CNRS Nantes University UFIP UFIP
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***  1abs  ***

elNémo ID: 22012923392058987

Job options:

ID        	=	 22012923392058987
JOBID     	=	 1abs
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 1abs

HEADER    OXYGEN STORAGE                          28-JAN-97   1ABS              
TITLE     PHOTOLYSED CARBONMONOXY-MYOGLOBIN AT 20 K                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: HEME BOUND TO HIS-93, PHOTOLYSED CO ATOP              
COMPND   7 HEME                                                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
SOURCE   4 ORGANISM_TAXID: 9755;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 OTHER_DETAILS: SYNTHETIC GENE                                        
KEYWDS    OXYGEN STORAGE, INTERMEDIATE IN LIGAND BINDING, RESPIRATORY           
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.SCHLICHTING,J.BERENDZEN,G.N.PHILLIPS JR.,R.M.SWEET                  
REVDAT   4   24-FEB-09 1ABS    1       VERSN                                    
REVDAT   3   03-MAY-05 1ABS    1       AUTHOR JRNL   REMARK                     
REVDAT   2   01-APR-03 1ABS    1       JRNL                                     
REVDAT   1   01-APR-97 1ABS    0                                                
JRNL        AUTH   I.SCHLICHTING,J.BERENDZEN,G.N.PHILLIPS JR.,                  
JRNL        AUTH 2 R.M.SWEET                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF PHOTOLYSED                              
JRNL        TITL 2 CARBONMONOXY-MYOGLOBIN.                                      
JRNL        REF    NATURE                        V. 371   808 1994              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7935843                                                      
JRNL        DOI    10.1038/371808A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.N.PHILLIPS JR.,R.M.ARDUINI,B.A.SPRINGER,                   
REMARK   1  AUTH 2 S.G.SLIGAR                                                   
REMARK   1  TITL   CRYSTAL STRUCTURE OF MYOGLOBIN FROM A SYNTHETIC              
REMARK   1  TITL 2 GENE                                                         
REMARK   1  REF    PROTEINS                      V.   7   358 1990              
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   B.A.SPRINGER,S.G.SLIGAR                                      
REMARK   1  TITL   HIGH-LEVEL EXPRESSION OF SPERM WHALE MYOGLOBIN IN            
REMARK   1  TITL 2 ESCHERICHIA COLI                                             
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  84  8961 1987              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 29798                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3348                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1225                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 119                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 6.40                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.06                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 7.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : N.A                                                     
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROLSQ.PRO                                     
REMARK   3  PARAMETER FILE  2  : PARAM19X.HEME                                  
REMARK   3  PARAMETER FILE  3  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  4  : SO4.PARM                                       
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : TOPH19X.HEME                                   
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : SO4.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HEME PARAMETERS WERE RELAXED TO           
REMARK   3  ALLOW FOR REFINEMENT OF UNLIGATED, PHOTOLYSED, AND CO-BOUND         
REMARK   3  COMPLEX.                                                            
REMARK   4                                                                      
REMARK   4 1ABS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAR-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 20                                 
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91                               
REMARK 200  MONOCHROMATOR                  : YES                                
REMARK 200  OPTICS                         : YES                                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, XSCALE                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30947                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.0                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: 2MGK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE COLLECTED UNDER CONTINUOUS ILLUMINATION USING      
REMARK 200  AN OPEN FLOW HELIUM CRYOSTAT FOR COOLING.                           
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 3.6 M      
REMARK 280  AMMONIUM SULFATE. CRYSTALS WER SOAKED FOR 1 HOUR IN A               
REMARK 280  THOROUGHLY DEGASSED AND N2 - SATURATED CRYOPROTECTANT SOLUTION      
REMARK 280  MADE BY ADDITION OF 100 MG SUCROSE, 100 MG GLUCOSE AND 8 MG NA      
REMARK 280  -DITHIONATE TO 1 ML OF 70% SATURATED AMMONIUM SULFATE WITH 50       
REMARK 280  MM TRIS. HCL PH 9.0. THEN THE SOLUTION WAS EXCHANGED AGAINST A      
REMARK 280  CO SATURATED ONE. DISTINCT COLOR CHANGES ACCOMPANIED THE            
REMARK 280  FORMATION OF UNLIGATED MYOGLOBIN FROM MET-MB AND MBCO FROM          
REMARK 280  UNLIGATED MB.                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  48   NE2   HIS A  48   CD2    -0.068                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP A   7   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP A   7   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TRP A  14   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP A  14   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  20       70.98   -162.04                                   
REMARK 500    LYS A  98       67.13     62.92                                   
REMARK 500    TYR A 151      -53.12   -122.04                                   
REMARK 500    GLN A 152       33.40     35.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A  94        -10.22                                           
REMARK 500    GLY A 150        -11.03                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 154                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 155                 
DBREF  1ABS A    0   153  UNP    P02185   MYG_PHYCA        1    154             
SEQRES   1 A  154  MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS          
SEQRES   2 A  154  VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY          
SEQRES   3 A  154  GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU          
SEQRES   4 A  154  THR LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR          
SEQRES   5 A  154  GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS          
SEQRES   6 A  154  GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS          
SEQRES   7 A  154  LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA          
SEQRES   8 A  154  GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR          
SEQRES   9 A  154  LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS          
SEQRES  10 A  154  SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY          
SEQRES  11 A  154  ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE          
SEQRES  12 A  154  ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                  
HET    SO4  A 156       5                                                       
HET    HEM  A 154      43                                                       
HET    CMO  A 155       2                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CMO CARBON MONOXIDE                                                  
HETSYN     HEM HEME                                                             
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
FORMUL   4  CMO    C O                                                          
FORMUL   5  HOH   *118(H2 O)                                                    
HELIX    1   A SER A    3  GLU A   18  1                                  16    
HELIX    2   B ASP A   20  SER A   35  1                                  16    
HELIX    3   C HIS A   36  LYS A   42  1                                   7    
HELIX    4   D THR A   51  ALA A   57  1                                   7    
HELIX    5   E SER A   58  LYS A   77  1                                  20    
HELIX    6   F LEU A   86  THR A   95  1                                  10    
HELIX    7   G PRO A  100  ARG A  118  1                                  19    
HELIX    8   H GLY A  124  LEU A  149  1                                  26    
LINK        FE   HEM A 154                 NE2 HIS A  93     1555   1555  2.25  
SITE     1 AC1  6 SER A   3  GLU A   4  THR A  51  GLU A  52                    
SITE     2 AC1  6 ALA A  53  HOH A 425                                          
SITE     1 AC2 17 LYS A  42  PHE A  43  ARG A  45  HIS A  64                    
SITE     2 AC2 17 VAL A  68  ALA A  71  LEU A  89  SER A  92                    
SITE     3 AC2 17 HIS A  93  HIS A  97  ILE A  99  TYR A 103                    
SITE     4 AC2 17 CMO A 155  HOH A 242  HOH A 303  HOH A 308                    
SITE     5 AC2 17 HOH A 309                                                     
SITE     1 AC3  5 LEU A  29  PHE A  43  VAL A  68  ILE A 107                    
SITE     2 AC3  5 HEM A 154                                                     
CRYST1   90.420   90.420   45.400  90.00  90.00 120.00 P 6           6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011060  0.006385  0.000000        0.00000                         
SCALE2      0.000000  0.012770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022026        0.00000                         
ATOM      1  N   MET A   0      23.612   8.367  -9.458  1.00 26.59           N  
ATOM      2  CA  MET A   0      23.871   9.800  -9.365  1.00 25.47           C  
ATOM      3  C   MET A   0      25.258  10.146  -9.871  1.00 23.93           C  
ATOM      4  O   MET A   0      26.193   9.343  -9.767  1.00 24.76           O  
ATOM      5  CB  MET A   0      23.749  10.277  -7.931  1.00 26.67           C  
ATOM      6  CG  MET A   0      24.410   9.317  -6.955  1.00 27.31           C  
ATOM      7  SD  MET A   0      23.997   9.709  -5.244  1.00 27.80           S  
ATOM      8  CE  MET A   0      24.625  11.379  -5.216  1.00 25.33           C  
ATOM      9  N   VAL A   1      25.410  11.314 -10.492  1.00 21.05           N  
ATOM     10  CA  VAL A   1      26.714  11.686 -11.004  1.00 17.92           C  
ATOM     11  C   VAL A   1      26.993  13.165 -10.812  1.00 15.00           C  
ATOM     12  O   VAL A   1      26.274  14.013 -11.332  1.00 15.16           O  
ATOM     13  CB  VAL A   1      26.807  11.327 -12.493  1.00 18.63           C  
ATOM     14  CG1 VAL A   1      28.216  11.571 -13.009  1.00 17.65           C  
ATOM     15  CG2 VAL A   1      26.413   9.872 -12.704  1.00 19.36           C  
ATOM     16  N   LEU A   2      28.106  13.504 -10.166  1.00 11.18           N  
ATOM     17  CA  LEU A   2      28.441  14.899  -9.950  1.00  9.10           C  
ATOM     18  C   LEU A   2      29.165  15.513 -11.144  1.00  8.17           C  
ATOM     19  O   LEU A   2      29.774  14.817 -11.960  1.00  8.04           O  
ATOM     20  CB  LEU A   2      29.360  15.038  -8.744  1.00  7.88           C  
ATOM     21  CG  LEU A   2      28.737  15.043  -7.355  1.00  6.71           C  
ATOM     22  CD1 LEU A   2      28.363  13.622  -6.956  1.00  5.77           C  
ATOM     23  CD2 LEU A   2      29.701  15.664  -6.349  1.00  5.62           C  
ATOM     24  N   SER A   3      28.925  16.792 -11.392  1.00  7.24           N  
ATOM     25  CA  SER A   3      29.616  17.466 -12.471  1.00  7.20           C  
ATOM     26  C   SER A   3      31.013  17.851 -11.998  1.00  7.02           C  
ATOM     27  O   SER A   3      31.312  17.776 -10.809  1.00  7.29           O  
ATOM     28  CB  SER A   3      28.864  18.735 -12.831  1.00  7.40           C  
ATOM     29  OG  SER A   3      28.994  19.670 -11.767  1.00  7.98           O  
ATOM     30  N   GLU A   4      31.927  18.195 -12.903  1.00  6.78           N  
ATOM     31  CA  GLU A   4      33.255  18.598 -12.476  1.00  6.62           C  
ATOM     32  C   GLU A   4      33.159  19.830 -11.589  1.00  6.33           C  
ATOM     33  O   GLU A   4      33.971  20.018 -10.685  1.00  6.74           O  
ATOM     34  CB  GLU A   4      34.131  18.900 -13.693  1.00  7.59           C  
ATOM     35  CG  GLU A   4      35.447  19.602 -13.350  1.00  8.85           C  
ATOM     36  CD  GLU A   4      36.494  18.692 -12.716  1.00  9.53           C  
ATOM     37  OE1 GLU A   4      36.221  17.506 -12.552  1.00  9.43           O  
ATOM     38  OE2 GLU A   4      37.592  19.162 -12.403  1.00 10.86           O  
ATOM     39  N   GLY A   5      32.246  20.752 -11.913  1.00  6.39           N  
ATOM     40  CA  GLY A   5      32.074  21.945 -11.100  1.00  5.78           C  
ATOM     41  C   GLY A   5      31.700  21.572  -9.665  1.00  5.38           C  
ATOM     42  O   GLY A   5      32.193  22.153  -8.701  1.00  5.09           O  
ATOM     43  N   GLU A   6      30.812  20.590  -9.494  1.00  5.67           N  
ATOM     44  CA  GLU A   6      30.444  20.169  -8.154  1.00  6.07           C  
ATOM     45  C   GLU A   6      31.646  19.544  -7.450  1.00  6.09           C  
ATOM     46  O   GLU A   6      31.935  19.867  -6.295  1.00  5.69           O  
ATOM     47  CB  GLU A   6      29.292  19.175  -8.224  1.00  7.00           C  
ATOM     48  CG  GLU A   6      27.976  19.882  -8.536  1.00  7.68           C  
ATOM     49  CD  GLU A   6      26.819  18.956  -8.901  1.00  8.98           C  
ATOM     50  OE1 GLU A   6      27.063  17.832  -9.329  1.00  8.53           O  
ATOM     51  OE2 GLU A   6      25.670  19.397  -8.843  1.00  9.52           O  
ATOM     52  N   TRP A   7      32.413  18.686  -8.142  1.00  5.53           N  
ATOM     53  CA  TRP A   7      33.590  18.100  -7.518  1.00  5.46           C  
ATOM     54  C   TRP A   7      34.575  19.197  -7.127  1.00  6.22           C  
ATOM     55  O   TRP A   7      35.233  19.101  -6.096  1.00  5.92           O  
ATOM     56  CB  TRP A   7      34.286  17.108  -8.455  1.00  5.56           C  
ATOM     57  CG  TRP A   7      33.602  15.741  -8.487  1.00  5.37           C  
ATOM     58  CD1 TRP A   7      33.057  15.257  -9.648  1.00  4.80           C  
ATOM     59  CD2 TRP A   7      33.417  14.894  -7.414  1.00  4.87           C  
ATOM     60  NE1 TRP A   7      32.508  14.107  -9.311  1.00  4.14           N  
ATOM     61  CE2 TRP A   7      32.678  13.859  -7.993  1.00  4.62           C  
ATOM     62  CE3 TRP A   7      33.752  14.847  -6.066  1.00  4.67           C  
ATOM     63  CZ2 TRP A   7      32.251  12.774  -7.239  1.00  4.55           C  
ATOM     64  CZ3 TRP A   7      33.329  13.755  -5.313  1.00  4.10           C  
ATOM     65  CH2 TRP A   7      32.582  12.733  -5.887  1.00  4.63           C  
ATOM     66  N   GLN A   8      34.720  20.271  -7.923  1.00  6.51           N  
ATOM     67  CA  GLN A   8      35.659  21.304  -7.528  1.00  7.10           C  
ATOM     68  C   GLN A   8      35.222  22.015  -6.252  1.00  6.28           C  
ATOM     69  O   GLN A   8      36.055  22.391  -5.429  1.00  5.59           O  
ATOM     70  CB  GLN A   8      35.869  22.300  -8.658  1.00  9.22           C  
ATOM     71  CG  GLN A   8      36.738  21.721  -9.773  1.00 11.92           C  
