CNRS Nantes University UFIP UFIP
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***  project  ***

elNémo ID: 22051117165295352

Job options:

ID        	=	 22051117165295352
JOBID     	=	 project
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 project

HEADER    OXYGEN TRANSPORT                        08-APR-11   3RGK              
TITLE     CRYSTAL STRUCTURE OF HUMAN MYOGLOBIN MUTANT K45R                      
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: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MB;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HEME, OXYGEN TRANSPORT                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.R.HUBBARD                                                           
REVDAT   1   27-APR-11 3RGK    0                                                
SPRSDE     27-APR-11 3RGK      2MM1                                             
JRNL        AUTH   S.R.HUBBARD,S.G.LAMBRIGHT,S.G.BOXER,W.A.HENDRICKSON          
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF A RECOMBINANT HUMAN MYOGLOBIN     
JRNL        TITL 2 MUTANT AT 2.8 A RESOLUTION                                   
JRNL        REF    J.MOL.BIOL.                   V.  20   215 1990              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   2342104                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16731                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 909                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1027                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.23                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.1890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1159                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 100                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.09000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.13000                                             
REMARK   3    B12 (A**2) : 0.04000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.103         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.726         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1283 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1753 ; 0.995 ; 2.076       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   161 ; 4.197 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;38.357 ;25.283       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   224 ;11.739 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     3 ;17.988 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   179 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   963 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   558 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   851 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.124 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.116 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.086 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   781 ; 0.670 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1216 ; 1.034 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   562 ; 1.931 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   530 ; 3.007 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3RGK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB064904.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-89                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : OTHER                              
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.10                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : FILM                               
REMARK 200  DETECTOR MANUFACTURER          : CEA REFLEX 25                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17640                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.08000                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2MM1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 250 MM TRIS-HCL, 80% AMMONIUM SULFATE,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       23.77333            
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       11.88667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       11.88667            
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       23.77333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 299  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 298  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   150                                                      
REMARK 465     PHE A   151                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  47    CG   CD   CE   NZ                                   
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     GLU A  59    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 140    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  79     -126.98     51.26                                   
REMARK 500    HIS A  81       69.97   -114.23                                   
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 154  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 200   O                                                      
REMARK 620 2 HEM A 154   NA   90.1                                              
REMARK 620 3 HEM A 154   NB   91.6  89.5                                        
REMARK 620 4 HEM A 154   NC   86.4 176.4  89.8                                  
REMARK 620 5 HEM A 154   ND   84.5  89.6 176.0  90.8                            
REMARK 620 6 HIS A  93   NE2 178.3  90.9  89.8  92.6  94.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 154                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302                 
DBREF  3RGK A    1   153  UNP    P02144   MYG_HUMAN        2    154             
SEQADV 3RGK ARG A   45  UNP  P02144    LYS    46 ENGINEERED MUTATION            
SEQADV 3RGK ALA A  110  UNP  P02144    CYS   111 ENGINEERED MUTATION            
SEQRES   1 A  153  GLY LEU SER ASP GLY GLU TRP GLN LEU VAL LEU ASN VAL          
SEQRES   2 A  153  TRP GLY LYS VAL GLU ALA ASP ILE PRO GLY HIS GLY GLN          
SEQRES   3 A  153  GLU VAL LEU ILE ARG LEU PHE LYS GLY HIS PRO GLU THR          
SEQRES   4 A  153  LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS SER GLU          
SEQRES   5 A  153  ASP GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY          
SEQRES   6 A  153  ALA THR VAL LEU THR ALA LEU GLY GLY ILE LEU LYS LYS          
SEQRES   7 A  153  LYS GLY HIS HIS GLU ALA GLU ILE LYS PRO LEU ALA GLN          
SEQRES   8 A  153  SER HIS ALA THR LYS HIS LYS ILE PRO VAL LYS TYR LEU          
SEQRES   9 A  153  GLU PHE ILE SER GLU ALA ILE ILE GLN VAL LEU GLN SER          
SEQRES  10 A  153  LYS HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA          
SEQRES  11 A  153  MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP MET ALA          
SEQRES  12 A  153  SER ASN TYR LYS GLU LEU GLY PHE GLN GLY                      
HET    HEM  A 154      43                                                       
HET    SO4  A 300       5                                                       
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SO4 SULFATE ION                                                      
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  HOH   *100(H2 O)                                                    
HELIX    1   1 SER A    3  GLU A   18  1                                  16    
HELIX    2   2 ASP A   20  HIS A   36  1                                  17    
HELIX    3   3 PRO A   37  LYS A   47  5                                  11    
HELIX    4   4 SER A   51  ALA A   57  1                                   7    
HELIX    5   5 SER A   58  LYS A   77  1                                  20    
HELIX    6   6 HIS A   82  LYS A   96  1                                  15    
HELIX    7   7 PRO A  100  HIS A  119  1                                  20    
HELIX    8   8 GLY A  124  LEU A  149  1                                  26    
LINK        FE   HEM A 154                 O   HOH A 200     1555   1555  2.12  
LINK         NE2 HIS A  93                FE   HEM A 154     1555   1555  2.16  
SITE     1 AC1 20 LYS A  42  PHE A  43  ARG A  45  HIS A  48                    
SITE     2 AC1 20 GLU A  54  ALA A  57  HIS A  64  VAL A  68                    
SITE     3 AC1 20 LEU A  89  SER A  92  HIS A  93  HIS A  97                    
SITE     4 AC1 20 ILE A  99  TYR A 103  PHE A 138  HOH A 200                    
SITE     5 AC1 20 HOH A 207  HOH A 211  HOH A 219  HOH A 290                    
SITE     1 AC2  6 LYS A  79  HIS A  81  LYS A 102  TYR A 103                    
SITE     2 AC2  6 LYS A 147  HOH A 212                                          
SITE     1 AC3  5 ARG A  45  LYS A  63  HIS A  64  THR A  67                    
SITE     2 AC3  5 HOH A 267                                                     
SITE     1 AC4  5 LYS A  34  SER A  51  GLU A  52  ASP A  53                    
SITE     2 AC4  5 LYS A  96                                                     
CRYST1   86.200   86.200   35.660  90.00  90.00 120.00 P 32 2 1      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      0.011601  0.006698  0.000000        0.00000                         
SCALE2      0.000000  0.013396  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028043        0.00000                         
ATOM      1  N   GLY A   1      -5.305  16.052  14.494  1.00 25.71           N  
ATOM      2  CA  GLY A   1      -4.718  17.420  14.606  1.00 25.07           C  
ATOM      3  C   GLY A   1      -3.276  17.379  15.070  1.00 24.60           C  
ATOM      4  O   GLY A   1      -2.544  16.424  14.782  1.00 25.45           O  
ATOM      5  N   LEU A   2      -2.867  18.418  15.792  1.00 23.41           N  
ATOM      6  CA  LEU A   2      -1.513  18.492  16.328  1.00 22.04           C  
ATOM      7  C   LEU A   2      -1.511  18.312  17.837  1.00 21.09           C  
ATOM      8  O   LEU A   2      -2.466  18.697  18.508  1.00 21.11           O  
ATOM      9  CB  LEU A   2      -0.867  19.834  15.974  1.00 21.77           C  
ATOM     10  CG  LEU A   2      -0.402  20.071  14.532  1.00 21.85           C  
ATOM     11  CD1 LEU A   2      -1.581  20.326  13.596  1.00 21.75           C  
ATOM     12  CD2 LEU A   2       0.575  21.239  14.484  1.00 22.11           C  
ATOM     13  N   SER A   3      -0.432  17.734  18.361  1.00 19.94           N  
ATOM     14  CA  SER A   3      -0.201  17.679  19.802  1.00 19.07           C  
ATOM     15  C   SER A   3       0.245  19.055  20.300  1.00 18.46           C  
ATOM     16  O   SER A   3       0.622  19.915  19.499  1.00 17.75           O  
ATOM     17  CB  SER A   3       0.867  16.629  20.124  1.00 19.09           C  
ATOM     18  OG  SER A   3       2.149  17.031  19.669  1.00 19.20           O  
ATOM     19  N   ASP A   4       0.219  19.269  21.615  1.00 18.01           N  
ATOM     20  CA  ASP A   4       0.721  20.527  22.162  1.00 17.45           C  
ATOM     21  C   ASP A   4       2.218  20.683  21.892  1.00 16.38           C  
ATOM     22  O   ASP A   4       2.682  21.787  21.648  1.00 15.58           O  
ATOM     23  CB  ASP A   4       0.423  20.671  23.657  1.00 18.35           C  
ATOM     24  CG  ASP A   4      -0.927  21.340  23.931  1.00 20.70           C  
ATOM     25  OD1 ASP A   4      -1.408  22.144  23.096  1.00 21.87           O  
ATOM     26  OD2 ASP A   4      -1.500  21.068  25.004  1.00 24.20           O  
ATOM     27  N   GLY A   5       2.960  19.574  21.931  1.00 15.27           N  
ATOM     28  CA  GLY A   5       4.391  19.606  21.600  1.00 14.04           C  
ATOM     29  C   GLY A   5       4.630  20.048  20.165  1.00 13.01           C  
ATOM     30  O   GLY A   5       5.558  20.813  19.888  1.00 12.92           O  
ATOM     31  N   GLU A   6       3.791  19.562  19.251  1.00 12.15           N  
ATOM     32  CA  GLU A   6       3.860  19.963  17.840  1.00 12.43           C  
ATOM     33  C   GLU A   6       3.505  21.442  17.653  1.00 10.85           C  
ATOM     34  O   GLU A   6       4.207  22.171  16.935  1.00 10.19           O  
ATOM     35  CB  GLU A   6       2.973  19.070  16.972  1.00 12.09           C  
ATOM     36  CG  GLU A   6       3.577  17.687  16.699  1.00 14.56           C  
ATOM     37  CD  GLU A   6       2.571  16.698  16.113  1.00 15.00           C  
ATOM     38  OE1 GLU A   6       1.367  16.827  16.386  1.00 18.28           O  
ATOM     39  OE2 GLU A   6       2.995  15.773  15.389  1.00 20.14           O  
ATOM     40  N   TRP A   7       2.430  21.890  18.306  1.00 10.28           N  
ATOM     41  CA  TRP A   7       2.073  23.315  18.257  1.00  9.89           C  
ATOM     42  C   TRP A   7       3.194  24.179  18.799  1.00  9.58           C  
ATOM     43  O   TRP A   7       3.474  25.262  18.272  1.00  9.17           O  
ATOM     44  CB  TRP A   7       0.765  23.612  19.004  1.00 10.15           C  
ATOM     45  CG  TRP A   7      -0.461  23.289  18.211  1.00 10.53           C  
ATOM     46  CD1 TRP A   7      -1.410  22.358  18.525  1.00 10.68           C  
ATOM     47  CD2 TRP A   7      -0.875  23.882  16.970  1.00 11.00           C  
ATOM     48  NE1 TRP A   7      -2.390  22.338  17.564  1.00 11.72           N  
ATOM     49  CE2 TRP A   7      -2.086  23.262  16.597  1.00 10.79           C  
ATOM     50  CE3 TRP A   7      -0.343  24.885  16.142  1.00 11.48           C  
ATOM     51  CZ2 TRP A   7      -2.775  23.599  15.421  1.00 11.00           C  
ATOM     52  CZ3 TRP A   7      -1.026  25.221  14.971  1.00 10.93           C  
ATOM     53  CH2 TRP A   7      -2.227  24.578  14.624  1.00 11.03           C  
ATOM     54  N   GLN A   8       3.853  23.690  19.847  1.00  9.25           N  
ATOM     55  CA  GLN A   8       4.970  24.410  20.437  1.00  9.73           C  
ATOM     56  C   GLN A   8       6.133  24.581  19.446  1.00  9.38           C  
ATOM     57  O   GLN A   8       6.712  25.660  19.355  1.00  9.54           O  
ATOM     58  CB  GLN A   8       5.429  23.702  21.710  1.00 10.21           C  
ATOM     59  CG  GLN A   8       6.263  24.558  22.626  1.00 12.35           C  
ATOM     60  CD  GLN A   8       6.626  23.819  23.891  1.00 14.37           C  
ATOM     61  OE1 GLN A   8       6.763  22.592  23.887  1.00 16.03           O  
ATOM     62  NE2 GLN A   8       6.790  24.554  24.983  1.00 15.11           N  
ATOM     63  N   LEU A   9       6.455  23.528  18.697  1.00  9.34           N  
ATOM     64  CA  LEU A   9       7.473  23.618  17.645  1.00  9.65           C  
ATOM     65  C   LEU A   9       7.091  24.660  16.603  1.00  9.66           C  
ATOM     66  O   LEU A   9       7.925  25.475  16.184  1.00  9.94           O  
ATOM     67  CB  LEU A   9       7.679  22.261  16.954  1.00  9.82           C  
ATOM     68  CG  LEU A   9       8.452  21.175  17.713  1.00 11.87           C  
ATOM     69  CD1 LEU A   9       8.396  19.866  16.937  1.00 13.47           C  
ATOM     70  CD2 LEU A   9       9.897  21.589  17.955  1.00 14.43           C  
ATOM     71  N   VAL A  10       5.828  24.640  16.197  1.00  9.33           N  
ATOM     72  CA  VAL A  10       5.337  25.583  15.195  1.00  9.42           C  
ATOM     73  C   VAL A  10       5.483  27.019  15.690  1.00  9.21           C  
ATOM     74  O   VAL A  10       6.012  27.886  14.987  1.00  9.67           O  
