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***  OXYGEN TRANSPORT 13-DEC-97 101M  ***

elNémo ID: 211108160546133634

Job options:

ID        	=	 211108160546133634
JOBID     	=	 OXYGEN TRANSPORT 13-DEC-97 101M
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXYGEN TRANSPORT                        13-DEC-97   101M              
TITLE     SPERM WHALE MYOGLOBIN F46V N-BUTYL ISOCYANIDE AT PH 9.0               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
SOURCE   4 ORGANISM_TAXID: 9755;                                                
SOURCE   5 ORGAN: SKELETAL;                                                     
SOURCE   6 TISSUE: SKELETAL MUSCLE;                                             
SOURCE   7 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: PHAGE RESISTANT TB1;                       
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PEMBL 19+                                 
KEYWDS    LIGAND BINDING, OXYGEN STORAGE, OXYGEN BINDING, HEME, OXYGEN          
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.D.SMITH,J.S.OLSON,G.N.PHILLIPS JR.                                  
REVDAT   6   03-NOV-21 101M    1       REMARK SEQADV LINK                       
REVDAT   5   07-MAR-18 101M    1       REMARK                                   
REVDAT   4   24-FEB-09 101M    1       VERSN                                    
REVDAT   3   03-MAY-05 101M    1       AUTHOR                                   
REVDAT   2   17-MAY-99 101M    1       JRNL   HELIX                             
REVDAT   1   08-APR-98 101M    0                                                
JRNL        AUTH   R.D.SMITH                                                    
JRNL        TITL   CORRELATIONS BETWEEN BOUND N-ALKYL ISOCYANIDE ORIENTATIONS   
JRNL        TITL 2 AND PATHWAYS FOR LIGAND BINDING IN RECOMBINANT MYOGLOBINS    
JRNL        REF    THESIS, RICE                               1999              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 5.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12340                          
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) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1220                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.07                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1287                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2090                       
REMARK   3   BIN FREE R VALUE                    : 0.2110                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 11.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 161                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1221                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.23                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.360                           
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) : 2.470 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.860 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 8.730 ; 2.500                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 12.900; 2.500                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAMETER.HEME                                 
REMARK   3  PARAMETER FILE  3  : PARAMETER.NBNC                                 
REMARK   3  PARAMETER FILE  4  : PARAM19.SOLV                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPOLOGY.HEME                                  
REMARK   3  TOPOLOGY FILE  3   : TOPOLOGY.NBNC                                  
REMARK   3  TOPOLOGY FILE  4   : TOPH19.SOLV                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 101M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170003.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 292                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : PINHOLE COLLIMATOR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13624                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.070                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 6.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.450                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: SPERM WHALE MYOGLOBIN 0M, D122N (DEOXY)              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.0 M AMMONIUM SULFATE, 20 MM TRIS,      
REMARK 280  1MM EDTA, PH 9.0                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 332  LIES ON A SPECIAL POSITION.                          
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    ASP A  20       75.97   -151.70                                   
REMARK 500    LYS A  98       70.18     56.03                                   
REMARK 500    TYR A 151      -71.27   -108.10                                   
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                             HEM A 155  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 HEM A 155   NA   89.5                                              
REMARK 620 3 HEM A 155   NB   83.7  93.0                                        
REMARK 620 4 HEM A 155   NC   88.6 177.6  88.1                                  
REMARK 620 5 HEM A 155   ND   91.6  89.9 174.5  88.8                            
REMARK 620 6 NBN A 156   C   175.7  86.2  97.1  95.7  87.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: HEM                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: LIGAND BINDING SITE.                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NBN A 156                 
DBREF  101M A    1   153  UNP    P02185   MYG_PHYCA        1    153             
SEQADV 101M VAL A   46  UNP  P02185    PHE    46 ENGINEERED MUTATION            
SEQADV 101M ASN A  122  UNP  P02185    ASP   122 ENGINEERED MUTATION            
SEQRES   1 A  154  MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS          
SEQRES   2 A  154  VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY          
SEQRES   3 A  154  GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU          
SEQRES   4 A  154  THR LEU GLU LYS PHE ASP ARG VAL LYS HIS LEU LYS THR          
SEQRES   5 A  154  GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS          
SEQRES   6 A  154  GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS          
SEQRES   7 A  154  LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA          
SEQRES   8 A  154  GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR          
SEQRES   9 A  154  LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS          
SEQRES  10 A  154  SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY          
SEQRES  11 A  154  ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE          
SEQRES  12 A  154  ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                  
HET    SO4  A 157       5                                                       
HET    HEM  A 155      43                                                       
HET    NBN  A 156       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     NBN N-BUTYL ISOCYANIDE                                               
HETSYN     HEM HEME                                                             
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
FORMUL   4  NBN    C5 H9 N                                                      
FORMUL   5  HOH   *138(H2 O)                                                    
HELIX    1   1 SER A    3  GLU A   18  1                                  16    
HELIX    2   2 ASP A   20  SER A   35  1                                  16    
HELIX    3   3 HIS A   36  LYS A   42  1                                   7    
HELIX    4   4 THR A   51  ALA A   57  1                                   7    
HELIX    5   5 SER A   58  LYS A   77  1                                  20    
HELIX    6   6 LEU A   86  ALA A   94  1                                   9    
HELIX    7   7 PRO A  100  ARG A  118  1                                  19    
HELIX    8   8 GLY A  124  LEU A  149  1                                  26    
LINK         NE2 HIS A  93                FE   HEM A 155     1555   1555  2.20  
LINK        FE   HEM A 155                 C   NBN A 156     1555   1555  2.11  
SITE     1 HEM  1 HEM A 155                                                     
SITE     1 AC1  6 SER A   3  GLU A   4  THR A  51  GLU A  52                    
SITE     2 AC1  6 HOH A 268  HOH A 282                                          
SITE     1 AC2 13 LYS A  42  PHE A  43  ARG A  45  LEU A  89                    
SITE     2 AC2 13 SER A  92  HIS A  93  HIS A  97  ILE A  99                    
SITE     3 AC2 13 TYR A 103  NBN A 156  HOH A 286  HOH A 287                    
SITE     4 AC2 13 HOH A 304                                                     
SITE     1 AC3  5 PHE A  43  HIS A  64  THR A  67  VAL A  68                    
SITE     2 AC3  5 HEM A 155                                                     
CRYST1   91.670   91.670   45.970  90.00  90.00 120.00 P 6           6          
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      0.010909  0.006298  0.000000        0.00000                         
SCALE2      0.000000  0.012596  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021753        0.00000                         
ATOM      1  N   MET A   0      24.277   8.374  -9.854  1.00 38.41           N  
ATOM      2  CA  MET A   0      24.404   9.859  -9.939  1.00 37.90           C  
ATOM      3  C   MET A   0      25.814  10.249 -10.359  1.00 36.65           C  
ATOM      4  O   MET A   0      26.748   9.469 -10.197  1.00 37.13           O  
ATOM      5  CB  MET A   0      24.070  10.495  -8.596  1.00 39.58           C  
ATOM      6  CG  MET A   0      24.880   9.939  -7.442  1.00 41.49           C  
ATOM      7  SD  MET A   0      24.262  10.555  -5.873  1.00 44.70           S  
ATOM      8  CE  MET A   0      24.822  12.266  -5.967  1.00 41.59           C  
ATOM      9  N   VAL A   1      25.964  11.453 -10.903  1.00 34.54           N  
ATOM     10  CA  VAL A   1      27.263  11.924 -11.359  1.00 32.46           C  
ATOM     11  C   VAL A   1      27.392  13.428 -11.115  1.00 30.70           C  
ATOM     12  O   VAL A   1      26.443  14.184 -11.327  1.00 31.42           O  
ATOM     13  CB  VAL A   1      27.455  11.631 -12.878  1.00 32.95           C  
ATOM     14  CG1 VAL A   1      28.756  12.209 -13.382  1.00 32.87           C  
ATOM     15  CG2 VAL A   1      27.432  10.131 -13.140  1.00 33.54           C  
ATOM     16  N   LEU A   2      28.555  13.855 -10.636  1.00 27.76           N  
ATOM     17  CA  LEU A   2      28.797  15.269 -10.390  1.00 25.21           C  
ATOM     18  C   LEU A   2      29.492  15.903 -11.585  1.00 24.21           C  
ATOM     19  O   LEU A   2      30.250  15.240 -12.306  1.00 23.80           O  
ATOM     20  CB  LEU A   2      29.688  15.470  -9.152  1.00 24.30           C  
ATOM     21  CG  LEU A   2      29.084  15.416  -7.751  1.00 22.96           C  
ATOM     22  CD1 LEU A   2      28.730  13.988  -7.390  1.00 22.03           C  
ATOM     23  CD2 LEU A   2      30.085  16.008  -6.776  1.00 21.94           C  
ATOM     24  N   SER A   3      29.236  17.185 -11.800  1.00 23.04           N  
ATOM     25  CA  SER A   3      29.898  17.894 -12.882  1.00 22.62           C  
ATOM     26  C   SER A   3      31.282  18.336 -12.384  1.00 22.06           C  
ATOM     27  O   SER A   3      31.565  18.268 -11.188  1.00 21.06           O  
ATOM     28  CB  SER A   3      29.061  19.097 -13.312  1.00 22.96           C  
ATOM     29  OG  SER A   3      28.916  20.026 -12.260  1.00 24.01           O  
ATOM     30  N   GLU A   4      32.151  18.759 -13.296  1.00 17.46           N  
ATOM     31  CA  GLU A   4      33.489  19.212 -12.922  1.00 24.04           C  
ATOM     32  C   GLU A   4      33.346  20.443 -12.019  1.00 21.74           C  
ATOM     33  O   GLU A   4      34.115  20.620 -11.076  1.00 20.06           O  
ATOM     34  CB  GLU A   4      34.316  19.551 -14.178  1.00 22.74           C  
ATOM     35  CG  GLU A   4      35.720  20.158 -13.921  1.00 18.42           C  
ATOM     36  CD  GLU A   4      36.690  19.210 -13.205  1.00 27.97           C  
ATOM     37  OE1 GLU A   4      36.449  17.987 -13.166  1.00 27.73           O  
ATOM     38  OE2 GLU A   4      37.711  19.692 -12.684  1.00 28.70           O  
ATOM     39  N   GLY A   5      32.351  21.280 -12.308  1.00 19.09           N  
ATOM     40  CA  GLY A   5      32.118  22.472 -11.504  1.00 18.12           C  
ATOM     41  C   GLY A   5      31.837  22.114 -10.053  1.00 18.29           C  
ATOM     42  O   GLY A   5      32.353  22.758  -9.137  1.00 17.54           O  
ATOM     43  N   GLU A   6      31.033  21.069  -9.845  1.00 16.68           N  
ATOM     44  CA  GLU A   6      30.702  20.617  -8.498  1.00 13.59           C  
ATOM     45  C   GLU A   6      31.945  20.007  -7.807  1.00 17.58           C  
ATOM     46  O   GLU A   6      32.199  20.278  -6.638  1.00 14.97           O  
ATOM     47  CB  GLU A   6      29.510  19.648  -8.533  1.00 13.04           C  
ATOM     48  CG  GLU A   6      28.179  20.319  -8.911  1.00 16.58           C  
ATOM     49  CD  GLU A   6      27.056  19.316  -9.262  1.00 18.86           C  
ATOM     50  OE1 GLU A   6      27.338  18.242  -9.832  1.00 23.67           O  
ATOM     51  OE2 GLU A   6      25.881  19.612  -8.979  1.00 29.24           O  
ATOM     52  N   TRP A   7      32.747  19.242  -8.545  1.00 15.06           N  
ATOM     53  CA  TRP A   7      33.970  18.675  -7.985  1.00 15.72           C  
ATOM     54  C   TRP A   7      34.932  19.799  -7.595  1.00 16.03           C  
ATOM     55  O   TRP A   7      35.645  19.687  -6.599  1.00 16.52           O  
ATOM     56  CB  TRP A   7      34.672  17.733  -8.986  1.00 15.72           C  
ATOM     57  CG  TRP A   7      34.046  16.382  -9.056  1.00 15.35           C  
ATOM     58  CD1 TRP A   7      33.473  15.795 -10.149  1.00 15.74           C  
ATOM     59  CD2 TRP A   7      33.874  15.466  -7.966  1.00 15.25           C  
ATOM     60  NE1 TRP A   7      32.940  14.573  -9.804  1.00 15.28           N  
ATOM     61  CE2 TRP A   7      33.168  14.345  -8.469  1.00 15.63           C  
ATOM     62  CE3 TRP A   7      34.237  15.486  -6.608  1.00 14.98           C  
ATOM     63  CZ2 TRP A   7      32.813  13.244  -7.652  1.00 15.14           C  
ATOM     64  CZ3 TRP A   7      33.884  14.394  -5.801  1.00 15.08           C  
ATOM     65  CH2 TRP A   7      33.178  13.290  -6.328  1.00 14.28           C  
ATOM     66  N   GLN A   8      34.973  20.871  -8.388  1.00 15.81           N  
ATOM     67  CA  GLN A   8      35.856  21.987  -8.080  1.00 16.01           C  
ATOM     68  C   GLN A   8      35.445  22.668  -6.769  1.00 15.78           C  
ATOM     69  O   GLN A   8      36.305  23.057  -5.973  1.00 15.65           O  
ATOM     70  CB  GLN A   8      35.893  22.989  -9.235  1.00 17.95           C  
ATOM     71  CG  GLN A   8      36.613  22.459 -10.451  1.00 25.32           C  
ATOM     72  CD  GLN A   8      38.055  22.125 -10.145  1.00 39.60           C  
ATOM     73  OE1 GLN A   8      38.883  23.023  -9.983  1.00 67.02           O  
ATOM     74  NE2 GLN A   8      38.366  20.830 -10.043  1.00 43.80           N  
ATOM     75  N   LEU A   9      34.141  22.788  -6.533  1.00 14.97           N  
ATOM     76  CA  LEU A   9      33.661  23.390  -5.284  1.00 14.87           C  
ATOM     77  C   LEU A   9      34.055  22.525  -4.081  1.00 14.68           C  
ATOM     78  O   LEU A   9      34.515  23.031  -3.061  1.00 14.85           O  
ATOM     79  CB  LEU A   9      32.141  23.586  -5.317  1.00 15.27           C  
ATOM     80  CG  LEU A   9      31.668  24.723  -6.235  1.00 15.96           C  
ATOM     81  CD1 LEU A   9      30.164  24.757  -6.306  1.00 15.80           C  
ATOM     82  CD2 LEU A   9      32.205  26.043  -5.730  1.00 16.40           C  
ATOM     83  N   VAL A  10      33.913  21.215  -4.236  1.00 13.96           N  