ATOM     72  CD  GLN A   8      38.046  21.101  -9.281  1.00 14.26           C  
ATOM     73  OE1 GLN A   8      38.723  21.619  -8.387  1.00 16.46           O  
ATOM     74  NE2 GLN A   8      38.448  19.960  -9.843  1.00 15.54           N  
ATOM     75  N   LEU A   9      33.916  22.189  -6.040  1.00  5.73           N  
ATOM     76  CA  LEU A   9      33.458  22.818  -4.809  1.00  5.38           C  
ATOM     77  C   LEU A   9      33.751  21.901  -3.622  1.00  5.42           C  
ATOM     78  O   LEU A   9      34.180  22.346  -2.552  1.00  5.26           O  
ATOM     79  CB  LEU A   9      31.962  23.089  -4.876  1.00  5.38           C  
ATOM     80  CG  LEU A   9      31.503  24.181  -5.843  1.00  6.77           C  
ATOM     81  CD1 LEU A   9      29.982  24.241  -5.905  1.00  6.66           C  
ATOM     82  CD2 LEU A   9      32.073  25.531  -5.433  1.00  7.04           C  
ATOM     83  N   VAL A  10      33.700  20.582  -3.853  1.00  4.60           N  
ATOM     84  CA  VAL A  10      33.974  19.625  -2.796  1.00  4.62           C  
ATOM     85  C   VAL A  10      35.461  19.646  -2.461  1.00  4.31           C  
ATOM     86  O   VAL A  10      35.876  19.751  -1.314  1.00  4.18           O  
ATOM     87  CB  VAL A  10      33.555  18.205  -3.257  1.00  4.07           C  
ATOM     88  CG1 VAL A  10      34.085  17.134  -2.306  1.00  3.86           C  
ATOM     89  CG2 VAL A  10      32.037  18.111  -3.365  1.00  4.68           C  
ATOM     90  N   LEU A  11      36.301  19.611  -3.482  1.00  5.05           N  
ATOM     91  CA  LEU A  11      37.730  19.605  -3.262  1.00  5.97           C  
ATOM     92  C   LEU A  11      38.266  20.948  -2.786  1.00  6.26           C  
ATOM     93  O   LEU A  11      39.232  20.995  -2.026  1.00  6.46           O  
ATOM     94  CB  LEU A  11      38.414  19.172  -4.548  1.00  7.03           C  
ATOM     95  CG  LEU A  11      38.025  17.790  -5.052  1.00  7.99           C  
ATOM     96  CD1 LEU A  11      38.715  17.482  -6.371  1.00  9.50           C  
ATOM     97  CD2 LEU A  11      38.373  16.736  -4.010  1.00  9.73           C  
ATOM     98  N   HIS A  12      37.554  22.049  -3.039  1.00  7.00           N  
ATOM     99  CA  HIS A  12      38.052  23.320  -2.567  1.00  7.99           C  
ATOM    100  C   HIS A  12      37.862  23.459  -1.070  1.00  6.88           C  
ATOM    101  O   HIS A  12      38.654  24.106  -0.390  1.00  7.05           O  
ATOM    102  CB  HIS A  12      37.387  24.460  -3.314  1.00 11.49           C  
ATOM    103  CG  HIS A  12      38.195  24.796  -4.556  1.00 15.84           C  
ATOM    104  ND1 HIS A  12      39.254  25.596  -4.535  1.00 18.10           N  
ATOM    105  CD2 HIS A  12      38.101  24.186  -5.778  1.00 17.75           C  
ATOM    106  CE1 HIS A  12      39.815  25.479  -5.722  1.00 18.99           C  
ATOM    107  NE2 HIS A  12      39.122  24.635  -6.465  1.00 19.38           N  
ATOM    108  N   VAL A  13      36.759  22.955  -0.529  1.00  5.80           N  
ATOM    109  CA  VAL A  13      36.612  23.039   0.910  1.00  5.18           C  
ATOM    110  C   VAL A  13      37.450  21.958   1.576  1.00  4.90           C  
ATOM    111  O   VAL A  13      37.957  22.147   2.680  1.00  4.86           O  
ATOM    112  CB  VAL A  13      35.142  22.930   1.337  1.00  5.09           C  
ATOM    113  CG1 VAL A  13      34.645  21.497   1.167  1.00  5.70           C  
ATOM    114  CG2 VAL A  13      35.001  23.379   2.790  1.00  4.94           C  
ATOM    115  N   TRP A  14      37.670  20.808   0.924  1.00  4.52           N  
ATOM    116  CA  TRP A  14      38.507  19.785   1.545  1.00  4.44           C  
ATOM    117  C   TRP A  14      39.940  20.287   1.690  1.00  4.38           C  
ATOM    118  O   TRP A  14      40.692  19.891   2.591  1.00  4.12           O  
ATOM    119  CB  TRP A  14      38.508  18.481   0.748  1.00  4.99           C  
ATOM    120  CG  TRP A  14      38.746  17.284   1.664  1.00  4.48           C  
ATOM    121  CD1 TRP A  14      39.946  16.624   1.696  1.00  5.78           C  
ATOM    122  CD2 TRP A  14      37.866  16.828   2.615  1.00  5.48           C  
ATOM    123  NE1 TRP A  14      39.826  15.758   2.684  1.00  4.49           N  
ATOM    124  CE2 TRP A  14      38.612  15.839   3.259  1.00  5.47           C  
ATOM    125  CE3 TRP A  14      36.571  17.122   3.015  1.00  5.67           C  
ATOM    126  CZ2 TRP A  14      38.066  15.125   4.315  1.00  5.94           C  
ATOM    127  CZ3 TRP A  14      36.030  16.410   4.075  1.00  5.97           C  
ATOM    128  CH2 TRP A  14      36.771  15.424   4.716  1.00  6.52           C  
ATOM    129  N   ALA A  15      40.367  21.145   0.761  1.00  4.32           N  
ATOM    130  CA  ALA A  15      41.701  21.701   0.846  1.00  4.46           C  
ATOM    131  C   ALA A  15      41.863  22.475   2.141  1.00  5.07           C  
ATOM    132  O   ALA A  15      42.964  22.616   2.666  1.00  5.44           O  
ATOM    133  CB  ALA A  15      41.910  22.681  -0.294  1.00  4.54           C  
ATOM    134  N   LYS A  16      40.787  23.081   2.643  1.00  5.12           N  
ATOM    135  CA  LYS A  16      40.892  23.822   3.893  1.00  5.45           C  
ATOM    136  C   LYS A  16      40.919  22.849   5.071  1.00  5.44           C  
ATOM    137  O   LYS A  16      41.615  23.060   6.074  1.00  4.93           O  
ATOM    138  CB  LYS A  16      39.723  24.789   4.046  1.00  6.36           C  
ATOM    139  CG  LYS A  16      39.538  25.712   2.848  1.00  7.01           C  
ATOM    140  CD  LYS A  16      40.778  26.573   2.634  1.00  9.54           C  
ATOM    141  CE  LYS A  16      40.833  27.049   1.188  1.00 11.84           C  
ATOM    142  NZ  LYS A  16      42.043  27.810   0.928  1.00 14.22           N  
ATOM    143  N   VAL A  17      40.125  21.774   4.983  1.00  5.16           N  
ATOM    144  CA  VAL A  17      40.151  20.762   6.020  1.00  5.19           C  
ATOM    145  C   VAL A  17      41.571  20.234   6.178  1.00  4.96           C  
ATOM    146  O   VAL A  17      42.073  20.022   7.286  1.00  5.15           O  
ATOM    147  CB  VAL A  17      39.230  19.603   5.613  1.00  5.74           C  
ATOM    148  CG1 VAL A  17      39.458  18.388   6.502  1.00  5.90           C  
ATOM    149  CG2 VAL A  17      37.781  20.061   5.651  1.00  6.09           C  
ATOM    150  N   GLU A  18      42.282  20.090   5.055  1.00  5.24           N  
ATOM    151  CA  GLU A  18      43.632  19.557   5.093  1.00  4.96           C  
ATOM    152  C   GLU A  18      44.652  20.477   5.756  1.00  4.82           C  
ATOM    153  O   GLU A  18      45.831  20.128   5.870  1.00  4.47           O  
ATOM    154  CB  GLU A  18      44.069  19.197   3.683  1.00  5.38           C  
ATOM    155  CG  GLU A  18      43.277  18.000   3.195  1.00  6.20           C  
ATOM    156  CD  GLU A  18      43.683  17.514   1.818  1.00  7.29           C  
ATOM    157  OE1 GLU A  18      44.053  18.336   0.980  1.00  7.06           O  
ATOM    158  OE2 GLU A  18      43.635  16.304   1.597  1.00  7.10           O  
ATOM    159  N   ALA A  19      44.298  21.739   6.017  1.00  4.94           N  
ATOM    160  CA  ALA A  19      45.247  22.597   6.703  1.00  4.81           C  
ATOM    161  C   ALA A  19      45.468  22.072   8.122  1.00  5.08           C  
ATOM    162  O   ALA A  19      46.540  22.237   8.698  1.00  5.45           O  
ATOM    163  CB  ALA A  19      44.686  24.005   6.813  1.00  4.78           C  
ATOM    164  N   ASP A  20      44.502  21.293   8.638  1.00  4.85           N  
ATOM    165  CA  ASP A  20      44.586  20.728   9.985  1.00  4.84           C  
ATOM    166  C   ASP A  20      43.598  19.570  10.098  1.00  3.93           C  
ATOM    167  O   ASP A  20      42.507  19.695  10.669  1.00  3.60           O  
ATOM    168  CB  ASP A  20      44.240  21.807  11.007  1.00  6.49           C  
ATOM    169  CG  ASP A  20      44.160  21.297  12.446  1.00  6.97           C  
ATOM    170  OD1 ASP A  20      44.679  20.228  12.739  1.00  7.28           O  
ATOM    171  OD2 ASP A  20      43.435  21.897  13.234  1.00 10.35           O  
ATOM    172  N   VAL A  21      43.893  18.465   9.431  1.00  3.19           N  
ATOM    173  CA  VAL A  21      42.953  17.363   9.450  1.00  3.82           C  
ATOM    174  C   VAL A  21      42.671  16.832  10.845  1.00  3.33           C  
ATOM    175  O   VAL A  21      41.520  16.535  11.166  1.00  3.26           O  
ATOM    176  CB  VAL A  21      43.400  16.229   8.496  1.00  4.54           C  
ATOM    177  CG1 VAL A  21      44.663  15.538   8.983  1.00  5.05           C  
ATOM    178  CG2 VAL A  21      42.276  15.215   8.341  1.00  4.76           C  
ATOM    179  N   ALA A  22      43.650  16.892  11.750  1.00  3.30           N  
ATOM    180  CA  ALA A  22      43.422  16.392  13.100  1.00  3.84           C  
ATOM    181  C   ALA A  22      42.365  17.211  13.844  1.00  3.95           C  
ATOM    182  O   ALA A  22      41.424  16.658  14.424  1.00  3.53           O  
ATOM    183  CB  ALA A  22      44.726  16.444  13.887  1.00  3.84           C  
ATOM    184  N   GLY A  23      42.427  18.545  13.752  1.00  2.93           N  
ATOM    185  CA  GLY A  23      41.437  19.369  14.423  1.00  2.87           C  
ATOM    186  C   GLY A  23      40.045  19.158  13.840  1.00  3.08           C  
ATOM    187  O   GLY A  23      39.054  19.132  14.567  1.00  3.32           O  
ATOM    188  N   HIS A  24      39.929  19.091  12.505  1.00  2.74           N  
ATOM    189  CA  HIS A  24      38.623  18.879  11.895  1.00  3.15           C  
ATOM    190  C   HIS A  24      38.060  17.509  12.276  1.00  3.45           C  
ATOM    191  O   HIS A  24      36.863  17.360  12.518  1.00  3.16           O  
ATOM    192  CB  HIS A  24      38.708  18.983  10.369  1.00  3.69           C  
ATOM    193  CG  HIS A  24      38.948  20.405   9.860  1.00  4.20           C  
ATOM    194  ND1 HIS A  24      40.132  21.014   9.919  1.00  5.11           N  
ATOM    195  CD2 HIS A  24      38.036  21.234   9.254  1.00  4.63           C  
ATOM    196  CE1 HIS A  24      39.956  22.204   9.365  1.00  4.48           C  
ATOM    197  NE2 HIS A  24      38.705  22.332   8.963  1.00  4.42           N  
ATOM    198  N   GLY A  25      38.914  16.478  12.346  1.00  2.75           N  
ATOM    199  CA  GLY A  25      38.446  15.150  12.712  1.00  3.36           C  
ATOM    200  C   GLY A  25      37.906  15.142  14.134  1.00  3.86           C  
ATOM    201  O   GLY A  25      36.937  14.450  14.437  1.00  3.72           O  
ATOM    202  N   GLN A  26      38.576  15.829  15.067  1.00  4.10           N  
ATOM    203  CA  GLN A  26      38.068  15.866  16.429  1.00  5.01           C  
ATOM    204  C   GLN A  26      36.687  16.503  16.456  1.00  4.73           C  
ATOM    205  O   GLN A  26      35.753  15.993  17.073  1.00  4.85           O  
ATOM    206  CB  GLN A  26      38.965  16.700  17.329  1.00  6.20           C  
ATOM    207  CG  GLN A  26      40.288  16.044  17.662  1.00  8.35           C  
ATOM    208  CD  GLN A  26      41.172  17.005  18.428  1.00  9.44           C  
ATOM    209  OE1 GLN A  26      41.423  18.126  17.987  1.00 10.65           O  
ATOM    210  NE2 GLN A  26      41.617  16.616  19.627  1.00 10.87           N  
ATOM    211  N   ASP A  27      36.543  17.667  15.822  1.00  4.36           N  
ATOM    212  CA  ASP A  27      35.254  18.340  15.806  1.00  4.62           C  
ATOM    213  C   ASP A  27      34.159  17.456  15.230  1.00  4.36           C  
ATOM    214  O   ASP A  27      33.039  17.411  15.734  1.00  3.72           O  
ATOM    215  CB  ASP A  27      35.328  19.601  14.952  1.00  6.09           C  
ATOM    216  CG  ASP A  27      36.019  20.776  15.619  1.00  7.21           C  
ATOM    217  OD1 ASP A  27      36.613  20.581  16.683  1.00  8.09           O  
ATOM    218  OD2 ASP A  27      36.178  21.801  14.948  1.00  7.86           O  
ATOM    219  N   ILE A  28      34.454  16.770  14.130  1.00  3.58           N  
ATOM    220  CA  ILE A  28      33.453  15.940  13.491  1.00  3.68           C  
ATOM    221  C   ILE A  28      33.072  14.715  14.316  1.00  3.71           C  
ATOM    222  O   ILE A  28      31.889  14.382  14.446  1.00  3.66           O  
ATOM    223  CB  ILE A  28      33.962  15.575  12.086  1.00  3.50           C  
ATOM    224  CG1 ILE A  28      33.897  16.806  11.185  1.00  4.39           C  
ATOM    225  CG2 ILE A  28      33.158  14.429  11.496  1.00  3.96           C  
ATOM    226  CD1 ILE A  28      34.586  16.615   9.820  1.00  4.27           C  
ATOM    227  N   LEU A  29      34.034  13.990  14.884  1.00  3.10           N  
ATOM    228  CA  LEU A  29      33.651  12.840  15.684  1.00  3.90           C  
ATOM    229  C   LEU A  29      32.909  13.273  16.945  1.00  4.56           C  
ATOM    230  O   LEU A  29      31.997  12.593  17.425  1.00  4.65           O  
ATOM    231  CB  LEU A  29      34.878  12.018  16.061  1.00  3.90           C  
ATOM    232  CG  LEU A  29      35.612  11.312  14.925  1.00  4.14           C  
ATOM    233  CD1 LEU A  29      36.813  10.532  15.442  1.00  5.32           C  
ATOM    234  CD2 LEU A  29      34.668  10.381  14.181  1.00  4.31           C  
ATOM    235  N   ILE A  30      33.354  14.351  17.583  1.00  5.20           N  
ATOM    236  CA  ILE A  30      32.679  14.812  18.782  1.00  5.93           C  
ATOM    237  C   ILE A  30      31.273  15.291  18.462  1.00  6.29           C  
ATOM    238  O   ILE A  30      30.331  14.988  19.193  1.00  5.77           O  
ATOM    239  CB  ILE A  30      33.502  15.929  19.445  1.00  6.49           C  
ATOM    240  CG1 ILE A  30      34.788  15.363  20.036  1.00  6.58           C  
ATOM    241  CG2 ILE A  30      32.673  16.637  20.512  1.00  6.89           C  
ATOM    242  CD1 ILE A  30      35.722  16.446  20.617  1.00  7.12           C  
ATOM    243  N   ARG A  31      31.070  15.901  17.287  1.00  6.46           N  
ATOM    244  CA  ARG A  31      29.739  16.366  16.920  1.00  7.83           C  
ATOM    245  C   ARG A  31      28.831  15.178  16.640  1.00  7.44           C  
ATOM    246  O   ARG A  31      27.690  15.131  17.100  1.00  7.38           O  
ATOM    247  CB  ARG A  31      29.864  17.311  15.719  1.00  9.49           C  
ATOM    248  CG  ARG A  31      28.719  17.339  14.713  1.00 13.04           C  
ATOM    249  CD  ARG A  31      27.374  17.600  15.360  1.00 17.43           C  
ATOM    250  NE  ARG A  31      27.259  18.919  15.943  1.00 19.24           N  
ATOM    251  CZ  ARG A  31      26.057  19.505  16.095  1.00 20.67           C  
ATOM    252  NH1 ARG A  31      25.007  19.140  15.353  1.00 21.36           N  
ATOM    253  NH2 ARG A  31      26.018  20.707  16.662  1.00 21.50           N  
ATOM    254  N   LEU A  32      29.414  14.095  16.125  1.00  6.27           N  
ATOM    255  CA  LEU A  32      28.648  12.891  15.863  1.00  6.66           C  
ATOM    256  C   LEU A  32      28.201  12.258  17.182  1.00  7.05           C  
ATOM    257  O   LEU A  32      27.048  11.846  17.341  1.00  6.73           O  
ATOM    258  CB  LEU A  32      29.528  11.895  15.113  1.00  6.49           C  
ATOM    259  CG  LEU A  32      29.009  10.465  14.943  1.00  6.37           C  
ATOM    260  CD1 LEU A  32      27.787  10.452  14.031  1.00  4.95           C  
ATOM    261  CD2 LEU A  32      30.108   9.566  14.379  1.00  4.62           C  
ATOM    262  N   PHE A  33      29.149  12.058  18.103  1.00  6.65           N  
ATOM    263  CA  PHE A  33      28.834  11.439  19.384  1.00  7.65           C  
ATOM    264  C   PHE A  33      27.854  12.275  20.204  1.00  9.22           C  
ATOM    265  O   PHE A  33      27.040  11.746  20.970  1.00  9.79           O  
ATOM    266  CB  PHE A  33      30.107  11.232  20.199  1.00  6.93           C  
ATOM    267  CG  PHE A  33      31.165  10.348  19.544  1.00  6.45           C  
ATOM    268  CD1 PHE A  33      30.801   9.349  18.647  1.00  6.85           C  