ATOM     75  CB  VAL A  10       3.867  25.280  14.800  1.00  9.31           C  
ATOM     76  CG1 VAL A  10       3.268  26.435  13.999  1.00  9.88           C  
ATOM     77  CG2 VAL A  10       3.782  23.976  14.001  1.00  9.49           C  
ATOM     78  N   LEU A  11       5.008  27.272  16.903  1.00  9.28           N  
ATOM     79  CA  LEU A  11       4.984  28.642  17.408  1.00  9.49           C  
ATOM     80  C   LEU A  11       6.361  29.197  17.770  1.00 10.10           C  
ATOM     81  O   LEU A  11       6.591  30.406  17.667  1.00 10.06           O  
ATOM     82  CB  LEU A  11       3.983  28.790  18.560  1.00  9.53           C  
ATOM     83  CG  LEU A  11       2.520  28.628  18.144  1.00 10.34           C  
ATOM     84  CD1 LEU A  11       1.608  28.792  19.352  1.00 11.83           C  
ATOM     85  CD2 LEU A  11       2.136  29.608  17.029  1.00 12.31           C  
ATOM     86  N   ASN A  12       7.272  28.316  18.173  1.00 10.61           N  
ATOM     87  CA  ASN A  12       8.639  28.730  18.431  1.00 11.32           C  
ATOM     88  C   ASN A  12       9.334  29.142  17.134  1.00 11.53           C  
ATOM     89  O   ASN A  12       9.982  30.188  17.085  1.00 12.06           O  
ATOM     90  CB  ASN A  12       9.438  27.645  19.131  1.00 11.41           C  
ATOM     91  CG  ASN A  12      10.817  28.126  19.515  1.00 11.86           C  
ATOM     92  OD1 ASN A  12      10.960  29.085  20.281  1.00 14.20           O  
ATOM     93  ND2 ASN A  12      11.831  27.490  18.969  1.00 12.86           N  
ATOM     94  N   VAL A  13       9.172  28.331  16.086  1.00 11.43           N  
ATOM     95  CA  VAL A  13       9.691  28.674  14.762  1.00 12.00           C  
ATOM     96  C   VAL A  13       9.075  29.982  14.275  1.00 11.82           C  
ATOM     97  O   VAL A  13       9.771  30.856  13.760  1.00 11.43           O  
ATOM     98  CB  VAL A  13       9.425  27.545  13.735  1.00 12.15           C  
ATOM     99  CG1 VAL A  13       9.714  28.023  12.303  1.00 13.47           C  
ATOM    100  CG2 VAL A  13      10.267  26.327  14.066  1.00 14.01           C  
ATOM    101  N   TRP A  14       7.767  30.132  14.462  1.00 11.77           N  
ATOM    102  CA  TRP A  14       7.108  31.351  14.022  1.00 12.88           C  
ATOM    103  C   TRP A  14       7.677  32.602  14.693  1.00 12.72           C  
ATOM    104  O   TRP A  14       7.739  33.664  14.069  1.00 13.11           O  
ATOM    105  CB  TRP A  14       5.587  31.289  14.191  1.00 13.17           C  
ATOM    106  CG  TRP A  14       4.961  32.258  13.244  1.00 14.28           C  
ATOM    107  CD1 TRP A  14       4.469  33.496  13.536  1.00 15.73           C  
ATOM    108  CD2 TRP A  14       4.845  32.098  11.830  1.00 14.37           C  
ATOM    109  NE1 TRP A  14       4.023  34.104  12.386  1.00 15.32           N  
ATOM    110  CE2 TRP A  14       4.246  33.271  11.324  1.00 15.89           C  
ATOM    111  CE3 TRP A  14       5.184  31.071  10.938  1.00 15.95           C  
ATOM    112  CZ2 TRP A  14       3.965  33.444   9.960  1.00 14.96           C  
ATOM    113  CZ3 TRP A  14       4.899  31.243   9.577  1.00 15.94           C  
ATOM    114  CH2 TRP A  14       4.298  32.422   9.109  1.00 15.64           C  
ATOM    115  N   GLY A  15       8.112  32.469  15.947  1.00 12.99           N  
ATOM    116  CA  GLY A  15       8.762  33.572  16.659  1.00 13.52           C  
ATOM    117  C   GLY A  15      10.007  34.070  15.938  1.00 13.91           C  
ATOM    118  O   GLY A  15      10.320  35.259  15.970  1.00 14.50           O  
ATOM    119  N   LYS A  16      10.719  33.154  15.290  1.00 14.04           N  
ATOM    120  CA  LYS A  16      11.903  33.499  14.494  1.00 14.40           C  
ATOM    121  C   LYS A  16      11.502  34.222  13.216  1.00 14.32           C  
ATOM    122  O   LYS A  16      12.188  35.153  12.784  1.00 14.55           O  
ATOM    123  CB  LYS A  16      12.721  32.248  14.184  1.00 14.92           C  
ATOM    124  CG  LYS A  16      13.286  31.611  15.445  1.00 16.85           C  
ATOM    125  CD  LYS A  16      13.675  30.177  15.235  1.00 19.74           C  
ATOM    126  CE  LYS A  16      13.827  29.466  16.582  1.00 21.56           C  
ATOM    127  NZ  LYS A  16      14.835  30.130  17.472  1.00 22.43           N  
ATOM    128  N   VAL A  17      10.391  33.794  12.619  1.00 13.61           N  
ATOM    129  CA  VAL A  17       9.811  34.487  11.464  1.00 13.86           C  
ATOM    130  C   VAL A  17       9.450  35.926  11.840  1.00 14.07           C  
ATOM    131  O   VAL A  17       9.731  36.859  11.092  1.00 13.55           O  
ATOM    132  CB  VAL A  17       8.573  33.738  10.912  1.00 13.68           C  
ATOM    133  CG1 VAL A  17       7.902  34.529   9.779  1.00 14.13           C  
ATOM    134  CG2 VAL A  17       8.977  32.350  10.442  1.00 14.67           C  
ATOM    135  N   GLU A  18       8.863  36.100  13.022  1.00 14.59           N  
ATOM    136  CA  GLU A  18       8.422  37.421  13.473  1.00 15.60           C  
ATOM    137  C   GLU A  18       9.537  38.453  13.617  1.00 15.81           C  
ATOM    138  O   GLU A  18       9.262  39.659  13.626  1.00 16.48           O  
ATOM    139  CB  GLU A  18       7.643  37.307  14.777  1.00 15.68           C  
ATOM    140  CG  GLU A  18       6.293  36.654  14.605  1.00 18.51           C  
ATOM    141  CD  GLU A  18       5.526  36.558  15.905  1.00 22.16           C  
ATOM    142  OE1 GLU A  18       6.135  36.225  16.949  1.00 24.19           O  
ATOM    143  OE2 GLU A  18       4.310  36.813  15.875  1.00 24.40           O  
ATOM    144  N   ALA A  19      10.779  37.979  13.732  1.00 15.90           N  
ATOM    145  CA  ALA A  19      11.950  38.851  13.789  1.00 16.27           C  
ATOM    146  C   ALA A  19      12.142  39.629  12.487  1.00 16.10           C  
ATOM    147  O   ALA A  19      12.681  40.735  12.492  1.00 16.96           O  
ATOM    148  CB  ALA A  19      13.198  38.040  14.107  1.00 16.37           C  
ATOM    149  N   ASP A  20      11.707  39.044  11.372  1.00 15.60           N  
ATOM    150  CA  ASP A  20      11.805  39.698  10.069  1.00 14.76           C  
ATOM    151  C   ASP A  20      10.648  39.278   9.154  1.00 13.99           C  
ATOM    152  O   ASP A  20      10.848  38.558   8.174  1.00 13.17           O  
ATOM    153  CB  ASP A  20      13.160  39.406   9.407  1.00 15.31           C  
ATOM    154  CG  ASP A  20      13.359  40.176   8.097  1.00 16.76           C  
ATOM    155  OD1 ASP A  20      12.559  41.089   7.780  1.00 17.88           O  
ATOM    156  OD2 ASP A  20      14.327  39.860   7.380  1.00 19.95           O  
ATOM    157  N   ILE A  21       9.446  39.746   9.483  1.00 13.39           N  
ATOM    158  CA  ILE A  21       8.242  39.420   8.709  1.00 13.20           C  
ATOM    159  C   ILE A  21       8.319  39.854   7.224  1.00 12.93           C  
ATOM    160  O   ILE A  21       8.024  39.047   6.336  1.00 12.30           O  
ATOM    161  CB  ILE A  21       6.951  39.951   9.407  1.00 13.46           C  
ATOM    162  CG1 ILE A  21       6.653  39.125  10.662  1.00 15.32           C  
ATOM    163  CG2 ILE A  21       5.750  39.963   8.453  1.00 13.98           C  
ATOM    164  CD1 ILE A  21       6.148  37.708  10.374  1.00 17.35           C  
ATOM    165  N   PRO A  22       8.723  41.111   6.952  1.00 12.84           N  
ATOM    166  CA  PRO A  22       8.816  41.553   5.546  1.00 12.69           C  
ATOM    167  C   PRO A  22       9.830  40.759   4.712  1.00 12.12           C  
ATOM    168  O   PRO A  22       9.531  40.407   3.565  1.00 12.14           O  
ATOM    169  CB  PRO A  22       9.237  43.026   5.664  1.00 12.95           C  
ATOM    170  CG  PRO A  22       8.833  43.426   7.068  1.00 13.11           C  
ATOM    171  CD  PRO A  22       9.094  42.197   7.880  1.00 13.34           C  
ATOM    172  N   GLY A  23      10.995  40.458   5.284  1.00 11.68           N  
ATOM    173  CA  GLY A  23      12.013  39.667   4.578  1.00 11.58           C  
ATOM    174  C   GLY A  23      11.523  38.266   4.241  1.00 10.82           C  
ATOM    175  O   GLY A  23      11.673  37.795   3.104  1.00 11.39           O  
ATOM    176  N   HIS A  24      10.913  37.600   5.220  1.00  9.77           N  
ATOM    177  CA  HIS A  24      10.336  36.269   4.996  1.00  9.37           C  
ATOM    178  C   HIS A  24       9.189  36.327   3.979  1.00  9.13           C  
ATOM    179  O   HIS A  24       9.107  35.488   3.074  1.00  8.60           O  
ATOM    180  CB  HIS A  24       9.829  35.673   6.311  1.00  9.50           C  
ATOM    181  CG  HIS A  24      10.907  35.132   7.200  1.00  9.30           C  
ATOM    182  ND1 HIS A  24      11.692  35.934   8.003  1.00 10.53           N  
ATOM    183  CD2 HIS A  24      11.297  33.857   7.446  1.00  8.35           C  
ATOM    184  CE1 HIS A  24      12.532  35.178   8.689  1.00  9.01           C  
ATOM    185  NE2 HIS A  24      12.313  33.913   8.368  1.00  9.00           N  
ATOM    186  N   GLY A  25       8.308  37.313   4.141  1.00  8.61           N  
ATOM    187  CA  GLY A  25       7.131  37.436   3.277  1.00  8.94           C  
ATOM    188  C   GLY A  25       7.491  37.704   1.833  1.00  9.19           C  
ATOM    189  O   GLY A  25       6.892  37.122   0.920  1.00  8.58           O  
ATOM    190  N   GLN A  26       8.486  38.564   1.617  1.00  9.90           N  
ATOM    191  CA  GLN A  26       8.935  38.848   0.249  1.00 11.40           C  
ATOM    192  C   GLN A  26       9.438  37.576  -0.431  1.00 10.76           C  
ATOM    193  O   GLN A  26       9.066  37.285  -1.576  1.00 10.90           O  
ATOM    194  CB  GLN A  26      10.014  39.936   0.214  1.00 11.43           C  
ATOM    195  CG  GLN A  26      10.313  40.385  -1.228  1.00 13.60           C  
ATOM    196  CD  GLN A  26      11.197  41.609  -1.345  1.00 14.53           C  
ATOM    197  OE1 GLN A  26      12.285  41.663  -0.768  1.00 18.89           O  
ATOM    198  NE2 GLN A  26      10.748  42.589  -2.146  1.00 18.19           N  
ATOM    199  N   GLU A  27      10.262  36.804   0.274  1.00 10.44           N  
ATOM    200  CA  GLU A  27      10.786  35.568  -0.304  1.00 11.02           C  
ATOM    201  C   GLU A  27       9.694  34.529  -0.582  1.00  9.50           C  
ATOM    202  O   GLU A  27       9.758  33.829  -1.594  1.00  9.09           O  
ATOM    203  CB  GLU A  27      11.921  34.980   0.539  1.00 11.01           C  
ATOM    204  CG  GLU A  27      12.594  33.786  -0.150  1.00 14.84           C  
ATOM    205  CD  GLU A  27      13.908  33.338   0.485  1.00 15.60           C  
ATOM    206  OE1 GLU A  27      14.483  34.079   1.315  1.00 22.43           O  
ATOM    207  OE2 GLU A  27      14.379  32.230   0.130  1.00 22.90           O  
ATOM    208  N   VAL A  28       8.692  34.425   0.295  1.00  8.28           N  
ATOM    209  CA  VAL A  28       7.573  33.514   0.034  1.00  7.70           C  
ATOM    210  C   VAL A  28       6.878  33.856  -1.291  1.00  7.45           C  
ATOM    211  O   VAL A  28       6.657  32.983  -2.123  1.00  7.26           O  
ATOM    212  CB  VAL A  28       6.551  33.517   1.201  1.00  7.66           C  
ATOM    213  CG1 VAL A  28       5.243  32.803   0.807  1.00  7.53           C  
ATOM    214  CG2 VAL A  28       7.171  32.851   2.428  1.00  8.18           C  
ATOM    215  N   LEU A  29       6.553  35.134  -1.487  1.00  7.80           N  
ATOM    216  CA  LEU A  29       5.875  35.552  -2.712  1.00  7.95           C  
ATOM    217  C   LEU A  29       6.731  35.344  -3.962  1.00  8.20           C  
ATOM    218  O   LEU A  29       6.216  34.927  -5.000  1.00  8.39           O  
ATOM    219  CB  LEU A  29       5.361  36.990  -2.607  1.00  8.55           C  
ATOM    220  CG  LEU A  29       4.235  37.171  -1.575  1.00  8.59           C  
ATOM    221  CD1 LEU A  29       3.762  38.626  -1.568  1.00 10.05           C  
ATOM    222  CD2 LEU A  29       3.061  36.224  -1.833  1.00 10.78           C  
ATOM    223  N   ILE A  30       8.032  35.612  -3.853  1.00  8.33           N  
ATOM    224  CA  ILE A  30       8.934  35.407  -4.992  1.00  9.02           C  
ATOM    225  C   ILE A  30       8.963  33.938  -5.408  1.00  8.98           C  
ATOM    226  O   ILE A  30       8.860  33.620  -6.591  1.00  8.78           O  
ATOM    227  CB  ILE A  30      10.360  35.934  -4.700  1.00  9.14           C  
ATOM    228  CG1 ILE A  30      10.341  37.466  -4.649  1.00 10.59           C  
ATOM    229  CG2 ILE A  30      11.352  35.420  -5.752  1.00 10.53           C  
ATOM    230  CD1 ILE A  30      11.596  38.091  -4.039  1.00 12.88           C  
ATOM    231  N   ARG A  31       9.094  33.043  -4.434  1.00  9.02           N  
ATOM    232  CA  ARG A  31       9.097  31.603  -4.736  1.00  9.90           C  
ATOM    233  C   ARG A  31       7.773  31.152  -5.335  1.00  9.41           C  
ATOM    234  O   ARG A  31       7.748  30.347  -6.262  1.00  9.47           O  
ATOM    235  CB  ARG A  31       9.407  30.784  -3.489  1.00  9.78           C  
ATOM    236  CG  ARG A  31      10.847  30.896  -3.035  1.00 13.49           C  
ATOM    237  CD  ARG A  31      11.149  29.855  -1.987  1.00 16.55           C  
ATOM    238  NE  ARG A  31      12.441  30.096  -1.344  1.00 21.00           N  
ATOM    239  CZ  ARG A  31      13.459  29.239  -1.341  1.00 21.03           C  
ATOM    240  NH1 ARG A  31      13.352  28.064  -1.948  1.00 20.81           N  
ATOM    241  NH2 ARG A  31      14.580  29.558  -0.710  1.00 21.19           N  
ATOM    242  N   LEU A  32       6.672  31.680  -4.805  1.00  8.96           N  
ATOM    243  CA  LEU A  32       5.354  31.389  -5.351  1.00  8.84           C  
ATOM    244  C   LEU A  32       5.213  31.830  -6.814  1.00  8.78           C  
ATOM    245  O   LEU A  32       4.793  31.040  -7.665  1.00  8.81           O  
ATOM    246  CB  LEU A  32       4.271  32.056  -4.504  1.00  8.79           C  
ATOM    247  CG  LEU A  32       2.831  31.820  -4.968  1.00  8.88           C  
ATOM    248  CD1 LEU A  32       2.403  30.375  -4.712  1.00 10.24           C  
ATOM    249  CD2 LEU A  32       1.919  32.799  -4.262  1.00  9.82           C  
ATOM    250  N   PHE A  33       5.570  33.084  -7.093  1.00  8.59           N  
ATOM    251  CA  PHE A  33       5.349  33.676  -8.406  1.00  9.35           C  
ATOM    252  C   PHE A  33       6.303  33.095  -9.450  1.00  9.52           C  
ATOM    253  O   PHE A  33       5.934  32.933 -10.610  1.00 10.53           O  
ATOM    254  CB  PHE A  33       5.517  35.195  -8.355  1.00  9.22           C  
ATOM    255  CG  PHE A  33       4.491  35.904  -7.515  1.00  8.86           C  
ATOM    256  CD1 PHE A  33       3.211  35.375  -7.333  1.00  9.70           C  
ATOM    257  CD2 PHE A  33       4.794  37.139  -6.952  1.00  9.43           C  
ATOM    258  CE1 PHE A  33       2.261  36.060  -6.562  1.00 11.18           C  
ATOM    259  CE2 PHE A  33       3.861  37.825  -6.188  1.00 10.54           C  
ATOM    260  CZ  PHE A  33       2.589  37.287  -5.993  1.00 10.67           C  
ATOM    261  N   LYS A  34       7.530  32.795  -9.039  1.00  9.88           N  
ATOM    262  CA  LYS A  34       8.504  32.216  -9.977  1.00 10.65           C  
ATOM    263  C   LYS A  34       8.230  30.737 -10.208  1.00 10.76           C  
ATOM    264  O   LYS A  34       8.352  30.243 -11.329  1.00 10.91           O  
ATOM    265  CB  LYS A  34       9.939  32.421  -9.482  1.00 11.16           C  