ATOM     84  CA  VAL A  10      34.247  20.256  -3.195  1.00 13.50           C  
ATOM     85  C   VAL A  10      35.742  20.293  -2.878  1.00 14.08           C  
ATOM     86  O   VAL A  10      36.144  20.446  -1.721  1.00 14.08           O  
ATOM     87  CB  VAL A  10      33.821  18.826  -3.640  1.00 13.81           C  
ATOM     88  CG1 VAL A  10      34.428  17.746  -2.739  1.00 13.51           C  
ATOM     89  CG2 VAL A  10      32.289  18.724  -3.657  1.00 13.28           C  
ATOM     90  N   LEU A  11      36.563  20.208  -3.915  1.00 14.31           N  
ATOM     91  CA  LEU A  11      38.005  20.200  -3.741  1.00 14.80           C  
ATOM     92  C   LEU A  11      38.590  21.529  -3.282  1.00 15.08           C  
ATOM     93  O   LEU A  11      39.613  21.537  -2.605  1.00 15.16           O  
ATOM     94  CB  LEU A  11      38.690  19.677  -5.007  1.00 15.74           C  
ATOM     95  CG  LEU A  11      38.310  18.212  -5.299  1.00 16.67           C  
ATOM     96  CD1 LEU A  11      38.911  17.765  -6.605  1.00 18.20           C  
ATOM     97  CD2 LEU A  11      38.778  17.300  -4.167  1.00 17.64           C  
ATOM     98  N   HIS A  12      37.915  22.640  -3.577  1.00 15.37           N  
ATOM     99  CA  HIS A  12      38.390  23.965  -3.145  1.00 15.95           C  
ATOM    100  C   HIS A  12      38.229  24.124  -1.625  1.00 15.98           C  
ATOM    101  O   HIS A  12      39.105  24.662  -0.963  1.00 16.51           O  
ATOM    102  CB  HIS A  12      37.650  25.092  -3.887  1.00 19.33           C  
ATOM    103  CG  HIS A  12      38.064  26.470  -3.467  1.00 28.57           C  
ATOM    104  ND1 HIS A  12      39.323  26.998  -3.668  1.00 38.92           N  
ATOM    105  CD2 HIS A  12      37.357  27.443  -2.836  1.00 35.58           C  
ATOM    106  CE1 HIS A  12      39.341  28.247  -3.167  1.00 37.34           C  
ATOM    107  NE2 HIS A  12      38.171  28.566  -2.650  1.00 33.72           N  
ATOM    108  N   VAL A  13      37.107  23.672  -1.070  1.00 15.74           N  
ATOM    109  CA  VAL A  13      36.934  23.758   0.379  1.00 15.64           C  
ATOM    110  C   VAL A  13      37.792  22.681   1.085  1.00 15.33           C  
ATOM    111  O   VAL A  13      38.342  22.921   2.160  1.00 15.39           O  
ATOM    112  CB  VAL A  13      35.424  23.682   0.816  1.00 16.72           C  
ATOM    113  CG1 VAL A  13      34.851  22.287   0.601  1.00 16.66           C  
ATOM    114  CG2 VAL A  13      35.283  24.085   2.288  1.00 17.08           C  
ATOM    115  N   TRP A  14      37.958  21.524   0.448  1.00 14.73           N  
ATOM    116  CA  TRP A  14      38.770  20.457   1.017  1.00 14.75           C  
ATOM    117  C   TRP A  14      40.241  20.879   1.166  1.00 14.64           C  
ATOM    118  O   TRP A  14      40.921  20.456   2.099  1.00 15.14           O  
ATOM    119  CB  TRP A  14      38.673  19.191   0.164  1.00 15.26           C  
ATOM    120  CG  TRP A  14      39.146  17.993   0.901  1.00 16.17           C  
ATOM    121  CD1 TRP A  14      40.356  17.387   0.782  1.00 16.11           C  
ATOM    122  CD2 TRP A  14      38.458  17.320   1.969  1.00 16.43           C  
ATOM    123  NE1 TRP A  14      40.477  16.388   1.722  1.00 16.54           N  
ATOM    124  CE2 TRP A  14      39.328  16.325   2.463  1.00 15.93           C  
ATOM    125  CE3 TRP A  14      37.191  17.471   2.561  1.00 16.69           C  
ATOM    126  CZ2 TRP A  14      38.983  15.480   3.522  1.00 16.79           C  
ATOM    127  CZ3 TRP A  14      36.842  16.622   3.626  1.00 17.61           C  
ATOM    128  CH2 TRP A  14      37.744  15.638   4.093  1.00 16.93           C  
ATOM    129  N   ALA A  15      40.726  21.722   0.254  1.00 14.42           N  
ATOM    130  CA  ALA A  15      42.095  22.214   0.312  1.00 14.00           C  
ATOM    131  C   ALA A  15      42.328  22.999   1.608  1.00 14.30           C  
ATOM    132  O   ALA A  15      43.427  22.982   2.156  1.00 14.23           O  
ATOM    133  CB  ALA A  15      42.389  23.080  -0.896  1.00 14.14           C  
ATOM    134  N   LYS A  16      41.270  23.635   2.124  1.00 15.22           N  
ATOM    135  CA  LYS A  16      41.345  24.400   3.376  1.00 17.82           C  
ATOM    136  C   LYS A  16      41.371  23.426   4.548  1.00 14.95           C  
ATOM    137  O   LYS A  16      42.124  23.616   5.491  1.00 18.06           O  
ATOM    138  CB  LYS A  16      40.146  25.350   3.539  1.00 11.85           C  
ATOM    139  CG  LYS A  16      39.931  26.312   2.396  1.00 15.52           C  
ATOM    140  CD  LYS A  16      41.171  27.093   2.107  1.00 22.34           C  
ATOM    141  CE  LYS A  16      41.010  27.867   0.817  1.00 43.61           C  
ATOM    142  NZ  LYS A  16      42.298  28.453   0.378  1.00 41.54           N  
ATOM    143  N   VAL A  17      40.524  22.398   4.491  1.00 12.40           N  
ATOM    144  CA  VAL A  17      40.473  21.367   5.522  1.00 12.29           C  
ATOM    145  C   VAL A  17      41.872  20.771   5.701  1.00 12.32           C  
ATOM    146  O   VAL A  17      42.329  20.560   6.829  1.00 12.74           O  
ATOM    147  CB  VAL A  17      39.496  20.242   5.116  1.00 12.43           C  
ATOM    148  CG1 VAL A  17      39.596  19.045   6.073  1.00 12.58           C  
ATOM    149  CG2 VAL A  17      38.088  20.787   5.082  1.00 13.47           C  
ATOM    150  N   GLU A  18      42.553  20.513   4.584  1.00 13.88           N  
ATOM    151  CA  GLU A  18      43.904  19.940   4.618  1.00 14.94           C  
ATOM    152  C   GLU A  18      44.991  20.813   5.262  1.00 16.26           C  
ATOM    153  O   GLU A  18      46.070  20.322   5.560  1.00 15.32           O  
ATOM    154  CB  GLU A  18      44.327  19.461   3.235  1.00 12.91           C  
ATOM    155  CG  GLU A  18      43.572  18.228   2.808  1.00 13.99           C  
ATOM    156  CD  GLU A  18      44.011  17.692   1.458  1.00 16.75           C  
ATOM    157  OE1 GLU A  18      44.559  18.458   0.644  1.00 21.92           O  
ATOM    158  OE2 GLU A  18      43.791  16.493   1.217  1.00 23.33           O  
ATOM    159  N   ALA A  19      44.708  22.090   5.501  1.00 14.20           N  
ATOM    160  CA  ALA A  19      45.686  22.946   6.169  1.00 14.94           C  
ATOM    161  C   ALA A  19      45.780  22.500   7.624  1.00 14.81           C  
ATOM    162  O   ALA A  19      46.773  22.759   8.295  1.00 15.01           O  
ATOM    163  CB  ALA A  19      45.259  24.418   6.110  1.00 14.54           C  
ATOM    164  N   ASP A  20      44.731  21.837   8.111  1.00 12.28           N  
ATOM    165  CA  ASP A  20      44.693  21.368   9.492  1.00 12.72           C  
ATOM    166  C   ASP A  20      43.810  20.117   9.606  1.00 18.12           C  
ATOM    167  O   ASP A  20      42.686  20.173  10.131  1.00 13.62           O  
ATOM    168  CB  ASP A  20      44.157  22.490  10.403  1.00 10.25           C  
ATOM    169  CG  ASP A  20      44.073  22.074  11.865  1.00 19.39           C  
ATOM    170  OD1 ASP A  20      44.848  21.187  12.301  1.00 17.74           O  
ATOM    171  OD2 ASP A  20      43.195  22.613  12.564  1.00 26.16           O  
ATOM    172  N   VAL A  21      44.343  18.987   9.164  1.00 14.51           N  
ATOM    173  CA  VAL A  21      43.597  17.741   9.183  1.00 16.06           C  
ATOM    174  C   VAL A  21      43.223  17.273  10.588  1.00 15.92           C  
ATOM    175  O   VAL A  21      42.095  16.857  10.810  1.00 16.38           O  
ATOM    176  CB  VAL A  21      44.360  16.610   8.409  1.00 17.48           C  
ATOM    177  CG1 VAL A  21      43.603  15.292   8.507  1.00 16.78           C  
ATOM    178  CG2 VAL A  21      44.521  17.021   6.937  1.00 17.19           C  
ATOM    179  N   ALA A  22      44.151  17.364  11.537  1.00 15.42           N  
ATOM    180  CA  ALA A  22      43.871  16.937  12.907  1.00 15.58           C  
ATOM    181  C   ALA A  22      42.787  17.773  13.591  1.00 15.11           C  
ATOM    182  O   ALA A  22      41.894  17.227  14.221  1.00 14.57           O  
ATOM    183  CB  ALA A  22      45.154  16.940  13.734  1.00 16.03           C  
ATOM    184  N   GLY A  23      42.865  19.094  13.443  1.00 14.85           N  
ATOM    185  CA  GLY A  23      41.882  19.978  14.035  1.00 13.95           C  
ATOM    186  C   GLY A  23      40.485  19.730  13.490  1.00 13.74           C  
ATOM    187  O   GLY A  23      39.507  19.711  14.255  1.00 13.81           O  
ATOM    188  N   HIS A  24      40.369  19.561  12.175  1.00 13.07           N  
ATOM    189  CA  HIS A  24      39.059  19.308  11.561  1.00 12.67           C  
ATOM    190  C   HIS A  24      38.525  17.941  11.970  1.00 12.65           C  
ATOM    191  O   HIS A  24      37.326  17.804  12.187  1.00 13.43           O  
ATOM    192  CB  HIS A  24      39.138  19.392  10.037  1.00 10.49           C  
ATOM    193  CG  HIS A  24      39.212  20.790   9.513  1.00 13.59           C  
ATOM    194  ND1 HIS A  24      40.371  21.531   9.447  1.00 10.53           N  
ATOM    195  CD2 HIS A  24      38.245  21.571   8.963  1.00 10.81           C  
ATOM    196  CE1 HIS A  24      40.078  22.706   8.860  1.00 11.16           C  
ATOM    197  NE2 HIS A  24      38.798  22.777   8.549  1.00 12.09           N  
ATOM    198  N   GLY A  25      39.410  16.943  12.063  1.00 12.41           N  
ATOM    199  CA  GLY A  25      39.014  15.593  12.468  1.00 13.17           C  
ATOM    200  C   GLY A  25      38.428  15.545  13.875  1.00 13.87           C  
ATOM    201  O   GLY A  25      37.460  14.826  14.124  1.00 13.35           O  
ATOM    202  N   GLN A  26      39.034  16.291  14.804  1.00 14.34           N  
ATOM    203  CA  GLN A  26      38.534  16.366  16.171  1.00 15.16           C  
ATOM    204  C   GLN A  26      37.140  17.000  16.198  1.00 15.26           C  
ATOM    205  O   GLN A  26      36.221  16.467  16.829  1.00 15.39           O  
ATOM    206  CB  GLN A  26      39.448  17.215  17.054  1.00 17.03           C  
ATOM    207  CG  GLN A  26      40.466  16.432  17.822  1.00 28.33           C  
ATOM    208  CD  GLN A  26      41.526  17.332  18.433  1.00 40.00           C  
ATOM    209  OE1 GLN A  26      42.133  18.162  17.746  1.00 36.88           O  
ATOM    210  NE2 GLN A  26      41.709  17.218  19.740  1.00 36.42           N  
ATOM    211  N   ASP A  27      37.003  18.168  15.568  1.00 10.78           N  
ATOM    212  CA  ASP A  27      35.721  18.874  15.540  1.00 12.70           C  
ATOM    213  C   ASP A  27      34.599  18.016  14.999  1.00 15.39           C  
ATOM    214  O   ASP A  27      33.494  18.020  15.527  1.00 12.27           O  
ATOM    215  CB  ASP A  27      35.820  20.133  14.669  1.00 11.23           C  
ATOM    216  CG  ASP A  27      36.637  21.235  15.311  1.00 27.34           C  
ATOM    217  OD1 ASP A  27      37.197  21.014  16.412  1.00 27.80           O  
ATOM    218  OD2 ASP A  27      36.720  22.323  14.702  1.00 23.75           O  
ATOM    219  N   ILE A  28      34.880  17.341  13.890  1.00 12.88           N  
ATOM    220  CA  ILE A  28      33.906  16.477  13.242  1.00 13.76           C  
ATOM    221  C   ILE A  28      33.472  15.291  14.124  1.00 14.47           C  
ATOM    222  O   ILE A  28      32.263  15.032  14.276  1.00 14.63           O  
ATOM    223  CB  ILE A  28      34.446  15.993  11.846  1.00 13.13           C  
ATOM    224  CG1 ILE A  28      34.381  17.154  10.842  1.00 13.35           C  
ATOM    225  CG2 ILE A  28      33.644  14.809  11.323  1.00 12.02           C  
ATOM    226  CD1 ILE A  28      35.210  16.957   9.578  1.00 12.89           C  
ATOM    227  N   LEU A  29      34.440  14.596  14.731  1.00 15.19           N  
ATOM    228  CA  LEU A  29      34.118  13.441  15.571  1.00 15.68           C  
ATOM    229  C   LEU A  29      33.400  13.853  16.847  1.00 16.10           C  
ATOM    230  O   LEU A  29      32.471  13.181  17.283  1.00 16.45           O  
ATOM    231  CB  LEU A  29      35.359  12.614  15.898  1.00 15.76           C  
ATOM    232  CG  LEU A  29      35.978  11.809  14.749  1.00 16.40           C  
ATOM    233  CD1 LEU A  29      37.043  10.854  15.303  1.00 16.35           C  
ATOM    234  CD2 LEU A  29      34.917  11.008  14.016  1.00 17.12           C  
ATOM    235  N   ILE A  30      33.818  14.971  17.432  1.00 16.13           N  
ATOM    236  CA  ILE A  30      33.178  15.463  18.644  1.00 16.60           C  
ATOM    237  C   ILE A  30      31.725  15.839  18.311  1.00 17.11           C  
ATOM    238  O   ILE A  30      30.798  15.495  19.058  1.00 17.25           O  
ATOM    239  CB  ILE A  30      33.974  16.652  19.250  1.00 15.99           C  
ATOM    240  CG1 ILE A  30      35.260  16.118  19.907  1.00 16.25           C  
ATOM    241  CG2 ILE A  30      33.113  17.437  20.245  1.00 16.34           C  
ATOM    242  CD1 ILE A  30      36.262  17.204  20.328  1.00 15.83           C  
ATOM    243  N   ARG A  31      31.529  16.494  17.168  1.00 16.96           N  
ATOM    244  CA  ARG A  31      30.191  16.862  16.720  1.00 17.72           C  
ATOM    245  C   ARG A  31      29.353  15.590  16.560  1.00 18.25           C  
ATOM    246  O   ARG A  31      28.242  15.514  17.080  1.00 18.06           O  
ATOM    247  CB  ARG A  31      30.274  17.644  15.403  1.00 19.03           C  
ATOM    248  CG  ARG A  31      28.959  17.951  14.704  1.00 27.75           C  
ATOM    249  CD  ARG A  31      27.820  18.210  15.662  1.00 35.54           C  
ATOM    250  NE  ARG A  31      27.590  19.622  15.937  1.00 55.89           N  
ATOM    251  CZ  ARG A  31      26.431  20.247  15.732  1.00 59.53           C  
ATOM    252  NH1 ARG A  31      25.407  19.623  15.163  1.00 55.77           N  
ATOM    253  NH2 ARG A  31      26.316  21.528  16.038  1.00 80.31           N  
ATOM    254  N   LEU A  32      29.923  14.573  15.913  1.00 18.72           N  
ATOM    255  CA  LEU A  32      29.229  13.303  15.710  1.00 18.89           C  
ATOM    256  C   LEU A  32      28.820  12.652  17.035  1.00 19.55           C  
ATOM    257  O   LEU A  32      27.656  12.283  17.216  1.00 19.27           O  
ATOM    258  CB  LEU A  32      30.107  12.321  14.912  1.00 18.43           C  
ATOM    259  CG  LEU A  32      29.518  10.900  14.774  1.00 18.35           C  
ATOM    260  CD1 LEU A  32      28.310  10.917  13.853  1.00 16.58           C  
ATOM    261  CD2 LEU A  32      30.569   9.897  14.281  1.00 17.13           C  
ATOM    262  N   PHE A  33      29.785  12.525  17.950  1.00 20.12           N  
ATOM    263  CA  PHE A  33      29.574  11.902  19.263  1.00 20.56           C  
ATOM    264  C   PHE A  33      28.594  12.652  20.164  1.00 21.82           C  
ATOM    265  O   PHE A  33      27.863  12.029  20.941  1.00 23.10           O  
ATOM    266  CB  PHE A  33      30.905  11.724  19.981  1.00 19.32           C  
ATOM    267  CG  PHE A  33      31.858  10.805  19.263  1.00 18.94           C  
ATOM    268  CD1 PHE A  33      31.375   9.740  18.495  1.00 17.83           C  
ATOM    269  CD2 PHE A  33      33.239  10.991  19.365  1.00 17.60           C  
ATOM    270  CE1 PHE A  33      32.254   8.878  17.843  1.00 17.15           C  
ATOM    271  CE2 PHE A  33      34.119  10.133  18.714  1.00 17.04           C  
ATOM    272  CZ  PHE A  33      33.617   9.072  17.951  1.00 17.09           C  
ATOM    273  N   LYS A  34      28.568  13.977  20.061  1.00 23.38           N  
ATOM    274  CA  LYS A  34      27.645  14.757  20.863  1.00 25.09           C  
ATOM    275  C   LYS A  34      26.242  14.704  20.284  1.00 25.17           C  
ATOM    276  O   LYS A  34      25.273  14.626  21.026  1.00 38.31           O  
ATOM    277  CB  LYS A  34      28.086  16.223  20.966  1.00 20.77           C  
ATOM    278  CG  LYS A  34      29.350  16.430  21.783  1.00 42.45           C  
ATOM    279  CD  LYS A  34      29.403  17.826  22.398  1.00 68.05           C  
ATOM    280  CE  LYS A  34      29.075  18.906  21.384  1.00 74.10           C  
ATOM    281  NZ  LYS A  34      29.655  20.230  21.749  1.00 58.94           N  