ATOM    269  CD2 PHE A  33      32.508  10.540  19.860  1.00  7.11           C  
ATOM    270  CE1 PHE A  33      31.780   8.550  18.072  1.00  6.09           C  
ATOM    271  CE2 PHE A  33      33.478   9.732  19.278  1.00  7.33           C  
ATOM    272  CZ  PHE A  33      33.111   8.740  18.385  1.00  7.03           C  
ATOM    273  N   LYS A  34      27.961  13.599  20.147  1.00  9.80           N  
ATOM    274  CA  LYS A  34      27.046  14.411  20.925  1.00 11.56           C  
ATOM    275  C   LYS A  34      25.644  14.478  20.329  1.00 11.35           C  
ATOM    276  O   LYS A  34      24.642  14.367  21.036  1.00 11.44           O  
ATOM    277  CB  LYS A  34      27.613  15.813  21.073  1.00 13.69           C  
ATOM    278  CG  LYS A  34      28.739  15.848  22.097  1.00 16.73           C  
ATOM    279  CD  LYS A  34      29.706  16.978  21.781  1.00 20.27           C  
ATOM    280  CE  LYS A  34      29.428  18.173  22.676  1.00 22.10           C  
ATOM    281  NZ  LYS A  34      28.804  19.240  21.916  1.00 23.30           N  
ATOM    282  N   SER A  35      25.538  14.504  19.004  1.00 10.97           N  
ATOM    283  CA  SER A  35      24.234  14.583  18.371  1.00 10.50           C  
ATOM    284  C   SER A  35      23.527  13.238  18.347  1.00 10.03           C  
ATOM    285  O   SER A  35      22.298  13.170  18.261  1.00  9.71           O  
ATOM    286  CB  SER A  35      24.393  15.085  16.949  1.00 11.12           C  
ATOM    287  OG  SER A  35      24.873  16.419  16.961  1.00 14.05           O  
ATOM    288  N   HIS A  36      24.307  12.163  18.220  1.00  9.76           N  
ATOM    289  CA  HIS A  36      23.740  10.829  18.182  1.00  9.38           C  
ATOM    290  C   HIS A  36      24.573   9.912  19.062  1.00  8.90           C  
ATOM    291  O   HIS A  36      25.394   9.142  18.585  1.00  8.44           O  
ATOM    292  CB  HIS A  36      23.745  10.316  16.748  1.00  9.71           C  
ATOM    293  CG  HIS A  36      23.041  11.262  15.785  1.00 10.08           C  
ATOM    294  ND1 HIS A  36      21.731  11.252  15.599  1.00 10.50           N  
ATOM    295  CD2 HIS A  36      23.618  12.218  14.995  1.00  9.94           C  
ATOM    296  CE1 HIS A  36      21.490  12.184  14.705  1.00 10.46           C  
ATOM    297  NE2 HIS A  36      22.621  12.759  14.344  1.00 10.35           N  
ATOM    298  N   PRO A  37      24.373   9.958  20.378  1.00  9.24           N  
ATOM    299  CA  PRO A  37      25.208   9.236  21.334  1.00  8.88           C  
ATOM    300  C   PRO A  37      25.266   7.730  21.120  1.00  9.07           C  
ATOM    301  O   PRO A  37      26.264   7.084  21.433  1.00  8.74           O  
ATOM    302  CB  PRO A  37      24.612   9.598  22.674  1.00  9.62           C  
ATOM    303  CG  PRO A  37      23.778  10.843  22.486  1.00  9.48           C  
ATOM    304  CD  PRO A  37      23.502  10.953  21.003  1.00  9.41           C  
ATOM    305  N   GLU A  38      24.239   7.154  20.498  1.00  9.05           N  
ATOM    306  CA  GLU A  38      24.238   5.719  20.246  1.00  9.49           C  
ATOM    307  C   GLU A  38      25.379   5.308  19.313  1.00  9.03           C  
ATOM    308  O   GLU A  38      25.899   4.187  19.379  1.00  9.26           O  
ATOM    309  CB  GLU A  38      22.896   5.307  19.647  1.00 10.11           C  
ATOM    310  CG  GLU A  38      22.651   5.896  18.264  1.00 11.92           C  
ATOM    311  CD  GLU A  38      21.709   7.098  18.248  1.00 13.59           C  
ATOM    312  OE1 GLU A  38      21.887   8.017  19.055  1.00 13.47           O  
ATOM    313  OE2 GLU A  38      20.959   7.223  17.280  1.00 14.89           O  
ATOM    314  N   THR A  39      25.900   6.258  18.525  1.00  8.36           N  
ATOM    315  CA  THR A  39      26.998   5.934  17.626  1.00  7.48           C  
ATOM    316  C   THR A  39      28.299   5.672  18.380  1.00  8.00           C  
ATOM    317  O   THR A  39      29.145   4.891  17.942  1.00  7.71           O  
ATOM    318  CB  THR A  39      27.210   7.049  16.583  1.00  7.15           C  
ATOM    319  OG1 THR A  39      27.655   8.200  17.293  1.00  6.22           O  
ATOM    320  CG2 THR A  39      25.954   7.341  15.775  1.00  6.96           C  
ATOM    321  N   LEU A  40      28.493   6.321  19.529  1.00  7.66           N  
ATOM    322  CA  LEU A  40      29.703   6.108  20.304  1.00  8.38           C  
ATOM    323  C   LEU A  40      29.786   4.672  20.820  1.00  8.68           C  
ATOM    324  O   LEU A  40      30.874   4.123  21.033  1.00  8.47           O  
ATOM    325  CB  LEU A  40      29.725   7.080  21.477  1.00  8.09           C  
ATOM    326  CG  LEU A  40      30.904   6.996  22.436  1.00  7.76           C  
ATOM    327  CD1 LEU A  40      32.223   7.202  21.712  1.00  7.98           C  
ATOM    328  CD2 LEU A  40      30.744   8.010  23.551  1.00  8.54           C  
ATOM    329  N   GLU A  41      28.627   4.038  21.023  1.00  9.94           N  
ATOM    330  CA  GLU A  41      28.594   2.671  21.508  1.00 11.26           C  
ATOM    331  C   GLU A  41      29.260   1.701  20.540  1.00 11.03           C  
ATOM    332  O   GLU A  41      29.591   0.564  20.904  1.00 10.80           O  
ATOM    333  CB  GLU A  41      27.154   2.240  21.726  1.00 13.80           C  
ATOM    334  CG  GLU A  41      26.553   2.796  23.009  1.00 18.93           C  
ATOM    335  CD  GLU A  41      25.064   2.485  23.163  1.00 21.83           C  
ATOM    336  OE1 GLU A  41      24.680   1.316  23.042  1.00 23.75           O  
ATOM    337  OE2 GLU A  41      24.276   3.433  23.171  1.00 25.16           O  
ATOM    338  N   LYS A  42      29.358   2.073  19.258  1.00  9.68           N  
ATOM    339  CA  LYS A  42      29.988   1.196  18.284  1.00  9.28           C  
ATOM    340  C   LYS A  42      31.506   1.165  18.412  1.00  8.82           C  
ATOM    341  O   LYS A  42      32.176   0.274  17.902  1.00  8.98           O  
ATOM    342  CB  LYS A  42      29.604   1.639  16.877  1.00  9.18           C  
ATOM    343  CG  LYS A  42      28.142   1.363  16.545  1.00  9.50           C  
ATOM    344  CD  LYS A  42      27.976  -0.078  16.079  1.00  9.98           C  
ATOM    345  CE  LYS A  42      26.510  -0.404  15.838  1.00 10.22           C  
ATOM    346  NZ  LYS A  42      26.340  -1.829  15.598  1.00 11.26           N  
ATOM    347  N   PHE A  43      32.084   2.076  19.183  1.00  8.57           N  
ATOM    348  CA  PHE A  43      33.527   2.108  19.344  1.00  9.24           C  
ATOM    349  C   PHE A  43      33.959   1.493  20.673  1.00 10.58           C  
ATOM    350  O   PHE A  43      33.937   2.152  21.711  1.00 10.54           O  
ATOM    351  CB  PHE A  43      34.008   3.552  19.300  1.00  7.75           C  
ATOM    352  CG  PHE A  43      33.680   4.243  17.986  1.00  6.74           C  
ATOM    353  CD1 PHE A  43      32.416   4.774  17.782  1.00  6.08           C  
ATOM    354  CD2 PHE A  43      34.653   4.353  17.007  1.00  6.74           C  
ATOM    355  CE1 PHE A  43      32.128   5.420  16.592  1.00  6.54           C  
ATOM    356  CE2 PHE A  43      34.350   5.001  15.822  1.00  5.65           C  
ATOM    357  CZ  PHE A  43      33.095   5.531  15.615  1.00  5.69           C  
ATOM    358  N   ASP A  44      34.496   0.278  20.665  1.00 11.88           N  
ATOM    359  CA  ASP A  44      34.917  -0.322  21.922  1.00 13.96           C  
ATOM    360  C   ASP A  44      36.120   0.387  22.525  1.00 13.64           C  
ATOM    361  O   ASP A  44      36.262   0.474  23.741  1.00 13.63           O  
ATOM    362  CB  ASP A  44      35.242  -1.792  21.720  1.00 16.79           C  
ATOM    363  CG  ASP A  44      33.994  -2.599  21.398  1.00 19.46           C  
ATOM    364  OD1 ASP A  44      32.885  -2.094  21.622  1.00 20.75           O  
ATOM    365  OD2 ASP A  44      34.131  -3.556  20.637  1.00 21.89           O  
ATOM    366  N   ARG A  45      36.888   1.081  21.700  1.00 12.82           N  
ATOM    367  CA  ARG A  45      38.051   1.793  22.187  1.00 13.11           C  
ATOM    368  C   ARG A  45      37.687   3.100  22.864  1.00 11.80           C  
ATOM    369  O   ARG A  45      38.516   3.676  23.566  1.00 11.56           O  
ATOM    370  CB  ARG A  45      38.938   2.198  21.023  1.00 15.12           C  
ATOM    371  CG  ARG A  45      39.943   1.157  20.592  1.00 18.21           C  
ATOM    372  CD  ARG A  45      40.553   1.619  19.277  1.00 19.85           C  
ATOM    373  NE  ARG A  45      41.876   2.131  19.495  1.00 21.49           N  
ATOM    374  CZ  ARG A  45      42.297   3.217  18.870  1.00 21.71           C  
ATOM    375  NH1 ARG A  45      41.704   3.600  17.738  1.00 21.81           N  
ATOM    376  NH2 ARG A  45      43.538   3.608  19.144  1.00 22.25           N  
ATOM    377  N   PHE A  46      36.624   3.736  22.362  1.00 10.83           N  
ATOM    378  CA  PHE A  46      36.242   5.047  22.849  1.00  9.90           C  
ATOM    379  C   PHE A  46      34.917   5.170  23.566  1.00 10.09           C  
ATOM    380  O   PHE A  46      34.640   6.249  24.095  1.00  9.83           O  
ATOM    381  CB  PHE A  46      36.209   6.011  21.665  1.00  9.78           C  
ATOM    382  CG  PHE A  46      37.473   5.955  20.811  1.00  9.28           C  
ATOM    383  CD1 PHE A  46      38.692   6.339  21.350  1.00  9.25           C  
ATOM    384  CD2 PHE A  46      37.410   5.520  19.489  1.00  9.79           C  
ATOM    385  CE1 PHE A  46      39.841   6.289  20.579  1.00  8.67           C  
ATOM    386  CE2 PHE A  46      38.570   5.474  18.728  1.00  8.62           C  
ATOM    387  CZ  PHE A  46      39.782   5.856  19.271  1.00  8.87           C  
ATOM    388  N   LYS A  47      34.150   4.097  23.766  1.00  9.57           N  
ATOM    389  CA  LYS A  47      32.860   4.282  24.407  1.00 10.62           C  
ATOM    390  C   LYS A  47      32.904   4.647  25.881  1.00 10.40           C  
ATOM    391  O   LYS A  47      31.876   4.953  26.484  1.00 10.67           O  
ATOM    392  CB  LYS A  47      31.973   3.067  24.210  1.00 11.38           C  
ATOM    393  CG  LYS A  47      32.616   1.779  24.657  1.00 13.29           C  
ATOM    394  CD  LYS A  47      31.623   0.655  24.437  1.00 15.18           C  
ATOM    395  CE  LYS A  47      32.171  -0.615  25.059  1.00 17.54           C  
ATOM    396  NZ  LYS A  47      31.232  -1.702  24.866  1.00 20.32           N  
ATOM    397  N   HIS A  48      34.066   4.594  26.516  1.00 10.38           N  
ATOM    398  CA  HIS A  48      34.113   4.973  27.916  1.00 10.40           C  
ATOM    399  C   HIS A  48      34.121   6.490  28.084  1.00 10.51           C  
ATOM    400  O   HIS A  48      34.003   7.003  29.200  1.00 10.41           O  
ATOM    401  CB  HIS A  48      35.362   4.408  28.565  1.00 10.40           C  
ATOM    402  CG  HIS A  48      36.612   4.910  27.865  1.00 11.51           C  
ATOM    403  ND1 HIS A  48      36.985   4.483  26.669  1.00 11.56           N  
ATOM    404  CD2 HIS A  48      37.473   5.874  28.307  1.00 11.68           C  
ATOM    405  CE1 HIS A  48      38.068   5.161  26.375  1.00 11.83           C  
ATOM    406  NE2 HIS A  48      38.357   5.993  27.354  1.00 12.12           N  
ATOM    407  N   LEU A  49      34.486   7.234  27.033  1.00  9.87           N  
ATOM    408  CA  LEU A  49      34.524   8.690  27.135  1.00  9.06           C  
ATOM    409  C   LEU A  49      33.153   9.239  27.514  1.00  8.44           C  
ATOM    410  O   LEU A  49      32.155   9.029  26.829  1.00  8.42           O  
ATOM    411  CB  LEU A  49      35.020   9.278  25.818  1.00  9.06           C  
ATOM    412  CG  LEU A  49      36.402   8.815  25.376  1.00  8.93           C  
ATOM    413  CD1 LEU A  49      36.635   9.117  23.905  1.00  9.62           C  
ATOM    414  CD2 LEU A  49      37.471   9.472  26.228  1.00  9.11           C  
ATOM    415  N   LYS A  50      33.092   9.994  28.613  1.00  8.53           N  
ATOM    416  CA  LYS A  50      31.825  10.516  29.111  1.00  8.80           C  
ATOM    417  C   LYS A  50      31.485  11.938  28.673  1.00  8.75           C  
ATOM    418  O   LYS A  50      30.332  12.348  28.762  1.00 10.36           O  
ATOM    419  CB  LYS A  50      31.844  10.516  30.637  1.00  8.97           C  
ATOM    420  CG  LYS A  50      32.180   9.166  31.262  1.00  7.97           C  
ATOM    421  CD  LYS A  50      32.163   9.298  32.784  1.00  8.49           C  
ATOM    422  CE  LYS A  50      32.510   7.977  33.453  1.00  8.41           C  
ATOM    423  NZ  LYS A  50      31.399   7.048  33.376  1.00  8.80           N  
ATOM    424  N   THR A  51      32.489  12.795  28.509  1.00  8.69           N  
ATOM    425  CA  THR A  51      32.233  14.182  28.164  1.00  7.98           C  
ATOM    426  C   THR A  51      33.011  14.675  26.957  1.00  8.22           C  
ATOM    427  O   THR A  51      33.971  14.048  26.507  1.00  7.71           O  
ATOM    428  CB  THR A  51      32.603  15.055  29.369  1.00  8.10           C  
ATOM    429  OG1 THR A  51      34.008  14.911  29.539  1.00  7.23           O  
ATOM    430  CG2 THR A  51      31.851  14.646  30.625  1.00  7.72           C  
ATOM    431  N   GLU A  52      32.636  15.856  26.447  1.00  8.44           N  
ATOM    432  CA  GLU A  52      33.353  16.432  25.328  1.00  8.62           C  
ATOM    433  C   GLU A  52      34.781  16.733  25.742  1.00  8.72           C  
ATOM    434  O   GLU A  52      35.712  16.645  24.940  1.00  8.77           O  
ATOM    435  CB  GLU A  52      32.687  17.716  24.857  1.00  9.85           C  
ATOM    436  CG  GLU A  52      33.408  18.321  23.659  1.00 12.50           C  
ATOM    437  CD  GLU A  52      32.761  19.588  23.111  1.00 14.26           C  
ATOM    438  OE1 GLU A  52      31.593  19.840  23.430  1.00 15.33           O  
ATOM    439  OE2 GLU A  52      33.370  20.227  22.245  1.00 14.71           O  
ATOM    440  N   ALA A  53      34.991  17.141  26.999  1.00  7.82           N  
ATOM    441  CA  ALA A  53      36.348  17.407  27.442  1.00  8.09           C  
ATOM    442  C   ALA A  53      37.190  16.139  27.364  1.00  7.71           C  
ATOM    443  O   ALA A  53      38.340  16.153  26.926  1.00  8.06           O  
ATOM    444  CB  ALA A  53      36.341  17.876  28.894  1.00  8.03           C  
ATOM    445  N   GLU A  54      36.621  14.996  27.757  1.00  7.58           N  
ATOM    446  CA  GLU A  54      37.371  13.753  27.691  1.00  7.58           C  
ATOM    447  C   GLU A  54      37.645  13.377  26.247  1.00  7.02           C  
ATOM    448  O   GLU A  54      38.753  13.006  25.879  1.00  6.51           O  
ATOM    449  CB  GLU A  54      36.596  12.628  28.376  1.00  8.24           C  
ATOM    450  CG  GLU A  54      36.773  12.665  29.890  1.00  9.48           C  
ATOM    451  CD  GLU A  54      36.006  11.594  30.657  1.00 10.91           C  
ATOM    452  OE1 GLU A  54      35.603  10.603  30.031  1.00 11.05           O  
ATOM    453  OE2 GLU A  54      36.130  11.594  31.893  1.00 10.60           O  
ATOM    454  N   MET A  55      36.693  13.661  25.370  1.00  6.93           N  
ATOM    455  CA  MET A  55      36.882  13.345  23.967  1.00  7.41           C  
ATOM    456  C   MET A  55      37.978  14.207  23.362  1.00  7.47           C  
ATOM    457  O   MET A  55      38.849  13.726  22.651  1.00  6.99           O  
ATOM    458  CB  MET A  55      35.594  13.601  23.207  1.00  7.60           C  
ATOM    459  CG  MET A  55      34.512  12.579  23.514  1.00  7.60           C  
ATOM    460  SD  MET A  55      32.886  13.119  22.928  1.00  7.95           S  
ATOM    461  CE  MET A  55      31.880  11.904  23.745  1.00  7.94           C  
ATOM    462  N   LYS A  56      37.988  15.493  23.705  1.00  8.40           N  
ATOM    463  CA  LYS A  56      38.984  16.407  23.174  1.00  9.66           C  
ATOM    464  C   LYS A  56      40.381  16.073  23.638  1.00  9.50           C  
ATOM    465  O   LYS A  56      41.354  16.267  22.911  1.00  9.88           O  