ATOM    266  CG  LYS A  34      10.484  33.830  -9.661  1.00 12.33           C  
ATOM    267  CD  LYS A  34      10.722  34.190 -11.131  1.00 15.65           C  
ATOM    268  CE  LYS A  34      11.806  33.327 -11.763  1.00 18.50           C  
ATOM    269  NZ  LYS A  34      11.915  33.584 -13.229  1.00 19.95           N  
ATOM    270  N   GLY A  35       7.860  30.025  -9.148  1.00 10.49           N  
ATOM    271  CA  GLY A  35       7.589  28.594  -9.256  1.00 10.84           C  
ATOM    272  C   GLY A  35       6.311  28.315 -10.024  1.00 11.22           C  
ATOM    273  O   GLY A  35       6.230  27.340 -10.777  1.00 11.89           O  
ATOM    274  N   HIS A  36       5.316  29.184  -9.842  1.00 10.94           N  
ATOM    275  CA  HIS A  36       4.004  28.996 -10.453  1.00 11.17           C  
ATOM    276  C   HIS A  36       3.495  30.339 -10.988  1.00 11.21           C  
ATOM    277  O   HIS A  36       2.702  31.014 -10.330  1.00 10.89           O  
ATOM    278  CB  HIS A  36       3.025  28.395  -9.433  1.00 11.68           C  
ATOM    279  CG  HIS A  36       3.577  27.221  -8.684  1.00 13.72           C  
ATOM    280  ND1 HIS A  36       3.468  25.927  -9.143  1.00 14.59           N  
ATOM    281  CD2 HIS A  36       4.253  27.148  -7.513  1.00 16.41           C  
ATOM    282  CE1 HIS A  36       4.045  25.105  -8.285  1.00 15.78           C  
ATOM    283  NE2 HIS A  36       4.536  25.822  -7.290  1.00 16.71           N  
ATOM    284  N   PRO A  37       3.955  30.736 -12.187  1.00 10.71           N  
ATOM    285  CA  PRO A  37       3.590  32.026 -12.792  1.00 10.98           C  
ATOM    286  C   PRO A  37       2.080  32.273 -12.933  1.00 10.79           C  
ATOM    287  O   PRO A  37       1.659  33.435 -12.984  1.00 11.36           O  
ATOM    288  CB  PRO A  37       4.269  31.975 -14.170  1.00 11.51           C  
ATOM    289  CG  PRO A  37       5.388  31.024 -13.989  1.00 10.87           C  
ATOM    290  CD  PRO A  37       4.898  29.980 -13.038  1.00 11.20           C  
ATOM    291  N   GLU A  38       1.277  31.210 -12.966  1.00 10.77           N  
ATOM    292  CA  GLU A  38      -0.178  31.356 -13.059  1.00 10.75           C  
ATOM    293  C   GLU A  38      -0.729  32.070 -11.820  1.00 11.05           C  
ATOM    294  O   GLU A  38      -1.758  32.742 -11.894  1.00 11.18           O  
ATOM    295  CB  GLU A  38      -0.890  30.003 -13.299  1.00 10.69           C  
ATOM    296  CG  GLU A  38      -0.823  28.994 -12.146  1.00 10.32           C  
ATOM    297  CD  GLU A  38       0.398  28.078 -12.196  1.00 10.37           C  
ATOM    298  OE1 GLU A  38       1.492  28.527 -12.611  1.00 11.79           O  
ATOM    299  OE2 GLU A  38       0.255  26.904 -11.802  1.00 12.02           O  
ATOM    300  N   THR A  39      -0.028  31.941 -10.692  1.00 10.60           N  
ATOM    301  CA  THR A  39      -0.448  32.603  -9.449  1.00 11.19           C  
ATOM    302  C   THR A  39      -0.284  34.119  -9.498  1.00 12.00           C  
ATOM    303  O   THR A  39      -1.058  34.848  -8.876  1.00 11.79           O  
ATOM    304  CB  THR A  39       0.284  32.048  -8.194  1.00 11.02           C  
ATOM    305  OG1 THR A  39       1.683  32.353  -8.266  1.00 10.36           O  
ATOM    306  CG2 THR A  39       0.074  30.527  -8.050  1.00 11.14           C  
ATOM    307  N   LEU A  40       0.723  34.593 -10.234  1.00 12.60           N  
ATOM    308  CA  LEU A  40       0.977  36.027 -10.348  1.00 13.74           C  
ATOM    309  C   LEU A  40      -0.173  36.722 -11.069  1.00 13.81           C  
ATOM    310  O   LEU A  40      -0.457  37.897 -10.818  1.00 14.28           O  
ATOM    311  CB  LEU A  40       2.312  36.279 -11.067  1.00 13.47           C  
ATOM    312  CG  LEU A  40       2.872  37.695 -11.222  1.00 13.84           C  
ATOM    313  CD1 LEU A  40       2.950  38.441  -9.896  1.00 14.97           C  
ATOM    314  CD2 LEU A  40       4.251  37.611 -11.870  1.00 14.73           C  
ATOM    315  N   GLU A  41      -0.851  35.975 -11.940  1.00 14.83           N  
ATOM    316  CA  GLU A  41      -1.994  36.492 -12.705  1.00 15.78           C  
ATOM    317  C   GLU A  41      -3.189  36.881 -11.837  1.00 15.56           C  
ATOM    318  O   GLU A  41      -4.042  37.641 -12.271  1.00 15.88           O  
ATOM    319  CB  GLU A  41      -2.428  35.490 -13.779  1.00 16.58           C  
ATOM    320  CG  GLU A  41      -1.371  35.258 -14.844  1.00 18.66           C  
ATOM    321  CD  GLU A  41      -0.966  36.547 -15.549  1.00 21.85           C  
ATOM    322  OE1 GLU A  41      -1.865  37.249 -16.060  1.00 23.96           O  
ATOM    323  OE2 GLU A  41       0.247  36.855 -15.589  1.00 23.53           O  
ATOM    324  N   LYS A  42      -3.240  36.368 -10.611  1.00 14.87           N  
ATOM    325  CA  LYS A  42      -4.311  36.720  -9.686  1.00 14.49           C  
ATOM    326  C   LYS A  42      -4.083  38.087  -9.032  1.00 14.30           C  
ATOM    327  O   LYS A  42      -4.993  38.623  -8.387  1.00 13.95           O  
ATOM    328  CB  LYS A  42      -4.465  35.636  -8.617  1.00 14.62           C  
ATOM    329  CG  LYS A  42      -4.943  34.286  -9.152  1.00 15.10           C  
ATOM    330  CD  LYS A  42      -6.417  34.326  -9.524  1.00 16.82           C  
ATOM    331  CE  LYS A  42      -6.930  32.966  -9.955  1.00 17.39           C  
ATOM    332  NZ  LYS A  42      -8.394  33.016 -10.248  1.00 18.49           N  
ATOM    333  N   PHE A  43      -2.881  38.641  -9.209  1.00 13.81           N  
ATOM    334  CA  PHE A  43      -2.497  39.923  -8.610  1.00 14.10           C  
ATOM    335  C   PHE A  43      -2.318  41.016  -9.663  1.00 14.76           C  
ATOM    336  O   PHE A  43      -1.209  41.207 -10.170  1.00 14.67           O  
ATOM    337  CB  PHE A  43      -1.170  39.799  -7.849  1.00 13.66           C  
ATOM    338  CG  PHE A  43      -1.245  38.985  -6.590  1.00 12.98           C  
ATOM    339  CD1 PHE A  43      -1.045  37.611  -6.624  1.00 12.64           C  
ATOM    340  CD2 PHE A  43      -1.484  39.603  -5.360  1.00 12.58           C  
ATOM    341  CE1 PHE A  43      -1.098  36.845  -5.452  1.00 12.31           C  
ATOM    342  CE2 PHE A  43      -1.532  38.846  -4.181  1.00 11.71           C  
ATOM    343  CZ  PHE A  43      -1.336  37.468  -4.232  1.00 11.91           C  
ATOM    344  N   ASP A  44      -3.389  41.741  -9.981  1.00 16.04           N  
ATOM    345  CA  ASP A  44      -3.267  42.951 -10.810  1.00 16.90           C  
ATOM    346  C   ASP A  44      -2.220  43.906 -10.236  1.00 16.47           C  
ATOM    347  O   ASP A  44      -1.526  44.608 -10.971  1.00 16.60           O  
ATOM    348  CB  ASP A  44      -4.607  43.685 -10.894  1.00 17.83           C  
ATOM    349  CG  ASP A  44      -5.568  43.039 -11.857  1.00 21.18           C  
ATOM    350  OD1 ASP A  44      -5.114  42.306 -12.767  1.00 25.36           O  
ATOM    351  OD2 ASP A  44      -6.789  43.282 -11.711  1.00 25.72           O  
ATOM    352  N   ARG A  45      -2.110  43.908  -8.910  1.00 16.21           N  
ATOM    353  CA  ARG A  45      -1.208  44.796  -8.182  1.00 16.22           C  
ATOM    354  C   ARG A  45       0.265  44.651  -8.588  1.00 16.42           C  
ATOM    355  O   ARG A  45       1.014  45.625  -8.565  1.00 16.39           O  
ATOM    356  CB  ARG A  45      -1.377  44.549  -6.684  1.00 16.27           C  
ATOM    357  CG  ARG A  45      -0.592  45.454  -5.763  1.00 16.39           C  
ATOM    358  CD  ARG A  45      -1.015  45.193  -4.334  1.00 17.97           C  
ATOM    359  NE  ARG A  45      -0.136  45.843  -3.367  1.00 17.17           N  
ATOM    360  CZ  ARG A  45      -0.281  45.755  -2.049  1.00 17.83           C  
ATOM    361  NH1 ARG A  45      -1.281  45.052  -1.527  1.00 17.50           N  
ATOM    362  NH2 ARG A  45       0.573  46.378  -1.253  1.00 18.42           N  
ATOM    363  N   PHE A  46       0.670  43.438  -8.955  1.00 16.32           N  
ATOM    364  CA  PHE A  46       2.080  43.154  -9.230  1.00 16.66           C  
ATOM    365  C   PHE A  46       2.348  42.843 -10.704  1.00 17.55           C  
ATOM    366  O   PHE A  46       3.319  42.156 -11.033  1.00 17.23           O  
ATOM    367  CB  PHE A  46       2.575  42.015  -8.324  1.00 16.25           C  
ATOM    368  CG  PHE A  46       2.379  42.284  -6.855  1.00 15.14           C  
ATOM    369  CD1 PHE A  46       2.867  43.455  -6.277  1.00 14.57           C  
ATOM    370  CD2 PHE A  46       1.710  41.368  -6.049  1.00 15.60           C  
ATOM    371  CE1 PHE A  46       2.683  43.716  -4.923  1.00 14.76           C  
ATOM    372  CE2 PHE A  46       1.525  41.620  -4.691  1.00 15.53           C  
ATOM    373  CZ  PHE A  46       2.012  42.794  -4.129  1.00 16.11           C  
ATOM    374  N   LYS A  47       1.500  43.386 -11.580  1.00 18.66           N  
ATOM    375  CA  LYS A  47       1.517  43.045 -13.008  1.00 19.60           C  
ATOM    376  C   LYS A  47       2.749  43.561 -13.747  1.00 20.02           C  
ATOM    377  O   LYS A  47       3.109  43.045 -14.802  1.00 20.81           O  
ATOM    378  CB  LYS A  47       0.235  43.532 -13.703  1.00 19.77           C  
ATOM    379  N   HIS A  48       3.400  44.576 -13.195  1.00 20.41           N  
ATOM    380  CA  HIS A  48       4.574  45.139 -13.848  1.00 20.60           C  
ATOM    381  C   HIS A  48       5.874  44.423 -13.459  1.00 20.33           C  
ATOM    382  O   HIS A  48       6.929  44.710 -14.018  1.00 20.52           O  
ATOM    383  CB  HIS A  48       4.655  46.645 -13.582  1.00 21.02           C  
ATOM    384  CG  HIS A  48       3.493  47.412 -14.133  1.00 22.78           C  
ATOM    385  ND1 HIS A  48       3.324  47.639 -15.483  1.00 24.41           N  
ATOM    386  CD2 HIS A  48       2.440  47.999 -13.516  1.00 23.98           C  
ATOM    387  CE1 HIS A  48       2.217  48.336 -15.673  1.00 24.78           C  
ATOM    388  NE2 HIS A  48       1.661  48.566 -14.496  1.00 24.78           N  
ATOM    389  N   LEU A  49       5.795  43.485 -12.518  1.00 19.74           N  
ATOM    390  CA  LEU A  49       6.989  42.785 -12.047  1.00 19.38           C  
ATOM    391  C   LEU A  49       7.241  41.517 -12.868  1.00 19.71           C  
ATOM    392  O   LEU A  49       6.563  40.496 -12.697  1.00 19.93           O  
ATOM    393  CB  LEU A  49       6.890  42.499 -10.544  1.00 19.02           C  
ATOM    394  CG  LEU A  49       6.600  43.705  -9.642  1.00 18.73           C  
ATOM    395  CD1 LEU A  49       6.427  43.263  -8.204  1.00 18.40           C  
ATOM    396  CD2 LEU A  49       7.677  44.788  -9.750  1.00 18.76           C  
ATOM    397  N   LYS A  50       8.220  41.597 -13.767  1.00 19.51           N  
ATOM    398  CA  LYS A  50       8.429  40.565 -14.791  1.00 19.96           C  
ATOM    399  C   LYS A  50       9.612  39.615 -14.560  1.00 19.28           C  
ATOM    400  O   LYS A  50       9.858  38.717 -15.382  1.00 20.18           O  
ATOM    401  CB  LYS A  50       8.541  41.216 -16.181  1.00 20.38           C  
ATOM    402  CG  LYS A  50       7.226  41.801 -16.719  1.00 22.67           C  
ATOM    403  CD  LYS A  50       6.261  40.704 -17.147  1.00 26.23           C  
ATOM    404  CE  LYS A  50       4.862  41.248 -17.419  1.00 27.83           C  
ATOM    405  NZ  LYS A  50       3.923  40.148 -17.788  1.00 30.33           N  
ATOM    406  N   SER A  51      10.338  39.809 -13.459  1.00 17.68           N  
ATOM    407  CA  SER A  51      11.508  38.990 -13.138  1.00 16.47           C  
ATOM    408  C   SER A  51      11.729  38.918 -11.637  1.00 15.72           C  
ATOM    409  O   SER A  51      11.222  39.755 -10.893  1.00 14.89           O  
ATOM    410  CB  SER A  51      12.764  39.556 -13.813  1.00 16.89           C  
ATOM    411  OG  SER A  51      13.187  40.758 -13.184  1.00 15.99           O  
ATOM    412  N   GLU A  52      12.492  37.922 -11.190  1.00 14.91           N  
ATOM    413  CA  GLU A  52      12.847  37.826  -9.782  1.00 15.04           C  
ATOM    414  C   GLU A  52      13.547  39.105  -9.307  1.00 13.90           C  
ATOM    415  O   GLU A  52      13.261  39.597  -8.216  1.00 13.42           O  
ATOM    416  CB  GLU A  52      13.719  36.594  -9.516  1.00 15.22           C  
ATOM    417  CG  GLU A  52      14.123  36.430  -8.055  1.00 16.76           C  
ATOM    418  CD  GLU A  52      14.789  35.093  -7.756  1.00 17.43           C  
ATOM    419  OE1 GLU A  52      14.850  34.219  -8.651  1.00 22.13           O  
ATOM    420  OE2 GLU A  52      15.248  34.920  -6.608  1.00 21.34           O  
ATOM    421  N   ASP A  53      14.449  39.650 -10.128  1.00 13.28           N  
ATOM    422  CA  ASP A  53      15.165  40.874  -9.739  1.00 12.97           C  
ATOM    423  C   ASP A  53      14.244  42.069  -9.513  1.00 12.13           C  
ATOM    424  O   ASP A  53      14.443  42.827  -8.570  1.00 11.89           O  
ATOM    425  CB  ASP A  53      16.248  41.243 -10.755  1.00 13.30           C  
ATOM    426  CG  ASP A  53      17.425  40.294 -10.725  1.00 15.32           C  
ATOM    427  OD1 ASP A  53      17.582  39.540  -9.734  1.00 16.57           O  
ATOM    428  OD2 ASP A  53      18.209  40.332 -11.689  1.00 18.81           O  
ATOM    429  N   GLU A  54      13.242  42.230 -10.373  1.00 11.51           N  
ATOM    430  CA  GLU A  54      12.239  43.271 -10.179  1.00 11.29           C  
ATOM    431  C   GLU A  54      11.414  43.034  -8.906  1.00 11.11           C  
ATOM    432  O   GLU A  54      11.147  43.962  -8.161  1.00 10.54           O  
ATOM    433  CB  GLU A  54      11.329  43.354 -11.392  1.00 12.10           C  
ATOM    434  CG  GLU A  54      12.032  43.865 -12.633  1.00 13.89           C  
ATOM    435  CD  GLU A  54      11.211  43.620 -13.872  1.00 16.69           C  
ATOM    436  OE1 GLU A  54      10.293  44.416 -14.136  1.00 17.80           O  
ATOM    437  OE2 GLU A  54      11.494  42.635 -14.583  1.00 19.44           O  
ATOM    438  N   MET A  55      11.026  41.784  -8.664  1.00 10.61           N  
ATOM    439  CA  MET A  55      10.272  41.436  -7.456  1.00 11.59           C  
ATOM    440  C   MET A  55      11.054  41.768  -6.193  1.00 11.26           C  
ATOM    441  O   MET A  55      10.498  42.293  -5.226  1.00 12.06           O  
ATOM    442  CB  MET A  55       9.905  39.950  -7.467  1.00 11.42           C  
ATOM    443  CG  MET A  55       8.996  39.570  -8.607  1.00 11.93           C  
ATOM    444  SD  MET A  55       8.686  37.796  -8.632  1.00 13.67           S  
ATOM    445  CE  MET A  55       7.918  37.609 -10.240  1.00 13.45           C  
ATOM    446  N   LYS A  56      12.351  41.466  -6.208  1.00 10.90           N  
ATOM    447  CA  LYS A  56      13.210  41.721  -5.059  1.00 11.45           C  
ATOM    448  C   LYS A  56      13.340  43.209  -4.744  1.00 11.35           C  
ATOM    449  O   LYS A  56      13.547  43.579  -3.597  1.00 12.20           O  
ATOM    450  CB  LYS A  56      14.588  41.106  -5.286  1.00 11.38           C  
ATOM    451  N   ALA A  57      13.214  44.051  -5.771  1.00 11.39           N  
ATOM    452  CA  ALA A  57      13.344  45.507  -5.638  1.00 11.46           C  
ATOM    453  C   ALA A  57      12.029  46.234  -5.328  1.00 11.52           C  
ATOM    454  O   ALA A  57      12.018  47.450  -5.128  1.00 12.07           O  
ATOM    455  CB  ALA A  57      13.985  46.083  -6.904  1.00 11.18           C  
ATOM    456  N   SER A  58      10.920  45.495  -5.296  1.00 11.76           N  