ATOM    282  N   SER A  35      26.131  14.777  18.961  1.00 26.05           N  
ATOM    283  CA  SER A  35      24.834  14.759  18.309  1.00 26.21           C  
ATOM    284  C   SER A  35      24.189  13.390  18.335  1.00 26.05           C  
ATOM    285  O   SER A  35      22.970  13.289  18.389  1.00 25.95           O  
ATOM    286  CB  SER A  35      24.960  15.191  16.854  1.00 26.90           C  
ATOM    287  OG  SER A  35      25.495  16.497  16.745  1.00 30.21           O  
ATOM    288  N   HIS A  36      25.013  12.347  18.240  1.00 25.46           N  
ATOM    289  CA  HIS A  36      24.534  10.971  18.219  1.00 25.07           C  
ATOM    290  C   HIS A  36      25.441  10.076  19.042  1.00 24.90           C  
ATOM    291  O   HIS A  36      26.194   9.289  18.490  1.00 25.25           O  
ATOM    292  CB  HIS A  36      24.470  10.443  16.774  1.00 23.40           C  
ATOM    293  CG  HIS A  36      23.718  11.332  15.835  1.00 21.61           C  
ATOM    294  ND1 HIS A  36      22.358  11.266  15.627  1.00 22.67           N  
ATOM    295  CD2 HIS A  36      24.160  12.339  15.040  1.00 23.65           C  
ATOM    296  CE1 HIS A  36      22.026  12.208  14.740  1.00 17.49           C  
ATOM    297  NE2 HIS A  36      23.084  12.890  14.349  1.00 22.98           N  
ATOM    298  N   PRO A  37      25.290  10.107  20.377  1.00 25.00           N  
ATOM    299  CA  PRO A  37      26.053   9.339  21.363  1.00 24.52           C  
ATOM    300  C   PRO A  37      26.122   7.836  21.124  1.00 24.44           C  
ATOM    301  O   PRO A  37      27.090   7.183  21.514  1.00 24.78           O  
ATOM    302  CB  PRO A  37      25.321   9.652  22.666  1.00 25.11           C  
ATOM    303  CG  PRO A  37      24.767  11.032  22.422  1.00 24.88           C  
ATOM    304  CD  PRO A  37      24.219  10.875  21.045  1.00 25.04           C  
ATOM    305  N   GLU A  38      25.106   7.280  20.478  1.00 20.50           N  
ATOM    306  CA  GLU A  38      25.099   5.847  20.204  1.00 27.23           C  
ATOM    307  C   GLU A  38      26.292   5.452  19.344  1.00 18.36           C  
ATOM    308  O   GLU A  38      26.814   4.359  19.481  1.00 31.79           O  
ATOM    309  CB  GLU A  38      23.779   5.401  19.539  1.00 20.46           C  
ATOM    310  CG  GLU A  38      23.458   6.000  18.159  1.00 21.91           C  
ATOM    311  CD  GLU A  38      22.672   7.310  18.209  1.00 38.03           C  
ATOM    312  OE1 GLU A  38      22.775   8.087  19.180  1.00 33.84           O  
ATOM    313  OE2 GLU A  38      21.940   7.573  17.243  1.00 40.21           O  
ATOM    314  N   THR A  39      26.760   6.365  18.497  1.00 22.46           N  
ATOM    315  CA  THR A  39      27.898   6.075  17.627  1.00 22.43           C  
ATOM    316  C   THR A  39      29.208   5.857  18.383  1.00 22.93           C  
ATOM    317  O   THR A  39      30.073   5.113  17.922  1.00 22.99           O  
ATOM    318  CB  THR A  39      28.123   7.196  16.564  1.00 22.12           C  
ATOM    319  OG1 THR A  39      28.520   8.416  17.210  1.00 21.24           O  
ATOM    320  CG2 THR A  39      26.868   7.424  15.751  1.00 20.86           C  
ATOM    321  N   LEU A  40      29.349   6.498  19.543  1.00 23.68           N  
ATOM    322  CA  LEU A  40      30.572   6.385  20.345  1.00 24.19           C  
ATOM    323  C   LEU A  40      30.847   4.950  20.795  1.00 24.28           C  
ATOM    324  O   LEU A  40      32.011   4.538  20.938  1.00 23.83           O  
ATOM    325  CB  LEU A  40      30.499   7.330  21.554  1.00 25.26           C  
ATOM    326  CG  LEU A  40      31.720   7.466  22.478  1.00 25.40           C  
ATOM    327  CD1 LEU A  40      32.932   7.943  21.688  1.00 26.19           C  
ATOM    328  CD2 LEU A  40      31.414   8.440  23.599  1.00 25.83           C  
ATOM    329  N   GLU A  41      29.770   4.184  20.962  1.00 26.00           N  
ATOM    330  CA  GLU A  41      29.857   2.786  21.382  1.00 24.55           C  
ATOM    331  C   GLU A  41      30.658   1.906  20.427  1.00 33.76           C  
ATOM    332  O   GLU A  41      31.209   0.890  20.838  1.00 35.66           O  
ATOM    333  CB  GLU A  41      28.461   2.190  21.522  1.00 33.39           C  
ATOM    334  CG  GLU A  41      27.648   2.725  22.678  1.00 55.70           C  
ATOM    335  CD  GLU A  41      26.298   2.048  22.772  1.00 67.02           C  
ATOM    336  OE1 GLU A  41      25.420   2.340  21.930  1.00 71.20           O  
ATOM    337  OE2 GLU A  41      26.125   1.206  23.678  1.00 75.40           O  
ATOM    338  N   LYS A  42      30.696   2.286  19.151  1.00 33.33           N  
ATOM    339  CA  LYS A  42      31.421   1.522  18.136  1.00 25.60           C  
ATOM    340  C   LYS A  42      32.934   1.611  18.273  1.00 19.95           C  
ATOM    341  O   LYS A  42      33.661   0.750  17.787  1.00 35.38           O  
ATOM    342  CB  LYS A  42      31.007   1.987  16.739  1.00 17.82           C  
ATOM    343  CG  LYS A  42      29.599   1.623  16.363  1.00 19.30           C  
ATOM    344  CD  LYS A  42      29.501   0.142  16.074  1.00 28.08           C  
ATOM    345  CE  LYS A  42      28.079  -0.270  15.763  1.00 28.38           C  
ATOM    346  NZ  LYS A  42      28.051  -1.731  15.563  1.00 36.87           N  
ATOM    347  N   PHE A  43      33.403   2.649  18.952  1.00 32.57           N  
ATOM    348  CA  PHE A  43      34.832   2.864  19.120  1.00 32.86           C  
ATOM    349  C   PHE A  43      35.357   2.428  20.479  1.00 32.97           C  
ATOM    350  O   PHE A  43      35.455   3.224  21.407  1.00 33.11           O  
ATOM    351  CB  PHE A  43      35.153   4.340  18.865  1.00 32.29           C  
ATOM    352  CG  PHE A  43      34.782   4.803  17.490  1.00 32.34           C  
ATOM    353  CD1 PHE A  43      35.677   4.666  16.431  1.00 31.95           C  
ATOM    354  CD2 PHE A  43      33.530   5.349  17.243  1.00 31.84           C  
ATOM    355  CE1 PHE A  43      35.323   5.066  15.151  1.00 32.26           C  
ATOM    356  CE2 PHE A  43      33.172   5.751  15.970  1.00 32.01           C  
ATOM    357  CZ  PHE A  43      34.071   5.609  14.920  1.00 32.21           C  
ATOM    358  N   ASP A  44      35.775   1.175  20.555  1.00 34.16           N  
ATOM    359  CA  ASP A  44      36.281   0.599  21.794  1.00 41.63           C  
ATOM    360  C   ASP A  44      37.401   1.387  22.443  1.00 43.44           C  
ATOM    361  O   ASP A  44      37.460   1.496  23.668  1.00 43.85           O  
ATOM    362  CB  ASP A  44      36.725  -0.847  21.562  1.00 49.83           C  
ATOM    363  CG  ASP A  44      35.608  -1.713  20.999  1.00 66.28           C  
ATOM    364  OD1 ASP A  44      34.412  -1.418  21.258  1.00 59.23           O  
ATOM    365  OD2 ASP A  44      35.929  -2.681  20.278  1.00 75.41           O  
ATOM    366  N   ARG A  45      38.255   1.984  21.623  1.00 41.73           N  
ATOM    367  CA  ARG A  45      39.378   2.737  22.144  1.00 41.45           C  
ATOM    368  C   ARG A  45      39.011   4.085  22.736  1.00 40.97           C  
ATOM    369  O   ARG A  45      39.814   4.665  23.468  1.00 41.65           O  
ATOM    370  CB  ARG A  45      40.441   2.938  21.053  1.00 43.13           C  
ATOM    371  CG  ARG A  45      41.785   2.307  21.396  1.00 53.08           C  
ATOM    372  CD  ARG A  45      42.910   2.709  20.435  1.00 64.99           C  
ATOM    373  NE  ARG A  45      42.767   2.098  19.118  1.00 80.05           N  
ATOM    374  CZ  ARG A  45      42.767   2.777  17.974  1.00 97.64           C  
ATOM    375  NH1 ARG A  45      42.885   4.102  17.980  1.00100.00           N  
ATOM    376  NH2 ARG A  45      42.632   2.133  16.821  1.00 91.43           N  
ATOM    377  N   VAL A  46      37.771   4.523  22.533  1.00 39.61           N  
ATOM    378  CA  VAL A  46      37.375   5.854  22.974  1.00 38.33           C  
ATOM    379  C   VAL A  46      35.954   5.971  23.580  1.00 38.11           C  
ATOM    380  O   VAL A  46      35.542   7.041  24.037  1.00 37.45           O  
ATOM    381  CB  VAL A  46      37.577   6.804  21.731  1.00 37.83           C  
ATOM    382  CG1 VAL A  46      36.278   7.176  21.064  1.00 36.87           C  
ATOM    383  CG2 VAL A  46      38.429   7.974  22.075  1.00 37.97           C  
ATOM    384  N   LYS A  47      35.254   4.844  23.672  1.00 29.21           N  
ATOM    385  CA  LYS A  47      33.882   4.813  24.172  1.00 23.48           C  
ATOM    386  C   LYS A  47      33.669   5.225  25.628  1.00 24.52           C  
ATOM    387  O   LYS A  47      32.547   5.503  26.027  1.00 33.62           O  
ATOM    388  CB  LYS A  47      33.280   3.426  23.946  1.00 23.59           C  
ATOM    389  CG  LYS A  47      33.623   2.411  25.019  1.00 40.22           C  
ATOM    390  CD  LYS A  47      32.863   1.109  24.831  1.00 52.55           C  
ATOM    391  CE  LYS A  47      33.774   0.036  24.272  1.00 62.41           C  
ATOM    392  NZ  LYS A  47      33.077  -1.260  24.087  1.00 74.01           N  
ATOM    393  N   HIS A  48      34.741   5.249  26.413  1.00 31.16           N  
ATOM    394  CA  HIS A  48      34.674   5.606  27.836  1.00 31.22           C  
ATOM    395  C   HIS A  48      34.701   7.112  28.107  1.00 30.83           C  
ATOM    396  O   HIS A  48      34.532   7.529  29.249  1.00 31.04           O  
ATOM    397  CB  HIS A  48      35.838   4.955  28.589  1.00 33.26           C  
ATOM    398  CG  HIS A  48      37.177   5.474  28.169  1.00 43.81           C  
ATOM    399  ND1 HIS A  48      37.694   5.329  26.897  1.00 49.90           N  
ATOM    400  CD2 HIS A  48      38.087   6.210  28.857  1.00 46.44           C  
ATOM    401  CE1 HIS A  48      38.876   5.973  26.846  1.00 53.26           C  
ATOM    402  NE2 HIS A  48      39.163   6.526  28.010  1.00 56.20           N  
ATOM    403  N   LEU A  49      35.003   7.911  27.083  1.00 30.17           N  
ATOM    404  CA  LEU A  49      35.045   9.375  27.217  1.00 29.27           C  
ATOM    405  C   LEU A  49      33.637   9.891  27.507  1.00 28.58           C  
ATOM    406  O   LEU A  49      32.695   9.606  26.782  1.00 28.38           O  
ATOM    407  CB  LEU A  49      35.611  10.026  25.952  1.00 29.06           C  
ATOM    408  CG  LEU A  49      36.958   9.519  25.428  1.00 28.57           C  
ATOM    409  CD1 LEU A  49      37.293  10.245  24.158  1.00 28.23           C  
ATOM    410  CD2 LEU A  49      38.053   9.730  26.445  1.00 28.89           C  
ATOM    411  N   LYS A  50      33.515  10.640  28.595  1.00 24.55           N  
ATOM    412  CA  LYS A  50      32.237  11.165  29.068  1.00 29.94           C  
ATOM    413  C   LYS A  50      31.906  12.604  28.683  1.00 23.26           C  
ATOM    414  O   LYS A  50      30.742  12.950  28.517  1.00 34.91           O  
ATOM    415  CB  LYS A  50      32.182  11.034  30.592  1.00 45.14           C  
ATOM    416  CG  LYS A  50      32.451   9.622  31.126  1.00 30.35           C  
ATOM    417  CD  LYS A  50      32.844   9.674  32.606  1.00 57.96           C  
ATOM    418  CE  LYS A  50      32.941   8.289  33.243  1.00 49.95           C  
ATOM    419  NZ  LYS A  50      31.612   7.630  33.359  1.00 51.06           N  
ATOM    420  N   THR A  51      32.924  13.448  28.564  1.00 24.12           N  
ATOM    421  CA  THR A  51      32.694  14.849  28.229  1.00 23.89           C  
ATOM    422  C   THR A  51      33.500  15.330  27.025  1.00 23.81           C  
ATOM    423  O   THR A  51      34.497  14.712  26.638  1.00 23.34           O  
ATOM    424  CB  THR A  51      33.052  15.780  29.435  1.00 24.11           C  
ATOM    425  OG1 THR A  51      34.460  15.699  29.704  1.00 24.05           O  
ATOM    426  CG2 THR A  51      32.269  15.384  30.695  1.00 24.04           C  
ATOM    427  N   GLU A  52      33.098  16.483  26.495  1.00 19.92           N  
ATOM    428  CA  GLU A  52      33.783  17.091  25.373  1.00 23.72           C  
ATOM    429  C   GLU A  52      35.220  17.425  25.737  1.00 23.12           C  
ATOM    430  O   GLU A  52      36.100  17.350  24.887  1.00 25.70           O  
ATOM    431  CB  GLU A  52      33.071  18.360  24.919  1.00 28.42           C  
ATOM    432  CG  GLU A  52      33.779  19.038  23.744  1.00 41.68           C  
ATOM    433  CD  GLU A  52      32.971  20.161  23.115  1.00 38.60           C  
ATOM    434  OE1 GLU A  52      31.764  20.277  23.415  1.00 41.28           O  
ATOM    435  OE2 GLU A  52      33.542  20.922  22.307  1.00 49.31           O  
ATOM    436  N   ALA A  53      35.454  17.798  26.997  1.00 21.99           N  
ATOM    437  CA  ALA A  53      36.800  18.129  27.454  1.00 21.32           C  
ATOM    438  C   ALA A  53      37.678  16.893  27.382  1.00 21.17           C  
ATOM    439  O   ALA A  53      38.845  16.975  27.014  1.00 20.69           O  
ATOM    440  CB  ALA A  53      36.765  18.670  28.881  1.00 22.00           C  
ATOM    441  N   GLU A  54      37.114  15.745  27.747  1.00 18.34           N  
ATOM    442  CA  GLU A  54      37.860  14.489  27.694  1.00 20.60           C  
ATOM    443  C   GLU A  54      38.137  14.149  26.245  1.00 22.25           C  
ATOM    444  O   GLU A  54      39.231  13.717  25.892  1.00 19.44           O  
ATOM    445  CB  GLU A  54      37.079  13.365  28.371  1.00 18.48           C  
ATOM    446  CG  GLU A  54      37.087  13.500  29.882  1.00 27.00           C  
ATOM    447  CD  GLU A  54      36.458  12.334  30.616  1.00 30.63           C  
ATOM    448  OE1 GLU A  54      35.749  11.528  29.990  1.00 34.98           O  
ATOM    449  OE2 GLU A  54      36.673  12.226  31.840  1.00 38.33           O  
ATOM    450  N   MET A  55      37.151  14.420  25.398  1.00 22.52           N  
ATOM    451  CA  MET A  55      37.272  14.165  23.970  1.00 22.24           C  
ATOM    452  C   MET A  55      38.367  15.021  23.334  1.00 22.17           C  
ATOM    453  O   MET A  55      39.210  14.508  22.593  1.00 21.68           O  
ATOM    454  CB  MET A  55      35.937  14.411  23.293  1.00 21.93           C  
ATOM    455  CG  MET A  55      34.971  13.294  23.521  1.00 22.76           C  
ATOM    456  SD  MET A  55      33.389  13.680  22.839  1.00 25.74           S  
ATOM    457  CE  MET A  55      32.348  12.662  23.891  1.00 25.19           C  
ATOM    458  N   LYS A  56      38.397  16.302  23.700  1.00 18.45           N  
ATOM    459  CA  LYS A  56      39.378  17.240  23.171  1.00 22.71           C  
ATOM    460  C   LYS A  56      40.781  16.919  23.590  1.00 23.43           C  
ATOM    461  O   LYS A  56      41.720  17.320  22.920  1.00 29.40           O  
ATOM    462  CB  LYS A  56      39.070  18.667  23.607  1.00 13.80           C  
ATOM    463  CG  LYS A  56      37.920  19.299  22.854  1.00 30.70           C  
ATOM    464  CD  LYS A  56      37.687  20.715  23.319  1.00 42.22           C  
ATOM    465  CE  LYS A  56      36.574  21.345  22.523  1.00 54.44           C  
ATOM    466  NZ  LYS A  56      36.199  22.686  23.043  1.00 94.11           N  
ATOM    467  N   ALA A  57      40.926  16.212  24.706  1.00 24.17           N  
ATOM    468  CA  ALA A  57      42.245  15.870  25.207  1.00 24.10           C  
ATOM    469  C   ALA A  57      42.712  14.501  24.759  1.00 24.17           C  
ATOM    470  O   ALA A  57      43.892  14.178  24.861  1.00 24.80           O  
ATOM    471  CB  ALA A  57      42.263  15.956  26.717  1.00 24.26           C  
ATOM    472  N   SER A  58      41.791  13.705  24.233  1.00 24.05           N  
ATOM    473  CA  SER A  58      42.106  12.360  23.794  1.00 23.68           C  
ATOM    474  C   SER A  58      43.023  12.299  22.565  1.00 24.43           C  
ATOM    475  O   SER A  58      42.718  12.859  21.509  1.00 24.53           O  
ATOM    476  CB  SER A  58      40.813  11.598  23.535  1.00 23.20           C  
ATOM    477  OG  SER A  58      41.107  10.316  23.022  1.00 23.93           O  
ATOM    478  N   GLU A  59      44.156  11.618  22.716  1.00 25.17           N  
ATOM    479  CA  GLU A  59      45.110  11.468  21.630  1.00 24.69           C  
ATOM    480  C   GLU A  59      44.585  10.444  20.637  1.00 26.92           C  