ATOM    466  CB  LYS A  56      38.679  17.826  23.619  1.00 10.86           C  
ATOM    467  CG  LYS A  56      37.421  18.380  22.979  1.00 13.27           C  
ATOM    468  CD  LYS A  56      37.526  19.892  22.945  1.00 15.16           C  
ATOM    469  CE  LYS A  56      36.261  20.486  22.360  1.00 16.41           C  
ATOM    470  NZ  LYS A  56      35.850  21.632  23.149  1.00 19.12           N  
ATOM    471  N   ALA A  57      40.502  15.539  24.855  1.00  9.93           N  
ATOM    472  CA  ALA A  57      41.809  15.209  25.396  1.00  9.92           C  
ATOM    473  C   ALA A  57      42.293  13.825  25.007  1.00  9.93           C  
ATOM    474  O   ALA A  57      43.427  13.448  25.296  1.00 10.66           O  
ATOM    475  CB  ALA A  57      41.738  15.262  26.915  1.00 10.03           C  
ATOM    476  N   SER A  58      41.490  13.061  24.270  1.00  9.25           N  
ATOM    477  CA  SER A  58      41.910  11.731  23.887  1.00  9.22           C  
ATOM    478  C   SER A  58      42.818  11.740  22.664  1.00  9.13           C  
ATOM    479  O   SER A  58      42.410  12.086  21.559  1.00  8.53           O  
ATOM    480  CB  SER A  58      40.679  10.883  23.618  1.00  8.30           C  
ATOM    481  OG  SER A  58      41.064   9.673  22.984  1.00  8.39           O  
ATOM    482  N   GLU A  59      44.083  11.376  22.840  1.00  9.72           N  
ATOM    483  CA  GLU A  59      45.009  11.366  21.726  1.00 11.10           C  
ATOM    484  C   GLU A  59      44.672  10.268  20.725  1.00 10.47           C  
ATOM    485  O   GLU A  59      44.787  10.454  19.517  1.00 10.04           O  
ATOM    486  CB  GLU A  59      46.429  11.192  22.259  1.00 13.33           C  
ATOM    487  CG  GLU A  59      47.489  11.127  21.162  1.00 17.79           C  
ATOM    488  CD  GLU A  59      47.769  12.462  20.488  1.00 20.20           C  
ATOM    489  OE1 GLU A  59      47.335  13.496  21.012  1.00 21.34           O  
ATOM    490  OE2 GLU A  59      48.518  12.469  19.503  1.00 22.68           O  
ATOM    491  N   ASP A  60      44.129   9.146  21.185  1.00 10.10           N  
ATOM    492  CA  ASP A  60      43.779   8.085  20.260  1.00  9.56           C  
ATOM    493  C   ASP A  60      42.586   8.500  19.404  1.00  8.75           C  
ATOM    494  O   ASP A  60      42.442   8.070  18.263  1.00  7.38           O  
ATOM    495  CB  ASP A  60      43.457   6.805  21.025  1.00 12.16           C  
ATOM    496  CG  ASP A  60      44.689   6.063  21.541  1.00 14.24           C  
ATOM    497  OD1 ASP A  60      45.804   6.448  21.198  1.00 16.10           O  
ATOM    498  OD2 ASP A  60      44.540   5.235  22.442  1.00 15.76           O  
ATOM    499  N   LEU A  61      41.595   9.167  20.005  1.00  7.95           N  
ATOM    500  CA  LEU A  61      40.441   9.612  19.229  1.00  7.59           C  
ATOM    501  C   LEU A  61      40.898  10.568  18.141  1.00  7.53           C  
ATOM    502  O   LEU A  61      40.286  10.649  17.074  1.00  6.38           O  
ATOM    503  CB  LEU A  61      39.403  10.330  20.094  1.00  7.09           C  
ATOM    504  CG  LEU A  61      38.076  10.684  19.421  1.00  6.91           C  
ATOM    505  CD1 LEU A  61      37.369   9.420  18.956  1.00  6.55           C  
ATOM    506  CD2 LEU A  61      37.172  11.453  20.370  1.00  7.35           C  
ATOM    507  N   LYS A  62      41.800  11.483  18.508  1.00  7.22           N  
ATOM    508  CA  LYS A  62      42.324  12.421  17.539  1.00  7.78           C  
ATOM    509  C   LYS A  62      42.990  11.668  16.395  1.00  7.24           C  
ATOM    510  O   LYS A  62      42.793  11.970  15.215  1.00  6.54           O  
ATOM    511  CB  LYS A  62      43.342  13.327  18.213  1.00  9.69           C  
ATOM    512  CG  LYS A  62      43.969  14.314  17.245  1.00 12.00           C  
ATOM    513  CD  LYS A  62      44.556  15.474  18.027  1.00 16.06           C  
ATOM    514  CE  LYS A  62      45.921  15.087  18.565  1.00 18.45           C  
ATOM    515  NZ  LYS A  62      46.815  16.238  18.550  1.00 21.17           N  
ATOM    516  N   LYS A  63      43.821  10.682  16.717  1.00  6.47           N  
ATOM    517  CA  LYS A  63      44.479   9.935  15.671  1.00  7.48           C  
ATOM    518  C   LYS A  63      43.479   9.161  14.836  1.00  6.69           C  
ATOM    519  O   LYS A  63      43.633   9.072  13.620  1.00  6.39           O  
ATOM    520  CB  LYS A  63      45.512   9.004  16.270  1.00  9.21           C  
ATOM    521  CG  LYS A  63      46.588   9.801  16.996  1.00 12.30           C  
ATOM    522  CD  LYS A  63      47.848   8.979  17.169  1.00 15.80           C  
ATOM    523  CE  LYS A  63      47.839   8.303  18.522  1.00 17.81           C  
ATOM    524  NZ  LYS A  63      46.690   7.426  18.651  1.00 20.37           N  
ATOM    525  N   HIS A  64      42.367   8.714  15.432  1.00  6.01           N  
ATOM    526  CA  HIS A  64      41.374   8.010  14.647  1.00  5.78           C  
ATOM    527  C   HIS A  64      40.714   8.982  13.688  1.00  5.15           C  
ATOM    528  O   HIS A  64      40.339   8.596  12.586  1.00  5.17           O  
ATOM    529  CB  HIS A  64      40.306   7.386  15.527  1.00  6.74           C  
ATOM    530  CG  HIS A  64      39.454   6.395  14.732  1.00  8.86           C  
ATOM    531  ND1 HIS A  64      39.982   5.386  14.048  1.00  9.65           N  
ATOM    532  CD2 HIS A  64      38.109   6.476  14.471  1.00  9.06           C  
ATOM    533  CE1 HIS A  64      38.991   4.862  13.362  1.00  9.52           C  
ATOM    534  NE2 HIS A  64      37.875   5.512  13.618  1.00  9.68           N  
ATOM    535  N   GLY A  65      40.368  10.185  14.170  1.00  4.38           N  
ATOM    536  CA  GLY A  65      39.754  11.184  13.314  1.00  3.67           C  
ATOM    537  C   GLY A  65      40.613  11.437  12.084  1.00  3.82           C  
ATOM    538  O   GLY A  65      40.106  11.616  10.979  1.00  3.54           O  
ATOM    539  N   VAL A  66      41.939  11.457  12.254  1.00  3.92           N  
ATOM    540  CA  VAL A  66      42.826  11.671  11.119  1.00  3.82           C  
ATOM    541  C   VAL A  66      42.739  10.493  10.159  1.00  3.67           C  
ATOM    542  O   VAL A  66      42.662  10.671   8.945  1.00  3.42           O  
ATOM    543  CB  VAL A  66      44.273  11.841  11.596  1.00  4.04           C  
ATOM    544  CG1 VAL A  66      45.211  11.847  10.394  1.00  3.75           C  
ATOM    545  CG2 VAL A  66      44.421  13.130  12.395  1.00  3.13           C  
ATOM    546  N   THR A  67      42.579   9.283  10.694  1.00  3.52           N  
ATOM    547  CA  THR A  67      42.459   8.113   9.842  1.00  4.14           C  
ATOM    548  C   THR A  67      41.164   8.148   9.038  1.00  3.56           C  
ATOM    549  O   THR A  67      41.134   7.910   7.825  1.00  2.84           O  
ATOM    550  CB  THR A  67      42.498   6.862  10.718  1.00  4.90           C  
ATOM    551  OG1 THR A  67      43.806   6.848  11.283  1.00  6.61           O  
ATOM    552  CG2 THR A  67      42.252   5.590   9.914  1.00  6.17           C  
ATOM    553  N   VAL A  68      40.064   8.479   9.716  1.00  3.75           N  
ATOM    554  CA  VAL A  68      38.763   8.572   9.070  1.00  3.34           C  
ATOM    555  C   VAL A  68      38.723   9.647   7.982  1.00  3.18           C  
ATOM    556  O   VAL A  68      38.319   9.392   6.848  1.00  3.56           O  
ATOM    557  CB  VAL A  68      37.691   8.876  10.141  1.00  3.42           C  
ATOM    558  CG1 VAL A  68      36.351   9.215   9.497  1.00  2.53           C  
ATOM    559  CG2 VAL A  68      37.552   7.687  11.080  1.00  2.96           C  
ATOM    560  N   LEU A  69      39.121  10.884   8.293  1.00  3.55           N  
ATOM    561  CA  LEU A  69      39.059  11.934   7.282  1.00  4.03           C  
ATOM    562  C   LEU A  69      40.037  11.728   6.140  1.00  3.90           C  
ATOM    563  O   LEU A  69      39.766  12.137   5.015  1.00  4.44           O  
ATOM    564  CB  LEU A  69      39.275  13.310   7.915  1.00  4.25           C  
ATOM    565  CG  LEU A  69      38.197  13.809   8.880  1.00  4.30           C  
ATOM    566  CD1 LEU A  69      38.400  15.288   9.197  1.00  3.79           C  
ATOM    567  CD2 LEU A  69      36.805  13.567   8.304  1.00  5.57           C  
ATOM    568  N   THR A  70      41.190  11.102   6.388  1.00  3.93           N  
ATOM    569  CA  THR A  70      42.142  10.873   5.311  1.00  4.16           C  
ATOM    570  C   THR A  70      41.584   9.834   4.341  1.00  3.97           C  
ATOM    571  O   THR A  70      41.752   9.943   3.126  1.00  3.37           O  
ATOM    572  CB  THR A  70      43.491  10.413   5.876  1.00  4.60           C  
ATOM    573  OG1 THR A  70      43.954  11.504   6.677  1.00  5.51           O  
ATOM    574  CG2 THR A  70      44.494  10.076   4.778  1.00  5.56           C  
ATOM    575  N   ALA A  71      40.886   8.814   4.857  1.00  3.31           N  
ATOM    576  CA  ALA A  71      40.283   7.822   3.974  1.00  3.13           C  
ATOM    577  C   ALA A  71      39.137   8.457   3.189  1.00  3.08           C  
ATOM    578  O   ALA A  71      38.975   8.227   1.990  1.00  3.33           O  
ATOM    579  CB  ALA A  71      39.695   6.684   4.790  1.00  3.16           C  
ATOM    580  N   LEU A  72      38.371   9.356   3.821  1.00  3.14           N  
ATOM    581  CA  LEU A  72      37.290  10.009   3.102  1.00  3.29           C  
ATOM    582  C   LEU A  72      37.856  10.936   2.036  1.00  3.63           C  
ATOM    583  O   LEU A  72      37.344  11.040   0.924  1.00  4.59           O  
ATOM    584  CB  LEU A  72      36.404  10.806   4.055  1.00  3.25           C  
ATOM    585  CG  LEU A  72      35.269  11.597   3.415  1.00  3.30           C  
ATOM    586  CD1 LEU A  72      34.361  10.682   2.598  1.00  4.10           C  
ATOM    587  CD2 LEU A  72      34.486  12.344   4.483  1.00  3.70           C  
ATOM    588  N   GLY A  73      38.912  11.672   2.367  1.00  3.81           N  
ATOM    589  CA  GLY A  73      39.520  12.570   1.395  1.00  3.89           C  
ATOM    590  C   GLY A  73      40.005  11.802   0.171  1.00  3.98           C  
ATOM    591  O   GLY A  73      39.992  12.324  -0.943  1.00  4.52           O  
ATOM    592  N   ALA A  74      40.627  10.635   0.377  1.00  3.95           N  
ATOM    593  CA  ALA A  74      41.099   9.833  -0.754  1.00  4.30           C  
ATOM    594  C   ALA A  74      39.935   9.408  -1.643  1.00  4.97           C  
ATOM    595  O   ALA A  74      40.034   9.405  -2.876  1.00  4.97           O  
ATOM    596  CB  ALA A  74      41.783   8.564  -0.254  1.00  4.33           C  
ATOM    597  N   ILE A  75      38.773   9.162  -1.029  1.00  4.56           N  
ATOM    598  CA  ILE A  75      37.596   8.774  -1.781  1.00  4.41           C  
ATOM    599  C   ILE A  75      37.033   9.970  -2.545  1.00  4.83           C  
ATOM    600  O   ILE A  75      36.874   9.909  -3.766  1.00  5.07           O  
ATOM    601  CB  ILE A  75      36.557   8.202  -0.805  1.00  4.25           C  
ATOM    602  CG1 ILE A  75      36.893   6.762  -0.439  1.00  3.70           C  
ATOM    603  CG2 ILE A  75      35.160   8.321  -1.399  1.00  5.20           C  
ATOM    604  CD1 ILE A  75      36.252   6.294   0.886  1.00  5.53           C  
ATOM    605  N   LEU A  76      37.040  11.159  -1.926  1.00  4.66           N  
ATOM    606  CA  LEU A  76      36.525  12.342  -2.602  1.00  4.74           C  
ATOM    607  C   LEU A  76      37.423  12.755  -3.762  1.00  4.71           C  
ATOM    608  O   LEU A  76      36.947  13.147  -4.827  1.00  4.58           O  
ATOM    609  CB  LEU A  76      36.412  13.506  -1.616  1.00  4.55           C  
ATOM    610  CG  LEU A  76      35.395  13.363  -0.484  1.00  4.25           C  
ATOM    611  CD1 LEU A  76      35.533  14.525   0.499  1.00  3.96           C  
ATOM    612  CD2 LEU A  76      33.971  13.283  -1.034  1.00  4.24           C  
ATOM    613  N   LYS A  77      38.741  12.587  -3.608  1.00  4.63           N  
ATOM    614  CA  LYS A  77      39.662  12.958  -4.670  1.00  4.91           C  
ATOM    615  C   LYS A  77      39.502  12.057  -5.895  1.00  5.21           C  
ATOM    616  O   LYS A  77      39.994  12.379  -6.979  1.00  5.34           O  
ATOM    617  CB  LYS A  77      41.091  12.909  -4.147  1.00  4.65           C  
ATOM    618  CG  LYS A  77      41.386  14.084  -3.223  1.00  5.29           C  
ATOM    619  CD  LYS A  77      42.691  13.858  -2.477  1.00  5.42           C  
ATOM    620  CE  LYS A  77      42.805  14.843  -1.318  1.00  5.41           C  
ATOM    621  NZ  LYS A  77      44.154  14.847  -0.771  1.00  6.31           N  
ATOM    622  N   LYS A  78      38.895  10.873  -5.723  1.00  5.29           N  
ATOM    623  CA  LYS A  78      38.669   9.978  -6.851  1.00  5.93           C  
ATOM    624  C   LYS A  78      37.492  10.447  -7.708  1.00  5.88           C  
ATOM    625  O   LYS A  78      37.230   9.913  -8.792  1.00  5.80           O  
ATOM    626  CB  LYS A  78      38.420   8.558  -6.358  1.00  6.99           C  
ATOM    627  CG  LYS A  78      39.719   7.830  -6.002  1.00  8.19           C  
ATOM    628  CD  LYS A  78      40.568   7.646  -7.254  1.00 10.81           C  
ATOM    629  CE  LYS A  78      41.866   6.943  -6.906  1.00 14.56           C  
ATOM    630  NZ  LYS A  78      41.829   5.555  -7.334  1.00 16.88           N  
ATOM    631  N   LYS A  79      36.756  11.451  -7.218  1.00  5.63           N  
ATOM    632  CA  LYS A  79      35.637  12.018  -7.958  1.00  5.54           C  
ATOM    633  C   LYS A  79      34.670  10.984  -8.525  1.00  5.78           C  
ATOM    634  O   LYS A  79      34.309  11.004  -9.711  1.00  5.64           O  
ATOM    635  CB  LYS A  79      36.176  12.925  -9.058  1.00  6.18           C  
ATOM    636  CG  LYS A  79      36.732  14.217  -8.467  1.00  8.07           C  
ATOM    637  CD  LYS A  79      37.862  14.790  -9.300  1.00 10.89           C  
ATOM    638  CE  LYS A  79      37.391  15.109 -10.706  1.00 12.19           C  
ATOM    639  NZ  LYS A  79      38.401  15.874 -11.428  1.00 12.84           N  
ATOM    640  N   GLY A  80      34.252  10.034  -7.682  1.00  4.26           N  
ATOM    641  CA  GLY A  80      33.302   9.027  -8.120  1.00  4.86           C  
ATOM    642  C   GLY A  80      33.943   7.686  -8.447  1.00  4.38           C  
ATOM    643  O   GLY A  80      33.277   6.645  -8.439  1.00  5.20           O  
ATOM    644  N   HIS A  81      35.186   7.707  -8.912  1.00  4.93           N  
ATOM    645  CA  HIS A  81      35.878   6.475  -9.250  1.00  4.96           C  
ATOM    646  C   HIS A  81      36.540   5.930  -7.995  1.00  5.28           C  
ATOM    647  O   HIS A  81      37.714   5.552  -8.021  1.00  5.74           O  
ATOM    648  CB  HIS A  81      36.940   6.783 -10.290  1.00  5.54           C  
ATOM    649  CG  HIS A  81      36.362   7.368 -11.568  1.00  6.01           C  
ATOM    650  ND1 HIS A  81      36.248   8.672 -11.783  1.00  7.68           N  
ATOM    651  CD2 HIS A  81      35.956   6.671 -12.671  1.00  6.31           C  
ATOM    652  CE1 HIS A  81      35.777   8.790 -13.007  1.00  6.64           C  
ATOM    653  NE2 HIS A  81      35.607   7.593 -13.532  1.00  8.64           N  
ATOM    654  N   HIS A  82      35.717   5.542  -7.026  1.00  5.28           N  
ATOM    655  CA  HIS A  82      36.240   5.092  -5.747  1.00  6.14           C  
ATOM    656  C   HIS A  82      35.956   3.634  -5.435  1.00  7.40           C  
ATOM    657  O   HIS A  82      36.088   3.201  -4.290  1.00  7.27           O  
ATOM    658  CB  HIS A  82      35.632   5.967  -4.659  1.00  5.83           C  
ATOM    659  CG  HIS A  82      34.118   6.104  -4.778  1.00  5.42           C  
ATOM    660  ND1 HIS A  82      33.488   7.254  -4.595  1.00  5.39           N  
ATOM    661  CD2 HIS A  82      33.213   5.121  -5.075  1.00  5.06           C  
