8.170  39.199  1.00 79.59           C  
ATOM    899  C   HIS A 126       8.589   9.221  40.110  1.00 79.84           C  
ATOM    900  O   HIS A 126       7.416   9.568  39.962  1.00 79.71           O  
ATOM    901  CB  HIS A 126       9.090   6.756  39.809  1.00 81.14           C  
ATOM    902  CG  HIS A 126       9.342   6.690  41.284  1.00 82.81           C  
ATOM    903  ND1 HIS A 126       8.340   6.846  42.217  1.00 82.42           N  
ATOM    904  CD2 HIS A 126      10.482   6.495  41.990  1.00 83.16           C  
ATOM    905  CE1 HIS A 126       8.850   6.753  43.434  1.00 83.34           C  
ATOM    906  NE2 HIS A 126      10.151   6.539  43.324  1.00 83.18           N  
ATOM    907  N   GLU A 127       9.390   9.762  41.023  1.00 79.86           N  
ATOM    908  CA  GLU A 127       8.891  10.763  41.953  1.00 79.92           C  
ATOM    909  C   GLU A 127       8.642  12.049  41.208  1.00 79.41           C  
ATOM    910  O   GLU A 127       7.581  12.673  41.342  1.00 78.46           O  
ATOM    911  CB  GLU A 127       9.907  10.998  43.058  1.00 80.92           C  
ATOM    912  CG  GLU A 127      10.441   9.718  43.661  1.00 83.51           C  
ATOM    913  CD  GLU A 127      11.354   9.969  44.835  1.00 85.10           C  
ATOM    914  OE1 GLU A 127      12.112   9.054  45.214  1.00 88.19           O  
ATOM    915  OE2 GLU A 127      11.297  11.083  45.401  1.00 85.59           O  
ATOM    916  N   PHE A 128       9.634  12.444  40.421  1.00 78.91           N  
ATOM    917  CA  PHE A 128       9.533  13.650  39.630  1.00 78.06           C  
ATOM    918  C   PHE A 128       8.246  13.620  38.818  1.00 78.32           C  
ATOM    919  O   PHE A 128       7.480  14.579  38.832  1.00 77.54           O  
ATOM    920  CB  PHE A 128      10.742  13.758  38.701  1.00 76.61           C  
ATOM    921  CG  PHE A 128      10.574  14.767  37.595  1.00 74.63           C  
ATOM    922  CD1 PHE A 128      10.237  16.089  37.876  1.00 73.99           C  
ATOM    923  CD2 PHE A 128      10.760  14.394  36.269  1.00 72.06           C  
ATOM    924  CE1 PHE A 128      10.088  17.027  36.846  1.00 72.23           C  
ATOM    925  CE2 PHE A 128      10.615  15.319  35.241  1.00 70.95           C  
ATOM    926  CZ  PHE A 128      10.280  16.635  35.527  1.00 70.90           C  
ATOM    927  N   VAL A 129       8.007  12.511  38.123  1.00 79.27           N  
ATOM    928  CA  VAL A 129       6.822  12.348  37.279  1.00 80.16           C  
ATOM    929  C   VAL A 129       5.538  12.507  38.088  1.00 80.58           C  
ATOM    930  O   VAL A 129       4.556  13.116  37.645  1.00 78.86           O  
ATOM    931  CB  VAL A 129       6.824  10.956  36.606  1.00 79.70           C  
ATOM    932  CG1 VAL A 129       5.679  10.851  35.619  1.00 79.16           C  
ATOM    933  CG2 VAL A 129       8.163  10.715  35.908  1.00 78.30           C  
ATOM    934  N   GLU A 130       5.553  11.942  39.284  1.00 81.90           N  
ATOM    935  CA  GLU A 130       4.408  12.014  40.158  1.00 83.83           C  
ATOM    936  C   GLU A 130       4.170  13.446  40.593  1.00 83.97           C  
ATOM    937  O   GLU A 130       3.043  13.941  40.520  1.00 83.83           O  
ATOM    938  CB  GLU A 130       4.637  11.125  41.371  1.00 85.97           C  
ATOM    939  CG  GLU A 130       4.442   9.647  41.085  1.00 90.28           C  
ATOM    940  CD  GLU A 130       5.357   8.757  41.910  1.00 93.48           C  
ATOM    941  OE1 GLU A 130       5.556   9.033  43.113  1.00 94.98           O  
ATOM    942  OE2 GLU A 130       5.873   7.762  41.356  1.00 95.52           O  
ATOM    943  N   LYS A 131       5.239  14.105  41.043  1.00 84.51           N  
ATOM    944  CA  LYS A 131       5.170  15.486  41.514  1.00 84.68           C  
ATOM    945  C   LYS A 131       4.699  16.395  40.401  1.00 85.11           C  
ATOM    946  O   LYS A 131       4.116  17.446  40.634  1.00 84.30           O  
ATOM    947  CB  LYS A 131       6.546  15.944  42.021  1.00 83.37           C  
ATOM    948  N   LEU A 132       4.956  15.967  39.178  1.00 87.38           N  
ATOM    949  CA  LEU A 132       4.574  16.738  38.015  1.00 89.56           C  
ATOM    950  C   LEU A 132       3.118  16.498  37.650  1.00 91.06           C  
ATOM    951  O   LEU A 132       2.342  17.445  37.484  1.00 91.01           O  
ATOM    952  CB  LEU A 132       5.473  16.360  36.845  1.00 90.02           C  
ATOM    953  CG  LEU A 132       5.353  17.224  35.599  1.00 89.73           C  
ATOM    954  CD1 LEU A 132       5.709  18.660  35.931  1.00 89.78           C  
ATOM    955  CD2 LEU A 132       6.286  16.678  34.541  1.00 90.08           C  
ATOM    956  N   GLN A 133       2.755  15.221  37.523  1.00 93.19           N  
ATOM    957  CA  GLN A 133       1.394  14.831  37.175  1.00 94.49           C  
ATOM    958  C   GLN A 133       0.460  15.318  38.267  1.00 95.66           C  
ATOM    959  O   GLN A 133      -0.728  15.518  38.033  1.00 95.11           O  
ATOM    960  CB  GLN A 133       1.302  13.307  37.034  1.00 94.61           C  
ATOM    961  N   ASP A 134       1.017  15.515  39.458  1.00 97.67           N  
ATOM    962  CA  ASP A 134       0.261  15.985  40.608  1.00 99.65           C  
ATOM    963  C   ASP A 134      -0.194  17.431  40.401  1.00100.72           C  
ATOM    964  O   ASP A 134      -1.385  17.744  40.497  1.00100.02           O  
ATOM    965  CB  ASP A 134       1.128  15.864  41.864  1.00100.01           C  
ATOM    966  CG  ASP A 134       0.355  16.141  43.131  1.00102.17           C  
ATOM    967  OD1 ASP A 134       0.674  15.524  44.175  1.00102.49           O  
ATOM    968  OD2 ASP A 134      -0.569  16.981  43.087  1.00103.03           O  
ATOM    969  N   ILE A 135       0.762  18.307  40.113  1.00102.69           N  
ATOM    970  CA  ILE A 135       0.480  19.714  39.867  1.00104.52           C  
ATOM    971  C   ILE A 135      -0.589  19.832  38.784  1.00105.87           C  
ATOM    972  O   ILE A 135      -1.656  20.403  39.000  1.00106.46           O  
ATOM    973  CB  ILE A 135       1.736  20.449  39.375  1.00104.24           C  
ATOM    974  CG1 ILE A 135       2.879  20.270  40.371  1.00104.09           C  
ATOM    975  CG2 ILE A 135       1.436  21.919  39.194  1.00105.14           C  
ATOM    976  CD1 ILE A 135       4.192  20.825  39.876  1.00103.37           C  
ATOM    977  N   GLN A 136      -0.286  19.284  37.615  1.00107.52           N  
ATOM    978  CA  GLN A 136      -1.208  19.328  36.491  1.00109.11           C  
ATOM    979  C   GLN A 136      -2.591  18.816  36.867  1.00109.69           C  
ATOM    980  O   GLN A 136      -3.603  19.390  36.469  1.00109.54           O  
ATOM    981  CB  GLN A 136      -0.654  18.501  35.329  1.00110.07           C  
ATOM    982  CG  GLN A 136       0.732  18.941  34.884  1.00111.25           C  
ATOM    983  CD  GLN A 136       1.223  18.197  33.657  1.00111.72           C  
ATOM    984  OE1 GLN A 136       1.369  16.976  33.671  1.00112.24           O  
ATOM    985  NE2 GLN A 136       1.484  18.938  32.583  1.00111.91           N  
ATOM    986  N   GLN A 137      -2.624  17.739  37.644  1.00110.70           N  
ATOM    987  CA  GLN A 137      -3.884  17.135  38.063  1.00111.53           C  
ATOM    988  C   GLN A 137      -4.521  17.822  39.267  1.00111.46           C  
ATOM    989  O   GLN A 137      -5.512  17.336  39.807  1.00112.11           O  
ATOM    990  CB  GLN A 137      -3.679  15.648  38.359  1.00111.53           C  
ATOM    991  N   ARG A 138      -3.964  18.949  39.692  1.00110.81           N  
ATOM    992  CA  ARG A 138      -4.548  19.658  40.821  1.00109.88           C  
ATOM    993  C   ARG A 138      -4.677  21.143  40.533  1.00109.23           C  
ATOM    994  O   ARG A 138      -4.889  21.938  41.450  1.00108.39           O  
ATOM    995  CB  ARG A 138      -3.705  19.460  42.076  1.00110.14           C  
ATOM    996  CG  ARG A 138      -2.413  20.233  42.062  1.00111.09           C  
ATOM    997  CD  ARG A 138      -1.734  20.147  43.405  1.00111.84           C  
ATOM    998  NE  ARG A 138      -0.516  20.946  43.450  1.00112.64           N  
ATOM    999  CZ  ARG A 138       0.294  21.003  44.501  1.00113.33           C  
ATOM   1000  NH1 ARG A 138       0.016  20.303  45.594  1.00113.67           N  
ATOM   1001  NH2 ARG A 138       1.384  21.758  44.463  1.00113.12           N  
ATOM   1002  N   GLY A 139      -4.547  21.514  39.260  1.00108.88           N  
ATOM   1003  CA  GLY A 139      -4.666  22.907  38.863  1.00108.31           C  
ATOM   1004  C   GLY A 139      -3.739  23.849  39.609  1.00107.78           C  
ATOM   1005  O   GLY A 139      -4.114  24.980  39.935  1.00108.46           O  
ATOM   1006  N   GLY A 140      -2.525  23.385  39.886  1.00106.59           N  
ATOM   1007  CA  GLY A 140      -1.566  24.214  40.592  1.00104.22           C  
ATOM   1008  C   GLY A 140      -1.009  25.333  39.724  1.00102.53           C  
ATOM   1009  O   GLY A 140      -1.488  25.559  38.603  1.00102.53           O  
ATOM   1010  N   GLU A 141       0.003  26.034  40.241  1.00100.03           N  
ATOM   1011  CA  GLU A 141       0.644  27.143  39.528  1.00 97.08           C  
ATOM   1012  C   GLU A 141       2.177  27.008  39.557  1.00 94.24           C  
ATOM   1013  O   GLU A 141       2.896  27.621  38.760  1.00 94.07           O  
ATOM   1014  CB  GLU A 141       0.243  28.477  40.159  1.00 97.47           C  
ATOM   1015  CG  GLU A 141       0.652  29.677  39.332  1.00 99.23           C  
ATOM   1016  CD  GLU A 141       0.834  30.920  40.172  1.00100.58           C  
ATOM   1017  OE1 GLU A 141       1.829  31.001  40.934  1.00 99.52           O  
ATOM   1018  OE2 GLU A 141      -0.024  31.822  40.073  1.00101.48           O  
ATOM   1019  N   GLU A 142       2.670  26.203  40.491  1.00 90.74           N  
ATOM   1020  CA  GLU A 142       4.096  25.969  40.613  1.00 87.22           C  
ATOM   1021  C   GLU A 142       4.669  25.378  39.320  1.00 84.61           C  
ATOM   1022  O   GLU A 142       3.949  24.764  38.524  1.00 85.08           O  
ATOM   1023  CB  GLU A 142       4.359  25.016  41.771  1.00 88.22           C  
ATOM   1024  CG  GLU A 142       5.812  24.610  41.904  1.00 89.78           C  
ATOM   1025  CD  GLU A 142       6.037  23.633  43.033  1.00 91.22           C  
ATOM   1026  OE1 GLU A 142       5.251  22.666  43.146  1.00 92.16           O  
ATOM   1027  OE2 GLU A 142       7.009  23.820  43.797  1.00 91.57           O  
ATOM   1028  N   ARG A 143       5.973  25.561  39.128  1.00 80.47           N  
ATOM   1029  CA  ARG A 143       6.677  25.059  37.954  1.00 76.05           C  
ATOM   1030  C   ARG A 143       7.918  24.272  38.372  1.00 73.14           C  
ATOM   1031  O   ARG A 143       8.492  24.524  39.424  1.00 72.79           O  
ATOM   1032  CB  ARG A 143       7.078  26.231  37.069  1.00 75.40           C  
ATOM   1033  CG  ARG A 143       5.905  27.006  36.536  1.00 75.21           C  
ATOM   1034  CD  ARG A 143       6.329  28.414  36.243  1.00 77.00           C  
ATOM   1035  NE  ARG A 143       5.342  29.144  35.460  1.00 79.61           N  
ATOM   1036  CZ  ARG A 143       5.063  28.864  34.193  1.00 80.46           C  
ATOM   1037  NH1 ARG A 143       5.701  27.868  33.586  1.00 80.63           N  
ATOM   1038  NH2 ARG A 143       4.173  29.587  33.526  1.00 80.93           N  
ATOM   1039  N   LEU A 144       8.327  23.322  37.540  1.00 70.46           N  
ATOM   1040  CA  LEU A 144       9.501  22.501  37.830  1.00 68.38           C  
ATOM   1041  C   LEU A 144      10.440  22.451  36.627  1.00 66.83           C  
ATOM   1042  O   LEU A 144      10.074  22.896  35.550  1.00 67.66           O  
ATOM   1043  CB  LEU A 144       9.066  21.085  38.186  1.00 68.06           C  
ATOM   1044  CG  LEU A 144       8.234  20.943  39.448  1.00 68.97           C  
ATOM   1045  CD1 LEU A 144       7.758  19.510  39.580  1.00 69.06           C  
ATOM   1046  CD2 LEU A 144       9.079  21.341  40.639  1.00 68.38           C  
ATOM   1047  N   TYR A 145      11.643  21.910  36.805  1.00 64.50           N  
ATOM   1048  CA  TYR A 145      12.611  21.806  35.712  1.00 62.67           C  
ATOM   1049  C   TYR A 145      13.674  20.808  36.135  1.00 61.91           C  
ATOM   1050  O   TYR A 145      14.356  21.024  37.128  1.00 61.75           O  
ATOM   1051  CB  TYR A 145      13.278  23.160  35.441  1.00 62.26           C  
ATOM   1052  CG  TYR A 145      13.687  23.385  34.000  1.00 61.59           C  
ATOM   1053  CD1 TYR A 145      14.346  22.396  33.272  1.00 61.58           C  
ATOM   1054  CD2 TYR A 145      13.403  24.592  33.363  1.00 61.84           C  
ATOM   1055  CE1 TYR A 145      14.708  22.603  31.938  1.00 62.86           C  
ATOM   1056  CE2 TYR A 145      13.761  24.813  32.039  1.00 63.10           C  
ATOM   1057  CZ  TYR A 145      14.412  23.816  31.331  1.00 63.68           C  
ATOM   1058  OH  TYR A 145      14.769  24.045  30.024  1.00 64.77           O  
ATOM   1059  N   LEU A 146      13.815  19.724  35.383  1.00 61.14           N  
ATOM   1060  CA  LEU A 146      14.799  18.711  35.727  1.00 60.37           C  
ATOM   1061  C   LEU A 146      16.068  18.923  34.942  1.00 60.19           C  
ATOM   1062  O   LEU A 146      16.053  18.966  33.716  1.00 61.59           O  
ATOM   1063  CB  LEU A 146      14.253  17.316  35.440  1.00 60.38           C  
ATOM   1064  CG  LEU A 146      15.143  16.107  35.752  1.00 61.24           C  
ATOM   1065  CD1 LEU A 146      14.251  14.927  36.051  1.00 62.38           C  
ATOM   1066  CD2 LEU A 146      16.073  15.784  34.593  1.00 60.19           C  
ATOM   1067  N   GLN A 147      17.169  19.042  35.660  1.00 58.79           N  
ATOM   1068  CA  GLN A 147      18.450  19.260  35.026  1.00 57.42           C  
ATOM   1069  C   GLN A 147      19.413  18.293  35.678  1.00 56.96           C  
ATOM   1070  O   GLN A 147      19.819  18.516  36.801  1.00 57.95           O  
ATOM   1071  CB  GLN A 147      18.890  20.699  35.281  1.00 56.71           C  
ATOM   1072  CG  GLN A 147      17.871  21.734  34.822  1.00 57.41           C  
ATOM   1073  CD  GLN A 147      18.251  23.158  35.194  1.00 58.67           C  
ATOM   1074  OE1 GLN A 147      17.551  24.112  34.839  1.00 57.16           O  
ATOM   1075  NE2 GLN A 147      19.353  23.310  35.921  1.00 58.67           N  
ATOM   1076  N   GLN A 148      19.777  17.225  34.986  1.00 56.81           N  
ATOM   1077  CA  GLN A 148      20.692  16.255  35.571  1.00 57.53           C  
ATOM   1078  C   GLN A 148      21.699  15.698  34.572  1.00 58.22           C  
ATOM   1079  O   GLN A 148      21.355  15.390  33.436  1.00 58.06           O  
ATOM   1080  CB  GLN A 148      19.886  15.116  36.214  1.00 59.14           C  
ATOM   1081  CG  GLN A 148      20.721  13.968  36.788  1.00 60.29           C  
ATOM   1082  CD  GLN A 148      21.674  14.416  37.879  1.00 61.84           C  
ATOM   1083  OE1 GLN A 148      21.274  15.083  38.837  1.00 63.08           O  
ATOM   1084  NE2 GLN A 148      22.944  14.040  37.748  1.00 62.49           N  
ATOM   1085  N   THR A 149      22.950  15.571  35.006  1.00 59.08           N  
ATOM   1086  CA  THR A 149      23.999  15.038  34.152  1.00 61.40           C  
ATOM   1087  C   THR A 149      23.744  13.562  33.852  1.00 64.52           C  
ATOM   1088  O   THR A 149      23.143  12.849  34.652  1.00 65.46           O  
ATOM   1089  CB  THR A 149      25.354  15.166  34.831  1.00 60.31           C  
ATOM   1090  OG1 THR A 149      25.499  16.499  35.328  1.00 58.42           O  
ATOM   1091  CG2 THR A 149      26.473  14.869  33.851  1.00 60.53           C  
ATOM   1092  N   LEU A 150      24.209  13.096  32.703  1.00 67.70           N  
ATOM   1093  CA  LEU A 150      24.009  11.703  32.343  1.00 71.47           C  
ATOM   1094  C   LEU A 150      25.194  10.870  32.773  1.00 75.17           C  
ATOM   1095  O   LEU A 150      26.121  10.659  31.991  1.00 75.66           O  
ATOM   1096  CB  LEU A 150      23.827  11.561  30.841  1.00 70.77           C  
ATOM   1097  CG  LEU A 150      22.626  12.272  30.241  1.00 71.35           C  
ATOM   1098  CD1 LEU A 150      22.538  11.957  28.757  1.00 70.35           C  
ATOM   1099  CD2 LEU A 150      21.374  11.814  30.965  1.00 71.84           C  
ATOM   1100  N   ASN A 151      25.153  10.385  34.011  1.00 79.24           N  
ATOM   1101  CA  ASN A 151      26.222   9.570  34.579  1.00 82.13           C  
ATOM   1102  C   ASN A 151      26.069   8.093  34.246  1.00 83.29           C  
ATOM   1103  O   ASN A 151      25.605   7.737  33.164  1.00 82.85           O  
ATOM   1104  CB  ASN A 151      26.260   9.769  36.093  1.00 83.72           C  
ATOM   1105  CG  ASN A 151      24.872   9.837  36.700  1.00 85.62           C  
ATOM   1106  OD1 ASN A 151      24.088   8.892  36.590  1.00 85.58           O  
ATOM   1107  ND2 ASN A 151      24.559  10.960  37.337  1.00 86.01           N  
ATOM   1108  N   ASP A 152      26.449   7.235  35.186  1.00 85.27           N  
ATOM   1109  CA  ASP A 152      26.385   5.796  34.971  1.00 86.79           C  
ATOM   1110  C   ASP A 152      25.146   5.166  35.581  1.00 85.81           C  
ATOM   1111  O   ASP A 152      24.780   4.050  35.233  1.00 84.83           O  
ATOM   1112  CB  ASP A 152      27.621   5.128  35.560  1.00 90.20           C  
ATOM   1113  CG  ASP A 152      28.877   5.933  35.331  1.00 94.40           C  
ATOM   1114  OD1 ASP A 152      29.185   6.253  34.156  1.00 95.74           O  
ATOM   1115  OD2 ASP A 152      29.559   6.251  36.330  1.00 96.59           O  
ATOM   1116  N   THR A 153      24.504   5.888  36.491  1.00 85.56           N  
ATOM   1117  CA  THR A 153      23.300   5.406  37.170  1.00 86.49           C  
ATOM   1118  C   THR A 153      22.120   5.322  36.190  1.00 86.10           C  
ATOM   1119  O   THR A 153      20.956   5.240  36.604  1.00 86.77           O  
ATOM   1120  CB  THR A 153      22.914   6.361  38.334  1.00 86.94           C  
ATOM   1121  OG1 THR A 153      24.109   6.890  38.924  1.00 86.88           O  
ATOM   1122  CG2 THR A 153      22.104   5.622  39.407  1.00 87.94           C  
ATOM   1123  N   VAL A 154      22.428   5.336  34.894  1.00 84.99           N  
ATOM   1124  CA  VAL A 154      21.403   5.305  33.858  1.00 82.78           C  
ATOM   1125  C   VAL A 154      21.032   3.890  33.445  1.00 81.78           C  
ATOM   1126  O   VAL A 154      21.887   3.011  33.369  1.00 81.17           O  
ATOM   1127  CB  VAL A 154      21.876   6.080  32.615  1.00 81.90           C  
ATOM   1128  CG1 VAL A 154      20.746   6.208  31.629  1.00 81.99           C  
ATOM   1129  CG2 VAL A 154      22.374   7.459  33.024  1.00 81.17           C  
ATOM   1130  N   GLY A 155      19.746   3.681  33.180  1.00 81.29           N  
ATOM   1131  CA  GLY A 155      19.267   2.375  32.780  1.00 80.89           C  
ATOM   1132  C   GLY A 155      20.010   1.812  31.585  1.00 81.09           C  
ATOM   1133  O   GLY A 155      20.650   2.543  30.836  1.00 81.58           O  
ATOM   1134  N   ARG A 156      19.903   0.501  31.405  1.00 81.40           N  
ATOM   1135  CA  ARG A 156      20.576  -0.195  30.309  1.00 80.61           C  
ATOM   1136  C   ARG A 156      20.053   0.259  28.946  1.00 78.04           C  
ATOM   1137  O   ARG A 156      20.821   0.637  28.061  1.00 76.90           O  
ATOM   1138  CB  ARG A 156      20.374  -1.718  30.451  1.00 83.56           C  
ATOM   1139  CG  ARG A 156      20.683  -2.296  31.858  1.00 87.45           C  
ATOM   1140  CD  ARG A 156      19.482  -3.066  32.475  1.00 89.29           C  
ATOM   1141  NE  ARG A 156      18.322  -2.209  32.741  1.00 89.54           N  
ATOM   1142  CZ  ARG A 156      18.245  -1.349  33.750  1.00 89.31           C  
ATOM   1143  NH1 ARG A 156      19.256  -1.246  34.596  1.00 89.31           N  
ATOM   1144  NH2 ARG A 156      17.176  -0.578  33.900  1.00 89.18           N  
ATOM   1145  N   LYS A 157      18.734   0.227  28.795  1.00 75.97           N  
ATOM   1146  CA  LYS A 157      18.091   0.588  27.541  1.00 73.80           C  
ATOM   1147  C   LYS A 157      18.420   2.001  27.100  1.00 72.08           C  
ATOM   1148  O   LYS A 157      18.565   2.275  25.903  1.00 71.88           O  
ATOM   1149  CB  LYS A 157      16.585   0.428  27.676  1.00 74.35           C  