ATOM    457  CA  SER A  58       9.606  46.103  -5.100  1.00 12.31           C  
ATOM    458  C   SER A  58       9.261  46.195  -3.620  1.00 12.48           C  
ATOM    459  O   SER A  58       9.050  45.168  -2.970  1.00 12.77           O  
ATOM    460  CB  SER A  58       8.527  45.288  -5.826  1.00 12.11           C  
ATOM    461  OG  SER A  58       7.229  45.762  -5.506  1.00 13.19           O  
ATOM    462  N   GLU A  59       9.178  47.418  -3.098  1.00 12.88           N  
ATOM    463  CA  GLU A  59       8.766  47.619  -1.701  1.00 12.74           C  
ATOM    464  C   GLU A  59       7.312  47.187  -1.505  1.00 12.73           C  
ATOM    465  O   GLU A  59       6.935  46.698  -0.441  1.00 12.77           O  
ATOM    466  CB  GLU A  59       8.944  49.082  -1.273  1.00 13.58           C  
ATOM    467  N   ASP A  60       6.501  47.362  -2.542  1.00 12.38           N  
ATOM    468  CA  ASP A  60       5.087  47.004  -2.462  1.00 12.55           C  
ATOM    469  C   ASP A  60       4.874  45.500  -2.324  1.00 11.88           C  
ATOM    470  O   ASP A  60       4.001  45.058  -1.569  1.00 11.84           O  
ATOM    471  CB  ASP A  60       4.332  47.534  -3.671  1.00 12.77           C  
ATOM    472  CG  ASP A  60       2.840  47.529  -3.454  1.00 14.96           C  
ATOM    473  OD1 ASP A  60       2.389  48.038  -2.403  1.00 18.54           O  
ATOM    474  OD2 ASP A  60       2.121  47.003  -4.320  1.00 17.18           O  
ATOM    475  N   LEU A  61       5.668  44.715  -3.052  1.00 11.51           N  
ATOM    476  CA ALEU A  61       5.619  43.264  -2.922  0.50 11.08           C  
ATOM    477  CA BLEU A  61       5.616  43.263  -2.925  0.50 11.10           C  
ATOM    478  C   LEU A  61       6.020  42.837  -1.514  1.00 11.10           C  
ATOM    479  O   LEU A  61       5.397  41.960  -0.922  1.00 10.50           O  
ATOM    480  CB ALEU A  61       6.502  42.583  -3.971  0.50 11.24           C  
ATOM    481  CB BLEU A  61       6.489  42.589  -3.990  0.50 11.28           C  
ATOM    482  CG ALEU A  61       6.396  41.055  -4.033  0.50 10.82           C  
ATOM    483  CG BLEU A  61       6.365  41.067  -4.133  0.50 11.03           C  
ATOM    484  CD1ALEU A  61       4.992  40.623  -4.421  0.50 11.21           C  
ATOM    485  CD1BLEU A  61       6.493  40.643  -5.590  0.50 11.51           C  
ATOM    486  CD2ALEU A  61       7.407  40.486  -5.005  0.50 11.17           C  
ATOM    487  CD2BLEU A  61       7.388  40.346  -3.271  0.50 11.50           C  
ATOM    488  N   LYS A  62       7.059  43.473  -0.979  1.00 10.97           N  
ATOM    489  CA  LYS A  62       7.510  43.185   0.373  1.00 11.27           C  
ATOM    490  C   LYS A  62       6.407  43.496   1.394  1.00 11.16           C  
ATOM    491  O   LYS A  62       6.185  42.729   2.333  1.00 11.57           O  
ATOM    492  CB  LYS A  62       8.771  43.986   0.681  1.00 11.80           C  
ATOM    493  CG  LYS A  62       9.460  43.565   1.955  1.00 13.62           C  
ATOM    494  CD  LYS A  62      10.562  44.533   2.344  1.00 18.48           C  
ATOM    495  CE  LYS A  62      11.838  44.269   1.586  1.00 21.77           C  
ATOM    496  NZ  LYS A  62      12.953  45.039   2.213  1.00 22.88           N  
ATOM    497  N   LYS A  63       5.717  44.616   1.184  1.00 11.08           N  
ATOM    498  CA  LYS A  63       4.612  45.050   2.038  1.00 11.47           C  
ATOM    499  C   LYS A  63       3.500  44.004   2.043  1.00 10.54           C  
ATOM    500  O   LYS A  63       2.993  43.634   3.104  1.00 10.30           O  
ATOM    501  CB  LYS A  63       4.057  46.399   1.562  1.00 11.71           C  
ATOM    502  CG  LYS A  63       3.018  47.000   2.499  1.00 13.73           C  
ATOM    503  CD  LYS A  63       2.341  48.247   1.917  1.00 15.06           C  
ATOM    504  CE  LYS A  63       3.277  49.449   1.857  1.00 20.17           C  
ATOM    505  NZ  LYS A  63       2.473  50.715   1.747  1.00 23.19           N  
ATOM    506  N   HIS A  64       3.123  43.515   0.866  1.00  9.31           N  
ATOM    507  CA  HIS A  64       2.058  42.524   0.836  1.00  9.15           C  
ATOM    508  C   HIS A  64       2.505  41.191   1.442  1.00  8.58           C  
ATOM    509  O   HIS A  64       1.705  40.485   2.082  1.00  8.69           O  
ATOM    510  CB  HIS A  64       1.481  42.313  -0.556  1.00  9.26           C  
ATOM    511  CG  HIS A  64       0.269  41.447  -0.539  1.00 10.27           C  
ATOM    512  ND1 HIS A  64      -0.901  41.836   0.072  1.00 10.42           N  
ATOM    513  CD2 HIS A  64       0.067  40.183  -0.981  1.00 10.63           C  
ATOM    514  CE1 HIS A  64      -1.791  40.862  -0.034  1.00 11.73           C  
ATOM    515  NE2 HIS A  64      -1.225  39.847  -0.662  1.00 10.53           N  
ATOM    516  N   GLY A  65       3.781  40.861   1.242  1.00  8.24           N  
ATOM    517  CA  GLY A  65       4.384  39.676   1.859  1.00  8.45           C  
ATOM    518  C   GLY A  65       4.214  39.703   3.365  1.00  8.56           C  
ATOM    519  O   GLY A  65       3.803  38.703   3.982  1.00  8.20           O  
ATOM    520  N   ALA A  66       4.521  40.854   3.955  1.00  8.35           N  
ATOM    521  CA  ALA A  66       4.316  41.063   5.389  1.00  9.12           C  
ATOM    522  C   ALA A  66       2.847  40.870   5.814  1.00  9.34           C  
ATOM    523  O   ALA A  66       2.566  40.225   6.831  1.00  9.94           O  
ATOM    524  CB  ALA A  66       4.810  42.443   5.775  1.00  9.21           C  
ATOM    525  N   THR A  67       1.916  41.425   5.042  1.00  9.51           N  
ATOM    526  CA  THR A  67       0.484  41.274   5.314  1.00  9.87           C  
ATOM    527  C   THR A  67       0.065  39.797   5.341  1.00  9.25           C  
ATOM    528  O   THR A  67      -0.648  39.353   6.251  1.00  9.83           O  
ATOM    529  CB  THR A  67      -0.342  42.072   4.289  1.00  9.66           C  
ATOM    530  OG1 THR A  67      -0.074  43.469   4.479  1.00 11.50           O  
ATOM    531  CG2 THR A  67      -1.857  41.815   4.447  1.00 10.16           C  
ATOM    532  N   VAL A  68       0.527  39.040   4.353  1.00  8.44           N  
ATOM    533  CA  VAL A  68       0.223  37.613   4.272  1.00  8.58           C  
ATOM    534  C   VAL A  68       0.723  36.867   5.520  1.00  8.36           C  
ATOM    535  O   VAL A  68      -0.042  36.152   6.161  1.00  8.66           O  
ATOM    536  CB  VAL A  68       0.795  36.992   2.974  1.00  8.65           C  
ATOM    537  CG1 VAL A  68       0.681  35.457   2.974  1.00  9.48           C  
ATOM    538  CG2 VAL A  68       0.093  37.577   1.769  1.00  8.33           C  
ATOM    539  N   LEU A  69       1.989  37.057   5.881  1.00  8.11           N  
ATOM    540  CA  LEU A  69       2.542  36.315   7.013  1.00  8.64           C  
ATOM    541  C   LEU A  69       1.987  36.754   8.370  1.00  8.86           C  
ATOM    542  O   LEU A  69       1.834  35.939   9.280  1.00  9.00           O  
ATOM    543  CB  LEU A  69       4.070  36.328   6.993  1.00  8.19           C  
ATOM    544  CG  LEU A  69       4.701  35.574   5.812  1.00  9.45           C  
ATOM    545  CD1 LEU A  69       6.178  35.364   6.062  1.00 12.26           C  
ATOM    546  CD2 LEU A  69       4.021  34.231   5.546  1.00 11.60           C  
ATOM    547  N   THR A  70       1.676  38.039   8.497  1.00  9.30           N  
ATOM    548  CA  THR A  70       1.013  38.554   9.700  1.00  9.75           C  
ATOM    549  C   THR A  70      -0.351  37.872   9.898  1.00  9.27           C  
ATOM    550  O   THR A  70      -0.683  37.449  11.014  1.00  9.19           O  
ATOM    551  CB  THR A  70       0.872  40.088   9.631  1.00 10.08           C  
ATOM    552  OG1 THR A  70       2.182  40.669   9.669  1.00 11.85           O  
ATOM    553  CG2 THR A  70       0.051  40.632  10.802  1.00 11.00           C  
ATOM    554  N   ALA A  71      -1.127  37.752   8.819  1.00  8.84           N  
ATOM    555  CA  ALA A  71      -2.439  37.092   8.889  1.00  9.08           C  
ATOM    556  C   ALA A  71      -2.288  35.613   9.226  1.00  8.94           C  
ATOM    557  O   ALA A  71      -3.031  35.070  10.039  1.00  8.87           O  
ATOM    558  CB  ALA A  71      -3.204  37.269   7.584  1.00  8.79           C  
ATOM    559  N   LEU A  72      -1.314  34.960   8.592  1.00  9.00           N  
ATOM    560  CA  LEU A  72      -1.032  33.558   8.877  1.00  8.79           C  
ATOM    561  C   LEU A  72      -0.589  33.336  10.332  1.00  9.05           C  
ATOM    562  O   LEU A  72      -1.041  32.393  10.982  1.00  9.25           O  
ATOM    563  CB  LEU A  72      -0.006  32.997   7.882  1.00  9.18           C  
ATOM    564  CG  LEU A  72       0.316  31.513   8.073  1.00  8.62           C  
ATOM    565  CD1 LEU A  72      -0.915  30.623   7.912  1.00  9.39           C  
ATOM    566  CD2 LEU A  72       1.430  31.074   7.125  1.00 10.02           C  
ATOM    567  N   GLY A  73       0.273  34.215  10.841  1.00  9.23           N  
ATOM    568  CA  GLY A  73       0.694  34.179  12.250  1.00  9.68           C  
ATOM    569  C   GLY A  73      -0.485  34.237  13.208  1.00  9.86           C  
ATOM    570  O   GLY A  73      -0.530  33.493  14.205  1.00 10.19           O  
ATOM    571  N   GLY A  74      -1.448  35.103  12.900  1.00 10.04           N  
ATOM    572  CA  GLY A  74      -2.670  35.231  13.702  1.00 10.32           C  
ATOM    573  C   GLY A  74      -3.437  33.920  13.767  1.00 10.26           C  
ATOM    574  O   GLY A  74      -3.961  33.544  14.814  1.00 11.04           O  
ATOM    575  N   ILE A  75      -3.500  33.223  12.639  1.00  9.37           N  
ATOM    576  CA  ILE A  75      -4.178  31.940  12.553  1.00  9.47           C  
ATOM    577  C   ILE A  75      -3.422  30.861  13.345  1.00  9.21           C  
ATOM    578  O   ILE A  75      -4.022  30.107  14.110  1.00  9.16           O  
ATOM    579  CB  ILE A  75      -4.369  31.507  11.074  1.00  9.59           C  
ATOM    580  CG1 ILE A  75      -5.396  32.416  10.384  1.00  9.47           C  
ATOM    581  CG2 ILE A  75      -4.773  30.043  10.982  1.00  9.66           C  
ATOM    582  CD1 ILE A  75      -5.371  32.336   8.851  1.00 10.38           C  
ATOM    583  N   LEU A  76      -2.103  30.805  13.175  1.00  9.01           N  
ATOM    584  CA  LEU A  76      -1.300  29.777  13.835  1.00  9.49           C  
ATOM    585  C   LEU A  76      -1.363  29.884  15.358  1.00  9.45           C  
ATOM    586  O   LEU A  76      -1.392  28.866  16.055  1.00  9.16           O  
ATOM    587  CB  LEU A  76       0.156  29.817  13.348  1.00  9.45           C  
ATOM    588  CG  LEU A  76       0.380  29.460  11.869  1.00  9.88           C  
ATOM    589  CD1 LEU A  76       1.827  29.704  11.498  1.00 10.63           C  
ATOM    590  CD2 LEU A  76      -0.015  28.016  11.542  1.00  9.91           C  
ATOM    591  N   LYS A  77      -1.418  31.113  15.862  1.00 10.50           N  
ATOM    592  CA  LYS A  77      -1.395  31.341  17.305  1.00 11.23           C  
ATOM    593  C   LYS A  77      -2.684  30.880  17.987  1.00 11.58           C  
ATOM    594  O   LYS A  77      -2.735  30.759  19.216  1.00 11.76           O  
ATOM    595  CB  LYS A  77      -1.120  32.809  17.609  1.00 11.75           C  
ATOM    596  CG  LYS A  77       0.335  33.187  17.395  1.00 14.13           C  
ATOM    597  CD  LYS A  77       0.530  34.671  17.475  1.00 17.54           C  
ATOM    598  CE  LYS A  77       1.929  35.053  17.050  1.00 19.08           C  
ATOM    599  NZ  LYS A  77       1.977  36.529  16.831  1.00 21.43           N  
ATOM    600  N   LYS A  78      -3.715  30.610  17.184  1.00 11.64           N  
ATOM    601  CA  LYS A  78      -4.981  30.070  17.696  1.00 11.91           C  
ATOM    602  C   LYS A  78      -5.004  28.539  17.672  1.00 12.01           C  
ATOM    603  O   LYS A  78      -6.019  27.924  18.024  1.00 11.76           O  
ATOM    604  CB  LYS A  78      -6.173  30.626  16.898  1.00 12.18           C  
ATOM    605  CG  LYS A  78      -6.392  32.134  17.019  1.00 15.09           C  
ATOM    606  CD  LYS A  78      -6.662  32.565  18.453  1.00 19.63           C  
ATOM    607  CE  LYS A  78      -6.920  34.060  18.531  1.00 21.25           C  
ATOM    608  NZ  LYS A  78      -6.567  34.591  19.881  1.00 24.11           N  
ATOM    609  N   LYS A  79      -3.897  27.921  17.248  1.00 11.96           N  
ATOM    610  CA  LYS A  79      -3.770  26.468  17.281  1.00 12.71           C  
ATOM    611  C   LYS A  79      -4.976  25.784  16.609  1.00 13.25           C  
ATOM    612  O   LYS A  79      -5.317  26.114  15.477  1.00 12.98           O  
ATOM    613  CB  LYS A  79      -3.527  25.987  18.727  1.00 12.90           C  
ATOM    614  CG  LYS A  79      -2.245  26.568  19.340  1.00 13.61           C  
ATOM    615  CD  LYS A  79      -2.211  26.463  20.855  1.00 16.90           C  
ATOM    616  CE  LYS A  79      -1.679  25.138  21.334  1.00 17.56           C  
ATOM    617  NZ  LYS A  79      -1.646  25.098  22.832  1.00 15.93           N  
ATOM    618  N   GLY A  80      -5.628  24.853  17.303  1.00 13.84           N  
ATOM    619  CA  GLY A  80      -6.727  24.094  16.708  1.00 14.76           C  
ATOM    620  C   GLY A  80      -8.070  24.808  16.611  1.00 15.30           C  
ATOM    621  O   GLY A  80      -8.987  24.304  15.947  1.00 16.87           O  
ATOM    622  N   HIS A  81      -8.193  25.965  17.262  1.00 14.47           N  
ATOM    623  CA  HIS A  81      -9.461  26.704  17.343  1.00 14.12           C  
ATOM    624  C   HIS A  81      -9.377  28.043  16.607  1.00 13.77           C  
ATOM    625  O   HIS A  81      -9.377  29.116  17.222  1.00 13.00           O  
ATOM    626  CB  HIS A  81      -9.883  26.898  18.809  1.00 14.06           C  
ATOM    627  CG  HIS A  81      -8.781  27.379  19.706  1.00 14.30           C  
ATOM    628  ND1 HIS A  81      -8.578  28.714  19.984  1.00 14.75           N  
ATOM    629  CD2 HIS A  81      -7.828  26.701  20.391  1.00 14.97           C  
ATOM    630  CE1 HIS A  81      -7.545  28.838  20.801  1.00 15.25           C  
ATOM    631  NE2 HIS A  81      -7.073  27.631  21.062  1.00 15.14           N  
ATOM    632  N   HIS A  82      -9.307  27.965  15.280  1.00 13.62           N  
ATOM    633  CA  HIS A  82      -9.025  29.140  14.455  1.00 13.79           C  
ATOM    634  C   HIS A  82     -10.128  29.532  13.458  1.00 14.24           C  
ATOM    635  O   HIS A  82      -9.861  30.255  12.499  1.00 13.80           O  
ATOM    636  CB  HIS A  82      -7.692  28.950  13.709  1.00 13.37           C  
ATOM    637  CG  HIS A  82      -7.664  27.750  12.810  1.00 14.01           C  
ATOM    638  ND1 HIS A  82      -6.492  27.128  12.442  1.00 13.41           N  
ATOM    639  CD2 HIS A  82      -8.662  27.048  12.224  1.00 14.39           C  
ATOM    640  CE1 HIS A  82      -6.767  26.100  11.660  1.00 14.11           C  
ATOM    641  NE2 HIS A  82      -8.076  26.030  11.510  1.00 14.09           N  
ATOM    642  N   GLU A  83     -11.357  29.074  13.683  1.00 14.79           N  
ATOM    643  CA  GLU A  83     -12.445  29.376  12.748  1.00 15.82           C  
ATOM    644  C   GLU A  83     -12.726  30.862  12.570  1.00 15.95           C  
ATOM    645  O   GLU A  83     -12.975  31.315  11.449  1.00 16.03           O  
ATOM    646  CB  GLU A  83     -13.724  28.613  13.112  1.00 16.47           C  
ATOM    647  CG  GLU A  83     -13.680  27.156  12.707  1.00 19.33           C  