ATOM    662  CE1 HIS A  82      32.205   6.993  -4.763  1.00  5.12           C  
ATOM    663  NE2 HIS A  82      32.041   5.712  -5.054  1.00  4.96           N  
ATOM    664  N   GLU A  83      35.798   2.820  -6.468  1.00  7.85           N  
ATOM    665  CA  GLU A  83      35.518   1.414  -6.272  1.00  9.25           C  
ATOM    666  C   GLU A  83      36.567   0.713  -5.411  1.00  8.47           C  
ATOM    667  O   GLU A  83      36.248  -0.046  -4.490  1.00  8.96           O  
ATOM    668  CB  GLU A  83      35.456   0.729  -7.637  1.00 11.45           C  
ATOM    669  CG  GLU A  83      34.358   1.269  -8.548  1.00 15.79           C  
ATOM    670  CD  GLU A  83      34.605   2.674  -9.106  1.00 17.86           C  
ATOM    671  OE1 GLU A  83      35.738   2.982  -9.493  1.00 18.70           O  
ATOM    672  OE2 GLU A  83      33.687   3.500  -9.032  1.00 20.77           O  
ATOM    673  N   ALA A  84      37.847   0.908  -5.710  1.00  8.08           N  
ATOM    674  CA  ALA A  84      38.873   0.228  -4.941  1.00  8.22           C  
ATOM    675  C   ALA A  84      38.912   0.664  -3.487  1.00  8.11           C  
ATOM    676  O   ALA A  84      39.234  -0.125  -2.589  1.00  8.28           O  
ATOM    677  CB  ALA A  84      40.240   0.514  -5.537  1.00  7.68           C  
ATOM    678  N   GLU A  85      38.744   1.964  -3.258  1.00  7.37           N  
ATOM    679  CA  GLU A  85      38.773   2.502  -1.908  1.00  6.67           C  
ATOM    680  C   GLU A  85      37.593   2.017  -1.077  1.00  6.43           C  
ATOM    681  O   GLU A  85      37.708   1.742   0.124  1.00  5.87           O  
ATOM    682  CB  GLU A  85      38.736   4.021  -1.983  1.00  7.07           C  
ATOM    683  CG  GLU A  85      40.028   4.631  -2.497  1.00  7.42           C  
ATOM    684  CD  GLU A  85      40.212   4.582  -4.013  1.00  8.36           C  
ATOM    685  OE1 GLU A  85      39.256   4.328  -4.751  1.00  7.88           O  
ATOM    686  OE2 GLU A  85      41.325   4.849  -4.461  1.00  9.81           O  
ATOM    687  N   LEU A  86      36.439   1.833  -1.714  1.00  5.80           N  
ATOM    688  CA  LEU A  86      35.269   1.395  -0.983  1.00  6.70           C  
ATOM    689  C   LEU A  86      35.288  -0.082  -0.615  1.00  6.57           C  
ATOM    690  O   LEU A  86      34.589  -0.515   0.290  1.00  6.56           O  
ATOM    691  CB  LEU A  86      34.017   1.686  -1.795  1.00  7.97           C  
ATOM    692  CG  LEU A  86      33.161   2.868  -1.373  1.00 10.21           C  
ATOM    693  CD1 LEU A  86      34.026   4.092  -1.128  1.00  9.90           C  
ATOM    694  CD2 LEU A  86      32.084   3.136  -2.417  1.00  9.69           C  
ATOM    695  N   LYS A  87      36.022  -0.920  -1.334  1.00  6.71           N  
ATOM    696  CA  LYS A  87      36.009  -2.332  -0.987  1.00  6.96           C  
ATOM    697  C   LYS A  87      36.410  -2.613   0.458  1.00  6.09           C  
ATOM    698  O   LYS A  87      35.660  -3.230   1.215  1.00  5.97           O  
ATOM    699  CB  LYS A  87      36.915  -3.098  -1.933  1.00  8.58           C  
ATOM    700  CG  LYS A  87      36.202  -3.466  -3.221  1.00 11.23           C  
ATOM    701  CD  LYS A  87      37.223  -3.538  -4.341  1.00 14.94           C  
ATOM    702  CE  LYS A  87      37.226  -4.922  -4.956  1.00 17.31           C  
ATOM    703  NZ  LYS A  87      36.697  -4.873  -6.308  1.00 18.35           N  
ATOM    704  N   PRO A  88      37.630  -2.271   0.874  1.00  5.59           N  
ATOM    705  CA  PRO A  88      38.086  -2.562   2.237  1.00  5.61           C  
ATOM    706  C   PRO A  88      37.238  -1.866   3.292  1.00  4.98           C  
ATOM    707  O   PRO A  88      36.964  -2.416   4.370  1.00  4.67           O  
ATOM    708  CB  PRO A  88      39.511  -2.058   2.263  1.00  5.71           C  
ATOM    709  CG  PRO A  88      39.684  -1.143   1.067  1.00  6.01           C  
ATOM    710  CD  PRO A  88      38.585  -1.496   0.084  1.00  5.78           C  
ATOM    711  N   LEU A  89      36.829  -0.625   2.995  1.00  4.65           N  
ATOM    712  CA  LEU A  89      36.020   0.124   3.938  1.00  4.23           C  
ATOM    713  C   LEU A  89      34.668  -0.538   4.162  1.00  4.18           C  
ATOM    714  O   LEU A  89      34.181  -0.666   5.280  1.00  4.81           O  
ATOM    715  CB  LEU A  89      35.834   1.546   3.425  1.00  4.50           C  
ATOM    716  CG  LEU A  89      35.243   2.549   4.408  1.00  6.18           C  
ATOM    717  CD1 LEU A  89      36.207   2.820   5.558  1.00  6.09           C  
ATOM    718  CD2 LEU A  89      34.876   3.834   3.681  1.00  6.08           C  
ATOM    719  N   ALA A  90      33.989  -0.892   3.079  1.00  3.89           N  
ATOM    720  CA  ALA A  90      32.700  -1.541   3.192  1.00  4.06           C  
ATOM    721  C   ALA A  90      32.807  -2.899   3.863  1.00  3.98           C  
ATOM    722  O   ALA A  90      31.990  -3.256   4.705  1.00  4.23           O  
ATOM    723  CB  ALA A  90      32.130  -1.785   1.802  1.00  5.02           C  
ATOM    724  N   GLN A  91      33.888  -3.631   3.623  1.00  4.46           N  
ATOM    725  CA  GLN A  91      33.991  -4.938   4.245  1.00  4.21           C  
ATOM    726  C   GLN A  91      34.193  -4.830   5.744  1.00  4.33           C  
ATOM    727  O   GLN A  91      33.531  -5.515   6.520  1.00  5.12           O  
ATOM    728  CB  GLN A  91      35.125  -5.750   3.649  1.00  3.75           C  
ATOM    729  CG  GLN A  91      35.202  -7.112   4.320  1.00  4.81           C  
ATOM    730  CD  GLN A  91      36.232  -8.055   3.714  1.00  4.75           C  
ATOM    731  OE1 GLN A  91      37.378  -7.686   3.468  1.00  5.77           O  
ATOM    732  NE2 GLN A  91      35.853  -9.313   3.482  1.00  3.93           N  
ATOM    733  N   SER A  92      35.055  -3.924   6.195  1.00  4.72           N  
ATOM    734  CA  SER A  92      35.264  -3.798   7.622  1.00  5.03           C  
ATOM    735  C   SER A  92      34.085  -3.131   8.320  1.00  5.43           C  
ATOM    736  O   SER A  92      33.665  -3.566   9.394  1.00  5.68           O  
ATOM    737  CB  SER A  92      36.520  -2.995   7.897  1.00  5.56           C  
ATOM    738  OG  SER A  92      36.336  -1.622   7.583  1.00  6.54           O  
ATOM    739  N   HIS A  93      33.381  -2.219   7.647  1.00  4.66           N  
ATOM    740  CA  HIS A  93      32.272  -1.557   8.311  1.00  4.89           C  
ATOM    741  C   HIS A  93      31.010  -2.402   8.312  1.00  5.41           C  
ATOM    742  O   HIS A  93      30.216  -2.348   9.255  1.00  5.39           O  
ATOM    743  CB  HIS A  93      32.012  -0.192   7.680  1.00  5.00           C  
ATOM    744  CG  HIS A  93      33.052   0.827   8.129  1.00  5.45           C  
ATOM    745  ND1 HIS A  93      34.360   0.637   7.980  1.00  5.36           N  
ATOM    746  CD2 HIS A  93      32.825   1.959   8.860  1.00  5.47           C  
ATOM    747  CE1 HIS A  93      34.939   1.630   8.620  1.00  5.83           C  
ATOM    748  NE2 HIS A  93      34.021   2.411   9.146  1.00  4.98           N  
ATOM    749  N   ALA A  94      30.894  -3.323   7.357  1.00  5.56           N  
ATOM    750  CA  ALA A  94      29.725  -4.169   7.317  1.00  6.34           C  
ATOM    751  C   ALA A  94      29.884  -5.425   8.171  1.00  6.54           C  
ATOM    752  O   ALA A  94      29.076  -5.682   9.058  1.00  6.65           O  
ATOM    753  CB  ALA A  94      29.486  -4.638   5.887  1.00  6.06           C  
ATOM    754  N   THR A  95      31.091  -5.983   8.185  1.00  7.25           N  
ATOM    755  CA  THR A  95      31.330  -7.240   8.882  1.00  8.46           C  
ATOM    756  C   THR A  95      31.956  -7.126  10.258  1.00  8.98           C  
ATOM    757  O   THR A  95      31.745  -7.988  11.103  1.00  9.29           O  
ATOM    758  CB  THR A  95      32.218  -8.140   7.994  1.00  8.59           C  
ATOM    759  OG1 THR A  95      31.661  -8.082   6.686  1.00 10.03           O  
ATOM    760  CG2 THR A  95      32.268  -9.577   8.482  1.00  8.17           C  
ATOM    761  N   LYS A  96      32.923  -6.244  10.439  1.00  8.83           N  
ATOM    762  CA  LYS A  96      33.555  -6.146  11.739  1.00 10.15           C  
ATOM    763  C   LYS A  96      32.941  -5.075  12.637  1.00 10.14           C  
ATOM    764  O   LYS A  96      32.357  -5.389  13.679  1.00 10.63           O  
ATOM    765  CB  LYS A  96      35.031  -5.847  11.563  1.00 11.62           C  
ATOM    766  CG  LYS A  96      35.768  -5.754  12.890  1.00 13.71           C  
ATOM    767  CD  LYS A  96      37.097  -5.053  12.667  1.00 17.01           C  
ATOM    768  CE  LYS A  96      38.215  -5.801  13.377  1.00 19.40           C  
ATOM    769  NZ  LYS A  96      38.406  -5.281  14.719  1.00 20.55           N  
ATOM    770  N   HIS A  97      32.844  -3.830  12.163  1.00  9.37           N  
ATOM    771  CA  HIS A  97      32.290  -2.781  12.998  1.00  8.92           C  
ATOM    772  C   HIS A  97      30.769  -2.789  13.029  1.00  9.17           C  
ATOM    773  O   HIS A  97      30.151  -2.325  13.997  1.00  8.79           O  
ATOM    774  CB  HIS A  97      32.802  -1.430  12.507  1.00  8.20           C  
ATOM    775  CG  HIS A  97      34.310  -1.413  12.289  1.00  7.49           C  
ATOM    776  ND1 HIS A  97      35.175  -1.854  13.190  1.00  7.61           N  
ATOM    777  CD2 HIS A  97      34.992  -0.955  11.189  1.00  8.02           C  
ATOM    778  CE1 HIS A  97      36.374  -1.678  12.669  1.00  7.57           C  
ATOM    779  NE2 HIS A  97      36.267  -1.139  11.467  1.00  8.07           N  
ATOM    780  N   LYS A  98      30.135  -3.245  11.946  1.00  9.86           N  
ATOM    781  CA  LYS A  98      28.684  -3.274  11.895  1.00 10.67           C  
ATOM    782  C   LYS A  98      28.096  -1.870  11.984  1.00 10.28           C  
ATOM    783  O   LYS A  98      27.262  -1.582  12.846  1.00 10.14           O  
ATOM    784  CB  LYS A  98      28.164  -4.117  13.042  1.00 13.36           C  
ATOM    785  CG  LYS A  98      27.024  -5.016  12.626  1.00 18.14           C  
ATOM    786  CD  LYS A  98      27.561  -6.139  11.758  1.00 21.19           C  
ATOM    787  CE  LYS A  98      28.179  -7.223  12.633  1.00 23.79           C  
ATOM    788  NZ  LYS A  98      29.508  -6.833  13.069  1.00 25.66           N  
ATOM    789  N   ILE A  99      28.325  -1.051  10.956  1.00  9.20           N  
ATOM    790  CA  ILE A  99      27.824   0.311  10.969  1.00  8.50           C  
ATOM    791  C   ILE A  99      26.639   0.436  10.023  1.00  8.87           C  
ATOM    792  O   ILE A  99      26.800   0.442   8.798  1.00  8.76           O  
ATOM    793  CB  ILE A  99      28.947   1.290  10.551  1.00  7.59           C  
ATOM    794  CG1 ILE A  99      30.214   1.104  11.389  1.00  7.17           C  
ATOM    795  CG2 ILE A  99      28.434   2.727  10.625  1.00  6.52           C  
ATOM    796  CD1 ILE A  99      29.952   1.108  12.910  1.00  7.16           C  
ATOM    797  N   PRO A 100      25.464   0.794  10.538  1.00  9.22           N  
ATOM    798  CA  PRO A 100      24.288   0.921   9.690  1.00 10.01           C  
ATOM    799  C   PRO A 100      24.374   2.138   8.782  1.00 10.30           C  
ATOM    800  O   PRO A 100      25.049   3.111   9.096  1.00  9.90           O  
ATOM    801  CB  PRO A 100      23.129   1.058  10.654  1.00 10.09           C  
ATOM    802  CG  PRO A 100      23.676   1.020  12.060  1.00 10.04           C  
ATOM    803  CD  PRO A 100      25.130   0.606  11.944  1.00  9.48           C  
ATOM    804  N   ILE A 101      23.755   2.088   7.603  1.00 10.68           N  
ATOM    805  CA  ILE A 101      23.787   3.237   6.712  1.00 11.39           C  
ATOM    806  C   ILE A 101      23.275   4.481   7.433  1.00 11.22           C  
ATOM    807  O   ILE A 101      23.738   5.594   7.208  1.00 11.13           O  
ATOM    808  CB  ILE A 101      22.902   2.963   5.480  1.00 12.78           C  
ATOM    809  CG1 ILE A 101      23.405   1.766   4.679  1.00 12.59           C  
ATOM    810  CG2 ILE A 101      22.808   4.221   4.615  1.00 12.71           C  
ATOM    811  CD1 ILE A 101      24.813   1.977   4.099  1.00 13.64           C  
ATOM    812  N   LYS A 102      22.294   4.307   8.314  1.00 11.03           N  
ATOM    813  CA  LYS A 102      21.738   5.429   9.046  1.00 10.84           C  
ATOM    814  C   LYS A 102      22.810   6.114   9.877  1.00  9.43           C  
ATOM    815  O   LYS A 102      22.768   7.332  10.056  1.00  8.58           O  
ATOM    816  CB  LYS A 102      20.593   4.934   9.927  1.00 13.35           C  
ATOM    817  CG  LYS A 102      20.222   5.893  11.045  1.00 16.80           C  
ATOM    818  CD  LYS A 102      19.521   7.129  10.493  1.00 19.65           C  
ATOM    819  CE  LYS A 102      18.474   7.612  11.495  1.00 20.78           C  
ATOM    820  NZ  LYS A 102      17.506   8.491  10.862  1.00 21.72           N  
ATOM    821  N   TYR A 103      23.824   5.363  10.335  1.00  7.91           N  
ATOM    822  CA  TYR A 103      24.897   5.978  11.098  1.00  6.71           C  
ATOM    823  C   TYR A 103      25.834   6.716  10.138  1.00  6.35           C  
ATOM    824  O   TYR A 103      26.561   7.640  10.523  1.00  5.58           O  
ATOM    825  CB  TYR A 103      25.676   4.922  11.880  1.00  6.86           C  
ATOM    826  CG  TYR A 103      25.003   4.471  13.179  1.00  6.77           C  
ATOM    827  CD1 TYR A 103      23.673   4.784  13.439  1.00  7.88           C  
ATOM    828  CD2 TYR A 103      25.729   3.716  14.090  1.00  7.25           C  
ATOM    829  CE1 TYR A 103      23.071   4.329  14.605  1.00  7.99           C  
ATOM    830  CE2 TYR A 103      25.136   3.261  15.254  1.00  7.85           C  
ATOM    831  CZ  TYR A 103      23.809   3.564  15.496  1.00  8.97           C  
ATOM    832  OH  TYR A 103      23.188   3.022  16.610  1.00  9.94           O  
ATOM    833  N   LEU A 104      25.966   6.212   8.901  1.00  5.87           N  
ATOM    834  CA  LEU A 104      26.801   6.891   7.923  1.00  5.23           C  
ATOM    835  C   LEU A 104      26.111   8.192   7.549  1.00  5.50           C  
ATOM    836  O   LEU A 104      26.740   9.196   7.216  1.00  5.06           O  
ATOM    837  CB  LEU A 104      27.008   6.004   6.697  1.00  5.83           C  
ATOM    838  CG  LEU A 104      27.902   4.775   6.888  1.00  5.87           C  
ATOM    839  CD1 LEU A 104      28.082   4.051   5.561  1.00  7.21           C  
ATOM    840  CD2 LEU A 104      29.257   5.160   7.461  1.00  6.24           C  
ATOM    841  N   GLU A 105      24.781   8.200   7.637  1.00  5.97           N  
ATOM    842  CA  GLU A 105      24.029   9.417   7.381  1.00  6.21           C  
ATOM    843  C   GLU A 105      24.337  10.408   8.501  1.00  5.81           C  
ATOM    844  O   GLU A 105      24.572  11.597   8.259  1.00  4.75           O  
ATOM    845  CB  GLU A 105      22.531   9.121   7.388  1.00  7.84           C  
ATOM    846  CG  GLU A 105      22.048   8.565   6.058  1.00 10.50           C  
ATOM    847  CD  GLU A 105      20.670   7.925   6.120  1.00 12.22           C  
ATOM    848  OE1 GLU A 105      20.011   8.012   7.160  1.00 12.20           O  
ATOM    849  OE2 GLU A 105      20.345   7.182   5.192  1.00 13.56           O  
ATOM    850  N   PHE A 106      24.400   9.903   9.752  1.00  5.26           N  
ATOM    851  CA  PHE A 106      24.706  10.754  10.899  1.00  4.96           C  
ATOM    852  C   PHE A 106      26.087  11.392  10.770  1.00  4.75           C  
ATOM    853  O   PHE A 106      26.256  12.589  11.035  1.00  4.59           O  
ATOM    854  CB  PHE A 106      24.661   9.951  12.194  1.00  5.07           C  
ATOM    855  CG  PHE A 106      23.263   9.482  12.613  1.00  6.17           C  
ATOM    856  CD1 PHE A 106      22.117  10.093  12.115  1.00  6.40           C  
ATOM    857  CD2 PHE A 106      23.145   8.443  13.530  1.00  5.68           C  
ATOM    858  CE1 PHE A 106      20.868   9.661  12.544  1.00  6.76           C  