ATOM   1150  CG  LYS A 157      15.896   0.154  26.361  1.00 76.37           C  
ATOM   1151  CD  LYS A 157      14.411  -0.082  26.596  1.00 79.65           C  
ATOM   1152  CE  LYS A 157      13.619  -0.246  25.297  1.00 81.81           C  
ATOM   1153  NZ  LYS A 157      12.136  -0.109  25.501  1.00 82.38           N  
ATOM   1154  N   ILE A 158      18.530   2.888  28.086  1.00 69.67           N  
ATOM   1155  CA  ILE A 158      18.853   4.277  27.825  1.00 65.90           C  
ATOM   1156  C   ILE A 158      20.294   4.382  27.371  1.00 65.43           C  
ATOM   1157  O   ILE A 158      20.633   5.243  26.585  1.00 65.29           O  
ATOM   1158  CB  ILE A 158      18.675   5.132  29.069  1.00 63.27           C  
ATOM   1159  CG1 ILE A 158      17.217   5.099  29.534  1.00 62.81           C  
ATOM   1160  CG2 ILE A 158      19.049   6.541  28.751  1.00 61.71           C  
ATOM   1161  CD1 ILE A 158      16.216   5.640  28.518  1.00 61.93           C  
ATOM   1162  N   VAL A 159      21.148   3.506  27.879  1.00 65.30           N  
ATOM   1163  CA  VAL A 159      22.544   3.509  27.468  1.00 65.16           C  
ATOM   1164  C   VAL A 159      22.641   3.158  25.981  1.00 65.56           C  
ATOM   1165  O   VAL A 159      23.566   3.577  25.283  1.00 65.31           O  
ATOM   1166  CB  VAL A 159      23.337   2.485  28.266  1.00 64.93           C  
ATOM   1167  CG1 VAL A 159      24.743   2.434  27.781  1.00 65.42           C  
ATOM   1168  CG2 VAL A 159      23.323   2.860  29.705  1.00 65.30           C  
ATOM   1169  N   MET A 160      21.677   2.371  25.509  1.00 66.22           N  
ATOM   1170  CA  MET A 160      21.629   1.967  24.110  1.00 66.09           C  
ATOM   1171  C   MET A 160      21.327   3.175  23.241  1.00 64.52           C  
ATOM   1172  O   MET A 160      21.888   3.336  22.156  1.00 65.07           O  
ATOM   1173  CB  MET A 160      20.553   0.899  23.904  1.00 69.29           C  
ATOM   1174  CG  MET A 160      20.959  -0.473  24.400  1.00 72.51           C  
ATOM   1175  SD  MET A 160      22.587  -0.976  23.757  1.00 78.69           S  
ATOM   1176  CE  MET A 160      22.160  -2.184  22.408  1.00 76.18           C  
ATOM   1177  N   ASP A 161      20.425   4.020  23.723  1.00 61.68           N  
ATOM   1178  CA  ASP A 161      20.061   5.220  22.994  1.00 58.81           C  
ATOM   1179  C   ASP A 161      21.280   6.158  22.953  1.00 57.16           C  
ATOM   1180  O   ASP A 161      21.638   6.702  21.906  1.00 58.05           O  
ATOM   1181  CB  ASP A 161      18.874   5.898  23.689  1.00 56.91           C  
ATOM   1182  CG  ASP A 161      17.657   4.978  23.818  1.00 56.11           C  
ATOM   1183  OD1 ASP A 161      17.557   3.996  23.056  1.00 56.12           O  
ATOM   1184  OD2 ASP A 161      16.788   5.254  24.672  1.00 54.35           O  
ATOM   1185  N   PHE A 162      21.921   6.321  24.102  1.00 55.25           N  
ATOM   1186  CA  PHE A 162      23.085   7.182  24.224  1.00 53.03           C  
ATOM   1187  C   PHE A 162      24.138   6.776  23.216  1.00 51.50           C  
ATOM   1188  O   PHE A 162      24.706   7.608  22.510  1.00 50.44           O  
ATOM   1189  CB  PHE A 162      23.673   7.072  25.629  1.00 55.10           C  
ATOM   1190  CG  PHE A 162      24.754   8.082  25.923  1.00 56.92           C  
ATOM   1191  CD1 PHE A 162      24.428   9.398  26.244  1.00 58.09           C  
ATOM   1192  CD2 PHE A 162      26.099   7.714  25.904  1.00 58.81           C  
ATOM   1193  CE1 PHE A 162      25.437  10.336  26.553  1.00 58.73           C  
ATOM   1194  CE2 PHE A 162      27.117   8.645  26.208  1.00 58.59           C  
ATOM   1195  CZ  PHE A 162      26.781   9.954  26.534  1.00 59.14           C  
ATOM   1196  N   LEU A 163      24.410   5.481  23.167  1.00 50.56           N  
ATOM   1197  CA  LEU A 163      25.406   4.978  22.244  1.00 49.91           C  
ATOM   1198  C   LEU A 163      24.949   5.225  20.815  1.00 50.42           C  
ATOM   1199  O   LEU A 163      25.764   5.225  19.882  1.00 50.58           O  
ATOM   1200  CB  LEU A 163      25.601   3.487  22.453  1.00 48.67           C  
ATOM   1201  CG  LEU A 163      26.370   3.054  23.688  1.00 47.83           C  
ATOM   1202  CD1 LEU A 163      26.472   1.534  23.696  1.00 45.81           C  
ATOM   1203  CD2 LEU A 163      27.750   3.698  23.670  1.00 46.77           C  
ATOM   1204  N   GLY A 164      23.639   5.432  20.662  1.00 50.05           N  
ATOM   1205  CA  GLY A 164      23.061   5.675  19.353  1.00 48.96           C  
ATOM   1206  C   GLY A 164      23.319   7.065  18.810  1.00 46.93           C  
ATOM   1207  O   GLY A 164      23.187   7.299  17.613  1.00 47.33           O  
ATOM   1208  N   PHE A 165      23.691   7.995  19.677  1.00 44.85           N  
ATOM   1209  CA  PHE A 165      23.953   9.352  19.219  1.00 43.22           C  
ATOM   1210  C   PHE A 165      24.993   9.376  18.104  1.00 42.90           C  
ATOM   1211  O   PHE A 165      25.803   8.463  17.973  1.00 42.15           O  
ATOM   1212  CB  PHE A 165      24.403  10.223  20.389  1.00 41.28           C  
ATOM   1213  CG  PHE A 165      23.334  10.432  21.428  1.00 39.89           C  
ATOM   1214  CD1 PHE A 165      22.054   9.886  21.263  1.00 37.93           C  
ATOM   1215  CD2 PHE A 165      23.602  11.174  22.570  1.00 37.76           C  
ATOM   1216  CE1 PHE A 165      21.060  10.080  22.232  1.00 35.93           C  
ATOM   1217  CE2 PHE A 165      22.613  11.369  23.543  1.00 35.57           C  
ATOM   1218  CZ  PHE A 165      21.342  10.817  23.367  1.00 36.08           C  
ATOM   1219  N   ASN A 166      24.958  10.427  17.295  1.00 43.08           N  
ATOM   1220  CA  ASN A 166      25.890  10.579  16.175  1.00 43.95           C  
ATOM   1221  C   ASN A 166      27.247  11.098  16.667  1.00 43.95           C  
ATOM   1222  O   ASN A 166      27.562  12.286  16.543  1.00 44.21           O  
ATOM   1223  CB  ASN A 166      25.297  11.533  15.111  1.00 45.73           C  
ATOM   1224  CG  ASN A 166      26.116  11.561  13.826  1.00 47.88           C  
ATOM   1225  OD1 ASN A 166      27.230  11.041  13.784  1.00 49.72           O  
ATOM   1226  ND2 ASN A 166      25.569  12.178  12.774  1.00 49.08           N  
ATOM   1227  N   TRP A 167      28.059  10.205  17.218  1.00 43.05           N  
ATOM   1228  CA  TRP A 167      29.361  10.607  17.737  1.00 42.20           C  
ATOM   1229  C   TRP A 167      30.366  10.809  16.611  1.00 42.87           C  
ATOM   1230  O   TRP A 167      31.387  11.477  16.767  1.00 42.09           O  
ATOM   1231  CB  TRP A 167      29.862   9.553  18.733  1.00 39.67           C  
ATOM   1232  CG  TRP A 167      28.932   9.391  19.922  1.00 38.64           C  
ATOM   1233  CD1 TRP A 167      28.010   8.393  20.133  1.00 37.72           C  
ATOM   1234  CD2 TRP A 167      28.777  10.301  20.995  1.00 37.68           C  
ATOM   1235  NE1 TRP A 167      27.291   8.645  21.270  1.00 36.75           N  
ATOM   1236  CE2 TRP A 167      27.738   9.813  21.822  1.00 38.46           C  
ATOM   1237  CE3 TRP A 167      29.411  11.500  21.341  1.00 37.66           C  
ATOM   1238  CZ2 TRP A 167      27.326  10.486  22.974  1.00 40.34           C  
ATOM   1239  CZ3 TRP A 167      29.004  12.169  22.479  1.00 40.12           C  
ATOM   1240  CH2 TRP A 167      27.969  11.658  23.287  1.00 40.56           C  
ATOM   1241  N   ASN A 168      30.063  10.242  15.458  1.00 43.82           N  
ATOM   1242  CA  ASN A 168      30.976  10.371  14.343  1.00 45.51           C  
ATOM   1243  C   ASN A 168      31.046  11.818  13.909  1.00 45.57           C  
ATOM   1244  O   ASN A 168      32.124  12.349  13.654  1.00 46.15           O  
ATOM   1245  CB  ASN A 168      30.531   9.470  13.185  1.00 46.67           C  
ATOM   1246  CG  ASN A 168      31.350   9.683  11.920  1.00 47.52           C  
ATOM   1247  OD1 ASN A 168      32.583   9.718  11.953  1.00 50.77           O  
ATOM   1248  ND2 ASN A 168      30.661   9.813  10.791  1.00 46.84           N  
ATOM   1249  N   TRP A 169      29.882  12.454  13.866  1.00 46.40           N  
ATOM   1250  CA  TRP A 169      29.756  13.838  13.421  1.00 47.15           C  
ATOM   1251  C   TRP A 169      30.250  14.835  14.455  1.00 47.00           C  
ATOM   1252  O   TRP A 169      31.084  15.705  14.167  1.00 45.91           O  
ATOM   1253  CB  TRP A 169      28.283  14.144  13.072  1.00 46.76           C  
ATOM   1254  CG  TRP A 169      28.034  15.584  12.743  1.00 47.61           C  
ATOM   1255  CD1 TRP A 169      28.284  16.227  11.554  1.00 48.50           C  
ATOM   1256  CD2 TRP A 169      27.619  16.604  13.660  1.00 46.47           C  
ATOM   1257  NE1 TRP A 169      28.061  17.584  11.685  1.00 47.50           N  
ATOM   1258  CE2 TRP A 169      27.651  17.838  12.970  1.00 47.06           C  
ATOM   1259  CE3 TRP A 169      27.229  16.591  15.009  1.00 44.50           C  
ATOM   1260  CZ2 TRP A 169      27.311  19.051  13.587  1.00 45.14           C  
ATOM   1261  CZ3 TRP A 169      26.894  17.791  15.616  1.00 44.65           C  
ATOM   1262  CH2 TRP A 169      26.939  19.005  14.909  1.00 44.92           C  
ATOM   1263  N   ILE A 170      29.732  14.691  15.666  1.00 47.18           N  
ATOM   1264  CA  ILE A 170      30.102  15.592  16.719  1.00 46.98           C  
ATOM   1265  C   ILE A 170      31.580  15.468  17.070  1.00 48.79           C  
ATOM   1266  O   ILE A 170      32.191  16.462  17.441  1.00 50.12           O  
ATOM   1267  CB  ILE A 170      29.235  15.357  17.953  1.00 45.76           C  
ATOM   1268  CG1 ILE A 170      29.319  16.577  18.866  1.00 43.76           C  
ATOM   1269  CG2 ILE A 170      29.670  14.091  18.663  1.00 43.76           C  
ATOM   1270  CD1 ILE A 170      28.130  16.758  19.780  1.00 40.92           C  
ATOM   1271  N   ASN A 171      32.161  14.273  16.940  1.00 49.51           N  
ATOM   1272  CA  ASN A 171      33.586  14.110  17.267  1.00 49.96           C  
ATOM   1273  C   ASN A 171      34.476  14.803  16.252  1.00 50.69           C  
ATOM   1274  O   ASN A 171      35.629  15.123  16.539  1.00 51.21           O  
ATOM   1275  CB  ASN A 171      33.979  12.628  17.364  1.00 49.51           C  
ATOM   1276  CG  ASN A 171      33.525  11.978  18.669  1.00 50.19           C  
ATOM   1277  OD1 ASN A 171      33.454  12.623  19.718  1.00 51.50           O  
ATOM   1278  ND2 ASN A 171      33.254  10.681  18.617  1.00 53.02           N  
ATOM   1279  N   LYS A 172      33.949  15.021  15.055  1.00 52.35           N  
ATOM   1280  CA  LYS A 172      34.722  15.697  14.030  1.00 54.36           C  
ATOM   1281  C   LYS A 172      34.629  17.199  14.244  1.00 54.86           C  
ATOM   1282  O   LYS A 172      35.547  17.929  13.890  1.00 55.19           O  
ATOM   1283  CB  LYS A 172      34.216  15.335  12.635  1.00 56.06           C  
ATOM   1284  CG  LYS A 172      34.502  13.907  12.227  1.00 58.93           C  
ATOM   1285  CD  LYS A 172      34.246  13.691  10.735  1.00 61.76           C  
ATOM   1286  CE  LYS A 172      32.773  13.866  10.364  1.00 63.63           C  
ATOM   1287  NZ  LYS A 172      32.526  13.573   8.919  1.00 64.17           N  
ATOM   1288  N   GLN A 173      33.521  17.665  14.814  1.00 55.82           N  
ATOM   1289  CA  GLN A 173      33.364  19.096  15.078  1.00 56.82           C  
ATOM   1290  C   GLN A 173      34.365  19.459  16.163  1.00 57.22           C  
ATOM   1291  O   GLN A 173      35.081  20.456  16.074  1.00 57.49           O  
ATOM   1292  CB  GLN A 173      31.949  19.418  15.572  1.00 56.65           C  
ATOM   1293  CG  GLN A 173      30.890  19.327  14.506  1.00 58.02           C  
ATOM   1294  CD  GLN A 173      31.203  20.210  13.328  1.00 59.14           C  
ATOM   1295  OE1 GLN A 173      31.351  21.423  13.473  1.00 58.30           O  
ATOM   1296  NE2 GLN A 173      31.327  19.608  12.153  1.00 60.90           N  
ATOM   1297  N   GLN A 174      34.401  18.630  17.195  1.00 57.18           N  
ATOM   1298  CA  GLN A 174      35.319  18.834  18.295  1.00 57.50           C  
ATOM   1299  C   GLN A 174      36.754  18.875  17.774  1.00 57.79           C  
ATOM   1300  O   GLN A 174      37.555  19.699  18.208  1.00 58.77           O  
ATOM   1301  CB  GLN A 174      35.162  17.695  19.293  1.00 57.64           C  
ATOM   1302  CG  GLN A 174      36.252  17.625  20.340  1.00 59.18           C  
ATOM   1303  CD  GLN A 174      36.133  16.390  21.207  1.00 60.28           C  
ATOM   1304  OE1 GLN A 174      36.195  15.260  20.716  1.00 60.49           O  
ATOM   1305  NE2 GLN A 174      35.955  16.598  22.505  1.00 61.39           N  
ATOM   1306  N   GLY A 175      37.061  17.973  16.842  1.00 57.38           N  
ATOM   1307  CA  GLY A 175      38.394  17.889  16.275  1.00 56.21           C  
ATOM   1308  C   GLY A 175      38.727  19.057  15.378  1.00 56.83           C  
ATOM   1309  O   GLY A 175      39.736  19.717  15.563  1.00 58.18           O  
ATOM   1310  N   LYS A 176      37.866  19.307  14.401  1.00 58.00           N  
ATOM   1311  CA  LYS A 176      38.072  20.412  13.469  1.00 58.76           C  
ATOM   1312  C   LYS A 176      38.203  21.765  14.160  1.00 58.94           C  
ATOM   1313  O   LYS A 176      38.983  22.613  13.744  1.00 59.77           O  
ATOM   1314  CB  LYS A 176      36.923  20.477  12.455  1.00 59.14           C  
ATOM   1315  CG  LYS A 176      37.167  19.649  11.208  1.00 61.98           C  
ATOM   1316  CD  LYS A 176      36.035  19.763  10.188  1.00 63.00           C  
ATOM   1317  CE  LYS A 176      34.746  19.135  10.689  1.00 62.18           C  
ATOM   1318  NZ  LYS A 176      33.781  18.946   9.571  1.00 62.19           N  
ATOM   1319  N   ARG A 177      37.437  21.962  15.219  1.00 58.69           N  
ATOM   1320  CA  ARG A 177      37.465  23.222  15.934  1.00 58.11           C  
ATOM   1321  C   ARG A 177      38.571  23.247  16.977  1.00 57.08           C  
ATOM   1322  O   ARG A 177      38.854  24.283  17.569  1.00 56.97           O  
ATOM   1323  CB  ARG A 177      36.113  23.446  16.596  1.00 59.76           C  
ATOM   1324  CG  ARG A 177      34.958  23.347  15.629  1.00 62.16           C  
ATOM   1325  CD  ARG A 177      34.928  24.552  14.728  1.00 65.31           C  
ATOM   1326  NE  ARG A 177      34.050  24.354  13.587  1.00 68.72           N  
ATOM   1327  CZ  ARG A 177      34.387  23.645  12.520  1.00 71.20           C  
ATOM   1328  NH1 ARG A 177      35.582  23.080  12.462  1.00 73.05           N  
ATOM   1329  NH2 ARG A 177      33.543  23.515  11.507  1.00 73.10           N  
ATOM   1330  N   GLY A 178      39.192  22.100  17.206  1.00 56.29           N  
ATOM   1331  CA  GLY A 178      40.254  22.033  18.199  1.00 54.95           C  
ATOM   1332  C   GLY A 178      39.798  22.269  19.634  1.00 54.40           C  
ATOM   1333  O   GLY A 178      40.592  22.672  20.491  1.00 54.05           O  
ATOM   1334  N   TRP A 179      38.518  22.018  19.898  1.00 54.33           N  
ATOM   1335  CA  TRP A 179      37.962  22.201  21.233  1.00 53.75           C  
ATOM   1336  C   TRP A 179      38.543  21.202  22.207  1.00 55.30           C  
ATOM   1337  O   TRP A 179      39.291  20.303  21.829  1.00 55.66           O  
ATOM   1338  CB  TRP A 179      36.449  22.019  21.222  1.00 51.76           C  
ATOM   1339  CG  TRP A 179      35.726  23.012  20.417  1.00 50.05           C  
ATOM   1340  CD1 TRP A 179      36.238  24.147  19.860  1.00 49.88           C  
ATOM   1341  CD2 TRP A 179      34.334  22.998  20.110  1.00 49.84           C  
ATOM   1342  NE1 TRP A 179      35.244  24.848  19.221  1.00 50.59           N  
ATOM   1343  CE2 TRP A 179      34.062  24.167  19.361  1.00 49.88           C  
ATOM   1344  CE3 TRP A 179      33.283  22.118  20.390  1.00 48.70           C  
ATOM   1345  CZ2 TRP A 179      32.780  24.475  18.895  1.00 50.87           C  
ATOM   1346  CZ3 TRP A 179      32.006  22.424  19.926  1.00 48.91           C  
ATOM   1347  CH2 TRP A 179      31.768  23.595  19.189  1.00 49.26           C  
ATOM   1348  N   GLY A 180      38.167  21.360  23.469  1.00 56.42           N  
ATOM   1349  CA  GLY A 180      38.652  20.474  24.505  1.00 56.95           C  
ATOM   1350  C   GLY A 180      37.783  19.253  24.560  1.00 57.85           C  
ATOM   1351  O   GLY A 180      37.114  18.922  23.588  1.00 57.69           O  
ATOM   1352  N   GLN A 181      37.778  18.601  25.714  1.00 59.60           N  
ATOM   1353  CA  GLN A 181      37.004  17.387  25.904  1.00 61.56           C  
ATOM   1354  C   GLN A 181      35.579  17.645  26.368  1.00 59.66           C  
ATOM   1355  O   GLN A 181      35.312  18.574  27.132  1.00 59.57           O  
ATOM   1356  CB  GLN A 181      37.709  16.467  26.913  1.00 65.75           C  
ATOM   1357  CG  GLN A 181      37.979  17.122  28.273  1.00 72.05           C  
ATOM   1358  CD  GLN A 181      37.768  16.165  29.447  1.00 75.85           C  
ATOM   1359  OE1 GLN A 181      38.330  15.066  29.481  1.00 77.64           O  
ATOM   1360  NE2 GLN A 181      36.963  16.588  30.419  1.00 76.62           N  
ATOM   1361  N   LEU A 182      34.665  16.810  25.894  1.00 57.55           N  
ATOM   1362  CA  LEU A 182      33.274  16.941  26.277  1.00 56.91           C  
ATOM   1363  C   LEU A 182      33.245  16.927  27.782  1.00 56.64           C  
ATOM   1364  O   LEU A 182      33.602  15.923  28.386  1.00 56.86           O  
ATOM   1365  CB  LEU A 182      32.457  15.766  25.751  1.00 56.13           C  
ATOM   1366  CG  LEU A 182      30.986  15.668  26.167  1.00 56.49           C  
ATOM   1367  CD1 LEU A 182      30.177  16.800  25.565  1.00 56.27           C  
ATOM   1368  CD2 LEU A 182      30.442  14.348  25.684  1.00 55.56           C  
ATOM   1369  N   THR A 183      32.829  18.032  28.388  1.00 56.37           N  
ATOM   1370  CA  THR A 183      32.754  18.098  29.838  1.00 56.91           C  
ATOM   1371  C   THR A 183      31.498  17.433  30.405  1.00 56.62           C  
ATOM   1372  O   THR A 183      31.562  16.802  31.446  1.00 58.84           O  
ATOM   1373  CB  THR A 183      32.796  19.538  30.346  1.00 57.43           C  
ATOM   1374  OG1 THR A 183      31.471  20.086  30.326  1.00 58.13           O  
ATOM   1375  CG2 THR A 183      33.718  20.368  29.473  1.00 57.42           C  
ATOM   1376  N   SER A 184      30.348  17.565  29.757  1.00 55.23           N  
ATOM   1377  CA  SER A 184      29.160  16.918  30.301  1.00 53.00           C  
ATOM   1378  C   SER A 184      27.985  17.002  29.354  1.00 52.57           C  
ATOM   1379  O   SER A 184      28.042  17.698  28.344  1.00 53.12           O  
ATOM   1380  CB  SER A 184      28.760  17.562  31.625  1.00 52.13           C  
ATOM   1381  OG  SER A 184      28.178  18.830  31.397  1.00 50.33           O  
ATOM   1382  N   ASN A 185      26.920  16.285  29.693  1.00 52.31           N  
ATOM   1383  CA  ASN A 185      25.694  16.245  28.912  1.00 51.11           C  
ATOM   1384  C   ASN A 185      24.556  16.356  29.902  1.00 50.98           C  
ATOM   1385  O   ASN A 185      24.410  15.500  30.767  1.00 52.59           O  
ATOM   1386  CB  ASN A 185      25.536  14.907  28.190  1.00 52.65           C  
ATOM   1387  CG  ASN A 185      26.594  14.674  27.141  1.00 54.11           C  
ATOM   1388  OD1 ASN A 185      27.723  14.284  27.445  1.00 56.73           O  
ATOM   1389  ND2 ASN A 185      26.228  14.895  25.883  1.00 54.90           N  
ATOM   1390  N   LEU A 186      23.744  17.392  29.787  1.00 50.85           N  
ATOM   1391  CA  LEU A 186      22.631  17.532  30.716  1.00 50.53           C  
ATOM   1392  C   LEU A 186      21.300  17.183  30.089  1.00 50.62           C  
ATOM   1393  O   LEU A 186      21.027  17.549  28.943  1.00 51.34           O  
ATOM   1394  CB  LEU A 186      22.535  18.955  31.243  1.00 50.13           C  
ATOM   1395  CG  LEU A 186      23.287  19.296  32.512  1.00 50.81           C  
ATOM   1396  CD1 LEU A 186      24.782  19.061  32.330  1.00 51.48           C  
ATOM   1397  CD2 LEU A 186      22.970  20.746  32.853  1.00 51.32           C  
ATOM   1398  N   LEU A 187      20.477  16.476  30.849  1.00 49.13           N  
ATOM   1399  CA  LEU A 187      19.149  16.115  30.394  1.00 47.33           C  
ATOM   1400  C   LEU A 187      18.231  17.213  30.932  1.00 46.60           C  
ATOM   1401  O   LEU A 187      18.132  17.413  32.139  1.00 45.13           O  