ATOM    648  CD  GLU A  83     -13.296  26.969  11.243  1.00 23.83           C  
ATOM    649  OE1 GLU A  83     -13.879  27.657  10.372  1.00 23.56           O  
ATOM    650  OE2 GLU A  83     -12.400  26.137  10.972  1.00 27.36           O  
ATOM    651  N   ALA A  84     -12.664  31.626  13.661  1.00 15.49           N  
ATOM    652  CA  ALA A  84     -12.920  33.063  13.590  1.00 15.78           C  
ATOM    653  C   ALA A  84     -11.922  33.789  12.688  1.00 15.68           C  
ATOM    654  O   ALA A  84     -12.286  34.761  12.025  1.00 16.07           O  
ATOM    655  CB  ALA A  84     -12.936  33.687  14.991  1.00 16.01           C  
ATOM    656  N   GLU A  85     -10.672  33.326  12.672  1.00 15.44           N  
ATOM    657  CA  GLU A  85      -9.626  33.944  11.855  1.00 15.99           C  
ATOM    658  C   GLU A  85      -9.699  33.477  10.408  1.00 15.61           C  
ATOM    659  O   GLU A  85      -9.424  34.250   9.490  1.00 15.97           O  
ATOM    660  CB  GLU A  85      -8.233  33.653  12.425  1.00 16.35           C  
ATOM    661  CG  GLU A  85      -7.921  34.372  13.730  1.00 19.13           C  
ATOM    662  CD  GLU A  85      -8.703  33.819  14.913  1.00 21.85           C  
ATOM    663  OE1 GLU A  85      -9.140  32.649  14.860  1.00 23.41           O  
ATOM    664  OE2 GLU A  85      -8.886  34.560  15.902  1.00 24.55           O  
ATOM    665  N   ILE A  86     -10.074  32.215  10.203  1.00 15.14           N  
ATOM    666  CA  ILE A  86     -10.168  31.662   8.846  1.00 14.90           C  
ATOM    667  C   ILE A  86     -11.391  32.173   8.057  1.00 14.27           C  
ATOM    668  O   ILE A  86     -11.285  32.445   6.860  1.00 13.58           O  
ATOM    669  CB  ILE A  86     -10.042  30.118   8.848  1.00 15.37           C  
ATOM    670  CG1 ILE A  86      -8.556  29.745   8.963  1.00 17.14           C  
ATOM    671  CG2 ILE A  86     -10.693  29.487   7.600  1.00 15.89           C  
ATOM    672  CD1 ILE A  86      -8.242  28.274   8.886  1.00 19.37           C  
ATOM    673  N   LYS A  87     -12.533  32.322   8.730  1.00 13.81           N  
ATOM    674  CA  LYS A  87     -13.794  32.686   8.055  1.00 14.13           C  
ATOM    675  C   LYS A  87     -13.680  33.901   7.113  1.00 12.82           C  
ATOM    676  O   LYS A  87     -13.989  33.773   5.932  1.00 12.42           O  
ATOM    677  CB  LYS A  87     -14.935  32.883   9.069  1.00 14.28           C  
ATOM    678  CG  LYS A  87     -16.324  32.972   8.441  1.00 16.95           C  
ATOM    679  CD  LYS A  87     -17.354  33.502   9.445  1.00 17.31           C  
ATOM    680  CE  LYS A  87     -18.716  33.709   8.779  1.00 21.92           C  
ATOM    681  NZ  LYS A  87     -19.748  34.148   9.771  1.00 25.58           N  
ATOM    682  N   PRO A  88     -13.243  35.070   7.626  1.00 12.41           N  
ATOM    683  CA  PRO A  88     -13.185  36.225   6.719  1.00 11.95           C  
ATOM    684  C   PRO A  88     -12.173  36.056   5.577  1.00 10.85           C  
ATOM    685  O   PRO A  88     -12.391  36.561   4.477  1.00 10.50           O  
ATOM    686  CB  PRO A  88     -12.786  37.382   7.641  1.00 12.36           C  
ATOM    687  CG  PRO A  88     -12.140  36.757   8.801  1.00 14.01           C  
ATOM    688  CD  PRO A  88     -12.819  35.435   8.992  1.00 12.90           C  
ATOM    689  N   LEU A  89     -11.078  35.350   5.844  1.00 10.79           N  
ATOM    690  CA  LEU A  89     -10.064  35.088   4.822  1.00 10.31           C  
ATOM    691  C   LEU A  89     -10.600  34.154   3.728  1.00 10.06           C  
ATOM    692  O   LEU A  89     -10.374  34.374   2.534  1.00  9.91           O  
ATOM    693  CB  LEU A  89      -8.809  34.492   5.470  1.00 11.04           C  
ATOM    694  CG  LEU A  89      -7.512  34.620   4.674  1.00 12.48           C  
ATOM    695  CD1 LEU A  89      -6.998  36.079   4.706  1.00 14.12           C  
ATOM    696  CD2 LEU A  89      -6.469  33.646   5.226  1.00 14.56           C  
ATOM    697  N   ALA A  90     -11.313  33.108   4.139  1.00 10.11           N  
ATOM    698  CA  ALA A  90     -11.971  32.207   3.192  1.00 10.40           C  
ATOM    699  C   ALA A  90     -12.989  32.970   2.336  1.00 10.97           C  
ATOM    700  O   ALA A  90     -13.055  32.788   1.123  1.00 11.13           O  
ATOM    701  CB  ALA A  90     -12.641  31.056   3.941  1.00 10.37           C  
ATOM    702  N   GLN A  91     -13.759  33.843   2.984  1.00 10.97           N  
ATOM    703  CA  GLN A  91     -14.745  34.680   2.313  1.00 12.29           C  
ATOM    704  C   GLN A  91     -14.110  35.542   1.217  1.00 11.37           C  
ATOM    705  O   GLN A  91     -14.543  35.505   0.069  1.00 11.85           O  
ATOM    706  CB  GLN A  91     -15.441  35.572   3.343  1.00 13.15           C  
ATOM    707  CG  GLN A  91     -16.572  36.405   2.778  1.00 17.62           C  
ATOM    708  CD  GLN A  91     -17.918  35.731   2.917  1.00 23.84           C  
ATOM    709  OE1 GLN A  91     -18.347  35.387   4.028  1.00 26.86           O  
ATOM    710  NE2 GLN A  91     -18.603  35.545   1.791  1.00 26.31           N  
ATOM    711  N   SER A  92     -13.082  36.314   1.567  1.00 10.42           N  
ATOM    712  CA  SER A  92     -12.450  37.190   0.586  1.00  9.96           C  
ATOM    713  C   SER A  92     -11.731  36.413  -0.517  1.00 10.16           C  
ATOM    714  O   SER A  92     -11.762  36.807  -1.680  1.00  9.80           O  
ATOM    715  CB  SER A  92     -11.491  38.168   1.254  1.00 10.44           C  
ATOM    716  OG  SER A  92     -10.350  37.489   1.753  1.00  9.16           O  
ATOM    717  N   HIS A  93     -11.096  35.303  -0.149  1.00  9.52           N  
ATOM    718  CA  HIS A  93     -10.293  34.555  -1.108  1.00  9.90           C  
ATOM    719  C   HIS A  93     -11.121  33.695  -2.052  1.00 11.13           C  
ATOM    720  O   HIS A  93     -10.725  33.490  -3.196  1.00 11.73           O  
ATOM    721  CB  HIS A  93      -9.171  33.789  -0.406  1.00  9.41           C  
ATOM    722  CG  HIS A  93      -8.032  34.677  -0.012  1.00  7.63           C  
ATOM    723  ND1 HIS A  93      -8.175  35.699   0.902  1.00  8.00           N  
ATOM    724  CD2 HIS A  93      -6.746  34.730  -0.438  1.00  7.57           C  
ATOM    725  CE1 HIS A  93      -7.020  36.330   1.039  1.00  7.25           C  
ATOM    726  NE2 HIS A  93      -6.139  35.764   0.233  1.00  7.52           N  
ATOM    727  N   ALA A  94     -12.281  33.237  -1.582  1.00 12.29           N  
ATOM    728  CA  ALA A  94     -13.230  32.555  -2.454  1.00 13.63           C  
ATOM    729  C   ALA A  94     -13.925  33.537  -3.394  1.00 14.61           C  
ATOM    730  O   ALA A  94     -13.829  33.408  -4.613  1.00 15.97           O  
ATOM    731  CB  ALA A  94     -14.263  31.774  -1.633  1.00 13.63           C  
ATOM    732  N   THR A  95     -14.595  34.535  -2.827  1.00 15.46           N  
ATOM    733  CA  THR A  95     -15.565  35.322  -3.587  1.00 16.48           C  
ATOM    734  C   THR A  95     -14.956  36.486  -4.368  1.00 16.40           C  
ATOM    735  O   THR A  95     -15.440  36.826  -5.454  1.00 16.85           O  
ATOM    736  CB  THR A  95     -16.738  35.816  -2.691  1.00 16.84           C  
ATOM    737  OG1 THR A  95     -16.287  36.854  -1.816  1.00 19.21           O  
ATOM    738  CG2 THR A  95     -17.317  34.669  -1.865  1.00 17.83           C  
ATOM    739  N   LYS A  96     -13.904  37.097  -3.825  1.00 15.03           N  
ATOM    740  CA  LYS A  96     -13.311  38.276  -4.460  1.00 14.86           C  
ATOM    741  C   LYS A  96     -12.033  37.953  -5.227  1.00 14.01           C  
ATOM    742  O   LYS A  96     -11.902  38.314  -6.400  1.00 14.49           O  
ATOM    743  CB  LYS A  96     -13.067  39.396  -3.434  1.00 15.16           C  
ATOM    744  CG  LYS A  96     -14.297  39.769  -2.604  1.00 17.60           C  
ATOM    745  CD  LYS A  96     -15.473  40.229  -3.468  1.00 21.86           C  
ATOM    746  CE  LYS A  96     -16.735  40.401  -2.626  1.00 23.35           C  
ATOM    747  NZ  LYS A  96     -17.947  40.634  -3.466  1.00 26.09           N  
ATOM    748  N   HIS A  97     -11.088  37.280  -4.575  1.00 13.08           N  
ATOM    749  CA  HIS A  97      -9.804  37.002  -5.215  1.00 12.18           C  
ATOM    750  C   HIS A  97      -9.836  35.739  -6.071  1.00 12.41           C  
ATOM    751  O   HIS A  97      -8.983  35.569  -6.951  1.00 12.39           O  
ATOM    752  CB  HIS A  97      -8.682  36.927  -4.175  1.00 12.06           C  
ATOM    753  CG  HIS A  97      -8.642  38.111  -3.261  1.00 11.41           C  
ATOM    754  ND1 HIS A  97      -8.722  39.409  -3.718  1.00 10.91           N  
ATOM    755  CD2 HIS A  97      -8.547  38.192  -1.912  1.00 11.27           C  
ATOM    756  CE1 HIS A  97      -8.672  40.240  -2.691  1.00 11.74           C  
ATOM    757  NE2 HIS A  97      -8.567  39.526  -1.585  1.00 10.83           N  
ATOM    758  N   LYS A  98     -10.803  34.865  -5.788  1.00 12.38           N  
ATOM    759  CA  LYS A  98     -11.048  33.647  -6.579  1.00 13.16           C  
ATOM    760  C   LYS A  98      -9.834  32.713  -6.569  1.00 12.79           C  
ATOM    761  O   LYS A  98      -9.293  32.333  -7.616  1.00 12.96           O  
ATOM    762  CB  LYS A  98     -11.496  34.011  -8.002  1.00 14.00           C  
ATOM    763  CG  LYS A  98     -12.800  34.813  -8.019  1.00 16.80           C  
ATOM    764  CD  LYS A  98     -13.157  35.307  -9.403  1.00 21.03           C  
ATOM    765  CE  LYS A  98     -14.344  36.262  -9.335  1.00 23.31           C  
ATOM    766  NZ  LYS A  98     -14.656  36.855 -10.666  1.00 25.50           N  
ATOM    767  N   ILE A  99      -9.423  32.337  -5.364  1.00 11.96           N  
ATOM    768  CA  ILE A  99      -8.209  31.561  -5.178  1.00 11.49           C  
ATOM    769  C   ILE A  99      -8.514  30.073  -4.978  1.00 11.29           C  
ATOM    770  O   ILE A  99      -9.104  29.689  -3.968  1.00 12.00           O  
ATOM    771  CB  ILE A  99      -7.358  32.102  -3.989  1.00 11.14           C  
ATOM    772  CG1 ILE A  99      -7.031  33.600  -4.160  1.00 11.39           C  
ATOM    773  CG2 ILE A  99      -6.081  31.274  -3.828  1.00 11.11           C  
ATOM    774  CD1 ILE A  99      -6.424  33.979  -5.520  1.00 10.67           C  
ATOM    775  N   PRO A 100      -8.101  29.222  -5.936  1.00 11.31           N  
ATOM    776  CA  PRO A 100      -8.351  27.780  -5.771  1.00 11.17           C  
ATOM    777  C   PRO A 100      -7.529  27.208  -4.623  1.00 10.95           C  
ATOM    778  O   PRO A 100      -6.475  27.755  -4.294  1.00 10.64           O  
ATOM    779  CB  PRO A 100      -7.911  27.174  -7.111  1.00 11.75           C  
ATOM    780  CG  PRO A 100      -7.036  28.186  -7.743  1.00 11.57           C  
ATOM    781  CD  PRO A 100      -7.394  29.543  -7.191  1.00 11.03           C  
ATOM    782  N   VAL A 101      -8.015  26.122  -4.022  1.00 10.76           N  
ATOM    783  CA  VAL A 101      -7.311  25.459  -2.924  1.00 11.29           C  
ATOM    784  C   VAL A 101      -5.891  25.030  -3.340  1.00 10.74           C  
ATOM    785  O   VAL A 101      -4.961  25.098  -2.529  1.00 10.51           O  
ATOM    786  CB  VAL A 101      -8.125  24.263  -2.362  1.00 11.64           C  
ATOM    787  CG1 VAL A 101      -7.339  23.519  -1.309  1.00 12.90           C  
ATOM    788  CG2 VAL A 101      -9.449  24.753  -1.784  1.00 12.86           C  
ATOM    789  N   LYS A 102      -5.722  24.618  -4.601  1.00 10.21           N  
ATOM    790  CA  LYS A 102      -4.395  24.261  -5.116  1.00 10.37           C  
ATOM    791  C   LYS A 102      -3.364  25.368  -4.876  1.00  9.79           C  
ATOM    792  O   LYS A 102      -2.204  25.084  -4.539  1.00 10.30           O  
ATOM    793  CB  LYS A 102      -4.455  23.936  -6.609  1.00 10.80           C  
ATOM    794  CG  LYS A 102      -3.161  23.359  -7.184  1.00 12.67           C  
ATOM    795  CD  LYS A 102      -3.182  23.365  -8.708  1.00 16.24           C  
ATOM    796  CE  LYS A 102      -4.089  22.282  -9.267  1.00 19.45           C  
ATOM    797  NZ  LYS A 102      -4.149  22.355 -10.751  1.00 19.55           N  
ATOM    798  N   TYR A 103      -3.782  26.625  -5.020  1.00  8.95           N  
ATOM    799  CA  TYR A 103      -2.843  27.740  -4.863  1.00  8.88           C  
ATOM    800  C   TYR A 103      -2.433  27.896  -3.402  1.00  8.63           C  
ATOM    801  O   TYR A 103      -1.345  28.397  -3.113  1.00  8.23           O  
ATOM    802  CB  TYR A 103      -3.405  29.049  -5.414  1.00  9.45           C  
ATOM    803  CG  TYR A 103      -3.542  29.118  -6.929  1.00 10.17           C  
ATOM    804  CD1 TYR A 103      -3.398  27.978  -7.730  1.00 11.34           C  
ATOM    805  CD2 TYR A 103      -3.855  30.328  -7.555  1.00 11.27           C  
ATOM    806  CE1 TYR A 103      -3.550  28.050  -9.121  1.00 12.60           C  
ATOM    807  CE2 TYR A 103      -4.009  30.410  -8.942  1.00 12.29           C  
ATOM    808  CZ  TYR A 103      -3.855  29.265  -9.712  1.00 11.49           C  
ATOM    809  OH  TYR A 103      -4.004  29.330 -11.081  1.00 12.60           O  
ATOM    810  N   LEU A 104      -3.309  27.467  -2.486  1.00  8.63           N  
ATOM    811  CA  LEU A 104      -2.964  27.458  -1.062  1.00  9.05           C  
ATOM    812  C   LEU A 104      -1.925  26.381  -0.767  1.00  9.23           C  
ATOM    813  O   LEU A 104      -1.072  26.565   0.100  1.00  9.33           O  
ATOM    814  CB  LEU A 104      -4.204  27.265  -0.187  1.00  9.07           C  
ATOM    815  CG  LEU A 104      -5.307  28.321  -0.310  1.00  9.66           C  
ATOM    816  CD1 LEU A 104      -6.468  27.928   0.586  1.00 11.86           C  
ATOM    817  CD2 LEU A 104      -4.802  29.715   0.056  1.00 10.45           C  
ATOM    818  N   GLU A 105      -1.992  25.269  -1.498  1.00  9.51           N  
ATOM    819  CA  GLU A 105      -0.943  24.248  -1.446  1.00 10.90           C  
ATOM    820  C   GLU A 105       0.388  24.828  -1.944  1.00  9.54           C  
ATOM    821  O   GLU A 105       1.421  24.657  -1.297  1.00  8.74           O  
ATOM    822  CB  GLU A 105      -1.340  23.009  -2.262  1.00 10.86           C  
ATOM    823  CG  GLU A 105      -2.739  22.481  -1.933  1.00 14.24           C  
ATOM    824  CD  GLU A 105      -3.127  21.213  -2.686  1.00 15.05           C  
ATOM    825  OE1 GLU A 105      -2.392  20.786  -3.606  1.00 21.07           O  
ATOM    826  OE2 GLU A 105      -4.195  20.651  -2.350  1.00 21.32           O  
ATOM    827  N   PHE A 106       0.352  25.538  -3.070  1.00  8.63           N  
ATOM    828  CA  PHE A 106       1.569  26.160  -3.613  1.00  7.90           C  
ATOM    829  C   PHE A 106       2.212  27.120  -2.613  1.00  7.65           C  
ATOM    830  O   PHE A 106       3.428  27.099  -2.423  1.00  7.70           O  
ATOM    831  CB  PHE A 106       1.282  26.930  -4.910  1.00  8.09           C  
ATOM    832  CG  PHE A 106       0.879  26.063  -6.087  1.00  9.03           C  
ATOM    833  CD1 PHE A 106       1.162  24.698  -6.124  1.00 10.59           C  
ATOM    834  CD2 PHE A 106       0.263  26.652  -7.189  1.00  9.77           C  
ATOM    835  CE1 PHE A 106       0.802  23.924  -7.238  1.00 10.94           C  
ATOM    836  CE2 PHE A 106      -0.098  25.883  -8.306  1.00 10.71           C  
ATOM    837  CZ  PHE A 106       0.175  24.530  -8.324  1.00 10.03           C  
ATOM    838  N   ILE A 107       1.416  27.985  -1.989  1.00  7.19           N  