ATOM    859  CE2 PHE A 106      21.892   8.027  13.950  1.00  5.88           C  
ATOM    860  CZ  PHE A 106      20.759   8.635  13.461  1.00  6.05           C  
ATOM    861  N   ILE A 107      27.120  10.626  10.389  1.00  3.96           N  
ATOM    862  CA  ILE A 107      28.425  11.249  10.259  1.00  3.96           C  
ATOM    863  C   ILE A 107      28.462  12.211   9.085  1.00  4.05           C  
ATOM    864  O   ILE A 107      29.205  13.187   9.105  1.00  3.48           O  
ATOM    865  CB  ILE A 107      29.570  10.222  10.160  1.00  4.04           C  
ATOM    866  CG1 ILE A 107      30.880  10.886  10.592  1.00  3.22           C  
ATOM    867  CG2 ILE A 107      29.666   9.643   8.753  1.00  3.25           C  
ATOM    868  CD1 ILE A 107      32.063   9.906  10.702  1.00  3.23           C  
ATOM    869  N   SER A 108      27.684  11.955   8.026  1.00  4.25           N  
ATOM    870  CA  SER A 108      27.662  12.885   6.908  1.00  4.04           C  
ATOM    871  C   SER A 108      27.080  14.210   7.384  1.00  4.38           C  
ATOM    872  O   SER A 108      27.554  15.293   7.037  1.00  3.91           O  
ATOM    873  CB  SER A 108      26.808  12.317   5.789  1.00  3.88           C  
ATOM    874  OG  SER A 108      27.391  11.129   5.242  1.00  4.08           O  
ATOM    875  N   GLU A 109      26.082  14.125   8.272  1.00  5.00           N  
ATOM    876  CA  GLU A 109      25.455  15.306   8.836  1.00  6.12           C  
ATOM    877  C   GLU A 109      26.450  16.064   9.709  1.00  4.86           C  
ATOM    878  O   GLU A 109      26.500  17.292   9.707  1.00  5.24           O  
ATOM    879  CB  GLU A 109      24.259  14.859   9.665  1.00  8.20           C  
ATOM    880  CG  GLU A 109      23.650  15.975  10.497  1.00 14.18           C  
ATOM    881  CD  GLU A 109      22.593  15.487  11.488  1.00 17.44           C  
ATOM    882  OE1 GLU A 109      22.667  14.322  11.898  1.00 18.61           O  
ATOM    883  OE2 GLU A 109      21.900  16.341  12.059  1.00 20.83           O  
ATOM    884  N   ALA A 110      27.304  15.332  10.418  1.00  4.39           N  
ATOM    885  CA  ALA A 110      28.300  15.960  11.268  1.00  3.98           C  
ATOM    886  C   ALA A 110      29.360  16.646  10.426  1.00  3.66           C  
ATOM    887  O   ALA A 110      29.875  17.709  10.791  1.00  3.45           O  
ATOM    888  CB  ALA A 110      28.997  14.905  12.121  1.00  3.57           C  
ATOM    889  N   ILE A 111      29.789  15.988   9.344  1.00  2.82           N  
ATOM    890  CA  ILE A 111      30.793  16.584   8.466  1.00  3.09           C  
ATOM    891  C   ILE A 111      30.288  17.913   7.907  1.00  2.78           C  
ATOM    892  O   ILE A 111      30.978  18.937   7.896  1.00  3.02           O  
ATOM    893  CB  ILE A 111      31.102  15.606   7.313  1.00  3.09           C  
ATOM    894  CG1 ILE A 111      31.881  14.401   7.821  1.00  3.30           C  
ATOM    895  CG2 ILE A 111      31.874  16.307   6.201  1.00  3.56           C  
ATOM    896  CD1 ILE A 111      31.799  13.189   6.880  1.00  3.92           C  
ATOM    897  N   ILE A 112      29.052  17.918   7.430  1.00  2.75           N  
ATOM    898  CA  ILE A 112      28.490  19.127   6.871  1.00  3.39           C  
ATOM    899  C   ILE A 112      28.352  20.216   7.930  1.00  3.74           C  
ATOM    900  O   ILE A 112      28.567  21.396   7.656  1.00  4.16           O  
ATOM    901  CB  ILE A 112      27.132  18.778   6.256  1.00  3.60           C  
ATOM    902  CG1 ILE A 112      27.310  18.060   4.926  1.00  4.01           C  
ATOM    903  CG2 ILE A 112      26.282  20.036   6.113  1.00  3.65           C  
ATOM    904  CD1 ILE A 112      26.004  17.406   4.437  1.00  4.51           C  
ATOM    905  N   HIS A 113      27.965  19.839   9.150  1.00  4.23           N  
ATOM    906  CA  HIS A 113      27.812  20.812  10.218  1.00  5.48           C  
ATOM    907  C   HIS A 113      29.132  21.498  10.543  1.00  4.80           C  
ATOM    908  O   HIS A 113      29.220  22.726  10.672  1.00  4.64           O  
ATOM    909  CB  HIS A 113      27.282  20.104  11.460  1.00  7.43           C  
ATOM    910  CG  HIS A 113      27.199  21.009  12.674  1.00 10.81           C  
ATOM    911  ND1 HIS A 113      26.129  21.733  12.950  1.00 13.27           N  
ATOM    912  CD2 HIS A 113      28.189  21.256  13.586  1.00 12.19           C  
ATOM    913  CE1 HIS A 113      26.447  22.443  14.009  1.00 12.50           C  
ATOM    914  NE2 HIS A 113      27.677  22.155  14.390  1.00 13.93           N  
ATOM    915  N   VAL A 114      30.198  20.716  10.668  1.00  3.53           N  
ATOM    916  CA  VAL A 114      31.492  21.291  10.987  1.00  3.85           C  
ATOM    917  C   VAL A 114      32.032  22.153   9.850  1.00  3.77           C  
ATOM    918  O   VAL A 114      32.652  23.189  10.080  1.00  4.19           O  
ATOM    919  CB  VAL A 114      32.461  20.152  11.336  1.00  3.86           C  
ATOM    920  CG1 VAL A 114      33.893  20.667  11.458  1.00  3.67           C  
ATOM    921  CG2 VAL A 114      32.004  19.492  12.630  1.00  4.17           C  
ATOM    922  N   LEU A 115      31.886  21.722   8.595  1.00  3.81           N  
ATOM    923  CA  LEU A 115      32.385  22.541   7.505  1.00  3.79           C  
ATOM    924  C   LEU A 115      31.571  23.828   7.401  1.00  3.92           C  
ATOM    925  O   LEU A 115      32.105  24.903   7.113  1.00  2.73           O  
ATOM    926  CB  LEU A 115      32.322  21.764   6.194  1.00  4.62           C  
ATOM    927  CG  LEU A 115      33.189  20.513   6.094  1.00  5.67           C  
ATOM    928  CD1 LEU A 115      33.073  19.889   4.711  1.00  5.62           C  
ATOM    929  CD2 LEU A 115      34.639  20.836   6.397  1.00  6.71           C  
ATOM    930  N   HIS A 116      30.252  23.745   7.635  1.00  4.30           N  
ATOM    931  CA  HIS A 116      29.424  24.936   7.566  1.00  4.89           C  
ATOM    932  C   HIS A 116      29.840  25.966   8.613  1.00  5.07           C  
ATOM    933  O   HIS A 116      29.913  27.163   8.345  1.00  5.14           O  
ATOM    934  CB  HIS A 116      27.967  24.536   7.771  1.00  5.54           C  
ATOM    935  CG  HIS A 116      27.021  25.712   8.001  1.00  6.24           C  
ATOM    936  ND1 HIS A 116      26.418  26.348   7.013  1.00  7.62           N  
ATOM    937  CD2 HIS A 116      26.618  26.230   9.204  1.00  5.88           C  
ATOM    938  CE1 HIS A 116      25.646  27.252   7.580  1.00  6.64           C  
ATOM    939  NE2 HIS A 116      25.762  27.177   8.894  1.00  8.46           N  
ATOM    940  N   SER A 117      30.280  25.524   9.789  1.00  5.56           N  
ATOM    941  CA  SER A 117      30.656  26.494  10.796  1.00  6.20           C  
ATOM    942  C   SER A 117      32.107  26.936  10.706  1.00  5.45           C  
ATOM    943  O   SER A 117      32.382  28.125  10.895  1.00  4.61           O  
ATOM    944  CB  SER A 117      30.389  25.960  12.189  1.00  8.29           C  
ATOM    945  OG  SER A 117      30.935  24.673  12.343  1.00 11.61           O  
ATOM    946  N   ARG A 118      33.026  26.053  10.276  1.00  3.98           N  
ATOM    947  CA  ARG A 118      34.429  26.435  10.191  1.00  4.07           C  
ATOM    948  C   ARG A 118      34.781  27.115   8.873  1.00  3.80           C  
ATOM    949  O   ARG A 118      35.602  28.032   8.856  1.00  3.56           O  
ATOM    950  CB  ARG A 118      35.335  25.204  10.332  1.00  4.72           C  
ATOM    951  CG  ARG A 118      35.476  24.688  11.761  1.00  6.36           C  
ATOM    952  CD  ARG A 118      36.349  23.430  11.859  1.00  7.24           C  
ATOM    953  NE  ARG A 118      37.750  23.773  11.716  1.00  9.87           N  
ATOM    954  CZ  ARG A 118      38.700  23.362  12.568  1.00  8.64           C  
ATOM    955  NH1 ARG A 118      38.481  22.409  13.474  1.00  9.44           N  
ATOM    956  NH2 ARG A 118      39.946  23.743  12.344  1.00  8.72           N  
ATOM    957  N   HIS A 119      34.028  26.832   7.800  1.00  4.13           N  
ATOM    958  CA  HIS A 119      34.368  27.371   6.490  1.00  4.22           C  
ATOM    959  C   HIS A 119      33.233  28.051   5.729  1.00  4.75           C  
ATOM    960  O   HIS A 119      33.009  27.744   4.549  1.00  4.66           O  
ATOM    961  CB  HIS A 119      34.922  26.230   5.634  1.00  4.07           C  
ATOM    962  CG  HIS A 119      36.205  25.653   6.222  1.00  4.13           C  
ATOM    963  ND1 HIS A 119      37.314  26.365   6.329  1.00  4.01           N  
ATOM    964  CD2 HIS A 119      36.370  24.448   6.848  1.00  4.25           C  
ATOM    965  CE1 HIS A 119      38.161  25.633   7.014  1.00  4.03           C  
ATOM    966  NE2 HIS A 119      37.600  24.478   7.321  1.00  4.96           N  
ATOM    967  N   PRO A 120      32.682  29.160   6.241  1.00  5.22           N  
ATOM    968  CA  PRO A 120      31.674  29.928   5.511  1.00  6.49           C  
ATOM    969  C   PRO A 120      32.219  30.476   4.188  1.00  6.82           C  
ATOM    970  O   PRO A 120      31.482  30.623   3.209  1.00  8.21           O  
ATOM    971  CB  PRO A 120      31.320  31.061   6.449  1.00  6.23           C  
ATOM    972  CG  PRO A 120      32.369  31.100   7.537  1.00  5.64           C  
ATOM    973  CD  PRO A 120      32.996  29.713   7.558  1.00  4.66           C  
ATOM    974  N   GLY A 121      33.539  30.699   4.103  1.00  6.98           N  
ATOM    975  CA  GLY A 121      34.138  31.243   2.886  1.00  6.97           C  
ATOM    976  C   GLY A 121      34.154  30.247   1.726  1.00  7.33           C  
ATOM    977  O   GLY A 121      34.384  30.613   0.563  1.00  7.74           O  
ATOM    978  N   ASN A 122      34.122  28.950   2.040  1.00  6.66           N  
ATOM    979  CA  ASN A 122      34.142  27.944   0.996  1.00  6.90           C  
ATOM    980  C   ASN A 122      33.006  26.942   1.147  1.00  6.24           C  
ATOM    981  O   ASN A 122      33.036  25.852   0.574  1.00  6.42           O  
ATOM    982  CB  ASN A 122      35.465  27.207   1.049  1.00  8.21           C  
ATOM    983  CG  ASN A 122      36.639  28.064   0.574  1.00  9.81           C  
ATOM    984  OD1 ASN A 122      37.338  28.657   1.394  1.00  9.13           O  
ATOM    985  ND2 ASN A 122      36.901  28.170  -0.715  1.00  0.00           N  
ATOM    986  N   PHE A 123      32.057  27.212   2.037  1.00  5.76           N  
ATOM    987  CA  PHE A 123      30.962  26.278   2.219  1.00  5.01           C  
ATOM    988  C   PHE A 123      29.602  26.954   2.201  1.00  5.64           C  
ATOM    989  O   PHE A 123      28.837  26.876   3.170  1.00  5.74           O  
ATOM    990  CB  PHE A 123      31.126  25.488   3.513  1.00  4.20           C  
ATOM    991  CG  PHE A 123      30.530  24.082   3.419  1.00  3.77           C  
ATOM    992  CD1 PHE A 123      31.055  23.160   2.516  1.00  3.39           C  
ATOM    993  CD2 PHE A 123      29.505  23.707   4.284  1.00  3.62           C  
ATOM    994  CE1 PHE A 123      30.563  21.867   2.496  1.00  3.59           C  
ATOM    995  CE2 PHE A 123      29.024  22.412   4.257  1.00  3.76           C  
ATOM    996  CZ  PHE A 123      29.554  21.491   3.368  1.00  3.53           C  
ATOM    997  N   GLY A 124      29.386  27.801   1.191  1.00  5.83           N  
ATOM    998  CA  GLY A 124      28.102  28.452   1.027  1.00  6.08           C  
ATOM    999  C   GLY A 124      27.053  27.418   0.607  1.00  6.09           C  
ATOM   1000  O   GLY A 124      27.370  26.244   0.456  1.00  5.04           O  
ATOM   1001  N   ALA A 125      25.900  27.871   0.112  1.00  6.28           N  
ATOM   1002  CA  ALA A 125      24.841  26.953  -0.278  1.00  6.21           C  
ATOM   1003  C   ALA A 125      25.219  26.012  -1.415  1.00  6.00           C  
ATOM   1004  O   ALA A 125      24.973  24.805  -1.341  1.00  5.28           O  
ATOM   1005  CB  ALA A 125      23.617  27.748  -0.714  1.00  6.29           C  
ATOM   1006  N   ASP A 126      25.783  26.531  -2.505  1.00  6.08           N  
ATOM   1007  CA  ASP A 126      26.141  25.650  -3.609  1.00  5.99           C  
ATOM   1008  C   ASP A 126      27.233  24.658  -3.217  1.00  6.08           C  
ATOM   1009  O   ASP A 126      27.172  23.470  -3.559  1.00  4.95           O  
ATOM   1010  CB  ASP A 126      26.587  26.466  -4.806  1.00  7.20           C  
ATOM   1011  CG  ASP A 126      25.444  27.244  -5.444  1.00  9.37           C  
ATOM   1012  OD1 ASP A 126      24.285  26.867  -5.259  1.00  8.76           O  
ATOM   1013  OD2 ASP A 126      25.697  28.365  -5.877  1.00 11.90           O  
ATOM   1014  N   ALA A 127      28.243  25.109  -2.468  1.00  5.49           N  
ATOM   1015  CA  ALA A 127      29.300  24.197  -2.043  1.00  5.14           C  
ATOM   1016  C   ALA A 127      28.746  23.115  -1.110  1.00  5.34           C  
ATOM   1017  O   ALA A 127      29.130  21.943  -1.175  1.00  4.96           O  
ATOM   1018  CB  ALA A 127      30.356  24.983  -1.281  1.00  5.25           C  
ATOM   1019  N   GLN A 128      27.850  23.491  -0.188  1.00  4.80           N  
ATOM   1020  CA  GLN A 128      27.278  22.509   0.713  1.00  4.27           C  
ATOM   1021  C   GLN A 128      26.449  21.504  -0.078  1.00  4.28           C  
ATOM   1022  O   GLN A 128      26.435  20.308   0.224  1.00  3.94           O  
ATOM   1023  CB  GLN A 128      26.397  23.186   1.762  1.00  5.11           C  
ATOM   1024  CG  GLN A 128      25.699  22.164   2.654  1.00  4.49           C  
ATOM   1025  CD  GLN A 128      25.044  22.752   3.898  1.00  5.73           C  
ATOM   1026  OE1 GLN A 128      25.462  23.774   4.425  1.00  6.01           O  
ATOM   1027  NE2 GLN A 128      24.029  22.078   4.429  1.00  6.42           N  
ATOM   1028  N   GLY A 129      25.718  21.975  -1.103  1.00  4.33           N  
ATOM   1029  CA  GLY A 129      24.923  21.065  -1.920  1.00  3.68           C  
ATOM   1030  C   GLY A 129      25.835  20.068  -2.642  1.00  4.13           C  
ATOM   1031  O   GLY A 129      25.497  18.890  -2.801  1.00  4.54           O  
ATOM   1032  N   ALA A 130      26.990  20.532  -3.140  1.00  3.88           N  
ATOM   1033  CA  ALA A 130      27.924  19.634  -3.810  1.00  3.57           C  
ATOM   1034  C   ALA A 130      28.470  18.594  -2.830  1.00  3.44           C  
ATOM   1035  O   ALA A 130      28.600  17.416  -3.159  1.00  3.38           O  
ATOM   1036  CB  ALA A 130      29.110  20.425  -4.343  1.00  4.20           C  
ATOM   1037  N   MET A 131      28.873  19.016  -1.625  1.00  3.19           N  
ATOM   1038  CA  MET A 131      29.380  18.066  -0.652  1.00  3.39           C  
ATOM   1039  C   MET A 131      28.293  17.057  -0.301  1.00  3.45           C  
ATOM   1040  O   MET A 131      28.562  15.867  -0.122  1.00  3.38           O  
ATOM   1041  CB  MET A 131      29.841  18.808   0.603  1.00  3.67           C  
ATOM   1042  CG  MET A 131      30.353  17.882   1.706  1.00  3.58           C  
ATOM   1043  SD  MET A 131      31.820  16.917   1.226  1.00  3.76           S  
ATOM   1044  CE  MET A 131      33.039  18.204   1.204  1.00  4.85           C  
ATOM   1045  N   ASN A 132      27.060  17.520  -0.072  1.00  3.61           N  
ATOM   1046  CA  ASN A 132      25.986  16.588   0.232  1.00  3.63           C  
ATOM   1047  C   ASN A 132      25.837  15.574  -0.908  1.00  4.02           C  
ATOM   1048  O   ASN A 132      25.571  14.386  -0.697  1.00  4.29           O  
ATOM   1049  CB  ASN A 132      24.669  17.336   0.419  1.00  3.89           C  
ATOM   1050  CG  ASN A 132      23.518  16.363   0.610  1.00  5.24           C  
ATOM   1051  OD1 ASN A 132      23.564  15.488   1.475  1.00  5.78           O  
ATOM   1052  ND2 ASN A 132      22.472  16.462  -0.210  1.00  5.76           N  
ATOM   1053  N   LYS A 133      25.927  16.045  -2.153  1.00  4.18           N  
ATOM   1054  CA  LYS A 133      25.818  15.141  -3.281  1.00  5.41           C  