ATOM   1402  CB  LEU A 187      18.746  14.759  30.969  1.00 46.75           C  
ATOM   1403  CG  LEU A 187      17.265  14.404  30.820  1.00 47.20           C  
ATOM   1404  CD1 LEU A 187      16.889  14.295  29.347  1.00 46.07           C  
ATOM   1405  CD2 LEU A 187      16.998  13.102  31.547  1.00 46.88           C  
ATOM   1406  N   LEU A 188      17.567  17.936  30.044  1.00 45.70           N  
ATOM   1407  CA  LEU A 188      16.705  19.007  30.495  1.00 45.19           C  
ATOM   1408  C   LEU A 188      15.266  18.741  30.133  1.00 45.53           C  
ATOM   1409  O   LEU A 188      14.921  18.678  28.959  1.00 45.48           O  
ATOM   1410  CB  LEU A 188      17.145  20.326  29.877  1.00 45.54           C  
ATOM   1411  CG  LEU A 188      18.633  20.629  29.993  1.00 44.96           C  
ATOM   1412  CD1 LEU A 188      18.988  21.805  29.112  1.00 44.49           C  
ATOM   1413  CD2 LEU A 188      18.970  20.920  31.437  1.00 46.42           C  
ATOM   1414  N   ILE A 189      14.433  18.582  31.151  1.00 45.51           N  
ATOM   1415  CA  ILE A 189      13.012  18.347  30.951  1.00 46.65           C  
ATOM   1416  C   ILE A 189      12.296  19.464  31.673  1.00 48.20           C  
ATOM   1417  O   ILE A 189      12.401  19.561  32.894  1.00 47.85           O  
ATOM   1418  CB  ILE A 189      12.577  17.032  31.573  1.00 45.34           C  
ATOM   1419  CG1 ILE A 189      13.445  15.914  31.018  1.00 45.44           C  
ATOM   1420  CG2 ILE A 189      11.115  16.772  31.277  1.00 44.16           C  
ATOM   1421  CD1 ILE A 189      13.194  14.615  31.650  1.00 44.59           C  
ATOM   1422  N   GLY A 190      11.582  20.310  30.931  1.00 50.14           N  
ATOM   1423  CA  GLY A 190      10.878  21.418  31.555  1.00 51.18           C  
ATOM   1424  C   GLY A 190       9.409  21.541  31.177  1.00 52.30           C  
ATOM   1425  O   GLY A 190       8.979  20.992  30.167  1.00 53.06           O  
ATOM   1426  N   MET A 191       8.643  22.266  31.992  1.00 53.27           N  
ATOM   1427  CA  MET A 191       7.209  22.478  31.766  1.00 54.65           C  
ATOM   1428  C   MET A 191       6.980  23.658  30.813  1.00 55.58           C  
ATOM   1429  O   MET A 191       7.815  24.553  30.714  1.00 56.13           O  
ATOM   1430  CB  MET A 191       6.501  22.774  33.098  1.00 55.39           C  
ATOM   1431  CG  MET A 191       6.501  21.624  34.115  1.00 56.62           C  
ATOM   1432  SD  MET A 191       5.762  22.034  35.737  1.00 60.44           S  
ATOM   1433  CE  MET A 191       4.194  22.871  35.267  1.00 57.74           C  
ATOM   1434  N   GLU A 192       5.857  23.665  30.108  1.00 56.23           N  
ATOM   1435  CA  GLU A 192       5.582  24.774  29.198  1.00 57.94           C  
ATOM   1436  C   GLU A 192       5.600  26.086  29.970  1.00 57.40           C  
ATOM   1437  O   GLU A 192       5.250  26.115  31.148  1.00 58.00           O  
ATOM   1438  CB  GLU A 192       4.214  24.597  28.558  1.00 61.06           C  
ATOM   1439  CG  GLU A 192       3.160  24.092  29.534  1.00 64.26           C  
ATOM   1440  CD  GLU A 192       1.814  23.892  28.871  1.00 67.12           C  
ATOM   1441  OE1 GLU A 192       1.788  23.505  27.680  1.00 67.36           O  
ATOM   1442  OE2 GLU A 192       0.781  24.098  29.541  1.00 67.19           O  
ATOM   1443  N   GLY A 193       6.005  27.167  29.310  1.00 56.26           N  
ATOM   1444  CA  GLY A 193       6.035  28.461  29.970  1.00 55.39           C  
ATOM   1445  C   GLY A 193       7.273  28.734  30.804  1.00 55.37           C  
ATOM   1446  O   GLY A 193       7.537  29.871  31.179  1.00 55.16           O  
ATOM   1447  N   ASN A 194       8.020  27.678  31.106  1.00 55.32           N  
ATOM   1448  CA  ASN A 194       9.257  27.781  31.873  1.00 54.24           C  
ATOM   1449  C   ASN A 194      10.261  28.670  31.167  1.00 54.16           C  
ATOM   1450  O   ASN A 194      10.401  28.598  29.940  1.00 55.48           O  
ATOM   1451  CB  ASN A 194       9.890  26.412  32.035  1.00 54.17           C  
ATOM   1452  CG  ASN A 194       9.368  25.693  33.227  1.00 55.86           C  
ATOM   1453  OD1 ASN A 194       8.365  26.097  33.818  1.00 56.27           O  
ATOM   1454  ND2 ASN A 194      10.041  24.620  33.606  1.00 55.52           N  
ATOM   1455  N   VAL A 195      10.990  29.477  31.938  1.00 52.61           N  
ATOM   1456  CA  VAL A 195      11.986  30.381  31.365  1.00 49.52           C  
ATOM   1457  C   VAL A 195      13.340  30.320  32.095  1.00 47.22           C  
ATOM   1458  O   VAL A 195      13.400  30.201  33.318  1.00 46.55           O  
ATOM   1459  CB  VAL A 195      11.455  31.848  31.364  1.00 49.28           C  
ATOM   1460  CG1 VAL A 195      12.476  32.782  30.761  1.00 47.37           C  
ATOM   1461  CG2 VAL A 195      10.180  31.934  30.549  1.00 47.73           C  
ATOM   1462  N   THR A 196      14.418  30.382  31.316  1.00 45.30           N  
ATOM   1463  CA  THR A 196      15.795  30.383  31.825  1.00 43.72           C  
ATOM   1464  C   THR A 196      16.363  31.758  31.441  1.00 43.35           C  
ATOM   1465  O   THR A 196      16.767  31.963  30.292  1.00 42.91           O  
ATOM   1466  CB  THR A 196      16.665  29.264  31.168  1.00 43.14           C  
ATOM   1467  OG1 THR A 196      16.310  27.997  31.723  1.00 44.24           O  
ATOM   1468  CG2 THR A 196      18.133  29.496  31.425  1.00 40.01           C  
ATOM   1469  N   PRO A 197      16.390  32.721  32.393  1.00 42.70           N  
ATOM   1470  CA  PRO A 197      16.887  34.092  32.217  1.00 42.01           C  
ATOM   1471  C   PRO A 197      18.216  34.181  31.471  1.00 41.44           C  
ATOM   1472  O   PRO A 197      19.015  33.249  31.504  1.00 42.22           O  
ATOM   1473  CB  PRO A 197      16.982  34.607  33.645  1.00 41.61           C  
ATOM   1474  CG  PRO A 197      15.807  33.958  34.290  1.00 41.35           C  
ATOM   1475  CD  PRO A 197      15.960  32.525  33.795  1.00 41.95           C  
ATOM   1476  N   ALA A 198      18.448  35.304  30.800  1.00 39.95           N  
ATOM   1477  CA  ALA A 198      19.671  35.505  30.036  1.00 38.37           C  
ATOM   1478  C   ALA A 198      20.961  35.310  30.845  1.00 38.32           C  
ATOM   1479  O   ALA A 198      21.069  35.738  32.006  1.00 37.38           O  
ATOM   1480  CB  ALA A 198      19.662  36.875  29.427  1.00 37.05           C  
ATOM   1481  N   HIS A 199      21.940  34.672  30.206  1.00 37.61           N  
ATOM   1482  CA  HIS A 199      23.234  34.396  30.826  1.00 37.73           C  
ATOM   1483  C   HIS A 199      24.176  33.823  29.774  1.00 38.52           C  
ATOM   1484  O   HIS A 199      23.792  33.624  28.628  1.00 39.95           O  
ATOM   1485  CB  HIS A 199      23.077  33.339  31.905  1.00 37.39           C  
ATOM   1486  CG  HIS A 199      22.818  31.971  31.369  1.00 37.89           C  
ATOM   1487  ND1 HIS A 199      21.559  31.540  30.988  1.00 37.68           N  
ATOM   1488  CD2 HIS A 199      23.647  30.918  31.156  1.00 38.59           C  
ATOM   1489  CE1 HIS A 199      21.630  30.281  30.570  1.00 38.61           C  
ATOM   1490  NE2 HIS A 199      22.884  29.882  30.666  1.00 38.73           N  
ATOM   1491  N   TYR A 200      25.409  33.539  30.151  1.00 37.97           N  
ATOM   1492  CA  TYR A 200      26.305  32.993  29.162  1.00 37.39           C  
ATOM   1493  C   TYR A 200      27.108  31.925  29.845  1.00 37.78           C  
ATOM   1494  O   TYR A 200      27.185  31.898  31.070  1.00 36.12           O  
ATOM   1495  CB  TYR A 200      27.203  34.097  28.610  1.00 37.78           C  
ATOM   1496  CG  TYR A 200      28.146  34.702  29.623  1.00 38.82           C  
ATOM   1497  CD1 TYR A 200      29.391  34.129  29.864  1.00 37.73           C  
ATOM   1498  CD2 TYR A 200      27.807  35.862  30.335  1.00 38.05           C  
ATOM   1499  CE1 TYR A 200      30.296  34.697  30.785  1.00 38.62           C  
ATOM   1500  CE2 TYR A 200      28.705  36.438  31.266  1.00 36.61           C  
ATOM   1501  CZ  TYR A 200      29.951  35.850  31.478  1.00 37.42           C  
ATOM   1502  OH  TYR A 200      30.880  36.412  32.339  1.00 38.09           O  
ATOM   1503  N   ASP A 201      27.690  31.028  29.059  1.00 39.41           N  
ATOM   1504  CA  ASP A 201      28.492  29.941  29.607  1.00 42.01           C  
ATOM   1505  C   ASP A 201      29.899  30.000  29.017  1.00 44.28           C  
ATOM   1506  O   ASP A 201      30.101  30.458  27.889  1.00 46.02           O  
ATOM   1507  CB  ASP A 201      27.853  28.573  29.301  1.00 41.71           C  
ATOM   1508  CG  ASP A 201      26.462  28.396  29.929  1.00 41.84           C  
ATOM   1509  OD1 ASP A 201      26.318  28.540  31.169  1.00 42.38           O  
ATOM   1510  OD2 ASP A 201      25.508  28.096  29.176  1.00 43.13           O  
ATOM   1511  N   GLU A 202      30.874  29.530  29.781  1.00 46.09           N  
ATOM   1512  CA  GLU A 202      32.260  29.556  29.340  1.00 47.30           C  
ATOM   1513  C   GLU A 202      32.661  28.338  28.474  1.00 46.99           C  
ATOM   1514  O   GLU A 202      33.842  28.092  28.234  1.00 49.27           O  
ATOM   1515  CB  GLU A 202      33.162  29.690  30.585  1.00 48.65           C  
ATOM   1516  CG  GLU A 202      33.096  31.069  31.283  1.00 52.22           C  
ATOM   1517  CD  GLU A 202      33.917  31.129  32.567  1.00 55.57           C  
ATOM   1518  OE1 GLU A 202      33.395  30.743  33.641  1.00 57.29           O  
ATOM   1519  OE2 GLU A 202      35.098  31.547  32.506  1.00 57.76           O  
ATOM   1520  N   GLN A 203      31.678  27.600  27.978  1.00 44.99           N  
ATOM   1521  CA  GLN A 203      31.998  26.439  27.169  1.00 42.88           C  
ATOM   1522  C   GLN A 203      31.221  26.447  25.878  1.00 41.07           C  
ATOM   1523  O   GLN A 203      30.231  27.164  25.763  1.00 41.42           O  
ATOM   1524  CB  GLN A 203      31.677  25.184  27.953  1.00 45.43           C  
ATOM   1525  CG  GLN A 203      32.339  25.179  29.300  1.00 52.47           C  
ATOM   1526  CD  GLN A 203      32.658  23.791  29.778  1.00 57.52           C  
ATOM   1527  OE1 GLN A 203      31.787  22.924  29.813  1.00 60.56           O  
ATOM   1528  NE2 GLN A 203      33.914  23.562  30.150  1.00 59.82           N  
ATOM   1529  N   GLN A 204      31.678  25.669  24.899  1.00 38.96           N  
ATOM   1530  CA  GLN A 204      30.981  25.592  23.622  1.00 36.85           C  
ATOM   1531  C   GLN A 204      29.784  24.669  23.849  1.00 36.27           C  
ATOM   1532  O   GLN A 204      29.897  23.691  24.578  1.00 37.86           O  
ATOM   1533  CB  GLN A 204      31.915  25.020  22.560  1.00 35.32           C  
ATOM   1534  CG  GLN A 204      33.176  25.834  22.371  1.00 33.95           C  
ATOM   1535  CD  GLN A 204      32.960  27.168  21.659  1.00 35.13           C  
ATOM   1536  OE1 GLN A 204      31.835  27.578  21.377  1.00 34.94           O  
ATOM   1537  NE2 GLN A 204      34.058  27.845  21.352  1.00 34.93           N  
ATOM   1538  N   ASN A 205      28.639  24.972  23.246  1.00 36.30           N  
ATOM   1539  CA  ASN A 205      27.446  24.157  23.471  1.00 36.17           C  
ATOM   1540  C   ASN A 205      26.670  23.764  22.213  1.00 36.88           C  
ATOM   1541  O   ASN A 205      26.527  24.554  21.273  1.00 37.82           O  
ATOM   1542  CB  ASN A 205      26.531  24.895  24.472  1.00 35.11           C  
ATOM   1543  CG  ASN A 205      25.194  24.190  24.721  1.00 35.62           C  
ATOM   1544  OD1 ASN A 205      25.027  22.998  24.451  1.00 38.31           O  
ATOM   1545  ND2 ASN A 205      24.237  24.927  25.283  1.00 35.21           N  
ATOM   1546  N   PHE A 206      26.208  22.517  22.205  1.00 37.27           N  
ATOM   1547  CA  PHE A 206      25.388  21.963  21.135  1.00 36.50           C  
ATOM   1548  C   PHE A 206      24.070  21.580  21.805  1.00 36.48           C  
ATOM   1549  O   PHE A 206      23.995  20.581  22.505  1.00 36.58           O  
ATOM   1550  CB  PHE A 206      26.050  20.724  20.535  1.00 37.02           C  
ATOM   1551  CG  PHE A 206      26.969  21.030  19.386  1.00 37.79           C  
ATOM   1552  CD1 PHE A 206      26.497  21.743  18.290  1.00 37.15           C  
ATOM   1553  CD2 PHE A 206      28.305  20.633  19.405  1.00 38.37           C  
ATOM   1554  CE1 PHE A 206      27.336  22.069  17.219  1.00 37.24           C  
ATOM   1555  CE2 PHE A 206      29.170  20.954  18.326  1.00 36.51           C  
ATOM   1556  CZ  PHE A 206      28.678  21.673  17.236  1.00 36.39           C  
ATOM   1557  N   PHE A 207      23.052  22.404  21.594  1.00 36.45           N  
ATOM   1558  CA  PHE A 207      21.720  22.253  22.185  1.00 36.46           C  
ATOM   1559  C   PHE A 207      20.903  21.313  21.298  1.00 37.51           C  
ATOM   1560  O   PHE A 207      20.460  21.721  20.229  1.00 39.08           O  
ATOM   1561  CB  PHE A 207      21.081  23.643  22.216  1.00 36.59           C  
ATOM   1562  CG  PHE A 207      19.954  23.808  23.201  1.00 35.31           C  
ATOM   1563  CD1 PHE A 207      18.621  23.825  22.777  1.00 35.17           C  
ATOM   1564  CD2 PHE A 207      20.228  24.055  24.538  1.00 35.85           C  
ATOM   1565  CE1 PHE A 207      17.575  24.098  23.677  1.00 37.60           C  
ATOM   1566  CE2 PHE A 207      19.199  24.333  25.452  1.00 35.93           C  
ATOM   1567  CZ  PHE A 207      17.870  24.357  25.023  1.00 38.17           C  
ATOM   1568  N   ALA A 208      20.688  20.072  21.735  1.00 37.42           N  
ATOM   1569  CA  ALA A 208      19.936  19.090  20.948  1.00 36.90           C  
ATOM   1570  C   ALA A 208      18.491  18.950  21.402  1.00 37.30           C  
ATOM   1571  O   ALA A 208      18.232  18.310  22.426  1.00 37.45           O  
ATOM   1572  CB  ALA A 208      20.632  17.756  21.027  1.00 35.20           C  
ATOM   1573  N   GLN A 209      17.559  19.538  20.639  1.00 37.94           N  
ATOM   1574  CA  GLN A 209      16.142  19.493  21.006  1.00 38.52           C  
ATOM   1575  C   GLN A 209      15.560  18.108  20.731  1.00 40.79           C  
ATOM   1576  O   GLN A 209      15.836  17.501  19.684  1.00 40.38           O  
ATOM   1577  CB  GLN A 209      15.350  20.570  20.256  1.00 36.17           C  
ATOM   1578  CG  GLN A 209      13.895  20.813  20.771  1.00 33.49           C  
ATOM   1579  CD  GLN A 209      13.809  21.156  22.271  1.00 33.28           C  
ATOM   1580  OE1 GLN A 209      14.824  21.344  22.944  1.00 32.97           O  
ATOM   1581  NE2 GLN A 209      12.583  21.245  22.789  1.00 31.12           N  
ATOM   1582  N   ILE A 210      14.762  17.609  21.680  1.00 41.97           N  
ATOM   1583  CA  ILE A 210      14.165  16.280  21.593  1.00 43.05           C  
ATOM   1584  C   ILE A 210      12.635  16.262  21.605  1.00 45.49           C  
ATOM   1585  O   ILE A 210      12.018  15.678  20.717  1.00 46.60           O  
ATOM   1586  CB  ILE A 210      14.692  15.373  22.754  1.00 41.75           C  
ATOM   1587  CG1 ILE A 210      16.141  15.003  22.482  1.00 39.38           C  
ATOM   1588  CG2 ILE A 210      13.849  14.087  22.907  1.00 40.09           C  
ATOM   1589  CD1 ILE A 210      16.792  14.369  23.659  1.00 39.06           C  
ATOM   1590  N   LYS A 211      12.019  16.876  22.605  1.00 45.94           N  
ATOM   1591  CA  LYS A 211      10.570  16.865  22.680  1.00 45.71           C  
ATOM   1592  C   LYS A 211      10.099  18.257  22.997  1.00 47.24           C  
ATOM   1593  O   LYS A 211      10.645  18.894  23.881  1.00 49.25           O  
ATOM   1594  CB  LYS A 211      10.108  15.937  23.790  1.00 45.98           C  
ATOM   1595  CG  LYS A 211       8.609  15.933  23.955  1.00 46.94           C  
ATOM   1596  CD  LYS A 211       8.182  15.049  25.104  1.00 49.58           C  
ATOM   1597  CE  LYS A 211       6.671  14.966  25.178  1.00 51.07           C  
ATOM   1598  NZ  LYS A 211       6.116  14.403  23.918  1.00 53.57           N  
ATOM   1599  N   GLY A 212       9.078  18.731  22.295  1.00 47.67           N  
ATOM   1600  CA  GLY A 212       8.588  20.075  22.553  1.00 47.13           C  
ATOM   1601  C   GLY A 212       9.360  21.136  21.787  1.00 46.99           C  
ATOM   1602  O   GLY A 212      10.266  20.813  21.012  1.00 46.36           O  
ATOM   1603  N   TYR A 213       8.990  22.402  21.972  1.00 47.51           N  
ATOM   1604  CA  TYR A 213       9.676  23.508  21.289  1.00 47.37           C  
ATOM   1605  C   TYR A 213      10.200  24.552  22.282  1.00 45.52           C  
ATOM   1606  O   TYR A 213       9.531  24.888  23.269  1.00 43.64           O  
ATOM   1607  CB  TYR A 213       8.753  24.205  20.261  1.00 49.23           C  
ATOM   1608  CG  TYR A 213       8.327  23.324  19.089  1.00 50.98           C  
ATOM   1609  CD1 TYR A 213       7.291  22.396  19.223  1.00 51.01           C  
ATOM   1610  CD2 TYR A 213       9.005  23.376  17.870  1.00 51.99           C  
ATOM   1611  CE1 TYR A 213       6.944  21.538  18.178  1.00 50.95           C  
ATOM   1612  CE2 TYR A 213       8.663  22.512  16.810  1.00 52.25           C  
ATOM   1613  CZ  TYR A 213       7.632  21.598  16.976  1.00 53.39           C  
ATOM   1614  OH  TYR A 213       7.298  20.743  15.945  1.00 55.31           O  
ATOM   1615  N   LYS A 214      11.407  25.047  22.005  1.00 44.64           N  
ATOM   1616  CA  LYS A 214      12.073  26.060  22.823  1.00 43.16           C  
ATOM   1617  C   LYS A 214      12.518  27.273  22.000  1.00 43.25           C  
ATOM   1618  O   LYS A 214      13.156  27.142  20.945  1.00 41.96           O  
ATOM   1619  CB  LYS A 214      13.297  25.470  23.521  1.00 41.23           C  
ATOM   1620  CG  LYS A 214      13.012  24.794  24.840  1.00 39.70           C  
ATOM   1621  CD  LYS A 214      14.309  24.298  25.398  1.00 38.06           C  
ATOM   1622  CE  LYS A 214      14.149  23.866  26.812  1.00 37.89           C  
ATOM   1623  NZ  LYS A 214      15.421  23.255  27.234  1.00 41.16           N  
ATOM   1624  N   ARG A 215      12.159  28.459  22.481  1.00 43.78           N  
ATOM   1625  CA  ARG A 215      12.534  29.692  21.810  1.00 43.71           C  
ATOM   1626  C   ARG A 215      13.815  30.128  22.469  1.00 43.21           C  
ATOM   1627  O   ARG A 215      13.871  30.245  23.701  1.00 44.71           O  
ATOM   1628  CB  ARG A 215      11.495  30.766  22.043  1.00 44.36           C  
ATOM   1629  CG  ARG A 215      11.829  32.082  21.391  1.00 44.24           C  
ATOM   1630  CD  ARG A 215      11.137  33.179  22.160  1.00 44.88           C  
ATOM   1631  NE  ARG A 215      11.038  34.398  21.382  1.00 46.15           N  
ATOM   1632  CZ  ARG A 215      10.407  35.492  21.796  1.00 46.80           C  
ATOM   1633  NH1 ARG A 215       9.815  35.527  22.989  1.00 44.74           N  
ATOM   1634  NH2 ARG A 215      10.356  36.552  21.007  1.00 47.99           N  
ATOM   1635  N   CYS A 216      14.838  30.369  21.655  1.00 41.78           N  
ATOM   1636  CA  CYS A 216      16.135  30.782  22.157  1.00 39.87           C  
ATOM   1637  C   CYS A 216      16.543  32.121  21.602  1.00 39.01           C  
ATOM   1638  O   CYS A 216      16.646  32.287  20.389  1.00 39.77           O  
ATOM   1639  CB  CYS A 216      17.200  29.790  21.741  1.00 40.90           C  
ATOM   1640  SG  CYS A 216      16.733  28.094  22.058  1.00 44.19           S  
ATOM   1641  N   ILE A 217      16.808  33.063  22.495  1.00 39.63           N  
ATOM   1642  CA  ILE A 217      17.251  34.389  22.090  1.00 39.31           C  
ATOM   1643  C   ILE A 217      18.698  34.594  22.559  1.00 38.64           C  
ATOM   1644  O   ILE A 217      18.950  34.587  23.762  1.00 40.62           O  
ATOM   1645  CB  ILE A 217      16.384  35.468  22.727  1.00 37.40           C  
ATOM   1646  CG1 ILE A 217      14.907  35.156  22.491  1.00 36.14           C  
ATOM   1647  CG2 ILE A 217      16.705  36.794  22.107  1.00 37.16           C  
ATOM   1648  CD1 ILE A 217      13.963  36.058  23.226  1.00 34.60           C  
ATOM   1649  N   LEU A 218      19.622  34.780  21.614  1.00 38.10           N  
ATOM   1650  CA  LEU A 218      21.060  34.962  21.886  1.00 37.44           C  
ATOM   1651  C   LEU A 218      21.582  36.385  21.634  1.00 38.70           C  
ATOM   1652  O   LEU A 218      21.041  37.122  20.804  1.00 38.83           O  
ATOM   1653  CB  LEU A 218      21.894  34.009  21.019  1.00 35.79           C  