ATOM    839  CA  ILE A 107       2.008  28.949  -1.065  1.00  7.50           C  
ATOM    840  C   ILE A 107       2.508  28.255   0.205  1.00  7.79           C  
ATOM    841  O   ILE A 107       3.486  28.692   0.797  1.00  7.76           O  
ATOM    842  CB  ILE A 107       1.098  30.157  -0.752  1.00  7.34           C  
ATOM    843  CG1 ILE A 107       1.943  31.315  -0.209  1.00  7.43           C  
ATOM    844  CG2 ILE A 107      -0.032  29.771   0.239  1.00  7.22           C  
ATOM    845  CD1 ILE A 107       1.171  32.637  -0.047  1.00  7.57           C  
ATOM    846  N   SER A 108       1.853  27.161   0.604  1.00  7.69           N  
ATOM    847  CA  SER A 108       2.344  26.356   1.731  1.00  8.48           C  
ATOM    848  C   SER A 108       3.749  25.804   1.468  1.00  8.54           C  
ATOM    849  O   SER A 108       4.632  25.876   2.326  1.00  8.76           O  
ATOM    850  CB  SER A 108       1.363  25.222   2.039  1.00  8.53           C  
ATOM    851  OG  SER A 108       0.119  25.764   2.448  1.00  9.96           O  
ATOM    852  N   GLU A 109       3.956  25.272   0.268  1.00  9.23           N  
ATOM    853  CA  GLU A 109       5.267  24.759  -0.137  1.00 10.98           C  
ATOM    854  C   GLU A 109       6.319  25.871  -0.114  1.00  9.43           C  
ATOM    855  O   GLU A 109       7.454  25.662   0.365  1.00  9.74           O  
ATOM    856  CB  GLU A 109       5.187  24.116  -1.529  1.00 10.96           C  
ATOM    857  CG  GLU A 109       4.274  22.893  -1.594  1.00 14.43           C  
ATOM    858  CD  GLU A 109       4.041  22.391  -3.016  1.00 15.56           C  
ATOM    859  OE1 GLU A 109       4.628  22.946  -3.975  1.00 22.37           O  
ATOM    860  OE2 GLU A 109       3.270  21.422  -3.172  1.00 22.75           O  
ATOM    861  N   ALA A 110       5.936  27.057  -0.596  1.00  8.22           N  
ATOM    862  CA  ALA A 110       6.836  28.222  -0.598  1.00  7.28           C  
ATOM    863  C   ALA A 110       7.237  28.595   0.825  1.00  6.88           C  
ATOM    864  O   ALA A 110       8.406  28.874   1.089  1.00  6.99           O  
ATOM    865  CB  ALA A 110       6.193  29.416  -1.311  1.00  7.81           C  
ATOM    866  N   ILE A 111       6.264  28.594   1.738  1.00  6.43           N  
ATOM    867  CA  ILE A 111       6.540  28.877   3.152  1.00  6.71           C  
ATOM    868  C   ILE A 111       7.548  27.879   3.741  1.00  7.18           C  
ATOM    869  O   ILE A 111       8.534  28.279   4.370  1.00  7.64           O  
ATOM    870  CB  ILE A 111       5.240  28.956   3.973  1.00  5.94           C  
ATOM    871  CG1 ILE A 111       4.424  30.180   3.512  1.00  6.84           C  
ATOM    872  CG2 ILE A 111       5.540  29.053   5.471  1.00  7.74           C  
ATOM    873  CD1 ILE A 111       2.966  30.149   3.916  1.00  6.39           C  
ATOM    874  N   ILE A 112       7.324  26.591   3.496  1.00  7.51           N  
ATOM    875  CA  ILE A 112       8.237  25.562   4.002  1.00  8.11           C  
ATOM    876  C   ILE A 112       9.652  25.796   3.476  1.00  8.22           C  
ATOM    877  O   ILE A 112      10.627  25.757   4.237  1.00  8.40           O  
ATOM    878  CB  ILE A 112       7.743  24.139   3.637  1.00  8.58           C  
ATOM    879  CG1 ILE A 112       6.417  23.832   4.357  1.00  9.84           C  
ATOM    880  CG2 ILE A 112       8.815  23.080   3.953  1.00  9.43           C  
ATOM    881  CD1 ILE A 112       6.499  23.878   5.871  1.00 11.30           C  
ATOM    882  N   GLN A 113       9.754  26.049   2.176  1.00  8.75           N  
ATOM    883  CA  GLN A 113      11.058  26.288   1.538  1.00  9.66           C  
ATOM    884  C   GLN A 113      11.803  27.481   2.132  1.00  9.45           C  
ATOM    885  O   GLN A 113      13.016  27.407   2.372  1.00  9.74           O  
ATOM    886  CB  GLN A 113      10.896  26.452   0.032  1.00 10.66           C  
ATOM    887  CG  GLN A 113      10.506  25.161  -0.661  1.00 13.48           C  
ATOM    888  CD  GLN A 113      10.460  25.303  -2.165  1.00 19.05           C  
ATOM    889  OE1 GLN A 113      11.012  26.255  -2.725  1.00 22.21           O  
ATOM    890  NE2 GLN A 113       9.814  24.349  -2.833  1.00 21.06           N  
ATOM    891  N   VAL A 114      11.076  28.567   2.385  1.00  8.86           N  
ATOM    892  CA  VAL A 114      11.661  29.777   2.962  1.00  9.20           C  
ATOM    893  C   VAL A 114      12.136  29.505   4.388  1.00  9.05           C  
ATOM    894  O   VAL A 114      13.207  29.958   4.790  1.00  8.92           O  
ATOM    895  CB  VAL A 114      10.675  30.955   2.899  1.00  9.47           C  
ATOM    896  CG1 VAL A 114      11.166  32.146   3.734  1.00 10.40           C  
ATOM    897  CG2 VAL A 114      10.474  31.358   1.444  1.00 10.10           C  
ATOM    898  N   LEU A 115      11.349  28.747   5.145  1.00  8.95           N  
ATOM    899  CA  LEU A 115      11.752  28.408   6.506  1.00 10.10           C  
ATOM    900  C   LEU A 115      13.008  27.528   6.519  1.00 10.49           C  
ATOM    901  O   LEU A 115      13.901  27.723   7.345  1.00 10.88           O  
ATOM    902  CB  LEU A 115      10.600  27.742   7.257  1.00 10.12           C  
ATOM    903  CG  LEU A 115       9.388  28.634   7.553  1.00 11.34           C  
ATOM    904  CD1 LEU A 115       8.306  27.826   8.246  1.00 11.76           C  
ATOM    905  CD2 LEU A 115       9.768  29.819   8.398  1.00 13.42           C  
ATOM    906  N   GLN A 116      13.074  26.575   5.595  1.00 10.54           N  
ATOM    907  CA  GLN A 116      14.268  25.743   5.421  1.00 11.68           C  
ATOM    908  C   GLN A 116      15.503  26.595   5.118  1.00 11.50           C  
ATOM    909  O   GLN A 116      16.585  26.373   5.682  1.00 12.45           O  
ATOM    910  CB  GLN A 116      14.047  24.746   4.281  1.00 11.17           C  
ATOM    911  CG  GLN A 116      13.095  23.609   4.604  1.00 12.84           C  
ATOM    912  CD  GLN A 116      12.828  22.733   3.392  1.00 13.24           C  
ATOM    913  OE1 GLN A 116      12.944  23.185   2.247  1.00 16.72           O  
ATOM    914  NE2 GLN A 116      12.467  21.480   3.634  1.00 15.09           N  
ATOM    915  N   SER A 117      15.321  27.573   4.230  1.00 11.52           N  
ATOM    916  CA ASER A 117      16.423  28.397   3.738  0.50 11.44           C  
ATOM    917  CA BSER A 117      16.423  28.399   3.739  0.50 11.67           C  
ATOM    918  C   SER A 117      16.960  29.362   4.790  1.00 11.61           C  
ATOM    919  O   SER A 117      18.176  29.526   4.927  1.00 11.61           O  
ATOM    920  CB ASER A 117      15.990  29.159   2.482  0.50 11.51           C  
ATOM    921  CB BSER A 117      15.994  29.179   2.495  0.50 11.77           C  
ATOM    922  OG ASER A 117      15.643  28.255   1.446  0.50 11.55           O  
ATOM    923  OG BSER A 117      17.057  29.992   2.035  0.50 13.20           O  
ATOM    924  N   LYS A 118      16.051  29.999   5.525  1.00 11.42           N  
ATOM    925  CA  LYS A 118      16.415  31.038   6.493  1.00 11.70           C  
ATOM    926  C   LYS A 118      16.756  30.509   7.881  1.00 11.62           C  
ATOM    927  O   LYS A 118      17.361  31.217   8.693  1.00 11.99           O  
ATOM    928  CB  LYS A 118      15.307  32.085   6.580  1.00 11.95           C  
ATOM    929  CG  LYS A 118      15.224  32.979   5.340  1.00 13.78           C  
ATOM    930  CD  LYS A 118      14.227  34.097   5.539  1.00 18.17           C  
ATOM    931  CE  LYS A 118      14.375  35.165   4.474  1.00 20.43           C  
ATOM    932  NZ  LYS A 118      15.667  35.913   4.603  1.00 22.18           N  
ATOM    933  N   HIS A 119      16.359  29.268   8.150  1.00 11.62           N  
ATOM    934  CA  HIS A 119      16.554  28.660   9.463  1.00 11.83           C  
ATOM    935  C   HIS A 119      16.996  27.191   9.366  1.00 12.03           C  
ATOM    936  O   HIS A 119      16.325  26.327   9.916  1.00 12.04           O  
ATOM    937  CB  HIS A 119      15.261  28.769  10.285  1.00 11.60           C  
ATOM    938  CG  HIS A 119      14.691  30.151  10.305  1.00 11.38           C  
ATOM    939  ND1 HIS A 119      15.175  31.139  11.135  1.00 11.49           N  
ATOM    940  CD2 HIS A 119      13.730  30.729   9.546  1.00 12.22           C  
ATOM    941  CE1 HIS A 119      14.511  32.260  10.911  1.00 12.17           C  
ATOM    942  NE2 HIS A 119      13.636  32.040   9.944  1.00 11.64           N  
ATOM    943  N  APRO A 120      18.163  26.927   8.743  0.50 12.13           N  
ATOM    944  N  BPRO A 120      18.091  26.905   8.629  0.50 12.83           N  
ATOM    945  CA APRO A 120      18.588  25.553   8.432  0.50 12.12           C  
ATOM    946  CA BPRO A 120      18.565  25.527   8.696  0.50 13.30           C  
ATOM    947  C  APRO A 120      18.778  24.642   9.655  0.50 12.09           C  
ATOM    948  C  BPRO A 120      19.101  25.290  10.101  0.50 13.69           C  
ATOM    949  O  APRO A 120      18.598  23.435   9.547  0.50 11.84           O  
ATOM    950  O  BPRO A 120      19.737  26.167  10.680  0.50 14.16           O  
ATOM    951  CB APRO A 120      19.921  25.753   7.697  0.50 12.33           C  
ATOM    952  CB BPRO A 120      19.690  25.481   7.657  0.50 13.48           C  
ATOM    953  CG APRO A 120      20.409  27.082   8.137  0.50 12.18           C  
ATOM    954  CG BPRO A 120      20.149  26.880   7.520  0.50 13.04           C  
ATOM    955  CD APRO A 120      19.175  27.916   8.328  0.50 12.13           C  
ATOM    956  CD BPRO A 120      18.933  27.735   7.748  0.50 12.91           C  
ATOM    957  N  AGLY A 121      19.128  25.203  10.808  0.50 12.11           N  
ATOM    958  N  BGLY A 121      18.816  24.131  10.666  0.50 14.13           N  
ATOM    959  CA AGLY A 121      19.313  24.373  11.998  0.50 12.78           C  
ATOM    960  CA BGLY A 121      19.149  23.920  12.060  0.50 13.76           C  
ATOM    961  C  AGLY A 121      18.010  24.155  12.744  0.50 13.12           C  
ATOM    962  C  BGLY A 121      17.904  24.054  12.906  0.50 13.77           C  
ATOM    963  O  AGLY A 121      17.591  23.024  13.002  0.50 13.14           O  
ATOM    964  O  BGLY A 121      17.401  23.044  13.404  0.50 13.61           O  
ATOM    965  N   ASP A 122      17.383  25.274  13.076  1.00 13.12           N  
ATOM    966  CA  ASP A 122      16.145  25.385  13.851  1.00 13.59           C  
ATOM    967  C   ASP A 122      14.974  24.661  13.194  1.00 13.20           C  
ATOM    968  O   ASP A 122      14.139  24.069  13.881  1.00 13.92           O  
ATOM    969  CB  ASP A 122      15.780  26.853  14.099  1.00 13.69           C  
ATOM    970  CG  ASP A 122      16.646  27.509  15.172  1.00 16.99           C  
ATOM    971  OD1 ASP A 122      17.218  26.792  16.025  1.00 18.90           O  
ATOM    972  OD2 ASP A 122      16.731  28.752  15.175  1.00 17.70           O  
ATOM    973  N   PHE A 123      14.925  24.698  11.868  1.00 12.41           N  
ATOM    974  CA  PHE A 123      13.819  24.098  11.131  1.00 11.89           C  
ATOM    975  C   PHE A 123      14.190  22.697  10.625  1.00 11.67           C  
ATOM    976  O   PHE A 123      14.324  22.453   9.414  1.00 12.22           O  
ATOM    977  CB  PHE A 123      13.365  25.034   9.997  1.00 12.04           C  
ATOM    978  CG  PHE A 123      12.001  24.714   9.445  1.00 11.48           C  
ATOM    979  CD1 PHE A 123      10.857  24.885  10.226  1.00 11.96           C  
ATOM    980  CD2 PHE A 123      11.857  24.285   8.131  1.00 12.00           C  
ATOM    981  CE1 PHE A 123       9.585  24.592   9.708  1.00 11.42           C  
ATOM    982  CE2 PHE A 123      10.599  23.995   7.604  1.00 11.88           C  
ATOM    983  CZ  PHE A 123       9.455  24.157   8.398  1.00 11.39           C  
ATOM    984  N   GLY A 124      14.387  21.785  11.577  1.00 11.45           N  
ATOM    985  CA  GLY A 124      14.733  20.397  11.275  1.00 11.01           C  
ATOM    986  C   GLY A 124      13.524  19.549  10.945  1.00 11.44           C  
ATOM    987  O   GLY A 124      12.412  20.073  10.765  1.00 11.15           O  
ATOM    988  N   ALA A 125      13.744  18.237  10.881  1.00 11.20           N  
ATOM    989  CA  ALA A 125      12.724  17.274  10.444  1.00 11.22           C  
ATOM    990  C   ALA A 125      11.453  17.324  11.284  1.00 11.35           C  
ATOM    991  O   ALA A 125      10.346  17.353  10.741  1.00 10.81           O  
ATOM    992  CB  ALA A 125      13.302  15.862  10.435  1.00 11.93           C  
ATOM    993  N   ASP A 126      11.612  17.321  12.604  1.00 10.96           N  
ATOM    994  CA  ASP A 126      10.462  17.363  13.510  1.00 11.73           C  
ATOM    995  C   ASP A 126       9.689  18.678  13.390  1.00 11.35           C  
ATOM    996  O   ASP A 126       8.459  18.666  13.311  1.00 11.07           O  
ATOM    997  CB  ASP A 126      10.893  17.125  14.963  1.00 12.66           C  
ATOM    998  CG  ASP A 126      11.224  15.661  15.250  1.00 16.08           C  
ATOM    999  OD1 ASP A 126      11.265  14.827  14.319  1.00 19.94           O  
ATOM   1000  OD2 ASP A 126      11.438  15.344  16.437  1.00 22.24           O  
ATOM   1001  N   ALA A 127      10.408  19.798  13.373  1.00 10.76           N  
ATOM   1002  CA  ALA A 127       9.775  21.113  13.211  1.00 10.59           C  
ATOM   1003  C   ALA A 127       9.072  21.211  11.861  1.00 10.36           C  
ATOM   1004  O   ALA A 127       7.969  21.753  11.774  1.00 10.16           O  
ATOM   1005  CB  ALA A 127      10.788  22.239  13.369  1.00 10.89           C  
ATOM   1006  N   GLN A 128       9.713  20.697  10.810  1.00 10.30           N  
ATOM   1007  CA  GLN A 128       9.105  20.709   9.481  1.00 10.36           C  
ATOM   1008  C   GLN A 128       7.833  19.858   9.437  1.00  9.95           C  
ATOM   1009  O   GLN A 128       6.840  20.262   8.828  1.00 10.50           O  
ATOM   1010  CB  GLN A 128      10.097  20.263   8.407  1.00 10.38           C  
ATOM   1011  CG  GLN A 128       9.513  20.312   7.000  1.00 12.42           C  
ATOM   1012  CD  GLN A 128      10.512  19.919   5.937  1.00 15.80           C  
ATOM   1013  OE1 GLN A 128      11.715  20.106   6.101  1.00 18.23           O  
ATOM   1014  NE2 GLN A 128      10.014  19.364   4.839  1.00 17.85           N  
ATOM   1015  N   GLY A 129       7.860  18.698  10.096  1.00  9.84           N  
ATOM   1016  CA  GLY A 129       6.685  17.821  10.156  1.00  9.62           C  
ATOM   1017  C   GLY A 129       5.502  18.529  10.804  1.00  9.64           C  
ATOM   1018  O   GLY A 129       4.364  18.469  10.308  1.00 10.16           O  
ATOM   1019  N   ALA A 130       5.776  19.208  11.909  1.00  9.01           N  
ATOM   1020  CA  ALA A 130       4.750  19.922  12.655  1.00  9.09           C  
ATOM   1021  C   ALA A 130       4.202  21.093  11.839  1.00  9.13           C  
ATOM   1022  O   ALA A 130       2.982  21.290  11.760  1.00  9.30           O  
ATOM   1023  CB  ALA A 130       5.302  20.400  14.008  1.00  9.50           C  
ATOM   1024  N   MET A 131       5.093  21.862  11.218  1.00  9.02           N  
ATOM   1025  CA  MET A 131       4.657  22.994  10.393  1.00  9.20           C  
ATOM   1026  C   MET A 131       3.817  22.521   9.210  1.00  9.59           C  
ATOM   1027  O   MET A 131       2.815  23.163   8.858  1.00  9.57           O  
ATOM   1028  CB  MET A 131       5.850  23.826   9.910  1.00  9.00           C  
ATOM   1029  CG  MET A 131       5.460  25.076   9.128  1.00 10.07           C  