ATOM    481  O   GLU A  59      44.823  10.556  19.445  1.00 27.57           O  
ATOM    482  CB  GLU A  59      46.472  11.027  22.172  1.00 33.92           C  
ATOM    483  CG  GLU A  59      47.664  11.638  21.445  1.00 62.87           C  
ATOM    484  CD  GLU A  59      47.721  13.156  21.577  1.00 74.28           C  
ATOM    485  OE1 GLU A  59      47.188  13.705  22.568  1.00 87.47           O  
ATOM    486  OE2 GLU A  59      48.308  13.806  20.687  1.00 76.06           O  
ATOM    487  N   ASP A  60      43.867   9.442  21.134  1.00 22.66           N  
ATOM    488  CA  ASP A  60      43.300   8.420  20.267  1.00 22.16           C  
ATOM    489  C   ASP A  60      42.200   9.002  19.389  1.00 20.24           C  
ATOM    490  O   ASP A  60      42.070   8.629  18.222  1.00 19.35           O  
ATOM    491  CB  ASP A  60      42.712   7.267  21.079  1.00 26.97           C  
ATOM    492  CG  ASP A  60      43.761   6.267  21.538  1.00 42.59           C  
ATOM    493  OD1 ASP A  60      44.819   6.131  20.876  1.00 46.70           O  
ATOM    494  OD2 ASP A  60      43.504   5.602  22.563  1.00 48.78           O  
ATOM    495  N   LEU A  61      41.395   9.898  19.948  1.00 18.12           N  
ATOM    496  CA  LEU A  61      40.315  10.489  19.167  1.00 18.57           C  
ATOM    497  C   LEU A  61      40.906  11.316  18.024  1.00 18.43           C  
ATOM    498  O   LEU A  61      40.434  11.243  16.889  1.00 18.14           O  
ATOM    499  CB  LEU A  61      39.399  11.328  20.057  1.00 18.74           C  
ATOM    500  CG  LEU A  61      38.104  11.870  19.443  1.00 19.52           C  
ATOM    501  CD1 LEU A  61      37.023  11.951  20.503  1.00 19.62           C  
ATOM    502  CD2 LEU A  61      38.343  13.244  18.821  1.00 19.57           C  
ATOM    503  N   LYS A  62      41.992  12.027  18.313  1.00 14.10           N  
ATOM    504  CA  LYS A  62      42.651  12.861  17.310  1.00 25.17           C  
ATOM    505  C   LYS A  62      43.225  12.008  16.175  1.00 19.47           C  
ATOM    506  O   LYS A  62      43.117  12.381  15.008  1.00 20.51           O  
ATOM    507  CB  LYS A  62      43.738  13.726  17.957  1.00 36.01           C  
ATOM    508  CG  LYS A  62      44.388  14.716  17.002  1.00 30.67           C  
ATOM    509  CD  LYS A  62      45.100  15.820  17.763  1.00 57.97           C  
ATOM    510  CE  LYS A  62      46.325  15.302  18.477  1.00 60.47           C  
ATOM    511  NZ  LYS A  62      46.959  16.349  19.326  1.00 95.13           N  
ATOM    512  N   LYS A  63      43.827  10.868  16.520  1.00 15.72           N  
ATOM    513  CA  LYS A  63      44.365   9.952  15.510  1.00 17.84           C  
ATOM    514  C   LYS A  63      43.220   9.405  14.638  1.00 16.64           C  
ATOM    515  O   LYS A  63      43.347   9.344  13.420  1.00 22.11           O  
ATOM    516  CB  LYS A  63      45.139   8.796  16.161  1.00 18.47           C  
ATOM    517  CG  LYS A  63      46.337   9.278  16.971  1.00 43.82           C  
ATOM    518  CD  LYS A  63      47.565   8.412  16.751  1.00 79.73           C  
ATOM    519  CE  LYS A  63      47.522   7.129  17.559  1.00 64.33           C  
ATOM    520  NZ  LYS A  63      47.697   7.392  19.011  1.00 81.18           N  
ATOM    521  N   HIS A  64      42.102   9.040  15.260  1.00 16.01           N  
ATOM    522  CA  HIS A  64      40.944   8.537  14.530  1.00 16.67           C  
ATOM    523  C   HIS A  64      40.443   9.582  13.535  1.00 17.00           C  
ATOM    524  O   HIS A  64      40.003   9.245  12.441  1.00 16.92           O  
ATOM    525  CB  HIS A  64      39.799   8.244  15.501  1.00 18.21           C  
ATOM    526  CG  HIS A  64      40.000   7.019  16.337  1.00 30.05           C  
ATOM    527  ND1 HIS A  64      39.083   6.654  17.294  1.00 35.15           N  
ATOM    528  CD2 HIS A  64      40.923   6.033  16.204  1.00 34.21           C  
ATOM    529  CE1 HIS A  64      39.458   5.462  17.709  1.00 36.97           C  
ATOM    530  NE2 HIS A  64      40.566   5.045  17.079  1.00 38.23           N  
ATOM    531  N   GLY A  65      40.433  10.842  13.969  1.00 16.46           N  
ATOM    532  CA  GLY A  65      39.978  11.919  13.114  1.00 15.97           C  
ATOM    533  C   GLY A  65      40.872  12.059  11.892  1.00 15.92           C  
ATOM    534  O   GLY A  65      40.372  12.239  10.788  1.00 15.66           O  
ATOM    535  N   VAL A  66      42.187  11.997  12.087  1.00 15.57           N  
ATOM    536  CA  VAL A  66      43.121  12.112  10.973  1.00 15.88           C  
ATOM    537  C   VAL A  66      42.898  10.960   9.979  1.00 16.30           C  
ATOM    538  O   VAL A  66      42.860  11.178   8.771  1.00 16.82           O  
ATOM    539  CB  VAL A  66      44.599  12.114  11.473  1.00 16.69           C  
ATOM    540  CG1 VAL A  66      45.577  11.864  10.302  1.00 15.99           C  
ATOM    541  CG2 VAL A  66      44.929  13.452  12.140  1.00 15.60           C  
ATOM    542  N   THR A  67      42.703   9.748  10.497  1.00 16.38           N  
ATOM    543  CA  THR A  67      42.479   8.562   9.666  1.00 16.57           C  
ATOM    544  C   THR A  67      41.226   8.663   8.791  1.00 16.36           C  
ATOM    545  O   THR A  67      41.277   8.380   7.593  1.00 16.00           O  
ATOM    546  CB  THR A  67      42.405   7.293  10.545  1.00 16.87           C  
ATOM    547  OG1 THR A  67      43.641   7.151  11.255  1.00 18.58           O  
ATOM    548  CG2 THR A  67      42.163   6.048   9.699  1.00 16.58           C  
ATOM    549  N   VAL A  68      40.107   9.072   9.383  1.00 16.09           N  
ATOM    550  CA  VAL A  68      38.866   9.207   8.628  1.00 16.32           C  
ATOM    551  C   VAL A  68      38.986  10.263   7.531  1.00 15.35           C  
ATOM    552  O   VAL A  68      38.536  10.046   6.420  1.00 14.58           O  
ATOM    553  CB  VAL A  68      37.665   9.643   9.519  1.00 17.46           C  
ATOM    554  CG1 VAL A  68      36.378   9.662   8.695  1.00 18.23           C  
ATOM    555  CG2 VAL A  68      37.495   8.717  10.660  1.00 19.48           C  
ATOM    556  N   LEU A  69      39.529  11.431   7.874  1.00 14.71           N  
ATOM    557  CA  LEU A  69      39.654  12.522   6.907  1.00 14.96           C  
ATOM    558  C   LEU A  69      40.646  12.233   5.800  1.00 14.27           C  
ATOM    559  O   LEU A  69      40.445  12.656   4.669  1.00 14.38           O  
ATOM    560  CB  LEU A  69      39.998  13.850   7.581  1.00 14.82           C  
ATOM    561  CG  LEU A  69      38.924  14.450   8.497  1.00 17.52           C  
ATOM    562  CD1 LEU A  69      39.251  15.935   8.752  1.00 16.43           C  
ATOM    563  CD2 LEU A  69      37.543  14.324   7.863  1.00 18.33           C  
ATOM    564  N   THR A  70      41.720  11.529   6.128  1.00 13.87           N  
ATOM    565  CA  THR A  70      42.713  11.167   5.120  1.00 14.57           C  
ATOM    566  C   THR A  70      42.090  10.168   4.107  1.00 14.49           C  
ATOM    567  O   THR A  70      42.221  10.350   2.900  1.00 14.32           O  
ATOM    568  CB  THR A  70      43.987  10.568   5.784  1.00 15.27           C  
ATOM    569  OG1 THR A  70      44.553  11.546   6.660  1.00 15.83           O  
ATOM    570  CG2 THR A  70      45.032  10.185   4.733  1.00 15.63           C  
ATOM    571  N   ALA A  71      41.373   9.154   4.598  1.00 13.91           N  
ATOM    572  CA  ALA A  71      40.723   8.185   3.707  1.00 13.99           C  
ATOM    573  C   ALA A  71      39.624   8.870   2.885  1.00 13.64           C  
ATOM    574  O   ALA A  71      39.512   8.641   1.686  1.00 13.91           O  
ATOM    575  CB  ALA A  71      40.120   7.012   4.509  1.00 12.95           C  
ATOM    576  N   LEU A  72      38.832   9.734   3.517  1.00 13.67           N  
ATOM    577  CA  LEU A  72      37.762  10.433   2.812  1.00 13.56           C  
ATOM    578  C   LEU A  72      38.342  11.348   1.756  1.00 13.74           C  
ATOM    579  O   LEU A  72      37.851  11.380   0.633  1.00 13.66           O  
ATOM    580  CB  LEU A  72      36.866  11.226   3.772  1.00 13.74           C  
ATOM    581  CG  LEU A  72      35.719  12.004   3.093  1.00 14.92           C  
ATOM    582  CD1 LEU A  72      34.791  11.045   2.310  1.00 15.38           C  
ATOM    583  CD2 LEU A  72      34.929  12.829   4.128  1.00 14.89           C  
ATOM    584  N   GLY A  73      39.400  12.070   2.109  1.00 13.67           N  
ATOM    585  CA  GLY A  73      40.041  12.954   1.151  1.00 14.46           C  
ATOM    586  C   GLY A  73      40.567  12.204  -0.077  1.00 14.58           C  
ATOM    587  O   GLY A  73      40.436  12.672  -1.205  1.00 14.49           O  
ATOM    588  N   ALA A  74      41.148  11.030   0.141  1.00 14.74           N  
ATOM    589  CA  ALA A  74      41.682  10.233  -0.967  1.00 15.76           C  
ATOM    590  C   ALA A  74      40.538   9.840  -1.920  1.00 15.76           C  
ATOM    591  O   ALA A  74      40.685   9.855  -3.145  1.00 16.76           O  
ATOM    592  CB  ALA A  74      42.388   9.006  -0.424  1.00 14.49           C  
ATOM    593  N   ILE A  75      39.377   9.565  -1.346  1.00 15.77           N  
ATOM    594  CA  ILE A  75      38.201   9.198  -2.121  1.00 15.47           C  
ATOM    595  C   ILE A  75      37.675  10.400  -2.919  1.00 15.48           C  
ATOM    596  O   ILE A  75      37.423  10.285  -4.112  1.00 15.82           O  
ATOM    597  CB  ILE A  75      37.102   8.619  -1.183  1.00 15.70           C  
ATOM    598  CG1 ILE A  75      37.531   7.225  -0.698  1.00 16.61           C  
ATOM    599  CG2 ILE A  75      35.762   8.545  -1.889  1.00 15.10           C  
ATOM    600  CD1 ILE A  75      36.747   6.718   0.506  1.00 18.63           C  
ATOM    601  N   LEU A  76      37.545  11.556  -2.277  1.00 15.31           N  
ATOM    602  CA  LEU A  76      37.043  12.747  -2.960  1.00 15.33           C  
ATOM    603  C   LEU A  76      37.938  13.174  -4.129  1.00 15.59           C  
ATOM    604  O   LEU A  76      37.455  13.603  -5.184  1.00 15.95           O  
ATOM    605  CB  LEU A  76      36.881  13.902  -1.967  1.00 15.64           C  
ATOM    606  CG  LEU A  76      35.798  13.730  -0.892  1.00 15.76           C  
ATOM    607  CD1 LEU A  76      35.865  14.909   0.091  1.00 16.66           C  
ATOM    608  CD2 LEU A  76      34.400  13.596  -1.515  1.00 15.59           C  
ATOM    609  N   LYS A  77      39.246  13.049  -3.939  1.00 10.96           N  
ATOM    610  CA  LYS A  77      40.200  13.416  -4.971  1.00 13.75           C  
ATOM    611  C   LYS A  77      40.129  12.553  -6.234  1.00 18.30           C  
ATOM    612  O   LYS A  77      40.689  12.927  -7.257  1.00 18.04           O  
ATOM    613  CB  LYS A  77      41.607  13.447  -4.396  1.00 14.38           C  
ATOM    614  CG  LYS A  77      41.799  14.594  -3.398  1.00 17.01           C  
ATOM    615  CD  LYS A  77      43.112  14.448  -2.663  1.00 16.79           C  
ATOM    616  CE  LYS A  77      43.349  15.610  -1.763  1.00 20.59           C  
ATOM    617  NZ  LYS A  77      44.698  15.538  -1.169  1.00 20.09           N  
ATOM    618  N   LYS A  78      39.450  11.406  -6.151  1.00 15.24           N  
ATOM    619  CA  LYS A  78      39.256  10.513  -7.302  1.00 18.28           C  
ATOM    620  C   LYS A  78      38.107  11.011  -8.180  1.00 18.94           C  
ATOM    621  O   LYS A  78      37.901  10.506  -9.282  1.00 19.00           O  
ATOM    622  CB  LYS A  78      38.948   9.074  -6.855  1.00 12.31           C  
ATOM    623  CG  LYS A  78      40.058   8.402  -6.058  1.00 25.64           C  
ATOM    624  CD  LYS A  78      41.390   8.455  -6.784  1.00 27.27           C  
ATOM    625  CE  LYS A  78      41.373   7.630  -8.053  1.00 32.49           C  
ATOM    626  NZ  LYS A  78      41.223   6.175  -7.763  1.00 55.16           N  
ATOM    627  N   LYS A  79      37.322  11.952  -7.656  1.00 15.11           N  
ATOM    628  CA  LYS A  79      36.200  12.535  -8.398  1.00 14.03           C  
ATOM    629  C   LYS A  79      35.218  11.516  -8.985  1.00 17.50           C  
ATOM    630  O   LYS A  79      34.814  11.616 -10.145  1.00 20.85           O  
ATOM    631  CB  LYS A  79      36.732  13.474  -9.488  1.00 12.58           C  
ATOM    632  CG  LYS A  79      37.537  14.629  -8.915  1.00 15.77           C  
ATOM    633  CD  LYS A  79      38.464  15.266  -9.921  1.00 26.30           C  
ATOM    634  CE  LYS A  79      37.734  15.964 -11.026  1.00 37.31           C  
ATOM    635  NZ  LYS A  79      38.682  16.840 -11.792  1.00 31.02           N  
ATOM    636  N   GLY A  80      34.828  10.543  -8.165  1.00 17.74           N  
ATOM    637  CA  GLY A  80      33.877   9.538  -8.600  1.00 17.93           C  
ATOM    638  C   GLY A  80      34.472   8.216  -9.068  1.00 18.43           C  
ATOM    639  O   GLY A  80      33.737   7.232  -9.162  1.00 19.23           O  
ATOM    640  N   HIS A  81      35.772   8.178  -9.369  1.00 17.70           N  
ATOM    641  CA  HIS A  81      36.424   6.948  -9.830  1.00 17.96           C  
ATOM    642  C   HIS A  81      37.072   6.331  -8.609  1.00 18.07           C  
ATOM    643  O   HIS A  81      38.284   6.169  -8.555  1.00 18.07           O  
ATOM    644  CB  HIS A  81      37.488   7.302 -10.869  1.00 17.33           C  
ATOM    645  CG  HIS A  81      36.923   7.926 -12.108  1.00 21.80           C  
ATOM    646  ND1 HIS A  81      36.884   9.285 -12.346  1.00 29.19           N  
ATOM    647  CD2 HIS A  81      36.331   7.349 -13.183  1.00 20.31           C  
ATOM    648  CE1 HIS A  81      36.285   9.484 -13.529  1.00 23.50           C  
ATOM    649  NE2 HIS A  81      35.932   8.338 -14.077  1.00 31.00           N  
ATOM    650  N   HIS A  82      36.249   5.908  -7.659  1.00 18.15           N  
ATOM    651  CA  HIS A  82      36.763   5.425  -6.381  1.00 18.12           C  
ATOM    652  C   HIS A  82      36.469   3.977  -6.004  1.00 18.26           C  
ATOM    653  O   HIS A  82      36.597   3.597  -4.836  1.00 17.89           O  
ATOM    654  CB  HIS A  82      36.205   6.348  -5.294  1.00 16.77           C  
ATOM    655  CG  HIS A  82      34.711   6.441  -5.314  1.00 15.19           C  
ATOM    656  ND1 HIS A  82      34.007   7.614  -5.167  1.00 16.60           N  
ATOM    657  CD2 HIS A  82      33.779   5.477  -5.529  1.00 16.77           C  
ATOM    658  CE1 HIS A  82      32.699   7.331  -5.300  1.00 20.03           C  
ATOM    659  NE2 HIS A  82      32.515   6.043  -5.521  1.00 21.22           N  
ATOM    660  N   GLU A  83      36.022   3.194  -6.972  1.00 19.59           N  
ATOM    661  CA  GLU A  83      35.699   1.797  -6.737  1.00 24.12           C  
ATOM    662  C   GLU A  83      36.800   1.024  -5.987  1.00 31.10           C  
ATOM    663  O   GLU A  83      36.516   0.307  -5.030  1.00 26.88           O  
ATOM    664  CB  GLU A  83      35.340   1.110  -8.066  1.00 36.52           C  
ATOM    665  CG  GLU A  83      36.267   1.451  -9.260  1.00 68.75           C  
ATOM    666  CD  GLU A  83      36.009   2.830  -9.890  1.00 69.80           C  
ATOM    667  OE1 GLU A  83      34.877   3.359  -9.777  1.00 67.91           O  
ATOM    668  OE2 GLU A  83      36.949   3.385 -10.503  1.00 42.41           O  
ATOM    669  N   ALA A  84      38.055   1.213  -6.380  1.00 25.65           N  
ATOM    670  CA  ALA A  84      39.162   0.519  -5.732  1.00 25.65           C  
ATOM    671  C   ALA A  84      39.333   0.911  -4.272  1.00 25.52           C  
ATOM    672  O   ALA A  84      39.651   0.067  -3.441  1.00 24.98           O  
ATOM    673  CB  ALA A  84      40.457   0.761  -6.482  1.00 25.75           C  
ATOM    674  N   GLU A  85      39.158   2.197  -3.977  1.00 23.55           N  
ATOM    675  CA  GLU A  85      39.296   2.714  -2.615  1.00 24.29           C  
ATOM    676  C   GLU A  85      38.138   2.293  -1.712  1.00 20.43           C  
ATOM    677  O   GLU A  85      38.310   2.139  -0.505  1.00 22.47           O  
ATOM    678  CB  GLU A  85      39.400   4.247  -2.620  1.00 27.01           C  