ATOM   1055  C   LYS A 133      26.942  14.102  -3.251  1.00  4.72           C  
ATOM   1056  O   LYS A 133      26.730  12.915  -3.517  1.00  4.94           O  
ATOM   1057  CB  LYS A 133      25.897  15.956  -4.562  1.00  6.89           C  
ATOM   1058  CG  LYS A 133      25.026  15.393  -5.664  1.00 10.56           C  
ATOM   1059  CD  LYS A 133      24.910  16.404  -6.794  1.00 12.44           C  
ATOM   1060  CE  LYS A 133      24.716  15.666  -8.110  1.00 14.93           C  
ATOM   1061  NZ  LYS A 133      24.453  16.612  -9.179  1.00 17.28           N  
ATOM   1062  N   ALA A 134      28.179  14.536  -2.973  1.00  4.36           N  
ATOM   1063  CA  ALA A 134      29.292  13.601  -2.929  1.00  3.96           C  
ATOM   1064  C   ALA A 134      29.122  12.587  -1.803  1.00  4.24           C  
ATOM   1065  O   ALA A 134      29.460  11.407  -1.957  1.00  4.18           O  
ATOM   1066  CB  ALA A 134      30.594  14.348  -2.683  1.00  3.87           C  
ATOM   1067  N   LEU A 135      28.611  13.026  -0.640  1.00  3.92           N  
ATOM   1068  CA  LEU A 135      28.419  12.098   0.461  1.00  3.93           C  
ATOM   1069  C   LEU A 135      27.232  11.169   0.208  1.00  4.86           C  
ATOM   1070  O   LEU A 135      27.245   9.998   0.613  1.00  4.75           O  
ATOM   1071  CB  LEU A 135      28.245  12.880   1.749  1.00  3.96           C  
ATOM   1072  CG  LEU A 135      29.472  13.676   2.193  1.00  3.97           C  
ATOM   1073  CD1 LEU A 135      29.142  14.565   3.389  1.00  4.98           C  
ATOM   1074  CD2 LEU A 135      30.621  12.735   2.520  1.00  4.25           C  
ATOM   1075  N   GLU A 136      26.211  11.637  -0.532  1.00  5.05           N  
ATOM   1076  CA  GLU A 136      25.094  10.767  -0.848  1.00  5.29           C  
ATOM   1077  C   GLU A 136      25.581   9.671  -1.802  1.00  5.17           C  
ATOM   1078  O   GLU A 136      25.092   8.537  -1.780  1.00  4.66           O  
ATOM   1079  CB  GLU A 136      23.986  11.566  -1.512  1.00  7.08           C  
ATOM   1080  CG  GLU A 136      23.221  12.424  -0.517  1.00  9.51           C  
ATOM   1081  CD  GLU A 136      21.944  13.050  -1.078  1.00 11.52           C  
ATOM   1082  OE1 GLU A 136      21.854  13.256  -2.292  1.00 12.66           O  
ATOM   1083  OE2 GLU A 136      21.145  13.538  -0.280  1.00 12.96           O  
ATOM   1084  N   LEU A 137      26.481  10.031  -2.738  1.00  4.34           N  
ATOM   1085  CA  LEU A 137      27.021   9.054  -3.676  1.00  4.70           C  
ATOM   1086  C   LEU A 137      27.835   8.025  -2.916  1.00  4.86           C  
ATOM   1087  O   LEU A 137      27.770   6.825  -3.181  1.00  5.08           O  
ATOM   1088  CB  LEU A 137      27.905   9.751  -4.702  1.00  4.43           C  
ATOM   1089  CG  LEU A 137      28.653   8.861  -5.688  1.00  4.73           C  
ATOM   1090  CD1 LEU A 137      27.662   8.178  -6.614  1.00  5.60           C  
ATOM   1091  CD2 LEU A 137      29.670   9.667  -6.496  1.00  4.83           C  
ATOM   1092  N   PHE A 138      28.658   8.503  -1.985  1.00  4.35           N  
ATOM   1093  CA  PHE A 138      29.453   7.621  -1.154  1.00  4.59           C  
ATOM   1094  C   PHE A 138      28.562   6.643  -0.383  1.00  3.92           C  
ATOM   1095  O   PHE A 138      28.775   5.437  -0.439  1.00  3.72           O  
ATOM   1096  CB  PHE A 138      30.257   8.477  -0.180  1.00  4.80           C  
ATOM   1097  CG  PHE A 138      30.771   7.720   1.038  1.00  5.23           C  
ATOM   1098  CD1 PHE A 138      31.821   6.821   0.907  1.00  5.14           C  
ATOM   1099  CD2 PHE A 138      30.185   7.933   2.277  1.00  5.27           C  
ATOM   1100  CE1 PHE A 138      32.280   6.134   2.021  1.00  5.28           C  
ATOM   1101  CE2 PHE A 138      30.653   7.241   3.382  1.00  5.99           C  
ATOM   1102  CZ  PHE A 138      31.697   6.342   3.256  1.00  5.45           C  
ATOM   1103  N   ARG A 139      27.454   7.119   0.210  1.00  4.35           N  
ATOM   1104  CA  ARG A 139      26.569   6.230   0.961  1.00  4.83           C  
ATOM   1105  C   ARG A 139      25.841   5.264   0.033  1.00  5.16           C  
ATOM   1106  O   ARG A 139      25.522   4.135   0.409  1.00  4.66           O  
ATOM   1107  CB  ARG A 139      25.557   7.033   1.790  1.00  4.79           C  
ATOM   1108  CG  ARG A 139      26.235   7.813   2.920  1.00  5.46           C  
ATOM   1109  CD  ARG A 139      25.239   8.382   3.926  1.00  4.42           C  
ATOM   1110  NE  ARG A 139      24.096   9.021   3.295  1.00  5.55           N  
ATOM   1111  CZ  ARG A 139      24.016  10.347   3.125  1.00  5.69           C  
ATOM   1112  NH1 ARG A 139      25.060  11.147   3.349  1.00  5.40           N  
ATOM   1113  NH2 ARG A 139      22.929  10.849   2.548  1.00  6.18           N  
ATOM   1114  N   LYS A 140      25.416   5.745  -1.139  1.00  5.30           N  
ATOM   1115  CA  LYS A 140      24.727   4.880  -2.087  1.00  5.72           C  
ATOM   1116  C   LYS A 140      25.621   3.727  -2.527  1.00  5.20           C  
ATOM   1117  O   LYS A 140      25.216   2.564  -2.547  1.00  4.62           O  
ATOM   1118  CB  LYS A 140      24.323   5.681  -3.315  1.00  7.46           C  
ATOM   1119  CG  LYS A 140      23.658   4.814  -4.376  1.00 10.63           C  
ATOM   1120  CD  LYS A 140      23.230   5.673  -5.547  1.00 13.61           C  
ATOM   1121  CE  LYS A 140      24.256   5.579  -6.656  1.00 16.61           C  
ATOM   1122  NZ  LYS A 140      25.486   6.259  -6.289  1.00 19.19           N  
ATOM   1123  N   ASP A 141      26.857   4.039  -2.907  1.00  4.52           N  
ATOM   1124  CA  ASP A 141      27.780   3.001  -3.334  1.00  5.31           C  
ATOM   1125  C   ASP A 141      28.185   2.090  -2.183  1.00  5.55           C  
ATOM   1126  O   ASP A 141      28.264   0.872  -2.340  1.00  5.38           O  
ATOM   1127  CB  ASP A 141      29.002   3.644  -3.967  1.00  5.90           C  
ATOM   1128  CG  ASP A 141      28.690   4.185  -5.357  1.00  6.87           C  
ATOM   1129  OD1 ASP A 141      27.555   4.033  -5.807  1.00  6.55           O  
ATOM   1130  OD2 ASP A 141      29.525   4.895  -5.918  1.00  7.37           O  
ATOM   1131  N   ILE A 142      28.328   2.637  -0.976  1.00  5.54           N  
ATOM   1132  CA  ILE A 142      28.680   1.810   0.172  1.00  6.62           C  
ATOM   1133  C   ILE A 142      27.532   0.868   0.519  1.00  5.88           C  
ATOM   1134  O   ILE A 142      27.734  -0.307   0.828  1.00  5.91           O  
ATOM   1135  CB  ILE A 142      29.004   2.713   1.371  1.00  7.95           C  
ATOM   1136  CG1 ILE A 142      30.480   3.059   1.379  1.00  9.57           C  
ATOM   1137  CG2 ILE A 142      28.581   2.051   2.676  1.00 10.28           C  
ATOM   1138  CD1 ILE A 142      31.351   1.893   1.876  1.00  9.84           C  
ATOM   1139  N   ALA A 143      26.296   1.352   0.412  1.00  5.40           N  
ATOM   1140  CA  ALA A 143      25.143   0.512   0.705  1.00  5.20           C  
ATOM   1141  C   ALA A 143      25.044  -0.635  -0.301  1.00  5.17           C  
ATOM   1142  O   ALA A 143      24.607  -1.743   0.016  1.00  5.86           O  
ATOM   1143  CB  ALA A 143      23.871   1.353   0.610  1.00  5.05           C  
ATOM   1144  N   ALA A 144      25.328  -0.373  -1.572  1.00  5.20           N  
ATOM   1145  CA  ALA A 144      25.266  -1.444  -2.554  1.00  6.04           C  
ATOM   1146  C   ALA A 144      26.323  -2.498  -2.237  1.00  6.54           C  
ATOM   1147  O   ALA A 144      26.106  -3.700  -2.378  1.00  7.01           O  
ATOM   1148  CB  ALA A 144      25.547  -0.875  -3.939  1.00  5.31           C  
ATOM   1149  N   LYS A 145      27.497  -2.062  -1.774  1.00  7.26           N  
ATOM   1150  CA  LYS A 145      28.535  -3.018  -1.427  1.00  8.72           C  
ATOM   1151  C   LYS A 145      28.106  -3.817  -0.203  1.00  8.46           C  
ATOM   1152  O   LYS A 145      28.392  -5.014  -0.109  1.00  7.57           O  
ATOM   1153  CB  LYS A 145      29.851  -2.314  -1.129  1.00 10.87           C  
ATOM   1154  CG  LYS A 145      30.169  -1.173  -2.084  1.00 14.39           C  
ATOM   1155  CD  LYS A 145      29.769  -1.518  -3.515  1.00 16.87           C  
ATOM   1156  CE  LYS A 145      29.793  -0.267  -4.387  1.00 16.22           C  
ATOM   1157  NZ  LYS A 145      28.532  -0.069  -5.060  1.00 15.96           N  
ATOM   1158  N   TYR A 146      27.544  -3.134   0.812  1.00  8.09           N  
ATOM   1159  CA  TYR A 146      27.063  -3.813   2.011  1.00  8.35           C  
ATOM   1160  C   TYR A 146      26.176  -4.973   1.585  1.00  8.93           C  
ATOM   1161  O   TYR A 146      26.325  -6.114   2.019  1.00  8.64           O  
ATOM   1162  CB  TYR A 146      26.194  -2.870   2.845  1.00  7.57           C  
ATOM   1163  CG  TYR A 146      26.902  -1.988   3.878  1.00  8.02           C  
ATOM   1164  CD1 TYR A 146      28.287  -1.971   4.001  1.00  7.62           C  
ATOM   1165  CD2 TYR A 146      26.123  -1.220   4.732  1.00  8.33           C  
ATOM   1166  CE1 TYR A 146      28.885  -1.205   4.994  1.00  8.05           C  
ATOM   1167  CE2 TYR A 146      26.715  -0.458   5.727  1.00  8.52           C  
ATOM   1168  CZ  TYR A 146      28.092  -0.463   5.858  1.00  8.04           C  
ATOM   1169  OH  TYR A 146      28.674   0.268   6.881  1.00  8.20           O  
ATOM   1170  N   LYS A 147      25.270  -4.691   0.653  1.00  9.53           N  
ATOM   1171  CA  LYS A 147      24.361  -5.706   0.155  1.00 10.90           C  
ATOM   1172  C   LYS A 147      25.104  -6.871  -0.491  1.00 10.42           C  
ATOM   1173  O   LYS A 147      24.832  -8.035  -0.198  1.00 10.19           O  
ATOM   1174  CB  LYS A 147      23.416  -5.065  -0.844  1.00 12.85           C  
ATOM   1175  CG  LYS A 147      22.134  -5.859  -1.008  1.00 17.17           C  
ATOM   1176  CD  LYS A 147      21.239  -5.207  -2.057  1.00 19.90           C  
ATOM   1177  CE  LYS A 147      20.576  -6.273  -2.927  1.00 21.46           C  
ATOM   1178  NZ  LYS A 147      19.853  -7.252  -2.127  1.00 22.85           N  
ATOM   1179  N   GLU A 148      26.142  -6.586  -1.278  1.00  9.64           N  
ATOM   1180  CA  GLU A 148      26.903  -7.655  -1.908  1.00  9.67           C  
ATOM   1181  C   GLU A 148      27.654  -8.485  -0.867  1.00  9.46           C  
ATOM   1182  O   GLU A 148      27.762  -9.708  -0.985  1.00  8.28           O  
ATOM   1183  CB  GLU A 148      27.921  -7.071  -2.889  1.00 10.48           C  
ATOM   1184  CG  GLU A 148      27.286  -6.407  -4.108  1.00 12.35           C  
ATOM   1185  CD  GLU A 148      28.257  -5.579  -4.953  1.00 14.42           C  
ATOM   1186  OE1 GLU A 148      29.472  -5.741  -4.825  1.00 14.30           O  
ATOM   1187  OE2 GLU A 148      27.797  -4.680  -5.659  1.00 16.93           O  
ATOM   1188  N   LEU A 149      28.013  -7.856   0.258  1.00  8.48           N  
ATOM   1189  CA  LEU A 149      28.753  -8.530   1.313  1.00  9.03           C  
ATOM   1190  C   LEU A 149      27.845  -9.300   2.276  1.00  9.88           C  
ATOM   1191  O   LEU A 149      28.308  -9.872   3.271  1.00  9.31           O  
ATOM   1192  CB  LEU A 149      29.577  -7.490   2.073  1.00  9.16           C  
ATOM   1193  CG  LEU A 149      30.690  -6.792   1.293  1.00  9.25           C  
ATOM   1194  CD1 LEU A 149      31.067  -5.469   1.957  1.00  8.89           C  
ATOM   1195  CD2 LEU A 149      31.908  -7.704   1.183  1.00  8.62           C  
ATOM   1196  N   GLY A 150      26.528  -9.114   2.152  1.00 10.07           N  
ATOM   1197  CA  GLY A 150      25.598  -9.826   3.010  1.00 11.73           C  
ATOM   1198  C   GLY A 150      25.135  -9.041   4.235  1.00 13.44           C  
ATOM   1199  O   GLY A 150      24.373  -9.582   5.045  1.00 13.43           O  
ATOM   1200  N   TYR A 151      25.219  -7.706   4.191  1.00 13.84           N  
ATOM   1201  CA  TYR A 151      24.809  -6.902   5.337  1.00 16.23           C  
ATOM   1202  C   TYR A 151      23.712  -5.892   5.015  1.00 18.51           C  
ATOM   1203  O   TYR A 151      22.622  -5.906   5.590  1.00 18.82           O  
ATOM   1204  CB  TYR A 151      26.023  -6.146   5.875  1.00 15.63           C  
ATOM   1205  CG  TYR A 151      25.714  -5.149   6.994  1.00 16.62           C  
ATOM   1206  CD1 TYR A 151      25.052  -5.571   8.135  1.00 17.02           C  
ATOM   1207  CD2 TYR A 151      26.159  -3.833   6.906  1.00 17.00           C  
ATOM   1208  CE1 TYR A 151      24.841  -4.692   9.183  1.00 16.92           C  
ATOM   1209  CE2 TYR A 151      25.948  -2.948   7.956  1.00 16.83           C  
ATOM   1210  CZ  TYR A 151      25.289  -3.390   9.087  1.00 16.88           C  
ATOM   1211  OH  TYR A 151      25.057  -2.517  10.135  1.00 16.62           O  
ATOM   1212  N   GLN A 152      23.936  -5.074   3.997  1.00 21.31           N  
ATOM   1213  CA  GLN A 152      22.989  -4.032   3.634  1.00 25.62           C  
ATOM   1214  C   GLN A 152      22.266  -3.388   4.814  1.00 26.73           C  
ATOM   1215  O   GLN A 152      21.059  -3.119   4.771  1.00 27.24           O  
ATOM   1216  CB  GLN A 152      21.968  -4.501   2.607  1.00 27.44           C  
ATOM   1217  CG  GLN A 152      21.679  -3.398   1.585  1.00 30.50           C  
ATOM   1218  CD  GLN A 152      21.983  -1.981   2.092  1.00 31.88           C  
ATOM   1219  OE1 GLN A 152      23.115  -1.633   2.439  1.00 32.25           O  
ATOM   1220  NE2 GLN A 152      20.964  -1.123   2.169  1.00 33.16           N  
ATOM   1221  N   GLY A 153      22.945  -3.274   5.952  1.00 27.40           N  
ATOM   1222  CA  GLY A 153      22.330  -2.629   7.090  1.00 27.96           C  
ATOM   1223  C   GLY A 153      22.545  -1.135   6.941  1.00 27.65           C  
ATOM   1224  O   GLY A 153      21.708  -0.362   7.402  1.00 26.72           O  
ATOM   1225  OXT GLY A 153      23.329  -0.789   6.063  1.00 28.94           O  
TER    1226      GLY A 153                                                      
HETATM 1227  S   SO4 A 156      31.115  18.416  28.575  1.00 17.99           S  
HETATM 1228  O1  SO4 A 156      30.621  19.744  28.335  1.00 18.68           O  
HETATM 1229  O2  SO4 A 156      30.552  17.532  27.599  1.00 17.30           O  
HETATM 1230  O3  SO4 A 156      30.702  17.976  29.865  1.00 17.07           O  
HETATM 1231  O4  SO4 A 156      32.547  18.424  28.490  1.00 16.95           O  
HETATM 1232 FE   HEM A 154      34.801   4.074  10.439  1.00  4.64          FE  
HETATM 1233  CHA HEM A 154      37.447   2.390  11.650  1.00  4.79           C  
HETATM 1234  CHB HEM A 154      36.751   5.382   8.055  1.00  4.69           C  
HETATM 1235  CHC HEM A 154      32.301   6.098   9.483  1.00  4.83           C  
HETATM 1236  CHD HEM A 154      33.065   3.274  13.212  1.00  5.32           C  
HETATM 1237  NA  HEM A 154      36.704   3.923   9.957  1.00  4.98           N  
HETATM 1238  C1A HEM A 154      37.648   3.136  10.495  1.00  4.90           C  
HETATM 1239  C2A HEM A 154      38.828   3.106   9.758  1.00  5.21           C  
HETATM 1240  C3A HEM A 154      38.610   3.968   8.707  1.00  4.99           C  
HETATM 1241  C4A HEM A 154      37.331   4.460   8.897  1.00  4.92           C  
HETATM 1242  CMA HEM A 154      39.569   4.296   7.567  1.00  5.49           C  
HETATM 1243  CAA HEM A 154      40.083   2.276  10.015  1.00  4.70           C  
HETATM 1244  CBA HEM A 154      40.194   1.064   9.094  1.00  6.55           C  
HETATM 1245  CGA HEM A 154      38.944   0.187   9.085  1.00  6.44           C  
HETATM 1246  O1A HEM A 154      38.642  -0.446  10.099  1.00  7.48           O  
HETATM 1247  O2A HEM A 154      38.293   0.116   8.045  1.00  7.76           O  
HETATM 1248  NB  HEM A 154      34.563   5.427   9.017  1.00  4.89           N  
HETATM 1249  C1B HEM A 154      35.437   5.811   8.083  1.00  4.55           C  
HETATM 1250  C2B HEM A 154      34.894   6.662   7.129  1.00  4.51           C  
HETATM 1251  C3B HEM A 154      33.606   6.877   7.562  1.00  4.26           C  