ATOM   1654  CG  LEU A 218      21.995  32.519  21.361  1.00 33.84           C  
ATOM   1655  CD1 LEU A 218      20.608  31.911  21.544  1.00 31.77           C  
ATOM   1656  CD2 LEU A 218      22.770  31.807  20.253  1.00 30.12           C  
ATOM   1657  N   PHE A 219      22.657  36.748  22.334  1.00 38.99           N  
ATOM   1658  CA  PHE A 219      23.275  38.061  22.196  1.00 38.12           C  
ATOM   1659  C   PHE A 219      24.777  37.859  22.145  1.00 37.56           C  
ATOM   1660  O   PHE A 219      25.332  37.065  22.906  1.00 37.67           O  
ATOM   1661  CB  PHE A 219      22.912  38.945  23.376  1.00 38.62           C  
ATOM   1662  CG  PHE A 219      21.431  39.118  23.572  1.00 39.45           C  
ATOM   1663  CD1 PHE A 219      20.724  38.292  24.443  1.00 40.05           C  
ATOM   1664  CD2 PHE A 219      20.754  40.142  22.917  1.00 40.06           C  
ATOM   1665  CE1 PHE A 219      19.357  38.489  24.672  1.00 39.47           C  
ATOM   1666  CE2 PHE A 219      19.394  40.351  23.135  1.00 39.76           C  
ATOM   1667  CZ  PHE A 219      18.694  39.523  24.017  1.00 41.28           C  
ATOM   1668  N   PRO A 220      25.446  38.554  21.245  1.00 37.10           N  
ATOM   1669  CA  PRO A 220      26.896  38.439  21.097  1.00 38.30           C  
ATOM   1670  C   PRO A 220      27.613  38.905  22.338  1.00 39.16           C  
ATOM   1671  O   PRO A 220      27.097  39.714  23.102  1.00 37.79           O  
ATOM   1672  CB  PRO A 220      27.199  39.306  19.903  1.00 37.03           C  
ATOM   1673  CG  PRO A 220      25.933  39.236  19.116  1.00 38.57           C  
ATOM   1674  CD  PRO A 220      24.882  39.379  20.163  1.00 39.35           C  
ATOM   1675  N   PRO A 221      28.835  38.408  22.550  1.00 40.81           N  
ATOM   1676  CA  PRO A 221      29.633  38.795  23.713  1.00 43.62           C  
ATOM   1677  C   PRO A 221      29.846  40.311  23.868  1.00 45.26           C  
ATOM   1678  O   PRO A 221      29.906  40.831  24.996  1.00 44.86           O  
ATOM   1679  CB  PRO A 221      30.936  38.027  23.483  1.00 41.96           C  
ATOM   1680  CG  PRO A 221      30.435  36.761  22.827  1.00 39.86           C  
ATOM   1681  CD  PRO A 221      29.468  37.303  21.812  1.00 40.25           C  
ATOM   1682  N   ASP A 222      29.940  41.019  22.742  1.00 46.06           N  
ATOM   1683  CA  ASP A 222      30.159  42.456  22.788  1.00 47.33           C  
ATOM   1684  C   ASP A 222      28.969  43.254  23.342  1.00 48.10           C  
ATOM   1685  O   ASP A 222      29.073  44.467  23.537  1.00 50.25           O  
ATOM   1686  CB  ASP A 222      30.571  42.987  21.404  1.00 47.65           C  
ATOM   1687  CG  ASP A 222      29.487  42.832  20.352  1.00 49.40           C  
ATOM   1688  OD1 ASP A 222      28.301  42.727  20.723  1.00 50.74           O  
ATOM   1689  OD2 ASP A 222      29.819  42.848  19.141  1.00 48.05           O  
ATOM   1690  N   GLN A 223      27.855  42.583  23.615  1.00 47.31           N  
ATOM   1691  CA  GLN A 223      26.671  43.257  24.157  1.00 46.52           C  
ATOM   1692  C   GLN A 223      26.810  43.337  25.674  1.00 44.82           C  
ATOM   1693  O   GLN A 223      25.851  43.628  26.393  1.00 44.23           O  
ATOM   1694  CB  GLN A 223      25.413  42.463  23.802  1.00 47.90           C  
ATOM   1695  CG  GLN A 223      25.174  42.314  22.309  1.00 53.96           C  
ATOM   1696  CD  GLN A 223      24.467  43.508  21.705  1.00 56.93           C  
ATOM   1697  OE1 GLN A 223      23.277  43.727  21.945  1.00 58.55           O  
ATOM   1698  NE2 GLN A 223      25.198  44.298  20.930  1.00 58.61           N  
ATOM   1699  N   PHE A 224      28.020  43.091  26.156  1.00 43.16           N  
ATOM   1700  CA  PHE A 224      28.289  43.096  27.583  1.00 42.05           C  
ATOM   1701  C   PHE A 224      27.706  44.300  28.318  1.00 42.02           C  
ATOM   1702  O   PHE A 224      27.063  44.153  29.372  1.00 39.64           O  
ATOM   1703  CB  PHE A 224      29.795  43.004  27.810  1.00 41.40           C  
ATOM   1704  CG  PHE A 224      30.177  42.784  29.250  1.00 41.83           C  
ATOM   1705  CD1 PHE A 224      30.242  43.853  30.137  1.00 41.40           C  
ATOM   1706  CD2 PHE A 224      30.440  41.505  29.729  1.00 42.08           C  
ATOM   1707  CE1 PHE A 224      30.561  43.650  31.478  1.00 39.78           C  
ATOM   1708  CE2 PHE A 224      30.760  41.293  31.072  1.00 40.79           C  
ATOM   1709  CZ  PHE A 224      30.819  42.372  31.946  1.00 39.97           C  
ATOM   1710  N   GLU A 225      27.930  45.488  27.750  1.00 43.22           N  
ATOM   1711  CA  GLU A 225      27.479  46.740  28.340  1.00 42.89           C  
ATOM   1712  C   GLU A 225      25.970  46.859  28.423  1.00 41.28           C  
ATOM   1713  O   GLU A 225      25.457  47.659  29.188  1.00 42.14           O  
ATOM   1714  CB  GLU A 225      28.029  47.955  27.558  1.00 45.33           C  
ATOM   1715  CG  GLU A 225      29.571  48.078  27.483  1.00 51.65           C  
ATOM   1716  CD  GLU A 225      30.075  49.529  27.290  1.00 55.39           C  
ATOM   1717  OE1 GLU A 225      30.309  50.238  28.296  1.00 55.91           O  
ATOM   1718  OE2 GLU A 225      30.249  49.969  26.131  1.00 57.83           O  
ATOM   1719  N   CYS A 226      25.258  46.064  27.636  1.00 41.89           N  
ATOM   1720  CA  CYS A 226      23.799  46.122  27.637  1.00 41.76           C  
ATOM   1721  C   CYS A 226      23.102  45.134  28.553  1.00 42.24           C  
ATOM   1722  O   CYS A 226      21.921  45.311  28.856  1.00 42.10           O  
ATOM   1723  CB  CYS A 226      23.253  45.879  26.237  1.00 40.74           C  
ATOM   1724  SG  CYS A 226      23.979  46.945  25.009  1.00 42.41           S  
ATOM   1725  N   LEU A 227      23.812  44.094  28.985  1.00 42.72           N  
ATOM   1726  CA  LEU A 227      23.182  43.080  29.813  1.00 41.94           C  
ATOM   1727  C   LEU A 227      23.545  43.046  31.292  1.00 40.42           C  
ATOM   1728  O   LEU A 227      23.032  42.219  32.040  1.00 40.86           O  
ATOM   1729  CB  LEU A 227      23.404  41.722  29.168  1.00 43.67           C  
ATOM   1730  CG  LEU A 227      22.788  41.727  27.766  1.00 44.08           C  
ATOM   1731  CD1 LEU A 227      23.387  40.621  26.919  1.00 44.02           C  
ATOM   1732  CD2 LEU A 227      21.268  41.609  27.883  1.00 43.55           C  
ATOM   1733  N   TYR A 228      24.434  43.937  31.696  1.00 39.40           N  
ATOM   1734  CA  TYR A 228      24.821  44.068  33.100  1.00 38.58           C  
ATOM   1735  C   TYR A 228      24.835  42.789  33.938  1.00 37.55           C  
ATOM   1736  O   TYR A 228      23.997  42.612  34.826  1.00 36.83           O  
ATOM   1737  CB  TYR A 228      23.888  45.074  33.779  1.00 36.79           C  
ATOM   1738  CG  TYR A 228      23.786  46.392  33.053  1.00 37.90           C  
ATOM   1739  CD1 TYR A 228      24.649  47.455  33.350  1.00 38.10           C  
ATOM   1740  CD2 TYR A 228      22.822  46.582  32.067  1.00 37.66           C  
ATOM   1741  CE1 TYR A 228      24.539  48.673  32.687  1.00 38.83           C  
ATOM   1742  CE2 TYR A 228      22.715  47.792  31.395  1.00 39.01           C  
ATOM   1743  CZ  TYR A 228      23.569  48.830  31.714  1.00 39.61           C  
ATOM   1744  OH  TYR A 228      23.436  50.033  31.071  1.00 41.39           O  
ATOM   1745  N   PRO A 229      25.793  41.889  33.685  1.00 37.00           N  
ATOM   1746  CA  PRO A 229      25.854  40.651  34.471  1.00 39.15           C  
ATOM   1747  C   PRO A 229      26.205  40.906  35.946  1.00 39.51           C  
ATOM   1748  O   PRO A 229      26.848  41.902  36.273  1.00 40.66           O  
ATOM   1749  CB  PRO A 229      26.952  39.863  33.765  1.00 36.78           C  
ATOM   1750  CG  PRO A 229      27.855  40.939  33.208  1.00 34.83           C  
ATOM   1751  CD  PRO A 229      26.837  41.910  32.647  1.00 35.70           C  
ATOM   1752  N   TYR A 230      25.785  40.017  36.838  1.00 38.32           N  
ATOM   1753  CA  TYR A 230      26.123  40.163  38.253  1.00 39.18           C  
ATOM   1754  C   TYR A 230      27.646  40.151  38.493  1.00 39.03           C  
ATOM   1755  O   TYR A 230      28.419  39.766  37.617  1.00 38.62           O  
ATOM   1756  CB  TYR A 230      25.547  39.007  39.044  1.00 37.86           C  
ATOM   1757  CG  TYR A 230      24.072  39.082  39.287  1.00 37.94           C  
ATOM   1758  CD1 TYR A 230      23.162  38.722  38.299  1.00 38.47           C  
ATOM   1759  CD2 TYR A 230      23.587  39.492  40.519  1.00 38.41           C  
ATOM   1760  CE1 TYR A 230      21.797  38.766  38.545  1.00 38.14           C  
ATOM   1761  CE2 TYR A 230      22.243  39.539  40.772  1.00 37.92           C  
ATOM   1762  CZ  TYR A 230      21.348  39.175  39.791  1.00 39.44           C  
ATOM   1763  OH  TYR A 230      20.004  39.207  40.079  1.00 42.82           O  
ATOM   1764  N   PRO A 231      28.094  40.553  39.703  1.00 37.86           N  
ATOM   1765  CA  PRO A 231      29.531  40.541  39.975  1.00 39.90           C  
ATOM   1766  C   PRO A 231      30.025  39.099  39.957  1.00 40.39           C  
ATOM   1767  O   PRO A 231      29.279  38.178  40.321  1.00 39.19           O  
ATOM   1768  CB  PRO A 231      29.616  41.150  41.373  1.00 38.71           C  
ATOM   1769  CG  PRO A 231      28.470  42.095  41.378  1.00 37.70           C  
ATOM   1770  CD  PRO A 231      27.383  41.223  40.804  1.00 38.03           C  
ATOM   1771  N   VAL A 232      31.273  38.905  39.537  1.00 41.03           N  
ATOM   1772  CA  VAL A 232      31.856  37.573  39.470  1.00 40.70           C  
ATOM   1773  C   VAL A 232      31.718  36.753  40.754  1.00 42.51           C  
ATOM   1774  O   VAL A 232      31.417  35.572  40.681  1.00 43.71           O  
ATOM   1775  CB  VAL A 232      33.339  37.644  39.091  1.00 39.56           C  
ATOM   1776  CG1 VAL A 232      33.992  36.306  39.292  1.00 38.06           C  
ATOM   1777  CG2 VAL A 232      33.477  38.031  37.642  1.00 37.44           C  
ATOM   1778  N   HIS A 233      31.932  37.355  41.922  1.00 43.88           N  
ATOM   1779  CA  HIS A 233      31.806  36.606  43.182  1.00 43.84           C  
ATOM   1780  C   HIS A 233      30.373  36.407  43.669  1.00 43.87           C  
ATOM   1781  O   HIS A 233      30.139  35.760  44.694  1.00 44.25           O  
ATOM   1782  CB  HIS A 233      32.612  37.284  44.287  1.00 43.56           C  
ATOM   1783  CG  HIS A 233      34.081  37.264  44.055  1.00 45.73           C  
ATOM   1784  ND1 HIS A 233      34.753  38.304  43.447  1.00 46.36           N  
ATOM   1785  CD2 HIS A 233      35.013  36.326  44.338  1.00 46.49           C  
ATOM   1786  CE1 HIS A 233      36.045  38.009  43.369  1.00 47.89           C  
ATOM   1787  NE2 HIS A 233      36.228  36.811  43.906  1.00 49.26           N  
ATOM   1788  N   HIS A 234      29.414  36.956  42.941  1.00 44.54           N  
ATOM   1789  CA  HIS A 234      28.019  36.819  43.324  1.00 45.62           C  
ATOM   1790  C   HIS A 234      27.463  35.465  42.876  1.00 46.57           C  
ATOM   1791  O   HIS A 234      27.823  34.956  41.815  1.00 47.05           O  
ATOM   1792  CB  HIS A 234      27.196  37.961  42.717  1.00 46.35           C  
ATOM   1793  CG  HIS A 234      25.782  38.009  43.206  1.00 47.87           C  
ATOM   1794  ND1 HIS A 234      24.854  37.034  42.907  1.00 48.72           N  
ATOM   1795  CD2 HIS A 234      25.149  38.894  44.018  1.00 48.81           C  
ATOM   1796  CE1 HIS A 234      23.715  37.308  43.512  1.00 48.64           C  
ATOM   1797  NE2 HIS A 234      23.864  38.429  44.193  1.00 48.24           N  
ATOM   1798  N   PRO A 235      26.590  34.850  43.693  1.00 46.75           N  
ATOM   1799  CA  PRO A 235      25.964  33.558  43.402  1.00 46.93           C  
ATOM   1800  C   PRO A 235      25.361  33.477  41.990  1.00 47.46           C  
ATOM   1801  O   PRO A 235      25.286  32.404  41.398  1.00 47.85           O  
ATOM   1802  CB  PRO A 235      24.890  33.451  44.479  1.00 46.13           C  
ATOM   1803  CG  PRO A 235      25.552  34.089  45.647  1.00 47.51           C  
ATOM   1804  CD  PRO A 235      26.206  35.316  45.040  1.00 48.26           C  
ATOM   1805  N   CYS A 236      24.936  34.618  41.456  1.00 47.05           N  
ATOM   1806  CA  CYS A 236      24.336  34.630  40.131  1.00 45.72           C  
ATOM   1807  C   CYS A 236      25.297  35.078  39.050  1.00 47.00           C  
ATOM   1808  O   CYS A 236      24.874  35.535  37.981  1.00 47.78           O  
ATOM   1809  CB  CYS A 236      23.105  35.521  40.125  1.00 45.18           C  
ATOM   1810  SG  CYS A 236      21.829  34.844  41.181  1.00 45.08           S  
ATOM   1811  N   ASP A 237      26.588  34.942  39.333  1.00 47.53           N  
ATOM   1812  CA  ASP A 237      27.624  35.318  38.378  1.00 47.99           C  
ATOM   1813  C   ASP A 237      27.280  34.753  36.993  1.00 48.49           C  
ATOM   1814  O   ASP A 237      26.751  33.645  36.884  1.00 49.86           O  
ATOM   1815  CB  ASP A 237      28.981  34.784  38.871  1.00 49.27           C  
ATOM   1816  CG  ASP A 237      30.052  34.747  37.776  1.00 51.69           C  
ATOM   1817  OD1 ASP A 237      30.230  35.756  37.054  1.00 52.76           O  
ATOM   1818  OD2 ASP A 237      30.736  33.704  37.634  1.00 52.28           O  
ATOM   1819  N   ARG A 238      27.557  35.532  35.948  1.00 46.63           N  
ATOM   1820  CA  ARG A 238      27.300  35.130  34.563  1.00 45.15           C  
ATOM   1821  C   ARG A 238      25.862  35.336  34.095  1.00 45.21           C  
ATOM   1822  O   ARG A 238      25.528  35.064  32.934  1.00 43.58           O  
ATOM   1823  CB  ARG A 238      27.735  33.678  34.331  1.00 43.96           C  
ATOM   1824  CG  ARG A 238      29.235  33.526  34.174  1.00 44.92           C  
ATOM   1825  CD  ARG A 238      29.568  32.300  33.382  1.00 47.43           C  
ATOM   1826  NE  ARG A 238      29.178  31.081  34.078  1.00 54.00           N  
ATOM   1827  CZ  ARG A 238      27.941  30.569  34.106  1.00 57.77           C  
ATOM   1828  NH1 ARG A 238      26.907  31.151  33.476  1.00 60.82           N  
ATOM   1829  NH2 ARG A 238      27.737  29.440  34.773  1.00 56.91           N  
ATOM   1830  N   GLN A 239      25.033  35.858  34.993  1.00 45.49           N  
ATOM   1831  CA  GLN A 239      23.640  36.128  34.677  1.00 46.71           C  
ATOM   1832  C   GLN A 239      23.337  37.617  34.595  1.00 45.77           C  
ATOM   1833  O   GLN A 239      23.960  38.433  35.281  1.00 45.74           O  
ATOM   1834  CB  GLN A 239      22.754  35.497  35.730  1.00 50.03           C  
ATOM   1835  CG  GLN A 239      22.796  34.000  35.648  1.00 59.12           C  
ATOM   1836  CD  GLN A 239      22.211  33.331  36.863  1.00 64.37           C  
ATOM   1837  OE1 GLN A 239      21.067  33.590  37.249  1.00 66.33           O  
ATOM   1838  NE2 GLN A 239      22.997  32.452  37.479  1.00 68.32           N  
ATOM   1839  N   SER A 240      22.370  37.969  33.755  1.00 43.97           N  
ATOM   1840  CA  SER A 240      22.001  39.361  33.583  1.00 41.43           C  
ATOM   1841  C   SER A 240      21.125  39.843  34.715  1.00 41.09           C  
ATOM   1842  O   SER A 240      20.215  39.158  35.158  1.00 41.00           O  
ATOM   1843  CB  SER A 240      21.258  39.559  32.275  1.00 39.39           C  
ATOM   1844  OG  SER A 240      20.798  40.888  32.179  1.00 40.00           O  
ATOM   1845  N   GLN A 241      21.396  41.049  35.171  1.00 41.53           N  
ATOM   1846  CA  GLN A 241      20.623  41.606  36.260  1.00 42.89           C  
ATOM   1847  C   GLN A 241      19.331  42.213  35.752  1.00 43.54           C  
ATOM   1848  O   GLN A 241      18.393  42.425  36.518  1.00 44.41           O  
ATOM   1849  CB  GLN A 241      21.431  42.674  36.963  1.00 42.54           C  
ATOM   1850  CG  GLN A 241      22.812  42.241  37.371  1.00 42.96           C  
ATOM   1851  CD  GLN A 241      23.570  43.371  38.014  1.00 42.97           C  
ATOM   1852  OE1 GLN A 241      23.285  43.749  39.151  1.00 41.76           O  
ATOM   1853  NE2 GLN A 241      24.522  43.941  37.285  1.00 43.04           N  
ATOM   1854  N   VAL A 242      19.301  42.494  34.458  1.00 44.16           N  
ATOM   1855  CA  VAL A 242      18.145  43.112  33.834  1.00 46.72           C  
ATOM   1856  C   VAL A 242      16.941  42.186  33.744  1.00 47.96           C  
ATOM   1857  O   VAL A 242      17.046  41.122  33.161  1.00 50.66           O  
ATOM   1858  CB  VAL A 242      18.490  43.556  32.413  1.00 46.72           C  
ATOM   1859  CG1 VAL A 242      17.311  44.283  31.799  1.00 46.60           C  
ATOM   1860  CG2 VAL A 242      19.730  44.431  32.435  1.00 47.19           C  
ATOM   1861  N   ASP A 243      15.810  42.601  34.317  1.00 49.27           N  
ATOM   1862  CA  ASP A 243      14.572  41.808  34.267  1.00 49.19           C  
ATOM   1863  C   ASP A 243      13.930  42.047  32.904  1.00 49.74           C  
ATOM   1864  O   ASP A 243      13.412  43.134  32.654  1.00 49.85           O  
ATOM   1865  CB  ASP A 243      13.592  42.266  35.346  1.00 49.24           C  
ATOM   1866  CG  ASP A 243      12.313  41.431  35.385  1.00 49.95           C  
ATOM   1867  OD1 ASP A 243      11.732  41.133  34.313  1.00 49.85           O  
ATOM   1868  OD2 ASP A 243      11.875  41.089  36.504  1.00 49.00           O  
ATOM   1869  N   PHE A 244      13.946  41.041  32.034  1.00 50.07           N  
ATOM   1870  CA  PHE A 244      13.380  41.167  30.693  1.00 49.85           C  
ATOM   1871  C   PHE A 244      11.897  41.460  30.634  1.00 51.91           C  
ATOM   1872  O   PHE A 244      11.407  42.033  29.653  1.00 51.04           O  
ATOM   1873  CB  PHE A 244      13.646  39.904  29.906  1.00 47.41           C  
ATOM   1874  CG  PHE A 244      15.010  39.852  29.312  1.00 46.07           C  
ATOM   1875  CD1 PHE A 244      16.121  40.238  30.054  1.00 45.28           C  
ATOM   1876  CD2 PHE A 244      15.187  39.396  28.016  1.00 45.18           C  
ATOM   1877  CE1 PHE A 244      17.406  40.165  29.508  1.00 44.78           C  
ATOM   1878  CE2 PHE A 244      16.452  39.317  27.459  1.00 45.13           C  
ATOM   1879  CZ  PHE A 244      17.569  39.703  28.211  1.00 45.68           C  
ATOM   1880  N   ASP A 245      11.181  41.053  31.678  1.00 53.65           N  
ATOM   1881  CA  ASP A 245       9.751  41.280  31.738  1.00 56.20           C  
ATOM   1882  C   ASP A 245       9.413  42.696  32.185  1.00 57.25           C  
ATOM   1883  O   ASP A 245       8.354  43.211  31.848  1.00 58.39           O  
ATOM   1884  CB  ASP A 245       9.090  40.286  32.677  1.00 59.00           C  
ATOM   1885  CG  ASP A 245       9.130  38.873  32.146  1.00 61.88           C  
ATOM   1886  OD1 ASP A 245       8.965  38.686  30.919  1.00 62.81           O  
ATOM   1887  OD2 ASP A 245       9.310  37.945  32.966  1.00 64.16           O  
ATOM   1888  N   ASN A 246      10.314  43.309  32.953  1.00 58.85           N  
ATOM   1889  CA  ASN A 246      10.147  44.688  33.442  1.00 58.66           C  
ATOM   1890  C   ASN A 246      11.518  45.371  33.586  1.00 55.72           C  
ATOM   1891  O   ASN A 246      12.043  45.557  34.685  1.00 56.14           O  
ATOM   1892  CB  ASN A 246       9.382  44.692  34.773  1.00 62.37           C  
ATOM   1893  CG  ASN A 246       9.052  46.097  35.257  1.00 67.47           C  
ATOM   1894  OD1 ASN A 246       8.696  46.976  34.464  1.00 69.53           O  
ATOM   1895  ND2 ASN A 246       9.161  46.314  36.564  1.00 69.21           N  
ATOM   1896  N   PRO A 247      12.118  45.754  32.448  1.00 53.03           N  
ATOM   1897  CA  PRO A 247      13.425  46.406  32.421  1.00 52.14           C  
ATOM   1898  C   PRO A 247      13.488  47.756  33.128  1.00 52.24           C  
ATOM   1899  O   PRO A 247      12.656  48.634  32.896  1.00 51.81           O  
ATOM   1900  CB  PRO A 247      13.717  46.507  30.926  1.00 51.22           C  
ATOM   1901  CG  PRO A 247      12.374  46.671  30.345  1.00 51.22           C  
ATOM   1902  CD  PRO A 247      11.565  45.647  31.087  1.00 51.27           C  
ATOM   1903  N   ASP A 248      14.492  47.908  33.988  1.00 51.86           N  
ATOM   1904  CA  ASP A 248      14.718  49.138  34.742  1.00 51.84           C  
ATOM   1905  C   ASP A 248      15.730  49.995  33.987  1.00 51.51           C  