ATOM   1030  SD  MET A 131       4.568  26.289  10.119  1.00 12.52           S  
ATOM   1031  CE  MET A 131       5.897  26.946  11.113  1.00 13.54           C  
ATOM   1032  N   ASN A 132       4.217  21.399   8.603  1.00 10.13           N  
ATOM   1033  CA AASN A 132       3.438  20.805   7.515  0.50 10.42           C  
ATOM   1034  CA BASN A 132       3.448  20.795   7.518  0.50 10.48           C  
ATOM   1035  C   ASN A 132       2.017  20.466   7.957  1.00 10.52           C  
ATOM   1036  O   ASN A 132       1.047  20.764   7.244  1.00 10.34           O  
ATOM   1037  CB AASN A 132       4.141  19.567   6.943  0.50 11.03           C  
ATOM   1038  CB BASN A 132       4.155  19.536   7.010  0.50 11.20           C  
ATOM   1039  CG AASN A 132       5.122  19.912   5.837  0.50 11.96           C  
ATOM   1040  CG BASN A 132       3.439  18.897   5.843  0.50 12.22           C  
ATOM   1041  OD1AASN A 132       4.883  20.820   5.041  0.50 13.78           O  
ATOM   1042  OD1BASN A 132       3.268  19.512   4.789  0.50 15.20           O  
ATOM   1043  ND2AASN A 132       6.225  19.178   5.776  0.50 13.48           N  
ATOM   1044  ND2BASN A 132       3.021  17.651   6.021  0.50 14.77           N  
ATOM   1045  N   LYS A 133       1.887  19.870   9.141  1.00 10.42           N  
ATOM   1046  CA  LYS A 133       0.562  19.539   9.681  1.00 10.42           C  
ATOM   1047  C   LYS A 133      -0.271  20.788   9.931  1.00 10.16           C  
ATOM   1048  O   LYS A 133      -1.470  20.804   9.666  1.00  9.97           O  
ATOM   1049  CB  LYS A 133       0.680  18.732  10.970  1.00 11.15           C  
ATOM   1050  CG  LYS A 133       1.205  17.327  10.784  1.00 13.85           C  
ATOM   1051  CD  LYS A 133       1.137  16.568  12.109  1.00 19.24           C  
ATOM   1052  CE  LYS A 133       1.938  15.280  12.034  1.00 21.77           C  
ATOM   1053  NZ  LYS A 133       1.948  14.562  13.343  1.00 25.00           N  
ATOM   1054  N   ALA A 134       0.376  21.831  10.445  1.00  9.28           N  
ATOM   1055  CA  ALA A 134      -0.305  23.080  10.750  1.00  9.15           C  
ATOM   1056  C   ALA A 134      -0.823  23.748   9.481  1.00  9.21           C  
ATOM   1057  O   ALA A 134      -1.934  24.269   9.458  1.00  8.97           O  
ATOM   1058  CB  ALA A 134       0.622  24.015  11.520  1.00  8.77           C  
ATOM   1059  N   LEU A 135      -0.018  23.723   8.419  1.00  8.99           N  
ATOM   1060  CA  LEU A 135      -0.435  24.308   7.144  1.00  9.18           C  
ATOM   1061  C   LEU A 135      -1.488  23.461   6.448  1.00  9.79           C  
ATOM   1062  O   LEU A 135      -2.385  23.995   5.785  1.00  9.74           O  
ATOM   1063  CB  LEU A 135       0.775  24.540   6.234  1.00  9.17           C  
ATOM   1064  CG  LEU A 135       1.761  25.600   6.732  1.00  9.24           C  
ATOM   1065  CD1 LEU A 135       2.969  25.660   5.800  1.00 10.00           C  
ATOM   1066  CD2 LEU A 135       1.134  26.991   6.890  1.00 10.63           C  
ATOM   1067  N   GLU A 136      -1.395  22.145   6.611  1.00 10.15           N  
ATOM   1068  CA  GLU A 136      -2.435  21.248   6.091  1.00 12.21           C  
ATOM   1069  C   GLU A 136      -3.791  21.530   6.750  1.00 11.32           C  
ATOM   1070  O   GLU A 136      -4.818  21.579   6.067  1.00 11.40           O  
ATOM   1071  CB  GLU A 136      -2.039  19.781   6.277  1.00 12.05           C  
ATOM   1072  CG  GLU A 136      -3.021  18.790   5.652  1.00 15.53           C  
ATOM   1073  CD  GLU A 136      -2.597  17.344   5.824  1.00 16.29           C  
ATOM   1074  OE1 GLU A 136      -1.634  17.080   6.590  1.00 23.28           O  
ATOM   1075  OE2 GLU A 136      -3.223  16.466   5.179  1.00 22.65           O  
ATOM   1076  N   LEU A 137      -3.783  21.737   8.065  1.00 10.89           N  
ATOM   1077  CA  LEU A 137      -4.998  22.075   8.801  1.00 10.77           C  
ATOM   1078  C   LEU A 137      -5.583  23.405   8.321  1.00 10.41           C  
ATOM   1079  O   LEU A 137      -6.786  23.522   8.129  1.00 10.10           O  
ATOM   1080  CB  LEU A 137      -4.733  22.110  10.306  1.00 10.99           C  
ATOM   1081  CG  LEU A 137      -5.918  22.470  11.208  1.00 11.67           C  
ATOM   1082  CD1 LEU A 137      -6.974  21.364  11.216  1.00 14.51           C  
ATOM   1083  CD2 LEU A 137      -5.435  22.796  12.621  1.00 12.16           C  
ATOM   1084  N   PHE A 138      -4.714  24.390   8.103  1.00  9.49           N  
ATOM   1085  CA  PHE A 138      -5.116  25.675   7.543  1.00  9.29           C  
ATOM   1086  C   PHE A 138      -5.818  25.466   6.191  1.00  9.22           C  
ATOM   1087  O   PHE A 138      -6.902  26.009   5.952  1.00  9.38           O  
ATOM   1088  CB  PHE A 138      -3.882  26.582   7.410  1.00  9.24           C  
ATOM   1089  CG  PHE A 138      -4.075  27.752   6.478  1.00  9.19           C  
ATOM   1090  CD1 PHE A 138      -4.906  28.806   6.827  1.00 10.41           C  
ATOM   1091  CD2 PHE A 138      -3.409  27.788   5.250  1.00  9.98           C  
ATOM   1092  CE1 PHE A 138      -5.087  29.888   5.956  1.00 10.34           C  
ATOM   1093  CE2 PHE A 138      -3.588  28.858   4.367  1.00 10.45           C  
ATOM   1094  CZ  PHE A 138      -4.423  29.908   4.722  1.00 10.86           C  
ATOM   1095  N   ARG A 139      -5.207  24.658   5.331  1.00  8.84           N  
ATOM   1096  CA  ARG A 139      -5.732  24.431   3.983  1.00  9.53           C  
ATOM   1097  C   ARG A 139      -7.064  23.704   4.028  1.00  9.87           C  
ATOM   1098  O   ARG A 139      -8.021  24.113   3.358  1.00 10.33           O  
ATOM   1099  CB  ARG A 139      -4.740  23.652   3.132  1.00 10.04           C  
ATOM   1100  CG  ARG A 139      -3.585  24.479   2.675  1.00 11.26           C  
ATOM   1101  CD  ARG A 139      -2.875  23.818   1.507  1.00 14.33           C  
ATOM   1102  NE  ARG A 139      -2.579  22.404   1.740  1.00 15.53           N  
ATOM   1103  CZ  ARG A 139      -1.508  21.950   2.389  1.00 15.33           C  
ATOM   1104  NH1 ARG A 139      -0.618  22.794   2.902  1.00 15.12           N  
ATOM   1105  NH2 ARG A 139      -1.330  20.643   2.537  1.00 17.26           N  
ATOM   1106  N   LYS A 140      -7.127  22.641   4.827  1.00 10.21           N  
ATOM   1107  CA  LYS A 140      -8.355  21.864   4.973  1.00 10.37           C  
ATOM   1108  C   LYS A 140      -9.511  22.726   5.495  1.00 10.72           C  
ATOM   1109  O   LYS A 140     -10.653  22.616   5.027  1.00 10.62           O  
ATOM   1110  CB  LYS A 140      -8.134  20.655   5.888  1.00 10.85           C  
ATOM   1111  N   ASP A 141      -9.213  23.613   6.440  1.00 10.01           N  
ATOM   1112  CA  ASP A 141     -10.265  24.437   7.009  1.00 10.24           C  
ATOM   1113  C   ASP A 141     -10.677  25.557   6.065  1.00  9.70           C  
ATOM   1114  O   ASP A 141     -11.846  25.933   6.032  1.00  9.91           O  
ATOM   1115  CB  ASP A 141      -9.877  24.957   8.391  1.00 10.56           C  
ATOM   1116  CG  ASP A 141      -9.956  23.875   9.463  1.00 12.33           C  
ATOM   1117  OD1 ASP A 141     -10.525  22.796   9.194  1.00 14.57           O  
ATOM   1118  OD2 ASP A 141      -9.455  24.104  10.586  1.00 12.95           O  
ATOM   1119  N   MET A 142      -9.721  26.091   5.295  1.00  9.18           N  
ATOM   1120  CA  MET A 142     -10.070  27.019   4.217  1.00  8.98           C  
ATOM   1121  C   MET A 142     -11.000  26.327   3.214  1.00  8.98           C  
ATOM   1122  O   MET A 142     -12.036  26.886   2.843  1.00  9.24           O  
ATOM   1123  CB  MET A 142      -8.819  27.532   3.501  1.00  9.05           C  
ATOM   1124  CG  MET A 142      -8.028  28.559   4.308  1.00 10.04           C  
ATOM   1125  SD  MET A 142      -8.764  30.203   4.330  1.00 11.49           S  
ATOM   1126  CE  MET A 142      -8.355  30.817   2.696  1.00 12.58           C  
ATOM   1127  N   ALA A 143     -10.626  25.114   2.799  1.00  9.06           N  
ATOM   1128  CA  ALA A 143     -11.410  24.344   1.828  1.00  9.55           C  
ATOM   1129  C   ALA A 143     -12.828  24.061   2.329  1.00 10.16           C  
ATOM   1130  O   ALA A 143     -13.786  24.179   1.555  1.00  9.72           O  
ATOM   1131  CB  ALA A 143     -10.696  23.058   1.459  1.00  9.84           C  
ATOM   1132  N   SER A 144     -12.955  23.706   3.613  1.00 10.02           N  
ATOM   1133  CA ASER A 144     -14.252  23.436   4.227  0.33 10.37           C  
ATOM   1134  CA BSER A 144     -14.260  23.439   4.223  0.33 10.35           C  
ATOM   1135  CA CSER A 144     -14.267  23.431   4.197  0.33 10.47           C  
ATOM   1136  C   SER A 144     -15.123  24.695   4.232  1.00 10.51           C  
ATOM   1137  O   SER A 144     -16.316  24.648   3.916  1.00 10.51           O  
ATOM   1138  CB ASER A 144     -14.049  22.911   5.648  0.33 10.28           C  
ATOM   1139  CB BSER A 144     -14.098  22.905   5.646  0.33 10.26           C  
ATOM   1140  CB CSER A 144     -14.143  22.803   5.588  0.33 10.40           C  
ATOM   1141  OG ASER A 144     -15.227  22.319   6.154  0.33 10.08           O  
ATOM   1142  OG BSER A 144     -13.495  21.626   5.650  0.33  9.95           O  
ATOM   1143  OG CSER A 144     -13.613  23.720   6.527  0.33 10.83           O  
ATOM   1144  N   ASN A 145     -14.512  25.827   4.586  1.00 10.67           N  
ATOM   1145  CA  ASN A 145     -15.215  27.099   4.595  1.00 11.57           C  
ATOM   1146  C   ASN A 145     -15.670  27.518   3.201  1.00 11.71           C  
ATOM   1147  O   ASN A 145     -16.747  28.077   3.049  1.00 11.97           O  
ATOM   1148  CB  ASN A 145     -14.362  28.202   5.226  1.00 12.00           C  
ATOM   1149  CG  ASN A 145     -14.539  28.279   6.727  1.00 14.18           C  
ATOM   1150  OD1 ASN A 145     -15.362  29.051   7.225  1.00 17.14           O  
ATOM   1151  ND2 ASN A 145     -13.790  27.460   7.456  1.00 16.75           N  
ATOM   1152  N   TYR A 146     -14.840  27.247   2.196  1.00 12.26           N  
ATOM   1153  CA  TYR A 146     -15.204  27.456   0.793  1.00 13.29           C  
ATOM   1154  C   TYR A 146     -16.525  26.761   0.457  1.00 14.63           C  
ATOM   1155  O   TYR A 146     -17.347  27.317  -0.271  1.00 14.90           O  
ATOM   1156  CB  TYR A 146     -14.113  26.900  -0.127  1.00 12.73           C  
ATOM   1157  CG  TYR A 146     -12.947  27.825  -0.435  1.00 12.55           C  
ATOM   1158  CD1 TYR A 146     -12.673  28.956   0.337  1.00 13.29           C  
ATOM   1159  CD2 TYR A 146     -12.099  27.537  -1.495  1.00 14.34           C  
ATOM   1160  CE1 TYR A 146     -11.590  29.790   0.029  1.00 12.12           C  
ATOM   1161  CE2 TYR A 146     -11.021  28.355  -1.806  1.00 14.01           C  
ATOM   1162  CZ  TYR A 146     -10.769  29.474  -1.046  1.00 13.76           C  
ATOM   1163  OH  TYR A 146      -9.699  30.270  -1.382  1.00 12.67           O  
ATOM   1164  N   LYS A 147     -16.717  25.552   0.987  1.00 15.90           N  
ATOM   1165  CA  LYS A 147     -17.930  24.767   0.713  1.00 17.69           C  
ATOM   1166  C   LYS A 147     -19.165  25.376   1.368  1.00 18.54           C  
ATOM   1167  O   LYS A 147     -20.271  25.264   0.843  1.00 19.04           O  
ATOM   1168  CB  LYS A 147     -17.761  23.317   1.173  1.00 17.44           C  
ATOM   1169  CG  LYS A 147     -16.699  22.543   0.414  1.00 19.44           C  
ATOM   1170  CD  LYS A 147     -16.707  21.071   0.777  1.00 22.72           C  
ATOM   1171  CE  LYS A 147     -15.409  20.396   0.358  1.00 25.12           C  
ATOM   1172  NZ  LYS A 147     -15.442  18.919   0.597  1.00 27.15           N  
ATOM   1173  N   GLU A 148     -18.970  26.007   2.524  1.00 19.84           N  
ATOM   1174  CA  GLU A 148     -20.063  26.631   3.274  1.00 21.23           C  
ATOM   1175  C   GLU A 148     -20.517  27.919   2.614  1.00 22.36           C  
ATOM   1176  O   GLU A 148     -21.670  28.330   2.768  1.00 22.93           O  
ATOM   1177  CB  GLU A 148     -19.656  26.881   4.726  1.00 21.09           C  
ATOM   1178  CG  GLU A 148     -19.129  25.639   5.407  1.00 21.61           C  
ATOM   1179  CD  GLU A 148     -19.219  25.683   6.919  1.00 23.03           C  
ATOM   1180  OE1 GLU A 148     -20.184  26.267   7.458  1.00 23.46           O  
ATOM   1181  OE2 GLU A 148     -18.325  25.101   7.566  1.00 24.10           O  
ATOM   1182  N   LEU A 149     -19.601  28.554   1.883  1.00 23.39           N  
ATOM   1183  CA  LEU A 149     -19.914  29.726   1.066  1.00 24.50           C  
ATOM   1184  C   LEU A 149     -20.560  29.294  -0.246  1.00 25.06           C  
ATOM   1185  O   LEU A 149     -20.199  28.252  -0.809  1.00 26.01           O  
ATOM   1186  CB  LEU A 149     -18.643  30.533   0.774  1.00 24.64           C  
ATOM   1187  CG  LEU A 149     -17.864  31.060   1.982  1.00 25.51           C  
ATOM   1188  CD1 LEU A 149     -16.438  31.426   1.579  1.00 26.42           C  
ATOM   1189  CD2 LEU A 149     -18.574  32.238   2.633  1.00 27.24           C  
TER    1190      LEU A 149                                                      
HETATM 1191  CHA HEM A 154      -5.248  39.769  -0.250  1.00  7.67           C  
HETATM 1192  CHB HEM A 154      -3.774  36.790   3.280  1.00  7.05           C  
HETATM 1193  CHC HEM A 154      -2.879  33.328   0.013  1.00  7.69           C  
HETATM 1194  CHD HEM A 154      -4.342  36.262  -3.536  1.00  8.00           C  
HETATM 1195  C1A HEM A 154      -4.960  39.256   0.996  1.00  7.60           C  
HETATM 1196  C2A HEM A 154      -5.177  39.925   2.270  1.00  7.96           C  
HETATM 1197  C3A HEM A 154      -4.762  39.099   3.235  1.00  7.45           C  
HETATM 1198  C4A HEM A 154      -4.279  37.882   2.615  1.00  7.44           C  
HETATM 1199  CMA HEM A 154      -4.792  39.352   4.760  1.00  8.07           C  
HETATM 1200  CAA HEM A 154      -5.789  41.338   2.464  1.00  7.92           C  
HETATM 1201  CBA HEM A 154      -7.283  41.203   2.814  1.00  9.61           C  
HETATM 1202  CGA HEM A 154      -8.000  40.335   1.803  1.00 10.04           C  
HETATM 1203  O1A HEM A 154      -8.314  39.154   2.116  1.00 11.60           O  
HETATM 1204  O2A HEM A 154      -8.252  40.816   0.681  1.00 11.56           O  
HETATM 1205  C1B HEM A 154      -3.405  35.579   2.720  1.00  7.15           C  
HETATM 1206  C2B HEM A 154      -2.926  34.407   3.429  1.00  6.66           C  
HETATM 1207  C3B HEM A 154      -2.671  33.453   2.525  1.00  6.59           C  
HETATM 1208  C4B HEM A 154      -2.989  33.989   1.213  1.00  6.41           C  
HETATM 1209  CMB HEM A 154      -2.743  34.314   4.962  1.00  8.15           C  
HETATM 1210  CAB HEM A 154      -2.140  32.029   2.797  1.00  7.93           C  
HETATM 1211  CBB HEM A 154      -1.071  31.845   3.578  1.00  9.78           C  
HETATM 1212  C1C HEM A 154      -3.124  33.832  -1.241  1.00  5.49           C  
HETATM 1213  C2C HEM A 154      -2.772  33.214  -2.517  1.00  6.19           C  
HETATM 1214  C3C HEM A 154      -3.176  34.035  -3.503  1.00  7.01           C  
HETATM 1215  C4C HEM A 154      -3.787  35.190  -2.877  1.00  6.73           C  
HETATM 1216  CMC HEM A 154      -2.069  31.847  -2.657  1.00  7.31           C  
HETATM 1217  CAC HEM A 154      -3.064  33.891  -5.047  1.00  9.02           C  
HETATM 1218  CBC HEM A 154      -2.329  32.952  -5.654  1.00 10.36           C  
HETATM 1219  C1D HEM A 154      -4.658  37.483  -2.990  1.00  7.30           C  
HETATM 1220  C2D HEM A 154      -4.955  38.670  -3.769  1.00  7.81           C  