ATOM    679  CG  GLU A  85      40.721   4.830  -3.148  1.00 24.94           C  
ATOM    680  CD  GLU A  85      40.884   4.748  -4.668  1.00 36.11           C  
ATOM    681  OE1 GLU A  85      39.887   4.578  -5.409  1.00 37.64           O  
ATOM    682  OE2 GLU A  85      42.034   4.872  -5.131  1.00 54.23           O  
ATOM    683  N   LEU A  86      36.973   2.083  -2.310  1.00 21.53           N  
ATOM    684  CA  LEU A  86      35.787   1.702  -1.567  1.00 22.37           C  
ATOM    685  C   LEU A  86      35.717   0.249  -1.105  1.00 22.19           C  
ATOM    686  O   LEU A  86      35.101  -0.046  -0.087  1.00 22.24           O  
ATOM    687  CB  LEU A  86      34.534   2.016  -2.390  1.00 23.56           C  
ATOM    688  CG  LEU A  86      33.610   3.127  -1.892  1.00 25.46           C  
ATOM    689  CD1 LEU A  86      34.361   4.444  -1.730  1.00 26.00           C  
ATOM    690  CD2 LEU A  86      32.480   3.286  -2.891  1.00 26.41           C  
ATOM    691  N   LYS A  87      36.321  -0.663  -1.854  1.00 21.96           N  
ATOM    692  CA  LYS A  87      36.268  -2.081  -1.510  1.00 30.39           C  
ATOM    693  C   LYS A  87      36.767  -2.472  -0.118  1.00 23.62           C  
ATOM    694  O   LYS A  87      36.003  -3.037   0.668  1.00 20.01           O  
ATOM    695  CB  LYS A  87      36.927  -2.916  -2.610  1.00 31.09           C  
ATOM    696  CG  LYS A  87      36.128  -2.843  -3.882  1.00 42.74           C  
ATOM    697  CD  LYS A  87      36.898  -3.289  -5.102  1.00 56.03           C  
ATOM    698  CE  LYS A  87      36.889  -4.783  -5.250  1.00 45.89           C  
ATOM    699  NZ  LYS A  87      37.070  -5.172  -6.680  1.00 56.90           N  
ATOM    700  N   PRO A  88      38.035  -2.155   0.219  1.00 19.60           N  
ATOM    701  CA  PRO A  88      38.532  -2.521   1.549  1.00 19.38           C  
ATOM    702  C   PRO A  88      37.775  -1.793   2.658  1.00 19.80           C  
ATOM    703  O   PRO A  88      37.606  -2.324   3.758  1.00 19.67           O  
ATOM    704  CB  PRO A  88      39.992  -2.080   1.495  1.00 19.32           C  
ATOM    705  CG  PRO A  88      39.967  -0.918   0.532  1.00 18.97           C  
ATOM    706  CD  PRO A  88      39.085  -1.462  -0.553  1.00 19.16           C  
ATOM    707  N   LEU A  89      37.318  -0.580   2.345  1.00 19.25           N  
ATOM    708  CA  LEU A  89      36.583   0.254   3.280  1.00 19.30           C  
ATOM    709  C   LEU A  89      35.218  -0.349   3.610  1.00 18.74           C  
ATOM    710  O   LEU A  89      34.814  -0.405   4.769  1.00 17.93           O  
ATOM    711  CB  LEU A  89      36.372   1.625   2.653  1.00 21.41           C  
ATOM    712  CG  LEU A  89      36.099   2.774   3.608  1.00 23.97           C  
ATOM    713  CD1 LEU A  89      37.351   2.949   4.488  1.00 25.15           C  
ATOM    714  CD2 LEU A  89      35.817   4.050   2.803  1.00 25.28           C  
ATOM    715  N   ALA A  90      34.508  -0.786   2.577  1.00 17.83           N  
ATOM    716  CA  ALA A  90      33.192  -1.367   2.745  1.00 17.79           C  
ATOM    717  C   ALA A  90      33.278  -2.687   3.518  1.00 17.79           C  
ATOM    718  O   ALA A  90      32.428  -2.990   4.355  1.00 17.57           O  
ATOM    719  CB  ALA A  90      32.557  -1.585   1.375  1.00 18.05           C  
ATOM    720  N   GLN A  91      34.328  -3.459   3.250  1.00 17.80           N  
ATOM    721  CA  GLN A  91      34.500  -4.730   3.927  1.00 17.64           C  
ATOM    722  C   GLN A  91      34.746  -4.568   5.411  1.00 17.96           C  
ATOM    723  O   GLN A  91      34.133  -5.271   6.221  1.00 18.32           O  
ATOM    724  CB  GLN A  91      35.631  -5.558   3.314  1.00 17.05           C  
ATOM    725  CG  GLN A  91      35.748  -6.914   3.996  1.00 17.69           C  
ATOM    726  CD  GLN A  91      36.726  -7.845   3.320  1.00 20.82           C  
ATOM    727  OE1 GLN A  91      37.821  -7.446   2.950  1.00 21.27           O  
ATOM    728  NE2 GLN A  91      36.334  -9.106   3.171  1.00 14.83           N  
ATOM    729  N   SER A  92      35.650  -3.671   5.792  1.00 17.63           N  
ATOM    730  CA  SER A  92      35.897  -3.509   7.213  1.00 17.93           C  
ATOM    731  C   SER A  92      34.698  -2.906   7.964  1.00 18.26           C  
ATOM    732  O   SER A  92      34.383  -3.345   9.072  1.00 18.48           O  
ATOM    733  CB  SER A  92      37.194  -2.742   7.481  1.00 17.83           C  
ATOM    734  OG  SER A  92      37.106  -1.411   7.053  1.00 19.43           O  
ATOM    735  N   HIS A  93      33.977  -1.965   7.357  1.00 17.80           N  
ATOM    736  CA  HIS A  93      32.830  -1.391   8.053  1.00 18.32           C  
ATOM    737  C   HIS A  93      31.605  -2.282   8.092  1.00 19.08           C  
ATOM    738  O   HIS A  93      30.800  -2.170   9.008  1.00 19.46           O  
ATOM    739  CB  HIS A  93      32.471  -0.025   7.495  1.00 18.59           C  
ATOM    740  CG  HIS A  93      33.484   1.016   7.821  1.00 17.57           C  
ATOM    741  ND1 HIS A  93      34.771   0.972   7.333  1.00 24.61           N  
ATOM    742  CD2 HIS A  93      33.431   2.086   8.645  1.00 20.34           C  
ATOM    743  CE1 HIS A  93      35.468   1.971   7.840  1.00 24.73           C  
ATOM    744  NE2 HIS A  93      34.677   2.662   8.641  1.00 23.04           N  
ATOM    745  N   ALA A  94      31.466  -3.159   7.103  1.00 19.39           N  
ATOM    746  CA  ALA A  94      30.336  -4.073   7.035  1.00 20.34           C  
ATOM    747  C   ALA A  94      30.571  -5.311   7.893  1.00 21.10           C  
ATOM    748  O   ALA A  94      29.773  -5.619   8.771  1.00 21.89           O  
ATOM    749  CB  ALA A  94      30.087  -4.497   5.597  1.00 20.13           C  
ATOM    750  N   THR A  95      31.723  -5.944   7.702  1.00 21.61           N  
ATOM    751  CA  THR A  95      32.072  -7.190   8.386  1.00 22.02           C  
ATOM    752  C   THR A  95      32.761  -7.073   9.742  1.00 22.53           C  
ATOM    753  O   THR A  95      32.418  -7.798  10.669  1.00 23.24           O  
ATOM    754  CB  THR A  95      32.954  -8.061   7.466  1.00 22.32           C  
ATOM    755  OG1 THR A  95      32.448  -7.974   6.131  1.00 21.73           O  
ATOM    756  CG2 THR A  95      32.952  -9.541   7.916  1.00 21.45           C  
ATOM    757  N   LYS A  96      33.761  -6.211   9.859  1.00 21.64           N  
ATOM    758  CA  LYS A  96      34.454  -6.079  11.130  1.00 26.88           C  
ATOM    759  C   LYS A  96      33.743  -5.153  12.129  1.00 31.86           C  
ATOM    760  O   LYS A  96      33.320  -5.591  13.197  1.00 36.78           O  
ATOM    761  CB  LYS A  96      35.888  -5.612  10.898  1.00 28.79           C  
ATOM    762  CG  LYS A  96      36.850  -6.013  12.015  1.00 35.57           C  
ATOM    763  CD  LYS A  96      38.165  -5.271  11.876  1.00 55.25           C  
ATOM    764  CE  LYS A  96      39.330  -6.051  12.456  1.00 80.34           C  
ATOM    765  NZ  LYS A  96      39.794  -7.114  11.517  1.00 90.60           N  
ATOM    766  N   HIS A  97      33.578  -3.888  11.755  1.00 32.04           N  
ATOM    767  CA  HIS A  97      32.960  -2.882  12.619  1.00 32.23           C  
ATOM    768  C   HIS A  97      31.424  -2.860  12.656  1.00 32.70           C  
ATOM    769  O   HIS A  97      30.851  -2.412  13.653  1.00 33.29           O  
ATOM    770  CB  HIS A  97      33.467  -1.491  12.230  1.00 31.70           C  
ATOM    771  CG  HIS A  97      34.923  -1.448  11.869  1.00 33.74           C  
ATOM    772  ND1 HIS A  97      35.924  -2.049  12.601  1.00 32.24           N  
ATOM    773  CD2 HIS A  97      35.548  -0.834  10.830  1.00 33.36           C  
ATOM    774  CE1 HIS A  97      37.104  -1.781  12.004  1.00 28.00           C  
ATOM    775  NE2 HIS A  97      36.932  -1.044  10.923  1.00 33.21           N  
ATOM    776  N   LYS A  98      30.768  -3.316  11.581  1.00 30.50           N  
ATOM    777  CA  LYS A  98      29.296  -3.331  11.474  1.00 23.13           C  
ATOM    778  C   LYS A  98      28.686  -1.951  11.683  1.00 32.58           C  
ATOM    779  O   LYS A  98      27.986  -1.708  12.659  1.00 26.86           O  
ATOM    780  CB  LYS A  98      28.678  -4.327  12.447  1.00 27.87           C  
ATOM    781  CG  LYS A  98      28.118  -5.559  11.760  1.00 67.51           C  
ATOM    782  CD  LYS A  98      28.648  -6.835  12.384  1.00 60.67           C  
ATOM    783  CE  LYS A  98      30.163  -6.879  12.311  1.00 73.97           C  
ATOM    784  NZ  LYS A  98      30.711  -8.157  12.837  1.00 83.45           N  
ATOM    785  N   ILE A  99      28.905  -1.074  10.712  1.00 21.99           N  
ATOM    786  CA  ILE A  99      28.442   0.291  10.773  1.00 21.17           C  
ATOM    787  C   ILE A  99      27.270   0.460   9.842  1.00 21.88           C  
ATOM    788  O   ILE A  99      27.426   0.358   8.624  1.00 22.43           O  
ATOM    789  CB  ILE A  99      29.561   1.257  10.300  1.00 20.50           C  
ATOM    790  CG1 ILE A  99      30.873   0.961  11.034  1.00 20.26           C  
ATOM    791  CG2 ILE A  99      29.107   2.712  10.435  1.00 19.71           C  
ATOM    792  CD1 ILE A  99      30.785   0.967  12.536  1.00 20.31           C  
ATOM    793  N   PRO A 100      26.078   0.743  10.391  1.00 22.07           N  
ATOM    794  CA  PRO A 100      24.920   0.922   9.510  1.00 22.57           C  
ATOM    795  C   PRO A 100      25.006   2.221   8.682  1.00 23.19           C  
ATOM    796  O   PRO A 100      25.618   3.208   9.103  1.00 22.81           O  
ATOM    797  CB  PRO A 100      23.738   0.925  10.494  1.00 22.51           C  
ATOM    798  CG  PRO A 100      24.332   1.438  11.753  1.00 22.22           C  
ATOM    799  CD  PRO A 100      25.681   0.764  11.810  1.00 21.66           C  
ATOM    800  N   ILE A 101      24.423   2.196   7.488  1.00 23.79           N  
ATOM    801  CA  ILE A 101      24.424   3.358   6.599  1.00 24.96           C  
ATOM    802  C   ILE A 101      24.008   4.622   7.337  1.00 25.16           C  
ATOM    803  O   ILE A 101      24.564   5.687   7.102  1.00 25.83           O  
ATOM    804  CB  ILE A 101      23.487   3.124   5.362  1.00 25.80           C  
ATOM    805  CG1 ILE A 101      24.053   2.005   4.471  1.00 26.54           C  
ATOM    806  CG2 ILE A 101      23.274   4.405   4.571  1.00 26.60           C  
ATOM    807  CD1 ILE A 101      25.472   2.260   3.962  1.00 27.17           C  
ATOM    808  N   LYS A 102      23.025   4.490   8.222  1.00 21.86           N  
ATOM    809  CA  LYS A 102      22.502   5.598   9.034  1.00 20.48           C  
ATOM    810  C   LYS A 102      23.627   6.382   9.736  1.00 17.82           C  
ATOM    811  O   LYS A 102      23.554   7.603   9.864  1.00 18.65           O  
ATOM    812  CB  LYS A 102      21.533   5.024  10.082  1.00 26.50           C  
ATOM    813  CG  LYS A 102      20.949   6.017  11.042  1.00 49.26           C  
ATOM    814  CD  LYS A 102      19.785   6.806  10.436  1.00 72.73           C  
ATOM    815  CE  LYS A 102      18.800   7.307  11.515  1.00 95.55           C  
ATOM    816  NZ  LYS A 102      17.820   8.291  11.055  1.00 82.64           N  
ATOM    817  N   TYR A 103      24.650   5.676  10.212  1.00 16.72           N  
ATOM    818  CA  TYR A 103      25.770   6.334  10.882  1.00 16.88           C  
ATOM    819  C   TYR A 103      26.633   7.116   9.892  1.00 16.39           C  
ATOM    820  O   TYR A 103      27.285   8.086  10.272  1.00 16.20           O  
ATOM    821  CB  TYR A 103      26.632   5.325  11.640  1.00 16.57           C  
ATOM    822  CG  TYR A 103      26.030   4.762  12.921  1.00 17.87           C  
ATOM    823  CD1 TYR A 103      24.699   4.981  13.261  1.00 18.98           C  
ATOM    824  CD2 TYR A 103      26.801   3.979  13.772  1.00 18.35           C  
ATOM    825  CE1 TYR A 103      24.154   4.420  14.429  1.00 20.22           C  
ATOM    826  CE2 TYR A 103      26.278   3.418  14.922  1.00 19.76           C  
ATOM    827  CZ  TYR A 103      24.964   3.636  15.245  1.00 20.94           C  
ATOM    828  OH  TYR A 103      24.462   3.049  16.379  1.00 22.91           O  
ATOM    829  N   LEU A 104      26.675   6.663   8.637  1.00 16.33           N  
ATOM    830  CA  LEU A 104      27.444   7.353   7.598  1.00 15.99           C  
ATOM    831  C   LEU A 104      26.701   8.648   7.254  1.00 15.96           C  
ATOM    832  O   LEU A 104      27.323   9.662   6.922  1.00 15.10           O  
ATOM    833  CB  LEU A 104      27.647   6.465   6.369  1.00 16.49           C  
ATOM    834  CG  LEU A 104      28.432   5.162   6.632  1.00 17.26           C  
ATOM    835  CD1 LEU A 104      28.544   4.350   5.344  1.00 18.13           C  
ATOM    836  CD2 LEU A 104      29.811   5.451   7.185  1.00 16.64           C  
ATOM    837  N   GLU A 105      25.373   8.623   7.359  1.00 11.84           N  
ATOM    838  CA  GLU A 105      24.583   9.832   7.142  1.00 16.11           C  
ATOM    839  C   GLU A 105      24.880  10.814   8.294  1.00 15.21           C  
ATOM    840  O   GLU A 105      25.044  12.013   8.066  1.00 15.53           O  
ATOM    841  CB  GLU A 105      23.096   9.507   7.144  1.00 15.95           C  
ATOM    842  CG  GLU A 105      22.609   8.830   5.879  1.00 30.07           C  
ATOM    843  CD  GLU A 105      21.179   8.312   5.980  1.00 39.99           C  
ATOM    844  OE1 GLU A 105      20.511   8.546   6.946  1.00 37.58           O  
ATOM    845  OE2 GLU A 105      20.751   7.619   5.044  1.00 41.07           O  
ATOM    846  N   PHE A 106      24.962  10.292   9.523  1.00 15.05           N  
ATOM    847  CA  PHE A 106      25.255  11.114  10.696  1.00 15.17           C  
ATOM    848  C   PHE A 106      26.614  11.810  10.592  1.00 14.86           C  
ATOM    849  O   PHE A 106      26.725  12.979  10.954  1.00 14.34           O  
ATOM    850  CB  PHE A 106      25.234  10.287  11.985  1.00 16.09           C  
ATOM    851  CG  PHE A 106      23.864   9.765  12.376  1.00 17.81           C  
ATOM    852  CD1 PHE A 106      22.710  10.224  11.754  1.00 18.00           C  
ATOM    853  CD2 PHE A 106      23.739   8.826  13.396  1.00 17.99           C  
ATOM    854  CE1 PHE A 106      21.459   9.757  12.147  1.00 18.79           C  
ATOM    855  CE2 PHE A 106      22.487   8.360  13.790  1.00 18.31           C  
ATOM    856  CZ  PHE A 106      21.357   8.827  13.166  1.00 18.23           C  
ATOM    857  N   ILE A 107      27.648  11.092  10.149  1.00 14.34           N  
ATOM    858  CA  ILE A 107      28.968  11.707  10.027  1.00 14.48           C  
ATOM    859  C   ILE A 107      28.984  12.711   8.863  1.00 15.05           C  
ATOM    860  O   ILE A 107      29.715  13.709   8.907  1.00 15.26           O  
ATOM    861  CB  ILE A 107      30.134  10.663   9.904  1.00 14.62           C  
ATOM    862  CG1 ILE A 107      31.483  11.353  10.220  1.00 14.37           C  
ATOM    863  CG2 ILE A 107      30.164  10.034   8.505  1.00 13.15           C  
ATOM    864  CD1 ILE A 107      32.676  10.403  10.336  1.00 14.25           C  
ATOM    865  N   SER A 108      28.159  12.460   7.842  1.00 15.26           N  
ATOM    866  CA  SER A 108      28.047  13.363   6.693  1.00 15.68           C  
ATOM    867  C   SER A 108      27.545  14.710   7.184  1.00 15.90           C  
ATOM    868  O   SER A 108      28.077  15.757   6.805  1.00 16.25           O  
ATOM    869  CB  SER A 108      27.082  12.802   5.652  1.00 15.50           C  
ATOM    870  OG  SER A 108      27.672  11.680   5.004  1.00 17.49           O  
ATOM    871  N   GLU A 109      26.527  14.660   8.044  1.00 17.48           N  
ATOM    872  CA  GLU A 109      25.931  15.835   8.659  1.00 19.02           C  
ATOM    873  C   GLU A 109      26.971  16.580   9.497  1.00  9.86           C  
ATOM    874  O   GLU A 109      27.023  17.810   9.482  1.00 10.23           O  
ATOM    875  CB  GLU A 109      24.769  15.399   9.554  1.00 17.30           C  
ATOM    876  CG  GLU A 109      24.105  16.524  10.329  1.00 35.11           C  
ATOM    877  CD  GLU A 109      23.070  16.017  11.339  1.00 74.83           C  