ATOM   1906  O   ASP A 248      16.924  49.960  34.291  1.00 51.18           O  
ATOM   1907  CB  ASP A 248      15.281  48.803  36.114  1.00 54.18           C  
ATOM   1908  CG  ASP A 248      15.404  50.018  37.002  1.00 56.05           C  
ATOM   1909  OD1 ASP A 248      15.456  51.145  36.465  1.00 58.59           O  
ATOM   1910  OD2 ASP A 248      15.452  49.843  38.239  1.00 56.40           O  
ATOM   1911  N   TYR A 249      15.260  50.776  33.020  1.00 51.67           N  
ATOM   1912  CA  TYR A 249      16.174  51.586  32.218  1.00 52.49           C  
ATOM   1913  C   TYR A 249      16.925  52.637  33.009  1.00 53.30           C  
ATOM   1914  O   TYR A 249      17.759  53.359  32.466  1.00 52.42           O  
ATOM   1915  CB  TYR A 249      15.427  52.255  31.062  1.00 51.84           C  
ATOM   1916  CG  TYR A 249      14.725  51.278  30.146  1.00 53.11           C  
ATOM   1917  CD1 TYR A 249      15.407  50.199  29.578  1.00 52.77           C  
ATOM   1918  CD2 TYR A 249      13.373  51.429  29.851  1.00 53.44           C  
ATOM   1919  CE1 TYR A 249      14.754  49.299  28.739  1.00 53.46           C  
ATOM   1920  CE2 TYR A 249      12.712  50.540  29.017  1.00 53.87           C  
ATOM   1921  CZ  TYR A 249      13.404  49.483  28.464  1.00 53.48           C  
ATOM   1922  OH  TYR A 249      12.731  48.635  27.621  1.00 54.44           O  
ATOM   1923  N   GLU A 250      16.633  52.707  34.299  1.00 55.32           N  
ATOM   1924  CA  GLU A 250      17.285  53.663  35.175  1.00 57.20           C  
ATOM   1925  C   GLU A 250      18.648  53.098  35.533  1.00 55.41           C  
ATOM   1926  O   GLU A 250      19.671  53.744  35.343  1.00 56.35           O  
ATOM   1927  CB  GLU A 250      16.477  53.855  36.456  1.00 63.36           C  
ATOM   1928  CG  GLU A 250      16.368  55.289  36.901  1.00 70.99           C  
ATOM   1929  CD  GLU A 250      15.451  56.084  36.006  1.00 76.61           C  
ATOM   1930  OE1 GLU A 250      14.237  55.773  35.986  1.00 79.29           O  
ATOM   1931  OE2 GLU A 250      15.934  57.016  35.323  1.00 79.04           O  
ATOM   1932  N   ARG A 251      18.654  51.877  36.048  1.00 52.41           N  
ATOM   1933  CA  ARG A 251      19.898  51.254  36.444  1.00 50.73           C  
ATOM   1934  C   ARG A 251      20.667  50.712  35.265  1.00 49.67           C  
ATOM   1935  O   ARG A 251      21.903  50.800  35.208  1.00 49.25           O  
ATOM   1936  CB  ARG A 251      19.608  50.103  37.378  1.00 51.61           C  
ATOM   1937  CG  ARG A 251      18.562  50.402  38.407  1.00 56.27           C  
ATOM   1938  CD  ARG A 251      18.384  49.198  39.291  1.00 59.07           C  
ATOM   1939  NE  ARG A 251      19.666  48.801  39.855  1.00 61.46           N  
ATOM   1940  CZ  ARG A 251      19.919  47.594  40.347  1.00 62.37           C  
ATOM   1941  NH1 ARG A 251      18.966  46.668  40.349  1.00 61.29           N  
ATOM   1942  NH2 ARG A 251      21.128  47.297  40.806  1.00 62.56           N  
ATOM   1943  N   PHE A 252      19.915  50.134  34.333  1.00 48.30           N  
ATOM   1944  CA  PHE A 252      20.469  49.494  33.150  1.00 45.96           C  
ATOM   1945  C   PHE A 252      20.104  50.235  31.856  1.00 45.63           C  
ATOM   1946  O   PHE A 252      19.426  49.700  30.976  1.00 47.19           O  
ATOM   1947  CB  PHE A 252      19.945  48.065  33.090  1.00 44.02           C  
ATOM   1948  CG  PHE A 252      19.945  47.366  34.424  1.00 41.85           C  
ATOM   1949  CD1 PHE A 252      21.141  47.027  35.064  1.00 40.64           C  
ATOM   1950  CD2 PHE A 252      18.741  47.036  35.038  1.00 40.27           C  
ATOM   1951  CE1 PHE A 252      21.131  46.363  36.293  1.00 39.09           C  
ATOM   1952  CE2 PHE A 252      18.720  46.378  36.262  1.00 39.37           C  
ATOM   1953  CZ  PHE A 252      19.914  46.038  36.891  1.00 38.94           C  
ATOM   1954  N   PRO A 253      20.601  51.462  31.717  1.00 45.01           N  
ATOM   1955  CA  PRO A 253      20.326  52.282  30.535  1.00 43.26           C  
ATOM   1956  C   PRO A 253      20.598  51.678  29.162  1.00 42.39           C  
ATOM   1957  O   PRO A 253      19.850  51.916  28.218  1.00 41.57           O  
ATOM   1958  CB  PRO A 253      21.178  53.516  30.772  1.00 41.95           C  
ATOM   1959  CG  PRO A 253      22.309  53.000  31.621  1.00 41.99           C  
ATOM   1960  CD  PRO A 253      21.610  52.095  32.581  1.00 43.32           C  
ATOM   1961  N   ASN A 254      21.676  50.913  29.052  1.00 42.94           N  
ATOM   1962  CA  ASN A 254      22.035  50.330  27.771  1.00 42.89           C  
ATOM   1963  C   ASN A 254      21.252  49.125  27.343  1.00 42.26           C  
ATOM   1964  O   ASN A 254      21.576  48.519  26.322  1.00 42.39           O  
ATOM   1965  CB  ASN A 254      23.510  49.992  27.734  1.00 43.38           C  
ATOM   1966  CG  ASN A 254      24.354  51.191  27.460  1.00 45.12           C  
ATOM   1967  OD1 ASN A 254      25.003  51.723  28.351  1.00 45.23           O  
ATOM   1968  ND2 ASN A 254      24.336  51.645  26.213  1.00 46.11           N  
ATOM   1969  N   PHE A 255      20.241  48.747  28.109  1.00 41.36           N  
ATOM   1970  CA  PHE A 255      19.453  47.604  27.693  1.00 41.69           C  
ATOM   1971  C   PHE A 255      18.523  48.062  26.567  1.00 42.55           C  
ATOM   1972  O   PHE A 255      17.833  47.267  25.950  1.00 44.28           O  
ATOM   1973  CB  PHE A 255      18.609  47.087  28.840  1.00 40.67           C  
ATOM   1974  CG  PHE A 255      17.866  45.819  28.513  1.00 40.35           C  
ATOM   1975  CD1 PHE A 255      18.559  44.639  28.248  1.00 39.77           C  
ATOM   1976  CD2 PHE A 255      16.470  45.802  28.468  1.00 40.60           C  
ATOM   1977  CE1 PHE A 255      17.875  43.455  27.946  1.00 39.14           C  
ATOM   1978  CE2 PHE A 255      15.773  44.617  28.164  1.00 41.46           C  
ATOM   1979  CZ  PHE A 255      16.483  43.442  27.904  1.00 39.09           C  
ATOM   1980  N   GLN A 256      18.511  49.358  26.312  1.00 43.38           N  
ATOM   1981  CA  GLN A 256      17.659  49.888  25.267  1.00 42.36           C  
ATOM   1982  C   GLN A 256      18.405  49.862  23.967  1.00 41.93           C  
ATOM   1983  O   GLN A 256      17.892  50.336  22.959  1.00 44.25           O  
ATOM   1984  CB  GLN A 256      17.257  51.318  25.576  1.00 45.07           C  
ATOM   1985  CG  GLN A 256      16.952  51.527  27.025  1.00 48.63           C  
ATOM   1986  CD  GLN A 256      16.545  52.936  27.323  1.00 50.85           C  
ATOM   1987  OE1 GLN A 256      15.416  53.342  27.044  1.00 52.64           O  
ATOM   1988  NE2 GLN A 256      17.467  53.707  27.883  1.00 52.83           N  
ATOM   1989  N   ASN A 257      19.620  49.331  23.985  1.00 41.35           N  
ATOM   1990  CA  ASN A 257      20.403  49.232  22.746  1.00 42.59           C  
ATOM   1991  C   ASN A 257      20.627  47.792  22.358  1.00 43.91           C  
ATOM   1992  O   ASN A 257      21.229  47.512  21.325  1.00 43.89           O  
ATOM   1993  CB  ASN A 257      21.772  49.878  22.886  1.00 41.17           C  
ATOM   1994  CG  ASN A 257      21.685  51.310  23.266  1.00 40.06           C  
ATOM   1995  OD1 ASN A 257      21.922  51.668  24.413  1.00 39.34           O  
ATOM   1996  ND2 ASN A 257      21.325  52.149  22.307  1.00 38.20           N  
ATOM   1997  N   VAL A 258      20.154  46.877  23.193  1.00 45.17           N  
ATOM   1998  CA  VAL A 258      20.332  45.472  22.930  1.00 46.90           C  
ATOM   1999  C   VAL A 258      19.588  44.992  21.678  1.00 47.98           C  
ATOM   2000  O   VAL A 258      18.467  45.423  21.394  1.00 47.77           O  
ATOM   2001  CB  VAL A 258      19.895  44.669  24.158  1.00 46.35           C  
ATOM   2002  CG1 VAL A 258      18.404  44.421  24.128  1.00 46.35           C  
ATOM   2003  CG2 VAL A 258      20.651  43.395  24.227  1.00 47.38           C  
ATOM   2004  N   VAL A 259      20.228  44.097  20.930  1.00 50.62           N  
ATOM   2005  CA  VAL A 259      19.651  43.518  19.723  1.00 50.80           C  
ATOM   2006  C   VAL A 259      20.045  42.044  19.712  1.00 52.92           C  
ATOM   2007  O   VAL A 259      21.240  41.731  19.750  1.00 53.86           O  
ATOM   2008  CB  VAL A 259      20.228  44.145  18.458  1.00 49.87           C  
ATOM   2009  CG1 VAL A 259      19.487  43.630  17.274  1.00 48.68           C  
ATOM   2010  CG2 VAL A 259      20.120  45.637  18.521  1.00 49.69           C  
ATOM   2011  N   GLY A 260      19.060  41.145  19.649  1.00 53.08           N  
ATOM   2012  CA  GLY A 260      19.377  39.726  19.652  1.00 52.89           C  
ATOM   2013  C   GLY A 260      19.036  38.908  18.410  1.00 53.09           C  
ATOM   2014  O   GLY A 260      18.468  39.403  17.438  1.00 52.39           O  
ATOM   2015  N   TYR A 261      19.413  37.632  18.464  1.00 52.79           N  
ATOM   2016  CA  TYR A 261      19.149  36.690  17.386  1.00 52.32           C  
ATOM   2017  C   TYR A 261      18.254  35.611  17.965  1.00 51.21           C  
ATOM   2018  O   TYR A 261      18.624  34.970  18.943  1.00 49.96           O  
ATOM   2019  CB  TYR A 261      20.448  36.041  16.912  1.00 54.66           C  
ATOM   2020  CG  TYR A 261      21.494  37.001  16.405  1.00 59.07           C  
ATOM   2021  CD1 TYR A 261      22.040  36.847  15.133  1.00 61.15           C  
ATOM   2022  CD2 TYR A 261      21.979  38.032  17.212  1.00 60.93           C  
ATOM   2023  CE1 TYR A 261      23.046  37.691  14.674  1.00 62.71           C  
ATOM   2024  CE2 TYR A 261      22.992  38.886  16.760  1.00 61.74           C  
ATOM   2025  CZ  TYR A 261      23.518  38.705  15.486  1.00 62.86           C  
ATOM   2026  OH  TYR A 261      24.505  39.533  14.995  1.00 64.63           O  
ATOM   2027  N   GLU A 262      17.066  35.406  17.404  1.00 50.43           N  
ATOM   2028  CA  GLU A 262      16.222  34.351  17.946  1.00 49.55           C  
ATOM   2029  C   GLU A 262      15.890  33.262  16.954  1.00 48.56           C  
ATOM   2030  O   GLU A 262      16.224  33.358  15.767  1.00 46.47           O  
ATOM   2031  CB  GLU A 262      14.934  34.908  18.534  1.00 50.44           C  
ATOM   2032  CG  GLU A 262      14.093  35.674  17.585  1.00 53.52           C  
ATOM   2033  CD  GLU A 262      12.730  35.921  18.161  1.00 57.28           C  
ATOM   2034  OE1 GLU A 262      12.080  36.876  17.707  1.00 62.83           O  
ATOM   2035  OE2 GLU A 262      12.294  35.149  19.055  1.00 56.16           O  
ATOM   2036  N   THR A 263      15.236  32.218  17.467  1.00 48.32           N  
ATOM   2037  CA  THR A 263      14.828  31.042  16.693  1.00 48.63           C  
ATOM   2038  C   THR A 263      14.071  30.070  17.608  1.00 47.54           C  
ATOM   2039  O   THR A 263      14.165  30.141  18.844  1.00 47.85           O  
ATOM   2040  CB  THR A 263      16.063  30.290  16.077  1.00 47.88           C  
ATOM   2041  OG1 THR A 263      15.622  29.328  15.112  1.00 50.01           O  
ATOM   2042  CG2 THR A 263      16.819  29.529  17.137  1.00 46.54           C  
ATOM   2043  N   VAL A 264      13.300  29.173  16.999  1.00 47.29           N  
ATOM   2044  CA  VAL A 264      12.558  28.181  17.765  1.00 45.76           C  
ATOM   2045  C   VAL A 264      13.027  26.811  17.325  1.00 46.14           C  
ATOM   2046  O   VAL A 264      12.862  26.429  16.159  1.00 46.49           O  
ATOM   2047  CB  VAL A 264      11.052  28.288  17.521  1.00 43.86           C  
ATOM   2048  CG1 VAL A 264      10.303  27.256  18.344  1.00 40.67           C  
ATOM   2049  CG2 VAL A 264      10.599  29.663  17.905  1.00 43.41           C  
ATOM   2050  N   VAL A 265      13.640  26.090  18.264  1.00 45.81           N  
ATOM   2051  CA  VAL A 265      14.138  24.738  17.999  1.00 45.07           C  
ATOM   2052  C   VAL A 265      13.068  23.707  18.344  1.00 45.15           C  
ATOM   2053  O   VAL A 265      12.353  23.830  19.352  1.00 43.78           O  
ATOM   2054  CB  VAL A 265      15.461  24.399  18.804  1.00 43.60           C  
ATOM   2055  CG1 VAL A 265      16.644  25.165  18.230  1.00 42.08           C  
ATOM   2056  CG2 VAL A 265      15.288  24.709  20.286  1.00 42.45           C  
ATOM   2057  N   GLY A 266      12.966  22.691  17.489  1.00 44.70           N  
ATOM   2058  CA  GLY A 266      12.003  21.633  17.693  1.00 44.17           C  
ATOM   2059  C   GLY A 266      12.707  20.297  17.642  1.00 43.54           C  
ATOM   2060  O   GLY A 266      13.927  20.241  17.466  1.00 43.03           O  
ATOM   2061  N   PRO A 267      11.961  19.194  17.793  1.00 42.51           N  
ATOM   2062  CA  PRO A 267      12.547  17.854  17.762  1.00 41.23           C  
ATOM   2063  C   PRO A 267      13.443  17.628  16.554  1.00 40.71           C  
ATOM   2064  O   PRO A 267      13.058  17.907  15.416  1.00 41.00           O  
ATOM   2065  CB  PRO A 267      11.311  16.959  17.773  1.00 40.74           C  
ATOM   2066  CG  PRO A 267      10.371  17.746  18.678  1.00 41.26           C  
ATOM   2067  CD  PRO A 267      10.523  19.138  18.113  1.00 41.76           C  
ATOM   2068  N   GLY A 268      14.654  17.151  16.815  1.00 40.93           N  
ATOM   2069  CA  GLY A 268      15.586  16.882  15.739  1.00 41.98           C  
ATOM   2070  C   GLY A 268      16.545  18.015  15.420  1.00 43.15           C  
ATOM   2071  O   GLY A 268      17.575  17.785  14.765  1.00 43.18           O  
ATOM   2072  N   ASP A 269      16.212  19.233  15.856  1.00 43.36           N  
ATOM   2073  CA  ASP A 269      17.062  20.398  15.609  1.00 41.87           C  
ATOM   2074  C   ASP A 269      18.200  20.453  16.622  1.00 41.31           C  
ATOM   2075  O   ASP A 269      18.062  19.988  17.767  1.00 41.08           O  
ATOM   2076  CB  ASP A 269      16.266  21.707  15.718  1.00 42.62           C  
ATOM   2077  CG  ASP A 269      15.177  21.828  14.671  1.00 43.85           C  
ATOM   2078  OD1 ASP A 269      15.445  21.485  13.499  1.00 44.23           O  
ATOM   2079  OD2 ASP A 269      14.059  22.280  15.013  1.00 44.61           O  
ATOM   2080  N   VAL A 270      19.321  21.029  16.190  1.00 39.35           N  
ATOM   2081  CA  VAL A 270      20.494  21.202  17.037  1.00 37.92           C  
ATOM   2082  C   VAL A 270      20.980  22.653  16.898  1.00 37.44           C  
ATOM   2083  O   VAL A 270      21.262  23.114  15.794  1.00 37.18           O  
ATOM   2084  CB  VAL A 270      21.613  20.247  16.621  1.00 38.23           C  
ATOM   2085  CG1 VAL A 270      22.859  20.497  17.465  1.00 35.89           C  
ATOM   2086  CG2 VAL A 270      21.128  18.815  16.782  1.00 39.05           C  
ATOM   2087  N   LEU A 271      21.062  23.361  18.026  1.00 36.08           N  
ATOM   2088  CA  LEU A 271      21.496  24.761  18.051  1.00 34.67           C  
ATOM   2089  C   LEU A 271      22.893  24.905  18.599  1.00 34.17           C  
ATOM   2090  O   LEU A 271      23.196  24.371  19.649  1.00 34.66           O  
ATOM   2091  CB  LEU A 271      20.569  25.603  18.933  1.00 33.36           C  
ATOM   2092  CG  LEU A 271      21.046  27.026  19.264  1.00 34.29           C  
ATOM   2093  CD1 LEU A 271      21.322  27.836  18.005  1.00 33.11           C  
ATOM   2094  CD2 LEU A 271      19.975  27.699  20.083  1.00 32.11           C  
ATOM   2095  N   TYR A 272      23.732  25.650  17.897  1.00 33.75           N  
ATOM   2096  CA  TYR A 272      25.083  25.862  18.357  1.00 33.39           C  
ATOM   2097  C   TYR A 272      25.135  27.188  19.064  1.00 34.98           C  
ATOM   2098  O   TYR A 272      24.880  28.211  18.449  1.00 36.07           O  
ATOM   2099  CB  TYR A 272      26.044  25.905  17.185  1.00 33.12           C  
ATOM   2100  CG  TYR A 272      27.422  26.402  17.568  1.00 34.76           C  
ATOM   2101  CD1 TYR A 272      28.162  25.777  18.578  1.00 33.77           C  
ATOM   2102  CD2 TYR A 272      27.993  27.490  16.911  1.00 35.81           C  
ATOM   2103  CE1 TYR A 272      29.435  26.229  18.919  1.00 35.34           C  
ATOM   2104  CE2 TYR A 272      29.262  27.948  17.247  1.00 35.20           C  
ATOM   2105  CZ  TYR A 272      29.976  27.321  18.253  1.00 36.80           C  
ATOM   2106  OH  TYR A 272      31.201  27.855  18.606  1.00 39.29           O  
ATOM   2107  N   ILE A 273      25.471  27.165  20.351  1.00 34.92           N  
ATOM   2108  CA  ILE A 273      25.585  28.376  21.183  1.00 33.58           C  
ATOM   2109  C   ILE A 273      27.074  28.610  21.452  1.00 35.21           C  
ATOM   2110  O   ILE A 273      27.651  27.955  22.309  1.00 36.03           O  
ATOM   2111  CB  ILE A 273      24.882  28.182  22.552  1.00 31.90           C  
ATOM   2112  CG1 ILE A 273      23.409  27.825  22.330  1.00 30.06           C  
ATOM   2113  CG2 ILE A 273      25.032  29.441  23.411  1.00 33.70           C  
ATOM   2114  CD1 ILE A 273      22.640  27.659  23.598  1.00 21.23           C  
ATOM   2115  N   PRO A 274      27.704  29.548  20.732  1.00 35.87           N  
ATOM   2116  CA  PRO A 274      29.137  29.807  20.941  1.00 36.67           C  
ATOM   2117  C   PRO A 274      29.435  30.191  22.397  1.00 40.21           C  
ATOM   2118  O   PRO A 274      28.619  30.847  23.052  1.00 41.89           O  
ATOM   2119  CB  PRO A 274      29.413  30.931  19.949  1.00 36.63           C  
ATOM   2120  CG  PRO A 274      28.378  30.699  18.877  1.00 36.29           C  
ATOM   2121  CD  PRO A 274      27.157  30.440  19.704  1.00 35.33           C  
ATOM   2122  N   MET A 275      30.594  29.774  22.913  1.00 41.81           N  
ATOM   2123  CA  MET A 275      30.944  30.084  24.297  1.00 41.93           C  
ATOM   2124  C   MET A 275      30.893  31.595  24.474  1.00 42.26           C  
ATOM   2125  O   MET A 275      31.195  32.342  23.549  1.00 42.90           O  
ATOM   2126  CB  MET A 275      32.351  29.579  24.634  1.00 43.07           C  
ATOM   2127  CG  MET A 275      33.476  30.346  23.954  1.00 47.67           C  
ATOM   2128  SD  MET A 275      35.139  29.672  24.210  1.00 54.70           S  
ATOM   2129  CE  MET A 275      35.139  29.345  25.987  1.00 49.96           C  
ATOM   2130  N   TYR A 276      30.492  32.022  25.663  1.00 43.01           N  
ATOM   2131  CA  TYR A 276      30.388  33.435  26.013  1.00 43.28           C  
ATOM   2132  C   TYR A 276      29.225  34.174  25.363  1.00 43.01           C  
ATOM   2133  O   TYR A 276      29.055  35.376  25.574  1.00 44.83           O  
ATOM   2134  CB  TYR A 276      31.701  34.145  25.700  1.00 44.31           C  
ATOM   2135  CG  TYR A 276      32.779  33.869  26.724  1.00 47.59           C  
ATOM   2136  CD1 TYR A 276      32.649  34.318  28.042  1.00 48.37           C  
ATOM   2137  CD2 TYR A 276      33.941  33.175  26.378  1.00 48.96           C  
ATOM   2138  CE1 TYR A 276      33.657  34.088  28.990  1.00 50.12           C  
ATOM   2139  CE2 TYR A 276      34.953  32.937  27.324  1.00 49.83           C  
ATOM   2140  CZ  TYR A 276      34.804  33.398  28.625  1.00 50.31           C  
ATOM   2141  OH  TYR A 276      35.799  33.175  29.559  1.00 50.08           O  
ATOM   2142  N   TRP A 277      28.418  33.475  24.576  1.00 41.74           N  
ATOM   2143  CA  TRP A 277      27.273  34.133  23.966  1.00 40.44           C  
ATOM   2144  C   TRP A 277      26.096  34.099  24.927  1.00 40.67           C  
ATOM   2145  O   TRP A 277      25.758  33.051  25.477  1.00 41.98           O  
ATOM   2146  CB  TRP A 277      26.865  33.437  22.675  1.00 38.37           C  
ATOM   2147  CG  TRP A 277      27.596  33.942  21.500  1.00 37.52           C  
ATOM   2148  CD1 TRP A 277      28.939  33.876  21.276  1.00 36.97           C  
ATOM   2149  CD2 TRP A 277      27.033  34.605  20.373  1.00 38.26           C  
ATOM   2150  NE1 TRP A 277      29.255  34.457  20.068  1.00 37.13           N  
ATOM   2151  CE2 TRP A 277      28.095  34.915  19.492  1.00 38.30           C  
ATOM   2152  CE3 TRP A 277      25.730  34.968  20.017  1.00 39.42           C  
ATOM   2153  CZ2 TRP A 277      27.891  35.578  18.277  1.00 36.71           C  
ATOM   2154  CZ3 TRP A 277      25.526  35.624  18.803  1.00 37.70           C  
ATOM   2155  CH2 TRP A 277      26.600  35.924  17.954  1.00 37.02           C  
ATOM   2156  N   TRP A 278      25.466  35.241  25.141  1.00 40.23           N  
ATOM   2157  CA  TRP A 278      24.314  35.276  26.026  1.00 39.93           C  