HETATM 1221  C3D HEM A 154      -5.222  39.769  -2.755  1.00  8.54           C  
HETATM 1222  C4D HEM A 154      -5.066  39.140  -1.458  1.00  7.59           C  
HETATM 1223  CMD HEM A 154      -4.975  38.808  -5.306  1.00  9.56           C  
HETATM 1224  CAD HEM A 154      -5.555  41.244  -3.071  1.00  8.72           C  
HETATM 1225  CBD HEM A 154      -4.185  41.927  -3.157  1.00 12.68           C  
HETATM 1226  CGD HEM A 154      -4.294  43.389  -3.510  1.00 13.94           C  
HETATM 1227  O1D HEM A 154      -4.666  43.690  -4.669  1.00 16.65           O  
HETATM 1228  O2D HEM A 154      -3.996  44.248  -2.643  1.00 14.30           O  
HETATM 1229  NA  HEM A 154      -4.426  38.009   1.247  1.00  6.70           N  
HETATM 1230  NB  HEM A 154      -3.428  35.288   1.378  1.00  6.89           N  
HETATM 1231  NC  HEM A 154      -3.742  35.033  -1.508  1.00  6.95           N  
HETATM 1232  ND  HEM A 154      -4.738  37.800  -1.636  1.00  7.22           N  
HETATM 1233 FE   HEM A 154      -4.147  36.509  -0.127  1.00  7.80          FE  
HETATM 1234  S   SO4 A 300      -5.169  25.815 -12.060  1.00 32.06           S  
HETATM 1235  O1  SO4 A 300      -4.070  25.022 -11.507  1.00 31.51           O  
HETATM 1236  O2  SO4 A 300      -5.806  25.074 -13.144  1.00 33.05           O  
HETATM 1237  O3  SO4 A 300      -6.159  26.060 -11.007  1.00 33.35           O  
HETATM 1238  O4  SO4 A 300      -4.645  27.090 -12.536  1.00 31.25           O  
HETATM 1239  S   SO4 A 301      -0.894  45.417   1.857  1.00 40.50           S  
HETATM 1240  O1  SO4 A 301      -1.006  45.739   3.277  1.00 42.05           O  
HETATM 1241  O2  SO4 A 301       0.400  45.874   1.372  1.00 42.11           O  
HETATM 1242  O3  SO4 A 301      -0.999  43.980   1.647  1.00 40.70           O  
HETATM 1243  O4  SO4 A 301      -1.951  46.103   1.119  1.00 42.42           O  
HETATM 1244  S   SO4 A 302      14.872  36.246 -13.438  1.00 49.07           S  
HETATM 1245  O1  SO4 A 302      15.418  37.240 -12.509  1.00 48.11           O  
HETATM 1246  O2  SO4 A 302      14.965  36.746 -14.808  1.00 48.27           O  
HETATM 1247  O3  SO4 A 302      15.641  35.006 -13.333  1.00 49.31           O  
HETATM 1248  O4  SO4 A 302      13.471  35.976 -13.119  1.00 47.85           O  
HETATM 1249  O   HOH A 200      -2.201  37.243  -0.541  1.00 10.29           O  
HETATM 1250  O   HOH A 201      -3.741  25.927  10.993  1.00 13.06           O  
HETATM 1251  O   HOH A 202      13.237  19.875  14.153  1.00 15.87           O  
HETATM 1252  O   HOH A 203      -4.095  27.438  13.464  1.00 10.87           O  
HETATM 1253  O   HOH A 204       3.359  26.783 -13.382  1.00 24.07           O  
HETATM 1254  O   HOH A 205       7.820  20.927  21.670  1.00 11.36           O  
HETATM 1255  O   HOH A 206      16.866  42.986  -7.441  1.00 16.89           O  
HETATM 1256  O   HOH A 207       9.496  46.629 -12.457  1.00 15.91           O  
HETATM 1257  O   HOH A 208      -5.379  36.119  11.176  1.00 19.19           O  
HETATM 1258  O   HOH A 209       8.941  30.687 -13.996  1.00 26.69           O  
HETATM 1259  O   HOH A 210      -2.372  41.040   7.856  1.00 16.84           O  
HETATM 1260  O   HOH A 211      -3.868  42.433  -6.920  1.00 19.04           O  
HETATM 1261  O   HOH A 212      -5.675  23.717  20.150  1.00 29.27           O  
HETATM 1262  O   HOH A 213      -8.611  40.420  -6.335  1.00 20.33           O  
HETATM 1263  O   HOH A 214      19.084  28.284  11.969  1.00 14.32           O  
HETATM 1264  O   HOH A 215      -7.775  37.738  -8.050  1.00 20.01           O  
HETATM 1265  O   HOH A 216       6.986  16.806  14.545  1.00 26.49           O  
HETATM 1266  O   HOH A 217       4.125  21.651  24.908  1.00 33.46           O  
HETATM 1267  O   HOH A 218      13.807  20.450   7.614  1.00 21.62           O  
HETATM 1268  O   HOH A 219      -4.963  43.927  -0.108  1.00 20.58           O  
HETATM 1269  O   HOH A 220       5.350  27.537  -4.479  1.00 27.42           O  
HETATM 1270  O   HOH A 221      17.867  23.704   5.018  1.00 35.27           O  
HETATM 1271  O   HOH A 222       2.450  25.390 -11.260  1.00 27.94           O  
HETATM 1272  O   HOH A 223      -7.846  23.525  -6.219  1.00 14.80           O  
HETATM 1273  O   HOH A 224       2.393  35.371 -14.776  1.00 28.57           O  
HETATM 1274  O   HOH A 225     -13.553  23.452  -1.136  1.00 28.18           O  
HETATM 1275  O   HOH A 226      -5.958  41.102  -8.440  1.00 26.37           O  
HETATM 1276  O   HOH A 227      -4.359  29.704  21.052  1.00 30.56           O  
HETATM 1277  O   HOH A 228       2.440  16.871  23.477  1.00 33.46           O  
HETATM 1278  O   HOH A 229       7.903  26.742  -4.053  1.00 28.13           O  
HETATM 1279  O   HOH A 230       2.364  45.296   5.588  1.00 23.61           O  
HETATM 1280  O   HOH A 231      -5.170  20.840  16.636  1.00 28.88           O  
HETATM 1281  O   HOH A 232      -3.084  18.466   9.766  1.00 18.85           O  
HETATM 1282  O   HOH A 233       9.170  41.706  11.684  1.00 21.07           O  
HETATM 1283  O   HOH A 234     -15.414  19.507   4.140  1.00 35.83           O  
HETATM 1284  O   HOH A 235      17.078  30.321  13.034  1.00 27.91           O  
HETATM 1285  O   HOH A 236       6.118  27.501  21.191  1.00 24.57           O  
HETATM 1286  O   HOH A 237      19.677  22.334   6.415  1.00 30.80           O  
HETATM 1287  O   HOH A 238      -4.497  35.318  16.746  1.00 26.65           O  
HETATM 1288  O   HOH A 239       3.047  47.082  -6.856  1.00 20.76           O  
HETATM 1289  O   HOH A 240      -4.294  32.265 -12.228  1.00 28.30           O  
HETATM 1290  O   HOH A 241       2.954  36.885  13.227  1.00 28.35           O  
HETATM 1291  O   HOH A 242      17.097  21.912   8.223  1.00 28.62           O  
HETATM 1292  O   HOH A 243       8.360  33.100 -14.769  1.00 35.33           O  
HETATM 1293  O   HOH A 244       1.518  24.301 -13.291  1.00 32.80           O  
HETATM 1294  O   HOH A 245     -15.081  35.446  12.119  1.00 31.48           O  
HETATM 1295  O   HOH A 246       3.359  45.992 -10.653  1.00 21.34           O  
HETATM 1296  O   HOH A 247       7.329  49.115  -5.024  1.00 25.22           O  
HETATM 1297  O   HOH A 248       1.388  21.417   4.361  1.00 29.21           O  
HETATM 1298  O   HOH A 249      -2.508  37.496  16.960  1.00 38.96           O  
HETATM 1299  O   HOH A 250     -15.510  29.302   9.892  1.00 26.36           O  
HETATM 1300  O   HOH A 251      12.792  31.442  21.171  1.00 30.43           O  
HETATM 1301  O   HOH A 252     -10.593  32.261  17.074  1.00 23.95           O  
HETATM 1302  O   HOH A 253      14.576  35.331  11.980  1.00 28.12           O  
HETATM 1303  O   HOH A 254       7.666  17.026   6.592  1.00 33.99           O  
HETATM 1304  O   HOH A 255      10.969  25.085  17.459  1.00 32.29           O  
HETATM 1305  O   HOH A 256      15.910  21.568  15.095  1.00 28.78           O  
HETATM 1306  O   HOH A 257       5.321  45.934   6.288  1.00 34.06           O  
HETATM 1307  O   HOH A 258       9.668  16.287   8.388  1.00 34.41           O  
HETATM 1308  O   HOH A 259      -5.624  18.490   8.875  1.00 30.08           O  
HETATM 1309  O   HOH A 260      -7.629  36.138   9.211  1.00 29.56           O  
HETATM 1310  O   HOH A 261       7.578  23.192  27.402  1.00 32.52           O  
HETATM 1311  O   HOH A 262       5.947  24.677  -5.169  0.53 24.69           O  
HETATM 1312  O   HOH A 263       7.345  45.772   4.449  1.00 31.82           O  
HETATM 1313  O   HOH A 264     -13.625  24.430   9.082  1.00 34.36           O  
HETATM 1314  O   HOH A 265     -11.656  20.261   3.866  1.00 26.62           O  
HETATM 1315  O   HOH A 266       6.779  34.588 -12.741  1.00 26.96           O  
HETATM 1316  O   HOH A 267      -4.507  45.986   1.764  1.00 29.15           O  
HETATM 1317  O   HOH A 268      15.784  21.076   5.666  1.00 35.02           O  
HETATM 1318  O   HOH A 269     -10.933  25.287  14.461  1.00 31.67           O  
HETATM 1319  O   HOH A 270       7.785  24.318  13.037  1.00 36.53           O  
HETATM 1320  O   HOH A 271      -0.254  40.253 -12.690  1.00 31.33           O  
HETATM 1321  O   HOH A 272     -16.089  24.335   7.874  1.00 34.92           O  
HETATM 1322  O   HOH A 273       5.663  46.950  -7.323  1.00 29.64           O  
HETATM 1323  O   HOH A 274      10.386  49.662  -4.252  1.00 35.71           O  
HETATM 1324  O   HOH A 275      18.493  41.665  -5.663  1.00 30.54           O  
HETATM 1325  O   HOH A 276       0.512  37.993  13.508  1.00 28.43           O  
HETATM 1326  O   HOH A 277      -4.585  20.910   0.596  1.00 28.74           O  
HETATM 1327  O   HOH A 278      -2.528  38.621  12.915  1.00 29.13           O  
HETATM 1328  O   HOH A 279       3.963  16.209   8.735  1.00 23.47           O  
HETATM 1329  O   HOH A 280      -0.320  50.192 -13.832  1.00 31.23           O  
HETATM 1330  O   HOH A 281       7.959  47.453   1.941  1.00 38.61           O  
HETATM 1331  O   HOH A 282      -7.281  21.246   1.613  1.00 35.91           O  
HETATM 1332  O   HOH A 283       4.859  32.445  17.934  1.00 31.87           O  
HETATM 1333  O   HOH A 284      11.491  31.928  18.783  1.00 38.47           O  
HETATM 1334  O   HOH A 285      13.096  49.817  -4.343  1.00 30.73           O  
HETATM 1335  O   HOH A 286      -9.540  31.273  19.632  1.00 28.55           O  
HETATM 1336  O   HOH A 287      -9.416  30.102 -10.869  1.00 34.25           O  
HETATM 1337  O   HOH A 288     -13.150  21.803   8.614  1.00 35.74           O  
HETATM 1338  O   HOH A 289       6.210  51.647  -3.492  1.00 29.52           O  
HETATM 1339  O   HOH A 290      -4.899  46.276  -5.239  1.00 33.72           O  
HETATM 1340  O   HOH A 291     -13.800  19.323   7.301  1.00 32.44           O  
HETATM 1341  O   HOH A 292      -0.756  47.563 -11.028  1.00 31.62           O  
HETATM 1342  O   HOH A 293       5.008  15.997  19.964  1.00 37.52           O  
HETATM 1343  O   HOH A 294       7.940  22.603  -0.106  1.00 35.80           O  
HETATM 1344  O   HOH A 295      -9.802  22.974  13.029  1.00 37.10           O  
HETATM 1345  O   HOH A 296      13.338  24.458  16.368  1.00 42.96           O  
HETATM 1346  O   HOH A 297       4.633  16.446  13.504  1.00 36.17           O  
HETATM 1347  O   HOH A 298      12.554  21.834  -0.005  0.50 26.06           O  
HETATM 1348  O   HOH A 299      14.023  24.262   0.003  0.50 40.06           O  
CONECT  726 1233                                                                
CONECT 1191 1195 1222                                                           
CONECT 1192 1198 1205                                                           
CONECT 1193 1208 1212                                                           
CONECT 1194 1215 1219                                                           
CONECT 1195 1191 1196 1229                                                      
CONECT 1196 1195 1197 1200                                                      
CONECT 1197 1196 1198 1199                                                      
CONECT 1198 1192 1197 1229                                                      
CONECT 1199 1197                                                                
CONECT 1200 1196 1201                                                           
CONECT 1201 1200 1202                                                           
CONECT 1202 1201 1203 1204                                                      
CONECT 1203 1202                                                                
CONECT 1204 1202                                                                
CONECT 1205 1192 1206 1230                                                      
CONECT 1206 1205 1207 1209                                                      
CONECT 1207 1206 1208 1210                                                      
CONECT 1208 1193 1207 1230                                                      
CONECT 1209 1206                                                                
CONECT 1210 1207 1211                                                           
CONECT 1211 1210                                                                
CONECT 1212 1193 1213 1231                                                      
CONECT 1213 1212 1214 1216                                                      
CONECT 1214 1213 1215 1217                                                      
CONECT 1215 1194 1214 1231                                                      
CONECT 1216 1213                                                                
CONECT 1217 1214 1218                                                           
CONECT 1218 1217                                                                
CONECT 1219 1194 1220 1232                                                      
CONECT 1220 1219 1221 1223                                                      
CONECT 1221 1220 1222 1224                                                      
CONECT 1222 1191 1221 1232                                                      
CONECT 1223 1220                                                                
CONECT 1224 1221 1225                                                           
CONECT 1225 1224 1226                                                           
CONECT 1226 1225 1227 1228                                                      
CONECT 1227 1226                                                                
CONECT 1228 1226                                                                
CONECT 1229 1195 1198 1233                                                      
CONECT 1230 1205 1208 1233                                                      
CONECT 1231 1212 1215 1233                                                      
CONECT 1232 1219 1222 1233                                                      
CONECT 1233  726 1229 1230 1231                                                 
CONECT 1233 1232 1249                                                           
CONECT 1234 1235 1236 1237 1238                                                 
CONECT 1235 1234                                                                
CONECT 1236 1234                                                                
CONECT 1237 1234                                                                
CONECT 1238 1234                                                                
CONECT 1239 1240 1241 1242 1243                                                 
CONECT 1240 1239                                                                
CONECT 1241 1239                                                                
CONECT 1242 1239                                                                
CONECT 1243 1239                                                                
CONECT 1244 1245 1246 1247 1248                                                 
CONECT 1245 1244                                                                
CONECT 1246 1244                                                                
CONECT 1247 1244                                                                
CONECT 1248 1244                                                                
CONECT 1249 1233                                                                
MASTER      319    0    4    8    0    0   11    6 1317    1   61   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.