ATOM    878  OE1 GLU A 109      23.176  14.858  11.820  1.00 60.11           O  
ATOM    879  OE2 GLU A 109      22.145  16.795  11.664  1.00 88.99           O  
ATOM    880  N   ALA A 110      27.790  15.836  10.231  1.00 11.06           N  
ATOM    881  CA  ALA A 110      28.823  16.443  11.075  1.00 12.23           C  
ATOM    882  C   ALA A 110      29.872  17.166  10.216  1.00 12.35           C  
ATOM    883  O   ALA A 110      30.348  18.255  10.580  1.00 13.15           O  
ATOM    884  CB  ALA A 110      29.494  15.379  11.961  1.00 11.22           C  
ATOM    885  N   ILE A 111      30.210  16.571   9.071  1.00 11.96           N  
ATOM    886  CA  ILE A 111      31.192  17.159   8.161  1.00 12.38           C  
ATOM    887  C   ILE A 111      30.672  18.484   7.591  1.00 12.69           C  
ATOM    888  O   ILE A 111      31.343  19.516   7.658  1.00 12.48           O  
ATOM    889  CB  ILE A 111      31.555  16.179   7.013  1.00 12.70           C  
ATOM    890  CG1 ILE A 111      32.413  15.038   7.574  1.00 12.53           C  
ATOM    891  CG2 ILE A 111      32.315  16.930   5.885  1.00 11.83           C  
ATOM    892  CD1 ILE A 111      32.451  13.805   6.706  1.00 13.30           C  
ATOM    893  N   ILE A 112      29.443  18.457   7.105  1.00 13.31           N  
ATOM    894  CA  ILE A 112      28.832  19.645   6.544  1.00 14.91           C  
ATOM    895  C   ILE A 112      28.716  20.761   7.590  1.00 15.30           C  
ATOM    896  O   ILE A 112      28.997  21.930   7.286  1.00 15.30           O  
ATOM    897  CB  ILE A 112      27.467  19.295   5.938  1.00 15.57           C  
ATOM    898  CG1 ILE A 112      27.686  18.453   4.680  1.00 15.70           C  
ATOM    899  CG2 ILE A 112      26.644  20.576   5.645  1.00 16.14           C  
ATOM    900  CD1 ILE A 112      26.396  17.872   4.128  1.00 18.03           C  
ATOM    901  N   HIS A 113      28.366  20.386   8.825  1.00 14.97           N  
ATOM    902  CA  HIS A 113      28.230  21.342   9.908  1.00 15.13           C  
ATOM    903  C   HIS A 113      29.552  22.034  10.221  1.00 15.44           C  
ATOM    904  O   HIS A 113      29.598  23.249  10.435  1.00 15.64           O  
ATOM    905  CB  HIS A 113      27.730  20.650  11.178  1.00 17.79           C  
ATOM    906  CG  HIS A 113      27.597  21.579  12.347  1.00 23.44           C  
ATOM    907  ND1 HIS A 113      26.452  22.286  12.641  1.00 29.78           N  
ATOM    908  CD2 HIS A 113      28.524  21.990  13.250  1.00 24.06           C  
ATOM    909  CE1 HIS A 113      26.719  23.099  13.675  1.00 24.39           C  
ATOM    910  NE2 HIS A 113      27.966  22.954  14.080  1.00 29.30           N  
ATOM    911  N   VAL A 114      30.618  21.250  10.294  1.00 14.94           N  
ATOM    912  CA  VAL A 114      31.931  21.791  10.611  1.00 14.73           C  
ATOM    913  C   VAL A 114      32.499  22.683   9.505  1.00 14.66           C  
ATOM    914  O   VAL A 114      33.068  23.740   9.813  1.00 14.94           O  
ATOM    915  CB  VAL A 114      32.920  20.662  10.987  1.00 14.48           C  
ATOM    916  CG1 VAL A 114      34.340  21.219  11.164  1.00 13.11           C  
ATOM    917  CG2 VAL A 114      32.440  19.999  12.268  1.00 13.96           C  
ATOM    918  N   LEU A 115      32.338  22.280   8.237  1.00 13.94           N  
ATOM    919  CA  LEU A 115      32.835  23.092   7.122  1.00 13.91           C  
ATOM    920  C   LEU A 115      32.080  24.408   7.094  1.00 14.23           C  
ATOM    921  O   LEU A 115      32.648  25.463   6.832  1.00 13.51           O  
ATOM    922  CB  LEU A 115      32.666  22.375   5.781  1.00 14.09           C  
ATOM    923  CG  LEU A 115      33.424  21.045   5.668  1.00 15.85           C  
ATOM    924  CD1 LEU A 115      33.409  20.552   4.236  1.00 16.60           C  
ATOM    925  CD2 LEU A 115      34.834  21.202   6.155  1.00 15.79           C  
ATOM    926  N   HIS A 116      30.786  24.333   7.380  1.00 14.42           N  
ATOM    927  CA  HIS A 116      29.968  25.515   7.403  1.00 15.44           C  
ATOM    928  C   HIS A 116      30.475  26.489   8.469  1.00 16.15           C  
ATOM    929  O   HIS A 116      30.602  27.680   8.191  1.00 16.39           O  
ATOM    930  CB  HIS A 116      28.511  25.146   7.646  1.00 15.97           C  
ATOM    931  CG  HIS A 116      27.603  26.331   7.736  1.00 23.94           C  
ATOM    932  ND1 HIS A 116      27.213  27.089   6.653  1.00 27.64           N  
ATOM    933  CD2 HIS A 116      27.027  26.913   8.821  1.00 20.22           C  
ATOM    934  CE1 HIS A 116      26.432  28.083   7.102  1.00 23.91           C  
ATOM    935  NE2 HIS A 116      26.290  28.016   8.411  1.00 30.41           N  
ATOM    936  N   SER A 117      30.831  25.980   9.651  1.00 16.25           N  
ATOM    937  CA  SER A 117      31.319  26.838  10.732  1.00 17.46           C  
ATOM    938  C   SER A 117      32.694  27.451  10.476  1.00 16.93           C  
ATOM    939  O   SER A 117      32.892  28.658  10.634  1.00 16.79           O  
ATOM    940  CB  SER A 117      31.411  26.060  12.046  1.00 17.33           C  
ATOM    941  OG  SER A 117      30.143  25.595  12.424  1.00 23.22           O  
ATOM    942  N   ARG A 118      33.642  26.604  10.099  1.00 16.00           N  
ATOM    943  CA  ARG A 118      35.002  27.048   9.883  1.00 16.09           C  
ATOM    944  C   ARG A 118      35.311  27.709   8.563  1.00 16.42           C  
ATOM    945  O   ARG A 118      36.267  28.465   8.477  1.00 16.85           O  
ATOM    946  CB  ARG A 118      35.956  25.877  10.095  1.00 16.31           C  
ATOM    947  CG  ARG A 118      35.923  25.326  11.507  1.00 17.66           C  
ATOM    948  CD  ARG A 118      36.833  24.121  11.658  1.00 18.91           C  
ATOM    949  NE  ARG A 118      38.232  24.485  11.507  1.00 23.08           N  
ATOM    950  CZ  ARG A 118      39.221  23.958  12.218  1.00 28.58           C  
ATOM    951  NH1 ARG A 118      38.969  23.042  13.139  1.00 19.83           N  
ATOM    952  NH2 ARG A 118      40.465  24.345  11.995  1.00 22.14           N  
ATOM    953  N   HIS A 119      34.513  27.438   7.535  1.00 16.21           N  
ATOM    954  CA  HIS A 119      34.776  27.995   6.215  1.00 16.52           C  
ATOM    955  C   HIS A 119      33.570  28.657   5.558  1.00 16.96           C  
ATOM    956  O   HIS A 119      33.264  28.372   4.401  1.00 16.55           O  
ATOM    957  CB  HIS A 119      35.322  26.881   5.307  1.00 15.35           C  
ATOM    958  CG  HIS A 119      36.503  26.173   5.887  1.00 16.81           C  
ATOM    959  ND1 HIS A 119      37.754  26.740   6.014  1.00 17.07           N  
ATOM    960  CD2 HIS A 119      36.596  24.945   6.456  1.00 12.45           C  
ATOM    961  CE1 HIS A 119      38.553  25.864   6.649  1.00 15.79           C  
ATOM    962  NE2 HIS A 119      37.906  24.754   6.940  1.00 14.56           N  
ATOM    963  N   PRO A 120      32.924  29.613   6.253  1.00 17.60           N  
ATOM    964  CA  PRO A 120      31.752  30.293   5.690  1.00 18.44           C  
ATOM    965  C   PRO A 120      31.994  30.906   4.305  1.00 18.89           C  
ATOM    966  O   PRO A 120      31.163  30.775   3.420  1.00 19.93           O  
ATOM    967  CB  PRO A 120      31.416  31.353   6.755  1.00 18.40           C  
ATOM    968  CG  PRO A 120      32.734  31.641   7.386  1.00 18.17           C  
ATOM    969  CD  PRO A 120      33.343  30.256   7.512  1.00 17.55           C  
ATOM    970  N   GLY A 121      33.168  31.490   4.101  1.00 19.23           N  
ATOM    971  CA  GLY A 121      33.482  32.098   2.826  1.00 19.49           C  
ATOM    972  C   GLY A 121      33.638  31.118   1.674  1.00 19.88           C  
ATOM    973  O   GLY A 121      33.383  31.492   0.531  1.00 21.13           O  
ATOM    974  N   ASN A 122      34.066  29.885   1.947  1.00 18.33           N  
ATOM    975  CA  ASN A 122      34.224  28.896   0.881  1.00 17.56           C  
ATOM    976  C   ASN A 122      33.145  27.830   0.958  1.00 17.40           C  
ATOM    977  O   ASN A 122      33.271  26.768   0.330  1.00 18.22           O  
ATOM    978  CB  ASN A 122      35.603  28.215   0.956  1.00 16.47           C  
ATOM    979  CG  ASN A 122      36.744  29.175   0.651  1.00 23.94           C  
ATOM    980  OD1 ASN A 122      37.668  29.352   1.452  1.00 21.42           O  
ATOM    981  ND2 ASN A 122      36.674  29.812  -0.504  1.00 17.36           N  
ATOM    982  N   PHE A 123      32.082  28.095   1.714  1.00 16.20           N  
ATOM    983  CA  PHE A 123      31.031  27.091   1.861  1.00 15.22           C  
ATOM    984  C   PHE A 123      29.638  27.707   1.810  1.00 15.07           C  
ATOM    985  O   PHE A 123      28.854  27.581   2.755  1.00 14.90           O  
ATOM    986  CB  PHE A 123      31.233  26.291   3.167  1.00 14.16           C  
ATOM    987  CG  PHE A 123      30.680  24.889   3.137  1.00 13.87           C  
ATOM    988  CD1 PHE A 123      31.217  23.933   2.294  1.00 13.81           C  
ATOM    989  CD2 PHE A 123      29.654  24.508   4.002  1.00 13.82           C  
ATOM    990  CE1 PHE A 123      30.736  22.601   2.319  1.00 14.46           C  
ATOM    991  CE2 PHE A 123      29.175  23.194   4.037  1.00 13.98           C  
ATOM    992  CZ  PHE A 123      29.714  22.240   3.198  1.00 14.00           C  
ATOM    993  N   GLY A 124      29.374  28.424   0.723  1.00 14.89           N  
ATOM    994  CA  GLY A 124      28.066  29.008   0.499  1.00 14.52           C  
ATOM    995  C   GLY A 124      27.131  27.883   0.064  1.00 14.67           C  
ATOM    996  O   GLY A 124      27.517  26.713   0.061  1.00 13.74           O  
ATOM    997  N   ALA A 125      25.924  28.240  -0.357  1.00 14.54           N  
ATOM    998  CA  ALA A 125      24.917  27.259  -0.746  1.00 14.94           C  
ATOM    999  C   ALA A 125      25.330  26.324  -1.882  1.00 15.13           C  
ATOM   1000  O   ALA A 125      25.058  25.124  -1.837  1.00 15.68           O  
ATOM   1001  CB  ALA A 125      23.600  27.970  -1.090  1.00 14.69           C  
ATOM   1002  N   ASP A 126      25.955  26.880  -2.913  1.00 13.43           N  
ATOM   1003  CA  ASP A 126      26.388  26.088  -4.051  1.00 10.99           C  
ATOM   1004  C   ASP A 126      27.429  25.070  -3.619  1.00 14.91           C  
ATOM   1005  O   ASP A 126      27.315  23.908  -3.964  1.00 15.09           O  
ATOM   1006  CB  ASP A 126      26.948  26.989  -5.153  1.00 21.24           C  
ATOM   1007  CG  ASP A 126      25.867  27.804  -5.856  1.00 26.37           C  
ATOM   1008  OD1 ASP A 126      24.685  27.408  -5.820  1.00 25.47           O  
ATOM   1009  OD2 ASP A 126      26.209  28.840  -6.458  1.00 35.73           O  
ATOM   1010  N   ALA A 127      28.446  25.508  -2.875  1.00 13.00           N  
ATOM   1011  CA  ALA A 127      29.495  24.603  -2.377  1.00 13.19           C  
ATOM   1012  C   ALA A 127      28.926  23.532  -1.425  1.00 13.50           C  
ATOM   1013  O   ALA A 127      29.358  22.381  -1.455  1.00 14.17           O  
ATOM   1014  CB  ALA A 127      30.631  25.403  -1.677  1.00 12.59           C  
ATOM   1015  N   GLN A 128      27.973  23.902  -0.575  1.00 12.96           N  
ATOM   1016  CA  GLN A 128      27.375  22.922   0.329  1.00 13.45           C  
ATOM   1017  C   GLN A 128      26.566  21.885  -0.482  1.00 13.71           C  
ATOM   1018  O   GLN A 128      26.579  20.692  -0.161  1.00 14.19           O  
ATOM   1019  CB  GLN A 128      26.479  23.596   1.390  1.00 13.18           C  
ATOM   1020  CG  GLN A 128      25.765  22.583   2.295  1.00 15.46           C  
ATOM   1021  CD  GLN A 128      25.069  23.195   3.504  1.00 17.66           C  
ATOM   1022  OE1 GLN A 128      25.372  24.311   3.925  1.00 19.04           O  
ATOM   1023  NE2 GLN A 128      24.140  22.445   4.081  1.00 16.30           N  
ATOM   1024  N   GLY A 129      25.861  22.348  -1.516  1.00 13.17           N  
ATOM   1025  CA  GLY A 129      25.088  21.443  -2.354  1.00 13.25           C  
ATOM   1026  C   GLY A 129      26.014  20.439  -3.043  1.00 13.29           C  
ATOM   1027  O   GLY A 129      25.688  19.247  -3.146  1.00 13.24           O  
ATOM   1028  N   ALA A 130      27.172  20.913  -3.501  1.00 12.37           N  
ATOM   1029  CA  ALA A 130      28.145  20.044  -4.156  1.00 13.20           C  
ATOM   1030  C   ALA A 130      28.715  19.001  -3.176  1.00 13.32           C  
ATOM   1031  O   ALA A 130      28.837  17.822  -3.517  1.00 13.58           O  
ATOM   1032  CB  ALA A 130      29.268  20.869  -4.757  1.00 12.82           C  
ATOM   1033  N   MET A 131      29.046  19.439  -1.963  1.00 13.52           N  
ATOM   1034  CA  MET A 131      29.592  18.553  -0.926  1.00 14.15           C  
ATOM   1035  C   MET A 131      28.563  17.476  -0.540  1.00 13.73           C  
ATOM   1036  O   MET A 131      28.891  16.292  -0.427  1.00 12.90           O  
ATOM   1037  CB  MET A 131      30.018  19.379   0.312  1.00 14.76           C  
ATOM   1038  CG  MET A 131      30.675  18.564   1.445  1.00 15.74           C  
ATOM   1039  SD  MET A 131      32.201  17.676   0.927  1.00 18.67           S  
ATOM   1040  CE  MET A 131      33.349  18.957   1.034  1.00 16.91           C  
ATOM   1041  N   ASN A 132      27.317  17.899  -0.341  1.00 13.80           N  
ATOM   1042  CA  ASN A 132      26.253  16.967  -0.011  1.00 14.77           C  
ATOM   1043  C   ASN A 132      26.109  15.913  -1.129  1.00 15.12           C  
ATOM   1044  O   ASN A 132      25.927  14.725  -0.860  1.00 15.96           O  
ATOM   1045  CB  ASN A 132      24.925  17.699   0.156  1.00 13.92           C  
ATOM   1046  CG  ASN A 132      23.770  16.739   0.357  1.00 16.64           C  
ATOM   1047  OD1 ASN A 132      23.803  15.923   1.265  1.00 17.59           O  
ATOM   1048  ND2 ASN A 132      22.777  16.796  -0.521  1.00 18.26           N  
ATOM   1049  N   LYS A 133      26.201  16.364  -2.377  1.00 17.32           N  
ATOM   1050  CA  LYS A 133      26.084  15.489  -3.538  1.00 14.82           C  
ATOM   1051  C   LYS A 133      27.246  14.480  -3.574  1.00 17.90           C  
ATOM   1052  O   LYS A 133      27.050  13.289  -3.860  1.00 13.48           O  
ATOM   1053  CB  LYS A 133      26.057  16.345  -4.803  1.00 19.71           C  
ATOM   1054  CG  LYS A 133      25.420  15.682  -5.984  1.00 28.22           C  
ATOM   1055  CD  LYS A 133      25.308  16.625  -7.163  1.00 27.62           C  
ATOM   1056  CE  LYS A 133      24.914  15.859  -8.413  1.00 52.97           C  
ATOM   1057  NZ  LYS A 133      24.905  16.725  -9.614  1.00 74.53           N  
ATOM   1058  N   ALA A 134      28.442  14.950  -3.229  1.00 12.87           N  
ATOM   1059  CA  ALA A 134      29.630  14.091  -3.218  1.00 13.47           C  
ATOM   1060  C   ALA A 134      29.534  13.030  -2.115  1.00 13.87           C  
ATOM   1061  O   ALA A 134      29.860  11.859  -2.339  1.00 14.49           O  
ATOM   1062  CB  ALA A 134      30.910  14.939  -3.056  1.00 12.22           C  
ATOM   1063  N   LEU A 135      29.034  13.434  -0.946  1.00 13.82           N  
ATOM   1064  CA  LEU A 135      28.879  12.522   0.189  1.00 13.98           C  
ATOM   1065  C   LEU A 135      27.727  11.537  -0.044  1.00 14.11           C  
ATOM   1066  O   LEU A 135      27.775  10.407   0.425  1.00 14.20           O  
ATOM   1067  CB  LEU A 135      28.695  13.310   1.496  1.00 13.75           C  
ATOM   1068  CG  LEU A 135      29.929  14.062   2.025  1.00 14.13           C  
ATOM   1069  CD1 LEU A 135      29.580  14.870   3.284  1.00 13.81           C  
ATOM   1070  CD2 LEU A 135      31.034  13.075   2.339  1.00 13.90           C  
ATOM   1071  N   GLU A 136      26.679  11.973  -0.744  1.00 13.49           N  
ATOM   1072  CA  GLU A 136      25.573  11.074  -1.066  1.00 16.04           C  
ATOM   1073  C   GLU A 136      26.067   9.999  -2.047  1.00 14.96           C  
ATOM   1074  O   GLU A 136      25.653   8.831  -1.963  1.00 16.34           O  
ATOM   1075  CB  GLU A 136      24.414  11.828  -1.707  1.00 12.46           C  