ATOM   2158  C   TRP A 278      23.139  34.497  25.427  1.00 39.69           C  
ATOM   2159  O   TRP A 278      22.959  34.470  24.213  1.00 39.76           O  
ATOM   2160  CB  TRP A 278      23.854  36.715  26.252  1.00 39.49           C  
ATOM   2161  CG  TRP A 278      24.846  37.592  26.912  1.00 38.29           C  
ATOM   2162  CD1 TRP A 278      25.860  38.291  26.316  1.00 37.79           C  
ATOM   2163  CD2 TRP A 278      24.926  37.879  28.312  1.00 37.39           C  
ATOM   2164  NE1 TRP A 278      26.567  39.001  27.259  1.00 37.98           N  
ATOM   2165  CE2 TRP A 278      26.013  38.763  28.494  1.00 38.58           C  
ATOM   2166  CE3 TRP A 278      24.184  37.474  29.425  1.00 35.76           C  
ATOM   2167  CZ2 TRP A 278      26.374  39.251  29.757  1.00 39.10           C  
ATOM   2168  CZ3 TRP A 278      24.542  37.952  30.676  1.00 35.87           C  
ATOM   2169  CH2 TRP A 278      25.625  38.829  30.832  1.00 38.53           C  
ATOM   2170  N   HIS A 279      22.338  33.877  26.290  1.00 40.22           N  
ATOM   2171  CA  HIS A 279      21.152  33.168  25.823  1.00 41.33           C  
ATOM   2172  C   HIS A 279      19.985  33.090  26.803  1.00 41.21           C  
ATOM   2173  O   HIS A 279      20.134  32.746  27.973  1.00 40.73           O  
ATOM   2174  CB  HIS A 279      21.488  31.754  25.312  1.00 42.80           C  
ATOM   2175  CG  HIS A 279      22.392  30.968  26.206  1.00 45.60           C  
ATOM   2176  ND1 HIS A 279      23.746  31.206  26.290  1.00 46.79           N  
ATOM   2177  CD2 HIS A 279      22.148  29.904  27.010  1.00 46.48           C  
ATOM   2178  CE1 HIS A 279      24.300  30.321  27.104  1.00 47.56           C  
ATOM   2179  NE2 HIS A 279      23.351  29.515  27.555  1.00 48.02           N  
ATOM   2180  N   HIS A 280      18.813  33.430  26.287  1.00 41.44           N  
ATOM   2181  CA  HIS A 280      17.581  33.394  27.045  1.00 43.27           C  
ATOM   2182  C   HIS A 280      16.792  32.228  26.429  1.00 45.48           C  
ATOM   2183  O   HIS A 280      16.576  32.220  25.214  1.00 47.57           O  
ATOM   2184  CB  HIS A 280      16.854  34.713  26.835  1.00 42.86           C  
ATOM   2185  CG  HIS A 280      15.406  34.673  27.193  1.00 44.55           C  
ATOM   2186  ND1 HIS A 280      14.936  34.986  28.447  1.00 45.72           N  
ATOM   2187  CD2 HIS A 280      14.319  34.339  26.454  1.00 44.82           C  
ATOM   2188  CE1 HIS A 280      13.623  34.851  28.470  1.00 46.42           C  
ATOM   2189  NE2 HIS A 280      13.221  34.460  27.275  1.00 46.20           N  
ATOM   2190  N   ILE A 281      16.395  31.241  27.234  1.00 45.42           N  
ATOM   2191  CA  ILE A 281      15.652  30.093  26.699  1.00 45.32           C  
ATOM   2192  C   ILE A 281      14.293  29.923  27.343  1.00 46.77           C  
ATOM   2193  O   ILE A 281      14.170  29.885  28.556  1.00 48.32           O  
ATOM   2194  CB  ILE A 281      16.423  28.799  26.908  1.00 43.50           C  
ATOM   2195  CG1 ILE A 281      17.669  28.827  26.031  1.00 42.21           C  
ATOM   2196  CG2 ILE A 281      15.547  27.600  26.581  1.00 42.74           C  
ATOM   2197  CD1 ILE A 281      18.590  27.711  26.288  1.00 42.61           C  
ATOM   2198  N   GLU A 282      13.263  29.804  26.526  1.00 49.00           N  
ATOM   2199  CA  GLU A 282      11.937  29.645  27.087  1.00 51.50           C  
ATOM   2200  C   GLU A 282      11.181  28.549  26.359  1.00 51.58           C  
ATOM   2201  O   GLU A 282      11.346  28.377  25.152  1.00 50.32           O  
ATOM   2202  CB  GLU A 282      11.172  30.971  27.006  1.00 53.22           C  
ATOM   2203  CG  GLU A 282      10.913  31.447  25.577  1.00 55.73           C  
ATOM   2204  CD  GLU A 282      10.225  32.807  25.505  1.00 57.59           C  
ATOM   2205  OE1 GLU A 282      10.834  33.813  25.924  1.00 59.52           O  
ATOM   2206  OE2 GLU A 282       9.071  32.869  25.031  1.00 58.54           O  
ATOM   2207  N   SER A 283      10.370  27.806  27.108  1.00 52.96           N  
ATOM   2208  CA  SER A 283       9.552  26.733  26.555  1.00 54.42           C  
ATOM   2209  C   SER A 283       8.195  27.313  26.145  1.00 55.80           C  
ATOM   2210  O   SER A 283       7.477  27.886  26.983  1.00 56.45           O  
ATOM   2211  CB  SER A 283       9.328  25.616  27.589  1.00 53.92           C  
ATOM   2212  OG  SER A 283      10.534  24.977  27.986  1.00 53.19           O  
ATOM   2213  N   LEU A 284       7.861  27.159  24.859  1.00 56.34           N  
ATOM   2214  CA  LEU A 284       6.612  27.650  24.278  1.00 56.13           C  
ATOM   2215  C   LEU A 284       5.412  27.500  25.206  1.00 56.35           C  
ATOM   2216  O   LEU A 284       5.249  26.494  25.910  1.00 56.54           O  
ATOM   2217  CB  LEU A 284       6.343  26.940  22.941  1.00 55.97           C  
ATOM   2218  CG  LEU A 284       7.046  27.429  21.663  1.00 55.74           C  
ATOM   2219  CD1 LEU A 284       6.311  28.618  21.120  1.00 56.72           C  
ATOM   2220  CD2 LEU A 284       8.486  27.805  21.934  1.00 57.40           C  
ATOM   2221  N   LEU A 285       4.587  28.538  25.209  1.00 57.29           N  
ATOM   2222  CA  LEU A 285       3.395  28.585  26.027  1.00 57.79           C  
ATOM   2223  C   LEU A 285       2.395  27.580  25.499  1.00 59.32           C  
ATOM   2224  O   LEU A 285       2.120  27.537  24.297  1.00 59.63           O  
ATOM   2225  CB  LEU A 285       2.788  29.981  25.975  1.00 57.21           C  
ATOM   2226  CG  LEU A 285       3.642  31.110  26.546  1.00 56.65           C  
ATOM   2227  CD1 LEU A 285       3.134  32.433  26.010  1.00 57.22           C  
ATOM   2228  CD2 LEU A 285       3.597  31.080  28.065  1.00 54.19           C  
ATOM   2229  N   ASN A 286       1.860  26.765  26.402  1.00 60.70           N  
ATOM   2230  CA  ASN A 286       0.872  25.757  26.039  1.00 62.22           C  
ATOM   2231  C   ASN A 286       1.410  24.780  24.992  1.00 61.82           C  
ATOM   2232  O   ASN A 286       0.702  24.441  24.042  1.00 62.28           O  
ATOM   2233  CB  ASN A 286      -0.396  26.434  25.493  1.00 64.08           C  
ATOM   2234  CG  ASN A 286      -1.014  27.413  26.480  1.00 66.32           C  
ATOM   2235  OD1 ASN A 286      -1.276  27.070  27.636  1.00 66.43           O  
ATOM   2236  ND2 ASN A 286      -1.264  28.636  26.021  1.00 68.33           N  
ATOM   2237  N   GLY A 287       2.653  24.334  25.171  1.00 60.58           N  
ATOM   2238  CA  GLY A 287       3.257  23.411  24.225  1.00 58.84           C  
ATOM   2239  C   GLY A 287       3.722  22.123  24.875  1.00 57.78           C  
ATOM   2240  O   GLY A 287       4.710  21.515  24.457  1.00 58.55           O  
ATOM   2241  N   GLY A 288       3.008  21.697  25.907  1.00 56.05           N  
ATOM   2242  CA  GLY A 288       3.396  20.475  26.581  1.00 55.12           C  
ATOM   2243  C   GLY A 288       4.783  20.610  27.175  1.00 54.11           C  
ATOM   2244  O   GLY A 288       5.342  21.700  27.228  1.00 54.15           O  
ATOM   2245  N   ILE A 289       5.342  19.497  27.631  1.00 52.90           N  
ATOM   2246  CA  ILE A 289       6.673  19.530  28.211  1.00 50.55           C  
ATOM   2247  C   ILE A 289       7.695  19.578  27.098  1.00 50.87           C  
ATOM   2248  O   ILE A 289       7.369  19.341  25.931  1.00 52.13           O  
ATOM   2249  CB  ILE A 289       6.953  18.302  29.061  1.00 49.48           C  
ATOM   2250  CG1 ILE A 289       7.038  17.070  28.171  1.00 49.85           C  
ATOM   2251  CG2 ILE A 289       5.868  18.141  30.101  1.00 47.33           C  
ATOM   2252  CD1 ILE A 289       7.829  15.950  28.783  1.00 50.94           C  
ATOM   2253  N   THR A 290       8.937  19.872  27.476  1.00 49.85           N  
ATOM   2254  CA  THR A 290      10.055  19.977  26.541  1.00 48.03           C  
ATOM   2255  C   THR A 290      11.242  19.181  27.077  1.00 46.07           C  
ATOM   2256  O   THR A 290      11.550  19.210  28.267  1.00 45.94           O  
ATOM   2257  CB  THR A 290      10.503  21.458  26.342  1.00 48.14           C  
ATOM   2258  OG1 THR A 290      11.047  21.962  27.567  1.00 49.33           O  
ATOM   2259  CG2 THR A 290       9.318  22.331  25.911  1.00 47.44           C  
ATOM   2260  N   ILE A 291      11.910  18.475  26.181  1.00 44.25           N  
ATOM   2261  CA  ILE A 291      13.050  17.671  26.564  1.00 43.98           C  
ATOM   2262  C   ILE A 291      14.215  18.045  25.675  1.00 43.40           C  
ATOM   2263  O   ILE A 291      14.075  18.131  24.454  1.00 43.53           O  
ATOM   2264  CB  ILE A 291      12.747  16.185  26.389  1.00 44.40           C  
ATOM   2265  CG1 ILE A 291      11.496  15.817  27.188  1.00 43.82           C  
ATOM   2266  CG2 ILE A 291      13.933  15.373  26.838  1.00 43.66           C  
ATOM   2267  CD1 ILE A 291      11.043  14.401  26.951  1.00 44.19           C  
ATOM   2268  N   THR A 292      15.373  18.260  26.282  1.00 43.02           N  
ATOM   2269  CA  THR A 292      16.549  18.635  25.514  1.00 42.83           C  
ATOM   2270  C   THR A 292      17.779  17.969  26.102  1.00 42.14           C  
ATOM   2271  O   THR A 292      17.744  17.508  27.238  1.00 42.55           O  
ATOM   2272  CB  THR A 292      16.787  20.149  25.575  1.00 42.93           C  
ATOM   2273  OG1 THR A 292      15.552  20.841  25.366  1.00 44.74           O  
ATOM   2274  CG2 THR A 292      17.768  20.562  24.519  1.00 41.23           C  
ATOM   2275  N   VAL A 293      18.862  17.927  25.335  1.00 42.07           N  
ATOM   2276  CA  VAL A 293      20.111  17.354  25.823  1.00 43.22           C  
ATOM   2277  C   VAL A 293      21.236  18.212  25.264  1.00 44.91           C  
ATOM   2278  O   VAL A 293      21.368  18.312  24.050  1.00 46.39           O  
ATOM   2279  CB  VAL A 293      20.306  15.903  25.336  1.00 42.13           C  
ATOM   2280  CG1 VAL A 293      21.741  15.420  25.617  1.00 38.27           C  
ATOM   2281  CG2 VAL A 293      19.300  15.010  26.023  1.00 40.09           C  
ATOM   2282  N   ASN A 294      22.024  18.845  26.133  1.00 46.28           N  
ATOM   2283  CA  ASN A 294      23.119  19.682  25.645  1.00 47.91           C  
ATOM   2284  C   ASN A 294      24.460  18.962  25.693  1.00 47.47           C  
ATOM   2285  O   ASN A 294      24.599  17.955  26.379  1.00 47.13           O  
ATOM   2286  CB  ASN A 294      23.205  21.012  26.426  1.00 50.62           C  
ATOM   2287  CG  ASN A 294      23.603  20.830  27.891  1.00 54.61           C  
ATOM   2288  OD1 ASN A 294      24.595  20.174  28.212  1.00 56.72           O  
ATOM   2289  ND2 ASN A 294      22.829  21.431  28.788  1.00 56.17           N  
ATOM   2290  N   PHE A 295      25.434  19.482  24.946  1.00 47.66           N  
ATOM   2291  CA  PHE A 295      26.775  18.912  24.889  1.00 48.20           C  
ATOM   2292  C   PHE A 295      27.764  20.031  25.169  1.00 49.05           C  
ATOM   2293  O   PHE A 295      27.975  20.889  24.324  1.00 49.08           O  
ATOM   2294  CB  PHE A 295      27.062  18.338  23.499  1.00 48.43           C  
ATOM   2295  CG  PHE A 295      26.199  17.169  23.132  1.00 48.15           C  
ATOM   2296  CD1 PHE A 295      24.824  17.311  23.031  1.00 48.48           C  
ATOM   2297  CD2 PHE A 295      26.766  15.921  22.904  1.00 48.13           C  
ATOM   2298  CE1 PHE A 295      24.015  16.229  22.708  1.00 47.61           C  
ATOM   2299  CE2 PHE A 295      25.970  14.828  22.579  1.00 48.44           C  
ATOM   2300  CZ  PHE A 295      24.589  14.985  22.481  1.00 48.67           C  
ATOM   2301  N   TRP A 296      28.368  20.034  26.351  1.00 50.00           N  
ATOM   2302  CA  TRP A 296      29.316  21.090  26.680  1.00 50.92           C  
ATOM   2303  C   TRP A 296      30.763  20.679  26.491  1.00 50.38           C  
ATOM   2304  O   TRP A 296      31.208  19.701  27.077  1.00 50.68           O  
ATOM   2305  CB  TRP A 296      29.125  21.554  28.124  1.00 51.69           C  
ATOM   2306  CG  TRP A 296      28.070  22.592  28.303  1.00 55.02           C  
ATOM   2307  CD1 TRP A 296      27.630  23.469  27.369  1.00 56.61           C  
ATOM   2308  CD2 TRP A 296      27.400  22.924  29.526  1.00 57.86           C  
ATOM   2309  NE1 TRP A 296      26.728  24.344  27.923  1.00 56.50           N  
ATOM   2310  CE2 TRP A 296      26.568  24.032  29.248  1.00 57.50           C  
ATOM   2311  CE3 TRP A 296      27.425  22.403  30.821  1.00 61.35           C  
ATOM   2312  CZ2 TRP A 296      25.768  24.632  30.222  1.00 59.91           C  
ATOM   2313  CZ3 TRP A 296      26.624  23.001  31.802  1.00 62.97           C  
ATOM   2314  CH2 TRP A 296      25.808  24.106  31.491  1.00 62.41           C  
ATOM   2315  N   TYR A 297      31.489  21.443  25.677  1.00 50.69           N  
ATOM   2316  CA  TYR A 297      32.906  21.196  25.396  1.00 52.20           C  
ATOM   2317  C   TYR A 297      33.768  22.391  25.826  1.00 54.25           C  
ATOM   2318  O   TYR A 297      33.326  23.533  25.811  1.00 54.78           O  
ATOM   2319  CB  TYR A 297      33.144  20.962  23.894  1.00 51.18           C  
ATOM   2320  CG  TYR A 297      32.548  19.695  23.322  1.00 50.86           C  
ATOM   2321  CD1 TYR A 297      31.181  19.589  23.067  1.00 50.67           C  
ATOM   2322  CD2 TYR A 297      33.355  18.593  23.057  1.00 50.26           C  
ATOM   2323  CE1 TYR A 297      30.640  18.413  22.569  1.00 51.16           C  
ATOM   2324  CE2 TYR A 297      32.829  17.423  22.562  1.00 50.73           C  
ATOM   2325  CZ  TYR A 297      31.477  17.336  22.325  1.00 51.75           C  
ATOM   2326  OH  TYR A 297      30.976  16.143  21.882  1.00 54.36           O  
ATOM   2327  N   LYS A 298      35.007  22.128  26.202  1.00 57.11           N  
ATOM   2328  CA  LYS A 298      35.869  23.229  26.593  1.00 60.11           C  
ATOM   2329  C   LYS A 298      36.410  23.902  25.351  1.00 60.97           C  
ATOM   2330  O   LYS A 298      36.899  23.240  24.445  1.00 61.21           O  
ATOM   2331  CB  LYS A 298      37.021  22.740  27.461  1.00 62.27           C  
ATOM   2332  CG  LYS A 298      36.592  22.438  28.880  1.00 67.63           C  
ATOM   2333  CD  LYS A 298      37.766  22.066  29.771  1.00 71.11           C  
ATOM   2334  CE  LYS A 298      37.324  21.942  31.230  1.00 73.23           C  
ATOM   2335  NZ  LYS A 298      38.410  21.415  32.110  1.00 75.87           N  
ATOM   2336  N   GLY A 299      36.324  25.222  25.307  1.00 62.27           N  
ATOM   2337  CA  GLY A 299      36.824  25.936  24.151  1.00 64.60           C  
ATOM   2338  C   GLY A 299      38.251  25.569  23.792  1.00 66.47           C  
ATOM   2339  O   GLY A 299      38.973  24.935  24.569  1.00 65.68           O  
ATOM   2340  N   ALA A 300      38.659  25.964  22.592  1.00 69.01           N  
ATOM   2341  CA  ALA A 300      40.014  25.704  22.134  1.00 71.25           C  
ATOM   2342  C   ALA A 300      40.975  26.421  23.088  1.00 73.61           C  
ATOM   2343  O   ALA A 300      40.647  27.472  23.635  1.00 74.18           O  
ATOM   2344  CB  ALA A 300      40.190  26.227  20.707  1.00 70.14           C  
ATOM   2345  N   PRO A 301      42.169  25.856  23.304  1.00 76.07           N  
ATOM   2346  CA  PRO A 301      43.162  26.460  24.201  1.00 78.07           C  
ATOM   2347  C   PRO A 301      43.620  27.847  23.734  1.00 79.80           C  
ATOM   2348  O   PRO A 301      43.367  28.245  22.593  1.00 78.78           O  
ATOM   2349  CB  PRO A 301      44.288  25.433  24.189  1.00 77.59           C  
ATOM   2350  CG  PRO A 301      44.200  24.879  22.788  1.00 77.59           C  
ATOM   2351  CD  PRO A 301      42.719  24.669  22.629  1.00 77.22           C  
ATOM   2352  N   THR A 302      44.293  28.581  24.620  1.00 82.92           N  
ATOM   2353  CA  THR A 302      44.789  29.931  24.316  1.00 85.72           C  
ATOM   2354  C   THR A 302      46.041  29.890  23.425  1.00 86.57           C  
ATOM   2355  O   THR A 302      47.010  29.201  23.747  1.00 86.36           O  
ATOM   2356  CB  THR A 302      45.143  30.668  25.606  1.00 86.85           C  
ATOM   2357  OG1 THR A 302      44.087  30.504  26.564  1.00 87.22           O  
ATOM   2358  CG2 THR A 302      45.348  32.139  25.315  1.00 87.84           C  
ATOM   2359  N   PRO A 303      46.044  30.653  22.315  1.00 87.12           N  
ATOM   2360  CA  PRO A 303      47.140  30.734  21.340  1.00 88.46           C  
ATOM   2361  C   PRO A 303      48.552  30.838  21.896  1.00 90.54           C  
ATOM   2362  O   PRO A 303      49.529  30.579  21.175  1.00 91.77           O  
ATOM   2363  CB  PRO A 303      46.769  31.954  20.515  1.00 87.75           C  
ATOM   2364  CG  PRO A 303      45.300  31.884  20.497  1.00 87.34           C  
ATOM   2365  CD  PRO A 303      44.969  31.589  21.945  1.00 86.95           C  
ATOM   2366  N   LYS A 304      48.670  31.216  23.168  1.00 91.17           N  
ATOM   2367  CA  LYS A 304      49.983  31.349  23.780  1.00 91.09           C  
ATOM   2368  C   LYS A 304      50.782  32.478  23.154  1.00 90.88           C  
ATOM   2369  O   LYS A 304      51.933  32.702  23.520  1.00 90.90           O  
ATOM   2370  N   ARG A 305      50.165  33.178  22.203  1.00 90.19           N  
ATOM   2371  CA  ARG A 305      50.775  34.301  21.500  1.00 88.32           C  
ATOM   2372  C   ARG A 305      49.661  35.284  21.143  1.00 87.25           C  
ATOM   2373  O   ARG A 305      49.344  35.486  19.968  1.00 88.17           O  
ATOM   2374  CB  ARG A 305      51.473  33.807  20.235  1.00 87.83           C  
ATOM   2375  N   ILE A 306      49.067  35.889  22.174  1.00 84.99           N  
ATOM   2376  CA  ILE A 306      47.966  36.834  22.003  1.00 81.97           C  
ATOM   2377  C   ILE A 306      48.058  37.662  20.718  1.00 80.07           C  
ATOM   2378  O   ILE A 306      48.982  38.450  20.515  1.00 80.06           O  
ATOM   2379  CB  ILE A 306      47.870  37.752  23.230  1.00 80.41           C  
ATOM   2380  N   GLU A 307      47.090  37.472  19.840  1.00 77.84           N  
ATOM   2381  CA  GLU A 307      47.103  38.204  18.596  1.00 76.75           C  
ATOM   2382  C   GLU A 307      45.983  39.222  18.590  1.00 74.02           C  
ATOM   2383  O   GLU A 307      44.809  38.887  18.743  1.00 73.49           O  
ATOM   2384  CB  GLU A 307      46.976  37.238  17.422  1.00 79.88           C  
ATOM   2385  CG  GLU A 307      45.760  36.322  17.527  1.00 85.13           C  
ATOM   2386  CD  GLU A 307      45.600  35.414  16.319  1.00 88.35           C  
ATOM   2387  OE1 GLU A 307      44.583  34.688  16.232  1.00 88.63           O  
ATOM   2388  OE2 GLU A 307      46.497  35.424  15.447  1.00 90.01           O  
ATOM   2389  N   TYR A 308      46.363  40.477  18.420  1.00 71.38           N  
ATOM   2390  CA  TYR A 308      45.415  41.572  18.406  1.00 68.99           C  
ATOM   2391  C   TYR A 308      44.916  41.817  17.000  1.00 67.30           C  
ATOM   2392  O   TYR A 308      45.567  41.437  16.027  1.00 68.75           O  
ATOM   2393  CB  TYR A 308      46.092  42.818  18.957  1.00 68.93           C  
ATOM   2394  CG  TYR A 308      46.586  42.619  20.366  1.00 69.33           C  
ATOM   2395  CD1 TYR A 308      45.843  43.070  21.455  1.00 69.07           C  
ATOM   2396  CD2 TYR A 308      47.785  41.952  20.618  1.00 68.52           C  
ATOM   2397  CE1 TYR A 308      46.284  42.867  22.764  1.00 68.74           C  
ATOM   2398  CE2 TYR A 308      48.230  41.740  21.921  1.00 67.89           C  
ATOM   2399  CZ  TYR A 308      47.480  42.201  22.988  1.00 68.60           C  
ATOM   2400  OH  TYR A 308      47.930  42.011  24.277  1.00 68.29           O  
ATOM   2401  N   PRO A 309      43.747  42.454  16.868  1.00 65.36           N  
ATOM   2402  CA  PRO A 309      42.884  42.948  17.948  1.00 62.78           C  
ATOM   2403  C   PRO A 309      42.177  41.818  18.684  1.00 60.59           C  
ATOM   2404  O   PRO A 309      41.903  40.764  18.117  1.00 61.75           O  
ATOM   2405  CB  PRO A 309      41.903  43.841  17.216  1.00 63.26           C  
ATOM   2406  CG  PRO A 309      41.753  43.134  15.903  1.00 63.46           C  
ATOM   2407  CD  PRO A 309      43.179  42.791  15.554  1.00 64.61           C  
ATOM   2408  N   LEU A 310      41.872  42.049  19.950  1.00 56.63           N  
ATOM   2409  CA  LEU A 310      41.199  41.040  20.751  1.00 52.63           C  