HETATM 1252  C4B HEM A 154      33.463   6.125   8.720  1.00  4.41           C  
HETATM 1253  CMB HEM A 154      35.555   7.178   5.846  1.00  4.09           C  
HETATM 1254  CAB HEM A 154      32.626   7.655   6.945  1.00  4.03           C  
HETATM 1255  CBB HEM A 154      32.892   8.928   6.297  1.00  4.00           C  
HETATM 1256  NC  HEM A 154      33.006   4.513  11.147  1.00  5.48           N  
HETATM 1257  C1C HEM A 154      32.104   5.382  10.649  1.00  4.23           C  
HETATM 1258  C2C HEM A 154      30.971   5.522  11.445  1.00  4.83           C  
HETATM 1259  C3C HEM A 154      31.217   4.708  12.542  1.00  5.61           C  
HETATM 1260  C4C HEM A 154      32.457   4.143  12.319  1.00  4.99           C  
HETATM 1261  CMC HEM A 154      29.745   6.387  11.160  1.00  4.74           C  
HETATM 1262  CAC HEM A 154      30.391   4.429  13.634  1.00  5.81           C  
HETATM 1263  CBC HEM A 154      29.140   5.108  13.939  1.00  5.99           C  
HETATM 1264  ND  HEM A 154      35.164   3.018  12.063  1.00  5.00           N  
HETATM 1265  C1D HEM A 154      34.341   2.757  13.100  1.00  5.67           C  
HETATM 1266  C2D HEM A 154      34.899   1.915  14.045  1.00  5.53           C  
HETATM 1267  C3D HEM A 154      36.202   1.745  13.645  1.00  5.81           C  
HETATM 1268  C4D HEM A 154      36.298   2.382  12.418  1.00  4.77           C  
HETATM 1269  CMD HEM A 154      34.226   1.355  15.283  1.00  6.67           C  
HETATM 1270  CAD HEM A 154      37.320   1.127  14.449  1.00  7.88           C  
HETATM 1271  CBD HEM A 154      37.874   2.106  15.471  1.00 10.23           C  
HETATM 1272  CGD HEM A 154      39.043   1.536  16.250  1.00 12.90           C  
HETATM 1273  O1D HEM A 154      38.888   1.309  17.446  1.00 14.42           O  
HETATM 1274  O2D HEM A 154      40.156   1.597  15.741  1.00 14.37           O  
HETATM 1275  C   CMO A 155      33.477   7.527  12.310  1.00  5.86           C  
HETATM 1276  O   CMO A 155      34.423   6.970  12.544  0.88  7.01           O  
HETATM 1277  O   HOH A 202      25.583  14.067  13.252  1.00 11.30           O  
HETATM 1278  O   HOH A 203      21.821   7.214   2.949  0.91 10.98           O  
HETATM 1279  O   HOH A 204      30.490   6.340  -8.306  1.00  9.51           O  
HETATM 1280  O   HOH A 205      24.360  29.717   7.029  0.99 12.88           O  
HETATM 1281  O   HOH A 206      24.915  13.958   3.335  1.00  6.68           O  
HETATM 1282  O   HOH A 207      21.718  13.514   2.291  1.00 10.40           O  
HETATM 1283  O   HOH A 208      29.464   8.366 -10.028  0.96 10.64           O  
HETATM 1284  O   HOH A 209      30.055  11.210  -9.738  1.00  6.68           O  
HETATM 1285  O   HOH A 210      31.442  12.548 -11.785  1.00  6.18           O  
HETATM 1286  O   HOH A 211      34.216  12.639  33.361  1.00  6.67           O  
HETATM 1287  O   HOH A 213      45.862  15.919   5.694  1.00  7.56           O  
HETATM 1288  O   HOH A 215      46.301  18.148   7.703  1.00  4.98           O  
HETATM 1289  O   HOH A 216      43.917  14.169   5.598  0.98  8.09           O  
HETATM 1290  O   HOH A 217      44.831  12.034  -0.134  1.00 10.01           O  
HETATM 1291  O   HOH A 218      22.203  26.114  -3.627  1.00 12.68           O  
HETATM 1292  O   HOH A 219      33.999  25.129  -1.923  1.00  5.43           O  
HETATM 1293  O   HOH A 220      43.581   5.790  17.385  1.00 14.86           O  
HETATM 1294  O   HOH A 222      34.274   9.962  -4.766  1.00  4.97           O  
HETATM 1295  O   HOH A 223      43.419  10.437  -6.345  0.98 17.32           O  
HETATM 1296  O   HOH A 225      29.022  28.087  -2.415  1.00  8.66           O  
HETATM 1297  O   HOH A 226      36.316   1.946  25.979  1.00 13.41           O  
HETATM 1298  O   HOH A 228      46.676  16.986  11.107  1.00  4.91           O  
HETATM 1299  O   HOH A 232      47.144  19.406  12.353  1.00  5.75           O  
HETATM 1300  O   HOH A 234      40.927  13.910  14.523  1.00  6.38           O  
HETATM 1301  O   HOH A 236      25.431  16.872  13.306  1.00 12.33           O  
HETATM 1302  O   HOH A 237      19.593   5.650  15.581  0.65 13.08           O  
HETATM 1303  O   HOH A 239      26.661   6.625  24.002  0.83 12.07           O  
HETATM 1304  O   HOH A 240      34.870  -1.038  17.895  0.94 19.30           O  
HETATM 1305  O   HOH A 241      31.626  -1.969  16.350  0.81 11.13           O  
HETATM 1306  O   HOH A 242      36.668   1.226  18.712  1.00 11.96           O  
HETATM 1307  O   HOH A 246      44.401   8.424  24.194  1.00 17.35           O  
HETATM 1308  O   HOH A 247      43.126   6.539   6.392  0.97  9.66           O  
HETATM 1309  O   HOH A 248      26.545  30.167  -2.499  1.00 17.24           O  
HETATM 1310  O   HOH A 249      43.112  12.061   1.942  1.00  6.38           O  
HETATM 1311  O   HOH A 251      23.157  31.388   5.120  1.00 10.05           O  
HETATM 1312  O   HOH A 252      34.195  29.357  12.630  1.00  6.50           O  
HETATM 1313  O   HOH A 253      42.519  14.328   3.215  0.95  5.24           O  
HETATM 1314  O   HOH A 254      42.568   9.326  -3.932  1.00  8.79           O  
HETATM 1315  O   HOH A 255      39.993   5.719   1.071  0.83  4.29           O  
HETATM 1316  O   HOH A 256      39.288   9.967 -10.532  1.00  9.25           O  
HETATM 1317  O   HOH A 257      39.076   3.093  -7.396  1.00 11.41           O  
HETATM 1318  O   HOH A 259      39.495   3.029   1.630  0.82  7.12           O  
HETATM 1319  O   HOH A 260      40.526  -2.445  -3.208  0.68  8.73           O  
HETATM 1320  O   HOH A 262      27.095  24.659  11.518  1.00  9.56           O  
HETATM 1321  O   HOH A 263      30.669  30.193  10.824  1.00 15.21           O  
HETATM 1322  O   HOH A 266      18.602   5.262   4.529  0.65 44.23           O  
HETATM 1323  O   HOH A 267      31.067  -8.213  -4.243  1.00 10.30           O  
HETATM 1324  O   HOH A 268      18.839  14.970   0.963  0.96 36.67           O  
HETATM 1325  O   HOH A 269      31.900   1.262  -5.200  0.97 19.80           O  
HETATM 1326  O   HOH A 270      31.440   2.793  -7.138  1.00 15.36           O  
HETATM 1327  O   HOH A 275      24.170  -4.497  -4.136  0.70 11.26           O  
HETATM 1328  O   HOH A 280      28.144  22.522 -12.676  1.00 30.78           O  
HETATM 1329  O   HOH A 281      25.886  22.855  -5.914  1.00 12.28           O  
HETATM 1330  O   HOH A 282      31.831  21.412  -0.625  1.00  9.65           O  
HETATM 1331  O   HOH A 286      40.540  11.622  27.624  0.98 14.58           O  
HETATM 1332  O   HOH A 291      42.377   3.919   5.055  0.94 17.33           O  
HETATM 1333  O   HOH A 292      39.605  -9.109   4.853  0.84 10.91           O  
HETATM 1334  O   HOH A 293      31.864  -3.517  -3.725  1.00 23.63           O  
HETATM 1335  O   HOH A 294      40.550  13.874  20.484  0.97  9.50           O  
HETATM 1336  O   HOH A 296      27.877  11.492  23.635  1.00 19.96           O  
HETATM 1337  O   HOH A 299      45.228  10.501  25.614  0.74 14.66           O  
HETATM 1338  O   HOH A 303      39.237   0.368   5.450  1.00 10.94           O  
HETATM 1339  O   HOH A 304      23.401  14.966   5.558  0.76 11.45           O  
HETATM 1340  O   HOH A 307      31.152  28.801  -0.979  1.00  9.60           O  
HETATM 1341  O   HOH A 308      41.136   1.885  13.147  0.95 16.06           O  
HETATM 1342  O   HOH A 309      40.142  -0.595  12.434  0.94 10.96           O  
HETATM 1343  O   HOH A 311      25.059   1.766  18.568  1.00 14.83           O  
HETATM 1344  O   HOH A 313      20.256   3.299   1.528  0.70 21.69           O  
HETATM 1345  O   HOH A 314      22.747   1.704  -3.045  0.97 10.35           O  
HETATM 1346  O   HOH A 317      20.066   9.749  16.992  1.00 17.81           O  
HETATM 1347  O   HOH A 321      24.525  19.179   9.014  0.92 20.85           O  
HETATM 1348  O   HOH A 322      39.292  20.839  17.193  0.83 18.12           O  
HETATM 1349  O   HOH A 326      29.142  23.445  -9.605  0.94 20.92           O  
HETATM 1350  O   HOH A 327      33.105  24.819  -8.878  0.99 15.48           O  
HETATM 1351  O   HOH A 330      22.157  -2.658  -4.530  0.75 20.98           O  
HETATM 1352  O   HOH A 331      43.096   6.642  -3.449  0.83 10.53           O  
HETATM 1353  O   HOH A 332      44.573  10.213  -2.304  1.00 12.27           O  
HETATM 1354  O   HOH A 333      21.800  -0.782  -2.295  1.00 12.61           O  
HETATM 1355  O   HOH A 335      28.622  32.236   0.135  0.76 20.26           O  
HETATM 1356  O   HOH A 339      36.558  24.211  16.172  0.96 21.84           O  
HETATM 1357  O   HOH A 340      29.927  19.268  18.871  1.00 14.97           O  
HETATM 1358  O   HOH A 400      39.357   7.384  31.183  1.00 30.46           O  
HETATM 1359  O   HOH A 405      31.580   9.915  -3.406  1.00  8.94           O  
HETATM 1360  O   HOH A 412      37.772  26.328  14.530  1.00 14.37           O  
HETATM 1361  O   HOH A 419      28.560  10.073  28.791  0.79 27.01           O  
HETATM 1362  O   HOH A 420      42.917  16.331  -5.792  0.72 21.51           O  
HETATM 1363  O   HOH A 421      41.243  14.671  -7.450  0.88 19.04           O  
HETATM 1364  O   HOH A 422      47.483  17.674   4.171  1.00  6.77           O  
HETATM 1365  O   HOH A 423      38.998  27.403  -2.565  0.93 37.70           O  
HETATM 1366  O   HOH A 424      25.260  20.089  -6.160  0.83  8.95           O  
HETATM 1367  O   HOH A 425      30.954  21.254 -14.609  1.00 12.60           O  
HETATM 1368  O   HOH A 426      33.718  22.321 -14.738  1.00 35.68           O  
HETATM 1369  O   HOH A 427      43.918  25.645  -0.274  1.00 40.53           O  
HETATM 1370  O   HOH A 428      42.450  24.549  13.101  0.96 35.79           O  
HETATM 1371  O   HOH A 429      47.243  24.582  10.245  1.00 16.85           O  
HETATM 1372  O   HOH A 430      32.307  19.208  17.563  0.98 10.16           O  
HETATM 1373  O   HOH A 431      34.214  19.804  19.482  1.00 17.49           O  
HETATM 1374  O   HOH A 432      39.922  18.541  26.985  1.00 13.22           O  
HETATM 1375  O   HOH A 433      43.775  11.870  27.617  0.77 22.03           O  
HETATM 1376  O   HOH A 434      46.108   8.587  12.314  0.93 11.23           O  
HETATM 1377  O   HOH A 435      45.850   8.410   7.825  0.86 26.09           O  
HETATM 1378  O   HOH A 436      45.433   8.458   1.839  0.61 20.94           O  
HETATM 1379  O   HOH A 437      20.874   9.244   1.188  0.93 20.21           O  
HETATM 1380  O   HOH A 438      34.841  15.235 -13.230  1.00 10.92           O  
HETATM 1381  O   HOH A 439      42.162   2.084   0.365  0.74 20.85           O  
HETATM 1382  O   HOH A 440      39.151  25.885  10.356  1.00  4.27           O  
HETATM 1383  O   HOH A 441      33.484  22.835  14.553  1.00 18.85           O  
HETATM 1384  O   HOH A 442      32.097   5.676  30.849  0.96 15.77           O  
HETATM 1385  O   HOH A 443      32.078   1.692  28.711  1.00 24.37           O  
HETATM 1386  O   HOH A 444      34.435   0.534  27.860  0.75 20.04           O  
HETATM 1387  O   HOH A 445      47.805  10.615  13.242  0.95 13.20           O  
HETATM 1388  O   HOH A 446      47.290  12.934  14.508  0.87 15.89           O  
HETATM 1389  O   HOH A 448      30.276  -8.424  17.652  1.00 25.73           O  
HETATM 1390  O   HOH A 449      20.399   1.960   8.316  0.92 11.98           O  
HETATM 1391  O   HOH A 450      22.499   7.955  -0.977  0.92 15.92           O  
HETATM 1392  O   HOH A 451      22.786   1.478  -5.604  0.95 20.14           O  
HETATM 1393  O   HOH A 452      25.945   1.980  -6.656  0.96 22.37           O  
HETATM 1394  O   HOH A 453      26.886   4.911  -8.440  0.92 15.19           O  
CONECT  748 1232                                                                
CONECT 1227 1228 1229 1230 1231                                                 
CONECT 1228 1227                                                                
CONECT 1229 1227                                                                
CONECT 1230 1227                                                                
CONECT 1231 1227                                                                
CONECT 1232  748 1237 1248 1256                                                 
CONECT 1232 1264                                                                
CONECT 1233 1238 1268                                                           
CONECT 1234 1241 1249                                                           
CONECT 1235 1252 1257                                                           
CONECT 1236 1260 1265                                                           
CONECT 1237 1232 1238 1241                                                      
CONECT 1238 1233 1237 1239                                                      
CONECT 1239 1238 1240 1243                                                      
CONECT 1240 1239 1241 1242                                                      
CONECT 1241 1234 1237 1240                                                      
CONECT 1242 1240                                                                
CONECT 1243 1239 1244                                                           
CONECT 1244 1243 1245                                                           
CONECT 1245 1244 1246 1247                                                      
CONECT 1246 1245                                                                
CONECT 1247 1245                                                                
CONECT 1248 1232 1249 1252                                                      
CONECT 1249 1234 1248 1250                                                      
CONECT 1250 1249 1251 1253                                                      
CONECT 1251 1250 1252 1254                                                      
CONECT 1252 1235 1248 1251                                                      
CONECT 1253 1250                                                                
CONECT 1254 1251 1255                                                           
CONECT 1255 1254                                                                
CONECT 1256 1232 1257 1260                                                      
CONECT 1257 1235 1256 1258                                                      
CONECT 1258 1257 1259 1261                                                      
CONECT 1259 1258 1260 1262                                                      
CONECT 1260 1236 1256 1259                                                      
CONECT 1261 1258                                                                
CONECT 1262 1259 1263                                                           
CONECT 1263 1262                                                                
CONECT 1264 1232 1265 1268                                                      
CONECT 1265 1236 1264 1266                                                      
CONECT 1266 1265 1267 1269                                                      
CONECT 1267 1266 1268 1270                                                      
CONECT 1268 1233 1264 1267                                                      
CONECT 1269 1266                                                                
CONECT 1270 1267 1271                                                           
CONECT 1271 1270 1272                                                           
CONECT 1272 1271 1273 1274                                                      
CONECT 1273 1272                                                                
CONECT 1274 1272                                                                
CONECT 1275 1276                                                                
CONECT 1276 1275                                                                
MASTER      327    0    3    8    0    0    9    6 1393    1   52   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.