ATOM   1076  CG  GLU A 136      23.703  12.789  -0.789  1.00 44.80           C  
ATOM   1077  CD  GLU A 136      22.473  13.394  -1.432  1.00 52.55           C  
ATOM   1078  OE1 GLU A 136      22.235  13.142  -2.637  1.00 48.81           O  
ATOM   1079  OE2 GLU A 136      21.740  14.118  -0.728  1.00 56.19           O  
ATOM   1080  N   LEU A 137      26.900  10.421  -3.008  1.00 15.12           N  
ATOM   1081  CA  LEU A 137      27.482   9.515  -4.002  1.00 15.96           C  
ATOM   1082  C   LEU A 137      28.283   8.449  -3.238  1.00 15.89           C  
ATOM   1083  O   LEU A 137      28.123   7.250  -3.486  1.00 15.91           O  
ATOM   1084  CB  LEU A 137      28.393  10.273  -4.992  1.00 16.54           C  
ATOM   1085  CG  LEU A 137      29.149   9.382  -5.990  1.00 17.78           C  
ATOM   1086  CD1 LEU A 137      28.184   8.728  -6.969  1.00 19.20           C  
ATOM   1087  CD2 LEU A 137      30.192  10.163  -6.740  1.00 18.22           C  
ATOM   1088  N   PHE A 138      29.104   8.901  -2.290  1.00 15.56           N  
ATOM   1089  CA  PHE A 138      29.901   8.016  -1.440  1.00 16.09           C  
ATOM   1090  C   PHE A 138      29.003   7.006  -0.703  1.00 15.97           C  
ATOM   1091  O   PHE A 138      29.276   5.805  -0.743  1.00 16.01           O  
ATOM   1092  CB  PHE A 138      30.706   8.854  -0.438  1.00 17.10           C  
ATOM   1093  CG  PHE A 138      31.336   8.055   0.682  1.00 18.65           C  
ATOM   1094  CD1 PHE A 138      32.408   7.211   0.438  1.00 19.08           C  
ATOM   1095  CD2 PHE A 138      30.851   8.152   1.981  1.00 18.98           C  
ATOM   1096  CE1 PHE A 138      32.983   6.479   1.465  1.00 19.60           C  
ATOM   1097  CE2 PHE A 138      31.426   7.417   3.011  1.00 19.50           C  
ATOM   1098  CZ  PHE A 138      32.496   6.579   2.748  1.00 19.07           C  
ATOM   1099  N   ARG A 139      27.936   7.487  -0.055  1.00 15.51           N  
ATOM   1100  CA  ARG A 139      27.002   6.615   0.673  1.00 16.38           C  
ATOM   1101  C   ARG A 139      26.266   5.598  -0.209  1.00 16.38           C  
ATOM   1102  O   ARG A 139      25.990   4.478   0.225  1.00 17.17           O  
ATOM   1103  CB  ARG A 139      25.967   7.431   1.468  1.00 14.71           C  
ATOM   1104  CG  ARG A 139      26.585   8.244   2.606  1.00 21.56           C  
ATOM   1105  CD  ARG A 139      25.567   8.664   3.645  1.00 14.30           C  
ATOM   1106  NE  ARG A 139      24.454   9.404   3.064  1.00 18.17           N  
ATOM   1107  CZ  ARG A 139      24.460  10.703   2.777  1.00 21.08           C  
ATOM   1108  NH1 ARG A 139      25.530  11.459   3.004  1.00 20.58           N  
ATOM   1109  NH2 ARG A 139      23.378  11.247   2.255  1.00 16.97           N  
ATOM   1110  N   LYS A 140      25.890   6.026  -1.411  1.00 16.09           N  
ATOM   1111  CA  LYS A 140      25.192   5.173  -2.374  1.00 20.00           C  
ATOM   1112  C   LYS A 140      26.098   4.014  -2.808  1.00 21.76           C  
ATOM   1113  O   LYS A 140      25.676   2.863  -2.836  1.00 14.42           O  
ATOM   1114  CB  LYS A 140      24.790   5.986  -3.611  1.00 27.06           C  
ATOM   1115  CG  LYS A 140      23.972   5.206  -4.634  1.00 45.99           C  
ATOM   1116  CD  LYS A 140      23.402   6.100  -5.741  1.00 79.30           C  
ATOM   1117  CE  LYS A 140      24.365   6.287  -6.920  1.00 85.35           C  
ATOM   1118  NZ  LYS A 140      25.631   6.990  -6.564  1.00 82.64           N  
ATOM   1119  N   ASP A 141      27.341   4.329  -3.160  1.00 13.76           N  
ATOM   1120  CA  ASP A 141      28.285   3.302  -3.582  1.00 14.64           C  
ATOM   1121  C   ASP A 141      28.650   2.361  -2.438  1.00 18.09           C  
ATOM   1122  O   ASP A 141      28.698   1.146  -2.626  1.00 18.83           O  
ATOM   1123  CB  ASP A 141      29.519   3.943  -4.215  1.00 17.81           C  
ATOM   1124  CG  ASP A 141      29.211   4.607  -5.550  1.00 21.65           C  
ATOM   1125  OD1 ASP A 141      28.120   4.365  -6.097  1.00 22.33           O  
ATOM   1126  OD2 ASP A 141      30.043   5.385  -6.048  1.00 22.08           O  
ATOM   1127  N   ILE A 142      28.849   2.907  -1.243  1.00 19.69           N  
ATOM   1128  CA  ILE A 142      29.172   2.078  -0.082  1.00 20.48           C  
ATOM   1129  C   ILE A 142      28.030   1.100   0.235  1.00 20.33           C  
ATOM   1130  O   ILE A 142      28.283  -0.080   0.528  1.00 20.05           O  
ATOM   1131  CB  ILE A 142      29.456   2.930   1.190  1.00 21.51           C  
ATOM   1132  CG1 ILE A 142      30.911   3.387   1.209  1.00 23.16           C  
ATOM   1133  CG2 ILE A 142      29.196   2.110   2.455  1.00 22.03           C  
ATOM   1134  CD1 ILE A 142      31.869   2.331   1.774  1.00 24.63           C  
ATOM   1135  N   ALA A 143      26.786   1.591   0.204  1.00 19.87           N  
ATOM   1136  CA  ALA A 143      25.639   0.732   0.505  1.00 20.12           C  
ATOM   1137  C   ALA A 143      25.446  -0.353  -0.549  1.00 20.01           C  
ATOM   1138  O   ALA A 143      25.058  -1.458  -0.215  1.00 20.33           O  
ATOM   1139  CB  ALA A 143      24.379   1.531   0.717  1.00 19.82           C  
ATOM   1140  N   ALA A 144      25.776  -0.058  -1.804  1.00 19.98           N  
ATOM   1141  CA  ALA A 144      25.681  -1.066  -2.853  1.00 20.13           C  
ATOM   1142  C   ALA A 144      26.718  -2.168  -2.538  1.00 20.63           C  
ATOM   1143  O   ALA A 144      26.431  -3.366  -2.671  1.00 20.63           O  
ATOM   1144  CB  ALA A 144      25.962  -0.444  -4.200  1.00 19.92           C  
ATOM   1145  N   LYS A 145      27.908  -1.759  -2.090  1.00 14.94           N  
ATOM   1146  CA  LYS A 145      28.961  -2.703  -1.733  1.00 18.47           C  
ATOM   1147  C   LYS A 145      28.572  -3.526  -0.501  1.00 19.66           C  
ATOM   1148  O   LYS A 145      28.871  -4.722  -0.426  1.00 17.53           O  
ATOM   1149  CB  LYS A 145      30.280  -1.969  -1.501  1.00 17.80           C  
ATOM   1150  CG  LYS A 145      31.031  -1.636  -2.759  1.00 36.20           C  
ATOM   1151  CD  LYS A 145      30.080  -1.244  -3.902  1.00 73.26           C  
ATOM   1152  CE  LYS A 145      30.622  -0.117  -4.755  1.00 63.31           C  
ATOM   1153  NZ  LYS A 145      29.511   0.471  -5.560  1.00 26.86           N  
ATOM   1154  N   TYR A 146      27.903  -2.885   0.455  1.00 19.77           N  
ATOM   1155  CA  TYR A 146      27.428  -3.564   1.666  1.00 19.91           C  
ATOM   1156  C   TYR A 146      26.536  -4.755   1.286  1.00 19.89           C  
ATOM   1157  O   TYR A 146      26.667  -5.858   1.817  1.00 19.66           O  
ATOM   1158  CB  TYR A 146      26.589  -2.598   2.503  1.00 20.59           C  
ATOM   1159  CG  TYR A 146      27.328  -1.832   3.587  1.00 21.16           C  
ATOM   1160  CD1 TYR A 146      28.716  -1.668   3.565  1.00 20.53           C  
ATOM   1161  CD2 TYR A 146      26.618  -1.268   4.649  1.00 22.22           C  
ATOM   1162  CE1 TYR A 146      29.372  -0.960   4.584  1.00 20.93           C  
ATOM   1163  CE2 TYR A 146      27.263  -0.561   5.660  1.00 22.12           C  
ATOM   1164  CZ  TYR A 146      28.625  -0.411   5.625  1.00 21.42           C  
ATOM   1165  OH  TYR A 146      29.207   0.309   6.636  1.00 20.90           O  
ATOM   1166  N   LYS A 147      25.611  -4.506   0.371  1.00 19.69           N  
ATOM   1167  CA  LYS A 147      24.702  -5.535  -0.111  1.00 21.47           C  
ATOM   1168  C   LYS A 147      25.451  -6.695  -0.780  1.00 18.52           C  
ATOM   1169  O   LYS A 147      25.205  -7.858  -0.464  1.00 21.47           O  
ATOM   1170  CB  LYS A 147      23.851  -4.999  -1.248  1.00 20.52           C  
ATOM   1171  CG  LYS A 147      22.578  -5.867  -1.484  1.00 32.74           C  
ATOM   1172  CD  LYS A 147      21.612  -5.212  -2.434  1.00 64.47           C  
ATOM   1173  CE  LYS A 147      20.772  -6.289  -3.099  1.00 83.74           C  
ATOM   1174  NZ  LYS A 147      20.297  -7.337  -2.134  1.00 87.66           N  
ATOM   1175  N   GLU A 148      26.410  -6.374  -1.654  1.00 19.36           N  
ATOM   1176  CA  GLU A 148      27.194  -7.412  -2.326  1.00 21.36           C  
ATOM   1177  C   GLU A 148      27.942  -8.261  -1.300  1.00 26.24           C  
ATOM   1178  O   GLU A 148      28.101  -9.471  -1.484  1.00 21.22           O  
ATOM   1179  CB  GLU A 148      28.203  -6.801  -3.310  1.00 16.10           C  
ATOM   1180  CG  GLU A 148      27.557  -6.172  -4.525  1.00 36.64           C  
ATOM   1181  CD  GLU A 148      28.537  -5.386  -5.393  1.00 49.34           C  
ATOM   1182  OE1 GLU A 148      29.722  -5.777  -5.460  1.00 47.38           O  
ATOM   1183  OE2 GLU A 148      28.121  -4.372  -5.998  1.00 59.66           O  
ATOM   1184  N   LEU A 149      28.362  -7.623  -0.207  1.00 25.00           N  
ATOM   1185  CA  LEU A 149      29.106  -8.294   0.852  1.00 25.80           C  
ATOM   1186  C   LEU A 149      28.219  -9.028   1.854  1.00 26.62           C  
ATOM   1187  O   LEU A 149      28.722  -9.698   2.749  1.00 26.63           O  
ATOM   1188  CB  LEU A 149      30.013  -7.299   1.577  1.00 25.40           C  
ATOM   1189  CG  LEU A 149      31.141  -6.664   0.762  1.00 25.18           C  
ATOM   1190  CD1 LEU A 149      31.713  -5.460   1.501  1.00 24.78           C  
ATOM   1191  CD2 LEU A 149      32.225  -7.672   0.488  1.00 24.81           C  
ATOM   1192  N   GLY A 150      26.907  -8.890   1.717  1.00 27.83           N  
ATOM   1193  CA  GLY A 150      26.003  -9.589   2.616  1.00 30.10           C  
ATOM   1194  C   GLY A 150      25.544  -8.856   3.861  1.00 31.94           C  
ATOM   1195  O   GLY A 150      24.929  -9.453   4.737  1.00 31.56           O  
ATOM   1196  N   TYR A 151      25.821  -7.560   3.935  1.00 34.23           N  
ATOM   1197  CA  TYR A 151      25.428  -6.776   5.085  1.00 36.68           C  
ATOM   1198  C   TYR A 151      24.287  -5.834   4.754  1.00 38.75           C  
ATOM   1199  O   TYR A 151      23.153  -6.046   5.173  1.00 39.40           O  
ATOM   1200  CB  TYR A 151      26.624  -5.986   5.613  1.00 37.13           C  
ATOM   1201  CG  TYR A 151      26.319  -5.078   6.788  1.00 37.85           C  
ATOM   1202  CD1 TYR A 151      25.674  -5.557   7.914  1.00 38.50           C  
ATOM   1203  CD2 TYR A 151      26.670  -3.732   6.762  1.00 38.39           C  
ATOM   1204  CE1 TYR A 151      25.377  -4.720   8.988  1.00 38.95           C  
ATOM   1205  CE2 TYR A 151      26.380  -2.884   7.830  1.00 38.63           C  
ATOM   1206  CZ  TYR A 151      25.727  -3.385   8.936  1.00 39.03           C  
ATOM   1207  OH  TYR A 151      25.362  -2.543   9.964  1.00 39.21           O  
ATOM   1208  N   GLN A 152      24.585  -4.802   3.977  1.00 41.07           N  
ATOM   1209  CA  GLN A 152      23.594  -3.777   3.632  1.00 43.96           C  
ATOM   1210  C   GLN A 152      22.790  -3.325   4.860  1.00 45.06           C  
ATOM   1211  O   GLN A 152      21.587  -3.090   4.787  1.00 45.47           O  
ATOM   1212  CB  GLN A 152      22.653  -4.233   2.507  1.00 45.87           C  
ATOM   1213  CG  GLN A 152      21.736  -3.105   1.997  1.00 54.47           C  
ATOM   1214  CD  GLN A 152      22.377  -1.722   2.103  1.00 56.21           C  
ATOM   1215  OE1 GLN A 152      23.513  -1.506   1.692  1.00 52.86           O  
ATOM   1216  NE2 GLN A 152      21.644  -0.789   2.691  1.00 71.86           N  
ATOM   1217  N   GLY A 153      23.474  -3.227   5.994  1.00 45.98           N  
ATOM   1218  CA  GLY A 153      22.818  -2.798   7.211  1.00 47.07           C  
ATOM   1219  C   GLY A 153      22.695  -1.282   7.219  1.00 47.54           C  
ATOM   1220  O   GLY A 153      21.870  -0.745   7.992  1.00 48.11           O  
ATOM   1221  OXT GLY A 153      23.431  -0.634   6.445  1.00 48.02           O  
TER    1222      GLY A 153                                                      
HETATM 1223  S   SO4 A 157      30.746  18.706  28.896  1.00 47.98           S  
HETATM 1224  O1  SO4 A 157      30.697  20.077  28.620  1.00 48.06           O  
HETATM 1225  O2  SO4 A 157      31.104  18.021  27.725  1.00 47.52           O  
HETATM 1226  O3  SO4 A 157      29.468  18.179  29.331  1.00 47.79           O  
HETATM 1227  O4  SO4 A 157      31.722  18.578  29.881  1.00 47.85           O  
HETATM 1228  CHA HEM A 155      38.056   2.293  11.078  1.00 21.35           C  
HETATM 1229  CHB HEM A 155      37.306   5.212   7.384  1.00 18.29           C  
HETATM 1230  CHC HEM A 155      32.964   6.205   9.051  1.00 16.45           C  
HETATM 1231  CHD HEM A 155      33.598   3.200  12.667  1.00 19.12           C  
HETATM 1232  C1A HEM A 155      38.286   2.995   9.925  1.00 21.23           C  
HETATM 1233  C2A HEM A 155      39.557   3.037   9.214  1.00 21.38           C  
HETATM 1234  C3A HEM A 155      39.302   3.871   8.151  1.00 20.28           C  
HETATM 1235  C4A HEM A 155      37.919   4.323   8.239  1.00 19.51           C  
HETATM 1236  CMA HEM A 155      40.314   4.221   7.055  1.00 18.93           C  
HETATM 1237  CAA HEM A 155      40.877   2.216   9.299  1.00 23.71           C  
HETATM 1238  CBA HEM A 155      41.015   0.742   8.951  1.00 26.45           C  
HETATM 1239  CGA HEM A 155      39.678   0.033   8.861  1.00 28.72           C  
HETATM 1240  O1A HEM A 155      39.251  -0.566   9.881  1.00 30.24           O  
HETATM 1241  O2A HEM A 155      39.048   0.091   7.778  1.00 29.74           O  
HETATM 1242  C1B HEM A 155      36.020   5.716   7.478  1.00 17.24           C  
HETATM 1243  C2B HEM A 155      35.456   6.694   6.556  1.00 16.49           C  
HETATM 1244  C3B HEM A 155      34.224   6.980   7.014  1.00 16.26           C  
HETATM 1245  C4B HEM A 155      34.055   6.156   8.231  1.00 16.22           C  
HETATM 1246  CMB HEM A 155      36.090   7.246   5.263  1.00 16.42           C  
HETATM 1247  CAB HEM A 155      33.335   8.005   6.658  1.00 16.24           C  
HETATM 1248  CBB HEM A 155      33.491   9.122   5.794  1.00 17.32           C  
HETATM 1249  C1C HEM A 155      32.740   5.507  10.200  1.00 15.99           C  
HETATM 1250  C2C HEM A 155      31.615   5.707  11.080  1.00 16.52           C  
HETATM 1251  C3C HEM A 155      31.785   4.829  12.131  1.00 17.63           C  
HETATM 1252  C4C HEM A 155      33.028   4.126  11.834  1.00 17.34           C  
HETATM 1253  CMC HEM A 155      30.484   6.704  10.837  1.00 15.53           C  
HETATM 1254  CAC HEM A 155      31.081   4.630  13.357  1.00 17.63           C  
HETATM 1255  CBC HEM A 155      29.969   5.338  13.897  1.00 18.52           C  
HETATM 1256  C1D HEM A 155      34.852   2.615  12.500  1.00 21.31           C  
HETATM 1257  C2D HEM A 155      35.466   1.757  13.490  1.00 22.47           C  
HETATM 1258  C3D HEM A 155      36.729   1.540  13.083  1.00 23.41           C  
HETATM 1259  C4D HEM A 155      36.872   2.243  11.803  1.00 22.48           C  
HETATM 1260  CMD HEM A 155      34.783   1.147  14.698  1.00 22.53           C  
HETATM 1261  CAD HEM A 155      37.941   1.000  13.841  1.00 26.65           C  
HETATM 1262  CBD HEM A 155      38.463   1.843  15.019  1.00 30.96           C  
HETATM 1263  CGD HEM A 155      39.586   1.145  15.786  1.00 33.23           C  
HETATM 1264  O1D HEM A 155      39.326   0.697  16.930  1.00 35.48           O  
HETATM 1265  O2D HEM A 155      40.714   1.027  15.245  1.00 34.38           O  
HETATM 1266  NA  HEM A 155      37.312   3.780   9.325  1.00 19.73           N  
HETATM 1267  NB  HEM A 155      35.132   5.385   8.500  1.00 17.06           N  
HETATM 1268  NC  HEM A 155      33.591   4.565  10.657  1.00 17.07           N  
HETATM 1269  ND  HEM A 155      35.728   2.887  11.451  1.00 21.03           N  
HETATM 1270 FE   HEM A 155      35.502   4.204   9.980  1.00 18.78          FE  
HETATM 1271  C   NBN A 156      36.437   5.629  11.224  0.68 19.01           C  
HETATM 1272  N   NBN A 156      36.674   6.332  11.970  0.68 19.66           N  
HETATM 1273  C1  NBN A 156      37.691   6.621  13.103  0.68 19.98           C  