ATOM   2410  C   LEU A 310      39.728  40.911  20.399  1.00 51.38           C  
ATOM   2411  O   LEU A 310      39.087  41.875  19.983  1.00 52.14           O  
ATOM   2412  CB  LEU A 310      41.309  41.383  22.228  1.00 51.03           C  
ATOM   2413  CG  LEU A 310      42.511  40.892  23.031  1.00 49.99           C  
ATOM   2414  CD1 LEU A 310      43.733  40.728  22.140  1.00 49.23           C  
ATOM   2415  CD2 LEU A 310      42.751  41.873  24.180  1.00 48.20           C  
ATOM   2416  N   LYS A 311      39.197  39.709  20.575  1.00 48.75           N  
ATOM   2417  CA  LYS A 311      37.789  39.486  20.304  1.00 47.63           C  
ATOM   2418  C   LYS A 311      37.008  39.820  21.583  1.00 48.04           C  
ATOM   2419  O   LYS A 311      37.539  39.742  22.693  1.00 48.51           O  
ATOM   2420  CB  LYS A 311      37.551  38.030  19.873  1.00 45.60           C  
ATOM   2421  N   ALA A 312      35.755  40.221  21.412  1.00 49.40           N  
ATOM   2422  CA  ALA A 312      34.897  40.588  22.535  1.00 49.52           C  
ATOM   2423  C   ALA A 312      34.971  39.625  23.715  1.00 50.27           C  
ATOM   2424  O   ALA A 312      35.253  40.041  24.830  1.00 51.93           O  
ATOM   2425  CB  ALA A 312      33.440  40.718  22.067  1.00 49.80           C  
ATOM   2426  N   HIS A 313      34.731  38.337  23.474  1.00 50.62           N  
ATOM   2427  CA  HIS A 313      34.751  37.368  24.573  1.00 49.42           C  
ATOM   2428  C   HIS A 313      36.087  37.298  25.294  1.00 47.34           C  
ATOM   2429  O   HIS A 313      36.155  36.931  26.463  1.00 47.41           O  
ATOM   2430  CB  HIS A 313      34.351  35.971  24.079  1.00 51.78           C  
ATOM   2431  CG  HIS A 313      35.443  35.238  23.368  1.00 54.58           C  
ATOM   2432  ND1 HIS A 313      35.893  35.589  22.117  1.00 56.77           N  
ATOM   2433  CD2 HIS A 313      36.172  34.156  23.743  1.00 55.62           C  
ATOM   2434  CE1 HIS A 313      36.847  34.759  21.744  1.00 56.47           C  
ATOM   2435  NE2 HIS A 313      37.038  33.875  22.708  1.00 56.95           N  
ATOM   2436  N   GLN A 314      37.152  37.651  24.600  1.00 45.21           N  
ATOM   2437  CA  GLN A 314      38.447  37.634  25.244  1.00 44.70           C  
ATOM   2438  C   GLN A 314      38.544  38.721  26.306  1.00 43.92           C  
ATOM   2439  O   GLN A 314      39.150  38.507  27.359  1.00 44.11           O  
ATOM   2440  CB  GLN A 314      39.551  37.815  24.222  1.00 46.01           C  
ATOM   2441  CG  GLN A 314      39.792  36.571  23.408  1.00 50.68           C  
ATOM   2442  CD  GLN A 314      40.925  36.732  22.426  1.00 52.75           C  
ATOM   2443  OE1 GLN A 314      40.826  37.492  21.458  1.00 56.05           O  
ATOM   2444  NE2 GLN A 314      42.023  36.024  22.674  1.00 52.51           N  
ATOM   2445  N   LYS A 315      37.955  39.886  26.037  1.00 42.58           N  
ATOM   2446  CA  LYS A 315      37.976  40.993  26.994  1.00 40.81           C  
ATOM   2447  C   LYS A 315      37.144  40.636  28.220  1.00 39.91           C  
ATOM   2448  O   LYS A 315      37.508  40.971  29.340  1.00 40.29           O  
ATOM   2449  CB  LYS A 315      37.416  42.264  26.355  1.00 41.09           C  
ATOM   2450  CG  LYS A 315      38.265  42.772  25.213  1.00 42.44           C  
ATOM   2451  CD  LYS A 315      37.694  44.031  24.600  1.00 42.07           C  
ATOM   2452  CE  LYS A 315      38.616  44.543  23.508  1.00 42.61           C  
ATOM   2453  NZ  LYS A 315      38.099  45.772  22.847  1.00 45.74           N  
ATOM   2454  N   VAL A 316      36.028  39.951  27.999  1.00 38.71           N  
ATOM   2455  CA  VAL A 316      35.171  39.550  29.097  1.00 37.60           C  
ATOM   2456  C   VAL A 316      35.947  38.598  29.998  1.00 38.22           C  
ATOM   2457  O   VAL A 316      35.706  38.516  31.208  1.00 37.30           O  
ATOM   2458  CB  VAL A 316      33.941  38.835  28.572  1.00 37.62           C  
ATOM   2459  CG1 VAL A 316      32.914  38.717  29.667  1.00 37.33           C  
ATOM   2460  CG2 VAL A 316      33.383  39.584  27.376  1.00 36.60           C  
ATOM   2461  N   ALA A 317      36.875  37.868  29.393  1.00 38.52           N  
ATOM   2462  CA  ALA A 317      37.689  36.927  30.141  1.00 38.37           C  
ATOM   2463  C   ALA A 317      38.635  37.714  31.033  1.00 38.92           C  
ATOM   2464  O   ALA A 317      38.934  37.304  32.157  1.00 39.97           O  
ATOM   2465  CB  ALA A 317      38.475  36.073  29.189  1.00 36.33           C  
ATOM   2466  N   ILE A 318      39.105  38.845  30.507  1.00 39.84           N  
ATOM   2467  CA  ILE A 318      40.016  39.721  31.228  1.00 39.18           C  
ATOM   2468  C   ILE A 318      39.292  40.373  32.408  1.00 40.26           C  
ATOM   2469  O   ILE A 318      39.834  40.430  33.513  1.00 42.25           O  
ATOM   2470  CB  ILE A 318      40.546  40.834  30.324  1.00 38.89           C  
ATOM   2471  CG1 ILE A 318      41.423  40.240  29.214  1.00 37.70           C  
ATOM   2472  CG2 ILE A 318      41.304  41.850  31.159  1.00 39.98           C  
ATOM   2473  CD1 ILE A 318      41.978  41.258  28.229  1.00 36.70           C  
ATOM   2474  N   MET A 319      38.081  40.876  32.171  1.00 39.23           N  
ATOM   2475  CA  MET A 319      37.320  41.490  33.238  1.00 38.67           C  
ATOM   2476  C   MET A 319      37.095  40.482  34.349  1.00 40.46           C  
ATOM   2477  O   MET A 319      37.362  40.769  35.522  1.00 40.81           O  
ATOM   2478  CB  MET A 319      35.991  41.972  32.709  1.00 37.94           C  
ATOM   2479  CG  MET A 319      36.153  42.990  31.622  1.00 38.32           C  
ATOM   2480  SD  MET A 319      34.676  43.978  31.472  1.00 41.79           S  
ATOM   2481  CE  MET A 319      33.883  43.183  30.166  1.00 39.84           C  
ATOM   2482  N   ARG A 320      36.604  39.299  33.988  1.00 41.55           N  
ATOM   2483  CA  ARG A 320      36.360  38.250  34.971  1.00 41.58           C  
ATOM   2484  C   ARG A 320      37.601  37.996  35.817  1.00 42.28           C  
ATOM   2485  O   ARG A 320      37.505  37.825  37.027  1.00 42.32           O  
ATOM   2486  CB  ARG A 320      35.972  36.948  34.283  1.00 40.12           C  
ATOM   2487  CG  ARG A 320      34.626  36.981  33.608  1.00 39.81           C  
ATOM   2488  CD  ARG A 320      34.231  35.582  33.158  1.00 38.05           C  
ATOM   2489  NE  ARG A 320      34.145  34.602  34.249  1.00 37.42           N  
ATOM   2490  CZ  ARG A 320      33.126  34.501  35.105  1.00 37.92           C  
ATOM   2491  NH1 ARG A 320      32.085  35.325  35.025  1.00 37.98           N  
ATOM   2492  NH2 ARG A 320      33.142  33.563  36.043  1.00 39.05           N  
ATOM   2493  N   ASN A 321      38.759  37.966  35.155  1.00 44.82           N  
ATOM   2494  CA  ASN A 321      40.031  37.740  35.832  1.00 46.12           C  
ATOM   2495  C   ASN A 321      40.366  38.806  36.845  1.00 44.99           C  
ATOM   2496  O   ASN A 321      40.791  38.501  37.964  1.00 44.56           O  
ATOM   2497  CB  ASN A 321      41.177  37.699  34.848  1.00 50.67           C  
ATOM   2498  CG  ASN A 321      41.901  36.399  34.900  1.00 57.14           C  
ATOM   2499  OD1 ASN A 321      41.436  35.409  34.340  1.00 61.29           O  
ATOM   2500  ND2 ASN A 321      43.026  36.365  35.615  1.00 59.33           N  
ATOM   2501  N   ILE A 322      40.205  40.061  36.437  1.00 43.96           N  
ATOM   2502  CA  ILE A 322      40.483  41.179  37.315  1.00 43.15           C  
ATOM   2503  C   ILE A 322      39.660  41.062  38.595  1.00 43.13           C  
ATOM   2504  O   ILE A 322      40.203  41.174  39.694  1.00 43.84           O  
ATOM   2505  CB  ILE A 322      40.143  42.502  36.647  1.00 42.39           C  
ATOM   2506  CG1 ILE A 322      40.915  42.649  35.335  1.00 42.41           C  
ATOM   2507  CG2 ILE A 322      40.514  43.633  37.572  1.00 41.14           C  
ATOM   2508  CD1 ILE A 322      42.423  42.743  35.519  1.00 43.23           C  
ATOM   2509  N   GLU A 323      38.354  40.852  38.445  1.00 42.65           N  
ATOM   2510  CA  GLU A 323      37.455  40.707  39.586  1.00 43.11           C  
ATOM   2511  C   GLU A 323      37.897  39.558  40.510  1.00 43.75           C  
ATOM   2512  O   GLU A 323      37.893  39.685  41.736  1.00 43.71           O  
ATOM   2513  CB  GLU A 323      36.013  40.450  39.096  1.00 42.85           C  
ATOM   2514  CG  GLU A 323      35.363  41.626  38.318  1.00 43.95           C  
ATOM   2515  CD  GLU A 323      33.936  41.352  37.780  1.00 44.30           C  
ATOM   2516  OE1 GLU A 323      32.986  41.114  38.566  1.00 44.09           O  
ATOM   2517  OE2 GLU A 323      33.762  41.393  36.546  1.00 44.37           O  
ATOM   2518  N   LYS A 324      38.270  38.430  39.909  1.00 45.97           N  
ATOM   2519  CA  LYS A 324      38.705  37.257  40.662  1.00 46.36           C  
ATOM   2520  C   LYS A 324      39.948  37.524  41.463  1.00 47.18           C  
ATOM   2521  O   LYS A 324      39.984  37.264  42.658  1.00 47.47           O  
ATOM   2522  CB  LYS A 324      38.950  36.070  39.724  1.00 46.47           C  
ATOM   2523  CG  LYS A 324      37.817  35.069  39.773  1.00 49.40           C  
ATOM   2524  CD  LYS A 324      37.323  34.616  38.390  1.00 51.22           C  
ATOM   2525  CE  LYS A 324      38.236  33.590  37.713  1.00 53.37           C  
ATOM   2526  NZ  LYS A 324      37.599  32.957  36.505  1.00 52.95           N  
ATOM   2527  N   MET A 325      40.963  38.052  40.797  1.00 48.52           N  
ATOM   2528  CA  MET A 325      42.222  38.344  41.461  1.00 52.33           C  
ATOM   2529  C   MET A 325      42.143  39.475  42.471  1.00 51.59           C  
ATOM   2530  O   MET A 325      42.844  39.472  43.477  1.00 51.75           O  
ATOM   2531  CB  MET A 325      43.297  38.640  40.429  1.00 56.53           C  
ATOM   2532  CG  MET A 325      43.652  37.418  39.606  1.00 64.53           C  
ATOM   2533  SD  MET A 325      45.076  37.689  38.537  1.00 74.82           S  
ATOM   2534  CE  MET A 325      45.353  35.925  37.771  1.00 72.82           C  
ATOM   2535  N   LEU A 326      41.301  40.452  42.200  1.00 50.94           N  
ATOM   2536  CA  LEU A 326      41.141  41.550  43.130  1.00 49.74           C  
ATOM   2537  C   LEU A 326      40.471  41.043  44.422  1.00 49.42           C  
ATOM   2538  O   LEU A 326      40.773  41.507  45.508  1.00 50.16           O  
ATOM   2539  CB  LEU A 326      40.297  42.633  42.478  1.00 49.80           C  
ATOM   2540  CG  LEU A 326      40.295  43.996  43.150  1.00 50.04           C  
ATOM   2541  CD1 LEU A 326      41.731  44.462  43.311  1.00 51.00           C  
ATOM   2542  CD2 LEU A 326      39.486  44.972  42.306  1.00 48.68           C  
ATOM   2543  N   GLY A 327      39.556  40.090  44.301  1.00 49.29           N  
ATOM   2544  CA  GLY A 327      38.910  39.573  45.492  1.00 48.30           C  
ATOM   2545  C   GLY A 327      39.881  38.724  46.298  1.00 49.34           C  
ATOM   2546  O   GLY A 327      39.654  38.467  47.481  1.00 50.09           O  
ATOM   2547  N   GLU A 328      40.959  38.277  45.652  1.00 50.70           N  
ATOM   2548  CA  GLU A 328      41.973  37.441  46.315  1.00 51.63           C  
ATOM   2549  C   GLU A 328      42.893  38.326  47.112  1.00 49.93           C  
ATOM   2550  O   GLU A 328      43.151  38.085  48.287  1.00 49.56           O  
ATOM   2551  CB  GLU A 328      42.831  36.681  45.297  1.00 56.81           C  
ATOM   2552  CG  GLU A 328      42.137  35.529  44.578  1.00 65.92           C  
ATOM   2553  CD  GLU A 328      41.747  34.394  45.512  1.00 70.83           C  
ATOM   2554  OE1 GLU A 328      42.111  34.447  46.712  1.00 74.48           O  
ATOM   2555  OE2 GLU A 328      41.088  33.433  45.045  1.00 73.43           O  
ATOM   2556  N   ALA A 329      43.395  39.346  46.428  1.00 47.95           N  
ATOM   2557  CA  ALA A 329      44.290  40.310  47.022  1.00 47.05           C  
ATOM   2558  C   ALA A 329      43.666  40.960  48.249  1.00 47.32           C  
ATOM   2559  O   ALA A 329      44.292  41.011  49.301  1.00 48.10           O  
ATOM   2560  CB  ALA A 329      44.639  41.357  46.011  1.00 45.17           C  
ATOM   2561  N   LEU A 330      42.441  41.461  48.116  1.00 46.66           N  
ATOM   2562  CA  LEU A 330      41.762  42.110  49.236  1.00 46.56           C  
ATOM   2563  C   LEU A 330      41.310  41.121  50.308  1.00 47.84           C  
ATOM   2564  O   LEU A 330      40.918  41.514  51.410  1.00 47.71           O  
ATOM   2565  CB  LEU A 330      40.544  42.881  48.732  1.00 45.25           C  
ATOM   2566  CG  LEU A 330      40.801  43.936  47.661  1.00 45.89           C  
ATOM   2567  CD1 LEU A 330      39.480  44.584  47.275  1.00 45.70           C  
ATOM   2568  CD2 LEU A 330      41.788  44.974  48.186  1.00 45.28           C  
ATOM   2569  N   GLY A 331      41.361  39.836  49.971  1.00 49.99           N  
ATOM   2570  CA  GLY A 331      40.947  38.802  50.907  1.00 52.87           C  
ATOM   2571  C   GLY A 331      39.466  38.884  51.237  1.00 54.48           C  
ATOM   2572  O   GLY A 331      38.973  38.243  52.170  1.00 56.05           O  
ATOM   2573  N   ASN A 332      38.750  39.674  50.452  1.00 55.82           N  
ATOM   2574  CA  ASN A 332      37.338  39.850  50.680  1.00 56.67           C  
ATOM   2575  C   ASN A 332      36.648  40.332  49.426  1.00 55.80           C  
ATOM   2576  O   ASN A 332      36.881  41.441  48.952  1.00 57.08           O  
ATOM   2577  CB  ASN A 332      37.120  40.858  51.799  1.00 59.50           C  
ATOM   2578  CG  ASN A 332      35.665  41.196  51.989  1.00 62.86           C  
ATOM   2579  OD1 ASN A 332      34.812  40.306  52.090  1.00 64.47           O  
ATOM   2580  ND2 ASN A 332      35.365  42.486  52.053  1.00 63.84           N  
ATOM   2581  N   PRO A 333      35.771  39.496  48.876  1.00 54.01           N  
ATOM   2582  CA  PRO A 333      35.037  39.839  47.660  1.00 53.78           C  
ATOM   2583  C   PRO A 333      34.103  41.028  47.821  1.00 53.63           C  
ATOM   2584  O   PRO A 333      33.677  41.641  46.845  1.00 53.40           O  
ATOM   2585  CB  PRO A 333      34.293  38.552  47.355  1.00 52.96           C  
ATOM   2586  CG  PRO A 333      34.028  38.007  48.711  1.00 52.16           C  
ATOM   2587  CD  PRO A 333      35.344  38.190  49.396  1.00 53.14           C  
ATOM   2588  N   GLN A 334      33.787  41.362  49.058  1.00 55.26           N  
ATOM   2589  CA  GLN A 334      32.881  42.465  49.325  1.00 56.66           C  
ATOM   2590  C   GLN A 334      33.509  43.827  49.012  1.00 55.79           C  
ATOM   2591  O   GLN A 334      32.802  44.762  48.635  1.00 56.48           O  
ATOM   2592  CB  GLN A 334      32.436  42.425  50.793  1.00 61.06           C  
ATOM   2593  CG  GLN A 334      32.052  41.025  51.322  1.00 68.21           C  
ATOM   2594  CD  GLN A 334      30.937  40.345  50.523  1.00 73.35           C  
ATOM   2595  OE1 GLN A 334      29.816  40.856  50.421  1.00 75.49           O  
ATOM   2596  NE2 GLN A 334      31.236  39.169  49.977  1.00 75.00           N  
ATOM   2597  N   GLU A 335      34.832  43.927  49.151  1.00 54.63           N  
ATOM   2598  CA  GLU A 335      35.539  45.184  48.910  1.00 53.09           C  
ATOM   2599  C   GLU A 335      35.928  45.400  47.452  1.00 51.01           C  
ATOM   2600  O   GLU A 335      36.430  46.461  47.081  1.00 50.14           O  
ATOM   2601  CB  GLU A 335      36.791  45.256  49.790  1.00 55.76           C  
ATOM   2602  CG  GLU A 335      37.532  46.586  49.669  1.00 59.16           C  
ATOM   2603  CD  GLU A 335      38.632  46.750  50.695  1.00 62.05           C  
ATOM   2604  OE1 GLU A 335      39.318  47.793  50.640  1.00 62.53           O  
ATOM   2605  OE2 GLU A 335      38.805  45.853  51.554  1.00 61.49           O  
ATOM   2606  N   VAL A 336      35.697  44.382  46.636  1.00 48.97           N  
ATOM   2607  CA  VAL A 336      36.005  44.467  45.222  1.00 46.51           C  
ATOM   2608  C   VAL A 336      35.357  45.712  44.616  1.00 45.00           C  
ATOM   2609  O   VAL A 336      35.997  46.475  43.898  1.00 43.59           O  
ATOM   2610  CB  VAL A 336      35.504  43.202  44.502  1.00 46.54           C  
ATOM   2611  CG1 VAL A 336      35.658  43.346  43.006  1.00 46.13           C  
ATOM   2612  CG2 VAL A 336      36.286  41.996  44.991  1.00 46.51           C  
ATOM   2613  N   GLY A 337      34.088  45.934  44.921  1.00 43.69           N  
ATOM   2614  CA  GLY A 337      33.429  47.100  44.365  1.00 43.12           C  
ATOM   2615  C   GLY A 337      34.032  48.427  44.786  1.00 42.86           C  
ATOM   2616  O   GLY A 337      34.367  49.269  43.953  1.00 44.23           O  
ATOM   2617  N   PRO A 338      34.177  48.659  46.092  1.00 42.08           N  
ATOM   2618  CA  PRO A 338      34.743  49.912  46.588  1.00 41.35           C  
ATOM   2619  C   PRO A 338      36.072  50.270  45.957  1.00 41.96           C  
ATOM   2620  O   PRO A 338      36.321  51.424  45.618  1.00 43.07           O  
ATOM   2621  CB  PRO A 338      34.880  49.654  48.074  1.00 41.26           C  
ATOM   2622  CG  PRO A 338      33.708  48.778  48.346  1.00 40.82           C  
ATOM   2623  CD  PRO A 338      33.744  47.803  47.208  1.00 40.89           C  
ATOM   2624  N   LEU A 339      36.932  49.275  45.798  1.00 41.66           N  
ATOM   2625  CA  LEU A 339      38.235  49.534  45.228  1.00 41.95           C  
ATOM   2626  C   LEU A 339      38.179  49.920  43.756  1.00 40.45           C  
ATOM   2627  O   LEU A 339      38.958  50.744  43.290  1.00 40.93           O  
ATOM   2628  CB  LEU A 339      39.126  48.318  45.410  1.00 43.44           C  
ATOM   2629  CG  LEU A 339      40.601  48.641  45.192  1.00 45.09           C  
ATOM   2630  CD1 LEU A 339      41.069  49.641  46.245  1.00 45.40           C  
ATOM   2631  CD2 LEU A 339      41.408  47.373  45.274  1.00 46.45           C  
ATOM   2632  N   LEU A 340      37.255  49.316  43.025  1.00 39.47           N  
ATOM   2633  CA  LEU A 340      37.111  49.622  41.616  1.00 37.48           C  
ATOM   2634  C   LEU A 340      36.624  51.044  41.445  1.00 37.63           C  
ATOM   2635  O   LEU A 340      37.102  51.766  40.578  1.00 38.18           O  
ATOM   2636  CB  LEU A 340      36.139  48.647  40.951  1.00 36.70           C  
ATOM   2637  CG  LEU A 340      36.633  47.210  40.782  1.00 35.33           C  
ATOM   2638  CD1 LEU A 340      35.522  46.364  40.224  1.00 32.15           C  
ATOM   2639  CD2 LEU A 340      37.814  47.182  39.843  1.00 32.56           C  
ATOM   2640  N   ASN A 341      35.671  51.458  42.268  1.00 38.94           N  
ATOM   2641  CA  ASN A 341      35.177  52.829  42.159  1.00 40.46           C  
ATOM   2642  C   ASN A 341      36.268  53.820  42.537  1.00 40.50           C  
ATOM   2643  O   ASN A 341      36.407  54.871  41.912  1.00 41.31           O  
ATOM   2644  CB  ASN A 341      33.958  53.047  43.049  1.00 42.44           C  
ATOM   2645  CG  ASN A 341      32.702  52.409  42.493  1.00 45.21           C  
ATOM   2646  OD1 ASN A 341      32.191  52.826  41.448  1.00 45.73           O  
ATOM   2647  ND2 ASN A 341      32.204  51.388  43.176  1.00 46.50           N  
ATOM   2648  N   THR A 342      37.046  53.476  43.564  1.00 40.82           N  
ATOM   2649  CA  THR A 342      38.143  54.315  44.038  1.00 40.02           C  
ATOM   2650  C   THR A 342      39.152  54.512  42.911  1.00 40.53           C  
ATOM   2651  O   THR A 342      39.769  55.571  42.781  1.00 42.61           O  
ATOM   2652  CB  THR A 342      38.873  53.660  45.227  1.00 40.51           C  
ATOM   2653  OG1 THR A 342      37.992  53.591  46.349  1.00 41.30           O  
ATOM   2654  CG2 THR A 342      40.098  54.454  45.611  1.00 38.73           C  
ATOM   2655  N   MET A 343      39.300  53.476  42.093  1.00 40.05           N  
ATOM   2656  CA  MET A 343      40.229  53.470  40.984  1.00 38.91           C  
ATOM   2657  C   MET A 343      39.799  54.337  39.808  1.00 38.86           C  
ATOM   2658  O   MET A 343      40.631  54.955  39.141  1.00 38.64           O  
ATOM   2659  CB  MET A 343      40.389  52.042  40.497  1.00 39.81           C  
ATOM   2660  CG  MET A 343      41.807  51.542  40.484  1.00 42.41           C  
ATOM   2661  SD  MET A 343      41.915  50.051  39.499  1.00 42.91           S  
ATOM   2662  CE  MET A 343      40.897  48.981  40.456  1.00 44.57           C  
ATOM   2663  N   ILE A 344      38.491  54.377  39.565  1.00 38.94           N  
ATOM   2664  CA  ILE A 344      37.917  55.100  38.435  1.00 39.83           C  
ATOM   2665  C   ILE A 344      37.411  56.526  38.644  1.00 38.66           C  
ATOM   2666  O   ILE A 344      37.555  57.374  37.754  1.00 36.86           O  
ATOM   2667  CB  ILE A 344      36.782  54.276  37.853  1.00 41.82           C  
ATOM   2668  CG1 ILE A 344      37.373  52.991  37.293  1.00 44.88           C  
ATOM   2669  CG2 ILE A 344      36.063  55.020  36.751  1.00 43.38           C  
ATOM   2670  CD1 ILE A 344      36.363  51.920  37.003  1.00 48.11           C  
ATOM   2671  N   LYS A 345      36.796  56.778  39.793  1.00 39.06           N  
ATOM   2672  CA  LYS A 345      36.243  58.095  40.074  1.00 39.97           C  
ATOM   2673  C   LYS A 345      37.236  59.221  39.888  1.00 39.59           C  
ATOM   2674  O   LYS A 345      38.269  59.269  40.552  1.00 39.40           O  
ATOM   2675  CB  LYS A 345      35.688  58.157  41.494  1.00 41.43           C  
ATOM   2676  CG  LYS A 345      34.429  57.361  41.717  1.00 42.26           C  
ATOM   2677  CD  LYS A 345      33.952  57.440  43.176  1.00 46.23           C  
ATOM   2678  CE  LYS A 345      34.937  56.777  44.161  1.00 50.45           C  
ATOM   2679  NZ  LYS A 345      34.445  56.612  45.583  1.00 52.06           N  
ATOM   2680  N   GLY A 346      36.884  60.132  38.988  1.00 41.22           N  
ATOM   2681  CA  GLY A 346      37.705  61.291  38.700  1.00 42.11           C  
ATOM   2682  C   GLY A 346      39.019  60.988  38.002  1.00 43.26           C  
ATOM   2683  O   GLY A 346      39.869  61.874  37.881  1.00 45.15           O  
ATOM   2684  N   ARG A 347      39.198  59.752  37.541  1.00 42.43           N  
ATOM   2685  CA  ARG A 347      40.431  59.378  36.872  1.00 40.13           C  
ATOM   2686  C   ARG A 347      40.160  58.703  35.543  1.00 41.06           C  
ATOM   2687  O   ARG A 347      40.843  58.973  34.562  1.00 43.17           O  
ATOM   2688  CB  ARG A 347      41.253  58.424  37.733  1.00 38.23           C  
ATOM   2689  CG  ARG A 347      41.492  58.877  39.160  1.00 36.93           C  
ATOM   2690  CD  ARG A 347      42.795  58.278  39.693  1.00 37.37           C  
ATOM   2691  NE  ARG A 347      42.859  56.819  39.594  1.00 40.78           N  
ATOM   2692  CZ  ARG A 347      43.935  56.126  39.210  1.00 38.70           C  
ATOM   2693  NH1 ARG A 347      43.881  54.809  39.165  1.00 40.31           N  
ATOM   2694  NH2 ARG A 347      45.053  56.742  38.851  1.00 38.01           N  
ATOM   2695  N   TYR A 348      39.167  57.824  35.499  1.00 41.35           N  
ATOM   2696  CA  TYR A 348      38.892  57.146  34.243  1.00 41.72           C  
ATOM   2697  C   TYR A 348      37.502  57.381  33.682  1.00 43.41           C  
ATOM   2698  O   TYR A 348      37.160  56.856  32.633  1.00 44.19           O  
ATOM   2699  CB  TYR A 348      39.133  55.644  34.398  1.00 39.60           C  
ATOM   2700  CG  TYR A 348      40.595  55.247  34.423  1.00 38.07           C  
ATOM   2701  CD1 TYR A 348      41.374  55.301  33.265  1.00 37.26           C  
ATOM   2702  CD2 TYR A 348      41.210  54.833  35.605  1.00 37.30           C  
ATOM   2703  CE1 TYR A 348      42.728  54.952  33.285  1.00 35.74           C  
ATOM   2704  CE2 TYR A 348      42.565  54.485  35.634  1.00 36.81           C  
ATOM   2705  CZ  TYR A 348      43.317  54.548  34.468  1.00 36.08           C  
ATOM   2706  OH  TYR A 348      44.656  54.213  34.470  1.00 36.20           O  
ATOM   2707  N   ASN A 349      36.706  58.183  34.363  1.00 45.87           N  
ATOM   2708  CA  ASN A 349      35.362  58.421  33.871  1.00 48.72           C  
ATOM   2709  C   ASN A 349      35.143  59.878  33.487  1.00 49.94           C  
ATOM   2710  O   ASN A 349      35.867  60.762  33.941  1.00 52.03           O  
ATOM   2711  CB  ASN A 349      34.356  58.002  34.934  1.00 49.06           C  
ATOM   2712  CG  ASN A 349      34.571  58.725  36.239  1.00 51.13           C  
ATOM   2713  OD1 ASN A 349      35.377  59.650  36.323  1.00 51.71           O  
ATOM   2714  ND2 ASN A 349      33.852  58.306  37.271  1.00 52.24           N  
ATOM   2715  OXT ASN A 349      34.228  60.155  32.713  1.00 53.85           O  
TER    2716      ASN A 349                                                      
HETATM 2717 FE   FE2 A1350      23.298  28.003  29.363  1.00 47.48          FE  
HETATM 2718  S   SO4 A1352       0.476  25.214  43.691  1.00123.58           S  
HETATM 2719  O1  SO4 A1352      -0.807  24.555  43.981  1.00124.18           O  
HETATM 2720  O2  SO4 A1352       1.214  24.402  42.702  1.00123.36           O  
HETATM 2721  O3  SO4 A1352       0.209  26.555  43.145  1.00123.07           O  
HETATM 2722  O4  SO4 A1352       1.266  25.344  44.932  1.00123.12           O  
HETATM 2723  S   SO4 A1353       2.016  28.341  29.904  1.00141.31           S  
HETATM 2724  O1  SO4 A1353       1.017  29.021  29.061  1.00141.17           O  
HETATM 2725  O2  SO4 A1353       2.987  27.647  29.030  1.00141.23           O  
HETATM 2726  O3  SO4 A1353       2.696  29.345  30.746  1.00140.89           O  
HETATM 2727  O4  SO4 A1353       1.350  27.360  30.780  1.00140.95           O  
HETATM 2728  S   SO4 A1354      34.686  31.275  38.612  1.00135.76           S  
HETATM 2729  O1  SO4 A1354      35.225  32.311  39.513  1.00135.68           O  
HETATM 2730  O2  SO4 A1354      35.276  29.975  38.974  1.00135.70           O  
HETATM 2731  O3  SO4 A1354      33.223  31.205  38.779  1.00135.16           O  
HETATM 2732  O4  SO4 A1354      35.026  31.601  37.208  1.00134.97           O  
HETATM 2733  CD1 NDF A 400      19.964  26.253  33.016  1.00 48.08           C  
HETATM 2734  CE1 NDF A 400      21.092  26.391  33.835  1.00 48.26           C  
HETATM 2735  CZ  NDF A 400      22.163  25.529  33.687  1.00 49.22           C  
HETATM 2736  CE2 NDF A 400      22.118  24.517  32.717  1.00 49.85           C  
HETATM 2737  CD2 NDF A 400      21.004  24.379  31.909  1.00 48.66           C  
HETATM 2738  CG  NDF A 400      19.920  25.254  32.061  1.00 48.06           C  
HETATM 2739  CB  NDF A 400      18.677  25.085  31.183  1.00 46.26           C  
HETATM 2740  CA  NDF A 400      18.796  25.862  29.871  1.00 46.85           C  
HETATM 2741  C   NDF A 400      17.521  25.655  29.056  1.00 47.26           C  
HETATM 2742  O   NDF A 400      17.544  25.049  27.989  1.00 47.07           O  
HETATM 2743  OXT NDF A 400      16.444  26.101  29.474  1.00 46.86           O  
HETATM 2744  N   NDF A 400      19.969  25.367  29.136  1.00 47.11           N  
HETATM 2745  C2  NDF A 400      21.075  26.094  28.994  1.00 48.01           C  
HETATM 2746  O2' NDF A 400      21.184  27.241  29.427  1.00 48.64           O  
HETATM 2747  C1  NDF A 400      22.263  25.498  28.238  1.00 47.93           C  
HETATM 2748  O1  NDF A 400      22.142  24.400  27.674  1.00 50.02           O  
HETATM 2749  O2  NDF A 400      23.332  26.087  28.195  1.00 48.41           O  
HETATM 2750  CD1 NDF A 401      33.705  45.871  26.225  1.00 59.74           C  
HETATM 2751  CE1 NDF A 401      34.244  44.668  26.687  1.00 59.30           C  
HETATM 2752  CZ  NDF A 401      33.585  43.471  26.436  1.00 58.02           C  
HETATM 2753  CE2 NDF A 401      32.383  43.472  25.728  1.00 57.40           C  
HETATM 2754  CD2 NDF A 401      31.848  44.668  25.270  1.00 59.01           C  
HETATM 2755  CG  NDF A 401      32.515  45.870  25.511  1.00 60.45           C  
HETATM 2756  CB  NDF A 401      31.983  47.164  24.889  1.00 62.47           C  
HETATM 2757  CA  NDF A 401      32.928  47.688  23.801  1.00 65.56           C  
HETATM 2758  C   NDF A 401      32.263  48.848  23.065  1.00 65.10           C  
HETATM 2759  O   NDF A 401      31.808  48.696  21.936  1.00 65.47           O  
HETATM 2760  OXT NDF A 401      32.173  49.957  23.605  1.00 64.99           O  
HETATM 2761  N   NDF A 401      33.229  46.608  22.844  1.00 66.92           N  
HETATM 2762  C2  NDF A 401      34.462  46.161  22.627  1.00 68.68           C  
HETATM 2763  O2' NDF A 401      35.460  46.619  23.182  1.00 67.52           O  
HETATM 2764  C1  NDF A 401      34.643  45.024  21.614  1.00 69.27           C  
HETATM 2765  O1  NDF A 401      33.672  44.592  21.004  1.00 71.09           O  
HETATM 2766  O2  NDF A 401      35.761  44.539  21.421  1.00 69.54           O  
HETATM 2767  O   HOH A1001      30.969  28.512  42.237  1.00 61.06           O  
HETATM 2768  O   HOH A1002      26.825   8.521  30.108  1.00 52.29           O  
HETATM 2769  O   HOH A1003      27.257  30.854  26.286  1.00 39.94           O  
HETATM 2770  O   HOH A1004      17.540  39.159  37.404  1.00 38.55           O  
HETATM 2771  O   HOH A1005      26.040  15.234  39.636  1.00 43.38           O  
HETATM 2772  O   HOH A1006      38.228  30.181  39.285  1.00 62.10           O  
HETATM 2773  O   HOH A1007      28.980  37.804  36.104  1.00 32.38           O  
HETATM 2774  O   HOH A1008      18.919  56.736  28.428  1.00 41.39           O  
HETATM 2775  O   HOH A1009      31.049  39.640  19.727  1.00 37.99           O  
HETATM 2776  O   HOH A1010      27.304  38.654  15.248  1.00 60.98           O  
HETATM 2777  O   HOH A1011      16.408  47.202  22.341  1.00 38.01           O  
HETATM 2778  O   HOH A1012      31.820  35.893  16.981  1.00 53.79           O  
HETATM 2779  O   HOH A1013      32.919  39.860  34.290  1.00 32.52           O  
HETATM 2780  O   HOH A1014      15.662  43.062   7.973  1.00 73.41           O  
HETATM 2781  O   HOH A1015      15.316  38.296  35.982  1.00 54.20           O  
HETATM 2782  O   HOH A1016      36.362  11.690  21.493  1.00 48.73           O  
HETATM 2783  O   HOH A1017      17.130  38.707  33.167  1.00 56.37           O  
HETATM 2784  O   HOH A1018      34.725  16.377   8.183  1.00 67.57           O  
HETATM 2785  O   HOH A1019       7.390  36.257   9.590  1.00 70.25           O  
HETATM 2786  O   HOH A1020      15.870  52.289  40.004  1.00 47.63           O  
HETATM 2787  O   HOH A1021       5.489  12.633  28.071  1.00 35.37           O  
HETATM 2788  O   HOH A1022      30.084  37.090  27.837  1.00 50.13           O  
HETATM 2789  O   HOH A1023      13.993  24.179   7.476  1.00 51.95           O  
HETATM 2790  O   HOH A1024       3.990  32.724  35.626  1.00 52.82           O  
HETATM 2791  O   HOH A1025      11.068  19.546  14.440  1.00 57.18           O  
HETATM 2792  O   HOH A1026      28.973  47.531  20.022  1.00 35.31           O  
HETATM 2793  O   HOH A1027      12.037  33.352  14.763  1.00 68.30           O  
HETATM 2794  O   HOH A1028      17.590  30.424   7.714  1.00 60.56           O  
HETATM 2795  O   HOH A1029       7.276  16.965  20.543  1.00 49.30           O  
HETATM 2796  O   HOH A1030      31.616  41.170  44.785  1.00 40.66           O  
HETATM 2797  O   HOH A1031      15.120  51.491  22.443  1.00 43.41           O  
HETATM 2798  O   HOH A1032      15.574  30.848  12.942  1.00 52.26           O  
HETATM 2799  O   HOH A1033      38.486  61.225  34.048  1.00 61.16           O  
HETATM 2800  O   HOH A1034      29.010  39.529  27.212  1.00 37.78           O  
HETATM 2801  O   HOH A1035      20.053  18.264  13.766  1.00 40.84           O  
HETATM 2802  O   HOH A1036      17.941  17.218  18.182  1.00 33.63           O  
HETATM 2803  O   HOH A1037      32.820  40.054  42.783  1.00 33.35           O  
HETATM 2804  O   HOH A1038      27.973  28.376  25.176  1.00 34.06           O  
HETATM 2805  O   HOH A1039      33.312  37.748  20.831  1.00 40.10           O  
HETATM 2806  O   HOH A1040      26.291  31.763  38.918  1.00 38.76           O  
HETATM 2807  O   HOH A1041      25.732  51.572  31.366  1.00 55.25           O  
HETATM 2808  O   HOH A1042      15.325  18.898  12.231  1.00 54.88           O  
HETATM 2809  O   HOH A1043      26.382  13.461  38.008  1.00 54.89           O  
HETATM 2810  O   HOH A1044      38.084  49.024  54.061  1.00 45.94           O  
HETATM 2811  O   HOH A1045      23.914  27.497  31.205  1.00 41.96           O  
HETATM 2812  O   HOH A1046      12.847  36.075  14.321  1.00 45.82           O  
HETATM 2813  O   HOH A1047      11.408  21.770  13.714  1.00 49.47           O  
HETATM 2814  O   HOH A1048      28.829   8.807  31.620  1.00 57.41           O  
HETATM 2815  O   HOH A1049      28.397  16.800  37.561  1.00 66.42           O  
HETATM 2816  O   HOH A1050      28.703  14.161  37.568  1.00 76.91           O  
HETATM 2817  O   HOH A1051      38.388  50.293  49.301  1.00 58.80           O  
HETATM 2818  O   HOH A1052       7.289  12.450  22.312  1.00 56.08           O  
HETATM 2819  O   HOH A1053      42.866  35.577  49.786  1.00 45.09           O  
HETATM 2820  O   HOH A1054      13.524  41.578   7.576  1.00 61.83           O  
HETATM 2821  O   HOH A1055       8.134   5.928  24.219  1.00 60.13           O  
HETATM 2822  O   HOH A1056      18.583  26.917  37.235  1.00 36.72           O  
HETATM 2823  O   HOH A1057      19.815  32.077  34.590  1.00 34.48           O  
HETATM 2824  O   HOH A1058      28.235  27.281  33.000  1.00 45.83           O  
HETATM 2825  O   HOH A1059      11.221  48.758  36.849  1.00 64.13           O  
HETATM 2826  O   HOH A1060      35.794  49.749  51.792  1.00 48.50           O  
HETATM 2827  O   HOH A1061      36.187  14.946  24.610  1.00 63.87           O  
HETATM 2828  O   HOH A1062      10.948  13.732  19.466  1.00 41.46           O  
HETATM 2829  O   HOH A1063      49.054  40.581  16.581  1.00 61.06           O  
HETATM 2830  O   HOH A1064       3.653  33.461  32.839  1.00 60.11           O  
HETATM 2831  O   HOH A1065      12.681  39.853  12.150  1.00 63.71           O  
HETATM 2832  O   HOH A1066      14.534  26.606  14.257  1.00 49.23           O  
HETATM 2833  O   HOH A1067      19.312  14.950  16.800  1.00 40.90           O  
HETATM 2834  O   HOH A1068       4.750   5.905  24.076  1.00 72.39           O  
HETATM 2835  O   HOH A1069      15.479  27.373  48.474  1.00 57.64           O  
HETATM 2836  O   HOH A1070      38.230  13.715  25.290  1.00 52.59           O  
HETATM 2837  O   HOH A1071      17.532  27.975  35.440  1.00 50.67           O  
HETATM 2838  O   HOH A1072      16.254  36.438  30.274  1.00 43.97           O  
HETATM 2839  O   HOH A1073      30.403  38.803  33.974  1.00 40.43           O  
HETATM 2840  O   HOH A1074      26.069  27.244  26.433  1.00 35.57           O  
HETATM 2841  O   HOH A1075      23.533  46.839  20.727  1.00 50.38           O  
HETATM 2842  O   HOH A1076      18.859  53.948  39.930  1.00 79.11           O  
HETATM 2843  O   HOH A1077      38.596  29.999  23.733  1.00 57.51           O  
HETATM 2844  O   HOH A1078      34.177  39.767  18.480  1.00 39.54           O  
HETATM 2845  O   HOH A1079      41.536  43.961  52.009  1.00 45.29           O  
HETATM 2846  O   HOH A1080      13.192  26.554  29.282  1.00 54.88           O  
HETATM 2847  O   HOH A1081       6.618  24.003  25.807  1.00 45.03           O  
HETATM 2848  O   HOH A1082       7.487  31.069  26.103  1.00 59.00           O  
HETATM 2849  O   HOH A1083      14.445  37.997  32.699  1.00 53.38           O  
HETATM 2850  O   HOH A1084      29.437  30.842  36.299  1.00 46.18           O  
HETATM 2851  O   HOH A1085      31.422  46.831  19.629  1.00 49.79           O  
HETATM 2852  O   HOH A1086      27.341  45.056  31.654  1.00 41.69           O  
HETATM 2853  O   HOH A1087      13.742  21.168  28.509  1.00 41.80           O  
HETATM 2854  O   HOH A1088      19.004  15.544  13.155  1.00 47.93           O  
HETATM 2855  O   HOH A1089       3.467  13.592  26.226  1.00 62.95           O  
HETATM 2856  O   HOH A1090       5.221   9.901  28.641  1.00 51.58           O  
CONECT 1490 2717                                                                
CONECT 1510 2717                                                                
CONECT 2179 2717                                                                
CONECT 2717 1490 1510 2179 2746                                                 
CONECT 2717 2749 2811                                                           
CONECT 2718 2719 2720 2721 2722                                                 
CONECT 2719 2718                                                                
CONECT 2720 2718                                                                
CONECT 2721 2718                                                                
CONECT 2722 2718                                                                
CONECT 2723 2724 2725 2726 2727                                                 
CONECT 2724 2723                                                                
CONECT 2725 2723                                                                
CONECT 2726 2723                                                                
CONECT 2727 2723                                                                
CONECT 2728 2729 2730 2731 2732                                                 
CONECT 2729 2728                                                                
CONECT 2730 2728                                                                
CONECT 2731 2728                                                                
CONECT 2732 2728                                                                
CONECT 2733 2734 2738                                                           
CONECT 2734 2733 2735                                                           
CONECT 2735 2734 2736                                                           
CONECT 2736 2735 2737                                                           
CONECT 2737 2736 2738                                                           
CONECT 2738 2733 2737 2739                                                      
CONECT 2739 2738 2740                                                           
CONECT 2740 2739 2741 2744                                                      
CONECT 2741 2740 2742 2743                                                      
CONECT 2742 2741                                                                
CONECT 2743 2741                                                                
CONECT 2744 2740 2745                                                           
CONECT 2745 2744 2746 2747                                                      
CONECT 2746 2717 2745                                                           
CONECT 2747 2745 2748 2749                                                      
CONECT 2748 2747                                                                
CONECT 2749 2717 2747                                                           
CONECT 2750 2751 2755                                                           
CONECT 2751 2750 2752                                                           
CONECT 2752 2751 2753                                                           
CONECT 2753 2752 2754                                                           
CONECT 2754 2753 2755                                                           
CONECT 2755 2750 2754 2756                                                      
CONECT 2756 2755 2757                                                           
CONECT 2757 2756 2758 2761                                                      
CONECT 2758 2757 2759 2760                                                      
CONECT 2759 2758                                                                
CONECT 2760 2758                                                                
CONECT 2761 2757 2762                                                           
CONECT 2762 2761 2763 2764                                                      
CONECT 2763 2762                                                                
CONECT 2764 2762 2765 2766                                                      
CONECT 2765 2764                                                                
CONECT 2766 2764                                                                
CONECT 2811 2717                                                                
MASTER      376    0    6   15   14    0   12    6 2855    1   55   27          
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.