HETATM 1274  C2  NBN A 156      38.602   5.446  13.328  0.68 20.27           C  
HETATM 1275  C3  NBN A 156      39.713   5.441  12.363  0.68 20.94           C  
HETATM 1276  C4  NBN A 156      40.675   4.358  12.790  0.68 20.98           C  
HETATM 1277  O   HOH A 201      35.636  -2.996  15.255  0.36 12.26           O  
HETATM 1278  O   HOH A 202      32.694  19.805  17.167  0.84 19.38           O  
HETATM 1279  O   HOH A 203      26.221  14.314  13.400  0.89 28.18           O  
HETATM 1280  O   HOH A 204      22.566   7.494   2.350  0.87 36.92           O  
HETATM 1281  O   HOH A 205      30.932   6.438  -8.815  1.00 41.84           O  
HETATM 1282  O   HOH A 206      24.541  30.283   6.889  0.63 25.58           O  
HETATM 1283  O   HOH A 207      25.187  14.290   2.886  0.81 26.13           O  
HETATM 1284  O   HOH A 208      22.103  13.723   1.959  0.96 26.43           O  
HETATM 1285  O   HOH A 209      30.014   8.951  35.439  1.00 35.90           O  
HETATM 1286  O   HOH A 210      30.631  11.672  35.807  0.93 21.70           O  
HETATM 1287  O   HOH A 211      31.937  13.143 -12.160  1.00 17.10           O  
HETATM 1288  O   HOH A 212      34.706  13.187  33.417  1.00 24.72           O  
HETATM 1289  O   HOH A 213      35.965  30.906   4.862  0.88 25.13           O  
HETATM 1290  O   HOH A 214      37.788  28.957   4.292  1.00 23.24           O  
HETATM 1291  O   HOH A 215      47.139  19.251   7.852  1.00 21.52           O  
HETATM 1292  O   HOH A 216      35.554  33.553   5.043  1.00 35.51           O  
HETATM 1293  O   HOH A 217      45.287  12.661  -0.522  0.63 28.06           O  
HETATM 1294  O   HOH A 218      22.243  26.519  -4.167  0.53 36.19           O  
HETATM 1295  O   HOH A 219      34.356  25.644  -2.155  0.99 18.86           O  
HETATM 1296  O   HOH A 220      43.314   5.775  14.083  0.83 33.75           O  
HETATM 1297  O   HOH A 221      35.554  15.655 -13.704  0.69 27.98           O  
HETATM 1298  O   HOH A 222      35.044  10.234  -5.370  1.00 16.54           O  
HETATM 1299  O   HOH A 223      43.738  11.098  -7.107  0.70 39.04           O  
HETATM 1300  O   HOH A 224      41.663  19.566  -2.545  0.71 29.09           O  
HETATM 1301  O   HOH A 225      29.014  28.495  -2.787  1.00 22.71           O  
HETATM 1302  O   HOH A 226      47.114  17.474  10.936  0.85 16.95           O  
HETATM 1303  O   HOH A 227      49.157  23.679   7.865  0.45  6.24           O  
HETATM 1304  O   HOH A 228      39.456  -6.272   0.390  0.45 18.39           O  
HETATM 1305  O   HOH A 229      47.195  20.062  12.092  0.79 27.14           O  
HETATM 1306  O   HOH A 230      41.694  14.434  14.419  0.64 19.99           O  
HETATM 1307  O   HOH A 231      25.279  16.763  13.167  0.91 45.56           O  
HETATM 1308  O   HOH A 232      27.502   6.144  24.003  0.34 12.97           O  
HETATM 1309  O   HOH A 233      32.714  -1.677  16.431  0.37  7.65           O  
HETATM 1310  O   HOH A 234      43.562   6.760   6.302  0.56 19.34           O  
HETATM 1311  O   HOH A 235      26.622  30.313  -3.254  0.87 35.39           O  
HETATM 1312  O   HOH A 236      43.770  12.412   1.711  0.89 19.03           O  
HETATM 1313  O   HOH A 237      39.271  -4.219   4.681  0.55 22.84           O  
HETATM 1314  O   HOH A 238      34.830  29.856  12.497  0.81 23.30           O  
HETATM 1315  O   HOH A 239      42.908  14.832   3.150  1.00 41.54           O  
HETATM 1316  O   HOH A 240      43.209   9.837  -4.230  0.92 19.85           O  
HETATM 1317  O   HOH A 241      40.614   6.101   0.818  0.34  2.00           O  
HETATM 1318  O   HOH A 242      40.042  10.664 -11.016  0.76 38.98           O  
HETATM 1319  O   HOH A 243      40.074   3.074   1.213  0.83 38.72           O  
HETATM 1320  O   HOH A 244      27.467  25.351  11.096  1.00 41.86           O  
HETATM 1321  O   HOH A 245      31.263  30.732  11.225  1.00 34.25           O  
HETATM 1322  O   HOH A 246      20.885   2.219   8.815  0.51 14.38           O  
HETATM 1323  O   HOH A 247      19.343  15.372   1.025  0.88 50.46           O  
HETATM 1324  O   HOH A 248      33.427  28.236  -3.034  1.00 44.12           O  
HETATM 1325  O   HOH A 249      27.534 -10.802  -3.746  0.42 14.53           O  
HETATM 1326  O   HOH A 250      24.801  -4.357  -4.615  0.37  9.21           O  
HETATM 1327  O   HOH A 251      26.214  23.149  -6.451  1.00 27.31           O  
HETATM 1328  O   HOH A 252      31.921  21.850  -1.051  0.56 24.04           O  
HETATM 1329  O   HOH A 253      44.385  26.738  -0.823  1.00 39.65           O  
HETATM 1330  O   HOH A 254      40.900  12.361  27.622  0.35  6.66           O  
HETATM 1331  O   HOH A 255      44.897  21.387  15.094  0.51 19.22           O  
HETATM 1332  O   HOH A 256      39.769  26.352   9.925  1.00 24.54           O  
HETATM 1333  O   HOH A 257      28.113  30.114   4.349  0.73 32.35           O  
HETATM 1334  O   HOH A 258      41.236  14.703  20.600  0.98 21.47           O  
HETATM 1335  O   HOH A 259      27.920  12.176  23.647  0.45 25.64           O  
HETATM 1336  O   HOH A 260      40.653  19.211  27.130  0.96 35.73           O  
HETATM 1337  O   HOH A 261      38.995  12.758  33.007  0.56 26.01           O  
HETATM 1338  O   HOH A 262      31.185  29.366  -1.418  0.92 29.20           O  
HETATM 1339  O   HOH A 263      23.330   1.530  -3.772  0.93 38.08           O  
HETATM 1340  O   HOH A 264      39.105  21.814  26.599  1.00 52.76           O  
HETATM 1341  O   HOH A 265      28.047  -8.320   9.038  0.26  2.83           O  
HETATM 1342  O   HOH A 266      20.727   9.658  17.232  1.00 40.20           O  
HETATM 1343  O   HOH A 267      39.824  21.447  16.984  0.48 20.91           O  
HETATM 1344  O   HOH A 268      31.109  21.510  30.969  0.78 27.35           O  
HETATM 1345  O   HOH A 269      25.247  20.689  -6.664  0.53 13.05           O  
HETATM 1346  O   HOH A 270      41.890  15.172  -7.575  0.63 23.24           O  
HETATM 1347  O   HOH A 271      32.201  10.450  -3.509  0.82 32.30           O  
HETATM 1348  O   HOH A 272      48.852  20.024  14.408  0.96 44.55           O  
HETATM 1349  O   HOH A 273      45.087  10.967  -2.827  0.80 23.86           O  
HETATM 1350  O   HOH A 274      43.790   6.366  -3.654  0.72 43.34           O  
HETATM 1351  O   HOH A 275      36.756  24.689  15.999  0.85 45.09           O  
HETATM 1352  O   HOH A 276      21.803  13.659   9.652  0.96 43.48           O  
HETATM 1353  O   HOH A 277      20.646   5.769  15.588  0.37 15.34           O  
HETATM 1354  O   HOH A 278      44.830  25.158   2.252  0.98 49.70           O  
HETATM 1355  O   HOH A 279      32.937  25.419  -9.655  0.44 16.19           O  
HETATM 1356  O   HOH A 280      28.152  27.732  -8.564  0.94 51.07           O  
HETATM 1357  O   HOH A 281      35.196  30.717  -2.699  1.00 51.54           O  
HETATM 1358  O   HOH A 282      33.436  19.536  28.293  0.81 30.59           O  
HETATM 1359  O   HOH A 283      25.107  22.125 -10.155  0.55 34.20           O  
HETATM 1360  O   HOH A 284      39.237   3.162  -8.262  1.00 34.85           O  
HETATM 1361  O   HOH A 285      31.346  32.729  13.318  0.42 18.95           O  
HETATM 1362  O   HOH A 286      36.519  -0.178  17.896  0.90 38.54           O  
HETATM 1363  O   HOH A 287      38.564   2.732  18.719  0.55 17.78           O  
HETATM 1364  O   HOH A 288      30.132  10.659  26.140  0.36 18.38           O  
HETATM 1365  O   HOH A 289      36.854   4.464 -13.579  0.81 38.38           O  
HETATM 1366  O   HOH A 290      27.373   5.340  -8.830  0.54 26.40           O  
HETATM 1367  O   HOH A 291      32.075   1.884  -6.445  0.75 37.30           O  
HETATM 1368  O   HOH A 292      40.784  -2.354  -4.023  0.29 12.31           O  
HETATM 1369  O   HOH A 293      38.692  31.184  -2.441  0.66 32.11           O  
HETATM 1370  O   HOH A 294      47.194  24.955  10.604  0.84 44.93           O  
HETATM 1371  O   HOH A 295      34.034  31.418  14.962  0.52 36.13           O  
HETATM 1372  O   HOH A 296      31.071   7.595  27.503  0.63 32.87           O  
HETATM 1373  O   HOH A 297      33.788  23.237  30.704  0.64 39.14           O  
HETATM 1374  O   HOH A 298      25.278  17.607 -12.018  0.56 32.27           O  
HETATM 1375  O   HOH A 299      21.415   7.748  -8.816  0.48 29.69           O  
HETATM 1376  O   HOH A 300      42.482  29.132  -3.537  0.48 27.61           O  
HETATM 1377  O   HOH A 301      23.188  23.847  -3.514  0.46 25.13           O  
HETATM 1378  O   HOH A 302      22.959   7.257  -2.133  0.76 43.13           O  
HETATM 1379  O   HOH A 303      23.834  15.545   5.192  0.68 34.54           O  
HETATM 1380  O   HOH A 304      39.887  -0.633   5.129  0.60 35.31           O  
HETATM 1381  O   HOH A 305      29.072  -9.111   6.284  0.69 37.84           O  
HETATM 1382  O   HOH A 306      21.916   1.326   6.785  0.72 42.32           O  
HETATM 1383  O   HOH A 307      18.377   6.767   6.900  0.66 39.04           O  
HETATM 1384  O   HOH A 308      46.391   8.895   7.898  0.50 25.35           O  
HETATM 1385  O   HOH A 309      48.010   9.126  10.162  0.60 34.14           O  
HETATM 1386  O   HOH A 310      30.229  20.017  18.925  0.66 31.75           O  
HETATM 1387  O   HOH A 311      34.675  20.639  19.217  0.54 24.69           O  
HETATM 1388  O   HOH A 312      28.518  11.760  28.729  0.28 27.00           O  
HETATM 1389  O   HOH A 313      32.254   6.469  30.644  0.40 30.36           O  
HETATM 1390  O   HOH A 314      40.742   5.881 -10.852  0.37 30.46           O  
HETATM 1391  O   HOH A 315      27.168  23.526  -8.314  0.33 28.77           O  
HETATM 1392  O   HOH A 316      28.521  -2.349  -7.024  0.32 28.33           O  
HETATM 1393  O   HOH A 317      25.803   2.353  -6.384  0.31 28.65           O  
HETATM 1394  O   HOH A 318      44.136  16.467  -6.383  0.34 29.36           O  
HETATM 1395  O   HOH A 319      42.780  18.817  -5.108  0.27 27.67           O  
HETATM 1396  O   HOH A 320      31.586  -2.955  -4.495  0.37 29.62           O  
HETATM 1397  O   HOH A 321      22.068  -0.590  -3.191  0.34 28.19           O  
HETATM 1398  O   HOH A 322      31.577  -4.125  -2.549  0.35 30.63           O  
HETATM 1399  O   HOH A 323      40.063  -4.705  -1.916  0.31 30.62           O  
HETATM 1400  O   HOH A 324      40.744  30.579  -1.276  0.42 31.10           O  
HETATM 1401  O   HOH A 325      22.633  -4.018   0.119  0.49 32.42           O  
HETATM 1402  O   HOH A 326      39.728  -6.468   2.562  0.39 28.33           O  
HETATM 1403  O   HOH A 327      23.766  17.652   5.748  0.36 30.42           O  
HETATM 1404  O   HOH A 328      23.087  12.937   6.384  0.29 26.48           O  
HETATM 1405  O   HOH A 329      22.747  -7.645   7.662  0.25 25.89           O  
HETATM 1406  O   HOH A 330      19.691   9.411   8.942  0.25 28.30           O  
HETATM 1407  O   HOH A 331      29.536  29.990   9.576  0.30 29.08           O  
HETATM 1408  O   HOH A 332      45.870  26.406   8.824  0.07 28.54           O  
HETATM 1409  O   HOH A 333      45.836   8.820  12.130  0.38 28.79           O  
HETATM 1410  O   HOH A 334      19.316   5.243  12.172  0.36 28.54           O  
HETATM 1411  O   HOH A 335      48.889  17.640  14.045  0.39 30.76           O  
HETATM 1412  O   HOH A 336      34.630  23.523  14.046  0.26 26.99           O  
HETATM 1413  O   HOH A 337      25.803  18.817  18.514  0.38 33.79           O  
HETATM 1414  O   HOH A 338      31.249  21.185  20.442  0.36 29.67           O  
CONECT  744 1270                                                                
CONECT 1223 1224 1225 1226 1227                                                 
CONECT 1224 1223                                                                
CONECT 1225 1223                                                                
CONECT 1226 1223                                                                
CONECT 1227 1223                                                                
CONECT 1228 1232 1259                                                           
CONECT 1229 1235 1242                                                           
CONECT 1230 1245 1249                                                           
CONECT 1231 1252 1256                                                           
CONECT 1232 1228 1233 1266                                                      
CONECT 1233 1232 1234 1237                                                      
CONECT 1234 1233 1235 1236                                                      
CONECT 1235 1229 1234 1266                                                      
CONECT 1236 1234                                                                
CONECT 1237 1233 1238                                                           
CONECT 1238 1237 1239                                                           
CONECT 1239 1238 1240 1241                                                      
CONECT 1240 1239                                                                
CONECT 1241 1239                                                                
CONECT 1242 1229 1243 1267                                                      
CONECT 1243 1242 1244 1246                                                      
CONECT 1244 1243 1245 1247                                                      
CONECT 1245 1230 1244 1267                                                      
CONECT 1246 1243                                                                
CONECT 1247 1244 1248                                                           
CONECT 1248 1247                                                                
CONECT 1249 1230 1250 1268                                                      
CONECT 1250 1249 1251 1253                                                      
CONECT 1251 1250 1252 1254                                                      
CONECT 1252 1231 1251 1268                                                      
CONECT 1253 1250                                                                
CONECT 1254 1251 1255                                                           
CONECT 1255 1254                                                                
CONECT 1256 1231 1257 1269                                                      
CONECT 1257 1256 1258 1260                                                      
CONECT 1258 1257 1259 1261                                                      
CONECT 1259 1228 1258 1269                                                      
CONECT 1260 1257                                                                
CONECT 1261 1258 1262                                                           
CONECT 1262 1261 1263                                                           
CONECT 1263 1262 1264 1265                                                      
CONECT 1264 1263                                                                
CONECT 1265 1263                                                                
CONECT 1266 1232 1235 1270                                                      
CONECT 1267 1242 1245 1270                                                      
CONECT 1268 1249 1252 1270                                                      
CONECT 1269 1256 1259 1270                                                      
CONECT 1270  744 1266 1267 1268                                                 
CONECT 1270 1269 1271                                                           
CONECT 1271 1270 1272                                                           
CONECT 1272 1271 1273                                                           
CONECT 1273 1272 1274                                                           
CONECT 1274 1273 1275                                                           
CONECT 1275 1274 1276                                                           
CONECT 1276 1275                                                                
MASTER      275    0    3    8    0    0    9    6 1413    1   56   12          
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.