CNRS Nantes University US2B US2B
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***  myoglobin  ***

elNémo ID: 2411151859193473238

Job options:

ID        	=	 2411151859193473238
JOBID     	=	 myoglobin
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 myoglobin

HEADER    OXYGEN STORAGE                          14-JAN-91   5MBA              
TITLE     BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN.           
TITLE    2 CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: APLYSIA LIMACINA;                               
SOURCE   3 ORGANISM_COMMON: SLUG SEA HARE;                                      
SOURCE   4 ORGANISM_TAXID: 6502                                                 
KEYWDS    OXYGEN STORAGE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BOLOGNESI,S.ONESTI,G.GATTI,A.CODA,P.ASCENZI,M.BRUNORI               
REVDAT   5   23-OCT-24 5MBA    1       REMARK                                   
REVDAT   4   05-JUN-24 5MBA    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 5MBA    1       VERSN                                    
REVDAT   2   01-APR-03 5MBA    1       JRNL                                     
REVDAT   1   15-JUL-92 5MBA    0                                                
SPRSDE     15-JUL-92 5MBA      2MBA                                             
JRNL        AUTH   A.MATTEVI,G.GATTI,A.CODA,M.RIZZI,P.ASCENZI,M.BRUNORI,        
JRNL        AUTH 2 M.BOLOGNESI                                                  
JRNL        TITL   BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN.  
JRNL        TITL 2 CRYSTALLOGRAPHIC ANALYSIS AT 1.9 A RESOLUTION.               
JRNL        REF    J.MOL.RECOG.                  V.   4     1 1991              
JRNL        REFN                   ISSN 0952-3499                               
JRNL        PMID   1931125                                                      
JRNL        DOI    10.1002/JMR.300040102                                        
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.BOLOGNESI,F.FRIGERIO,C.LIONETTI,M.RIZZI,P.ASCENZI,         
REMARK   1  AUTH 2 M.BRUNORI                                                    
REMARK   1  TITL   APLYSIA LIMACINA MYOGLOBIN: MOLECULAR BASES FOR LIGAND       
REMARK   1  TITL 2 BINDING                                                      
REMARK   1  REF    STRUCTURE AND FUNCTION OF              161 1991              
REMARK   1  REF  2 INVERTEBRATE OXYGEN CARRIERS                                 
REMARK   1  PUBL   SPRINGER-VERLAG, NEW YORK                                    
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.BOLOGNESI,S.ONESTI,G.GATTI,A.CODA,P.ASCENZI,M.BRUNORI      
REMARK   1  TITL   APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.6 
REMARK   1  TITL 2 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    J.MOL.BIOL.                   V. 205   529 1989              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.BOLOGNESI,A.CODA,G.GATTI,P.ASCENZI,M.BRUNORI               
REMARK   1  TITL   CRYSTAL STRUCTURE OF FERRIC APLYSIA LIMACINA MYOGLOBIN AT    
REMARK   1  TITL 2 2.0 ANGSTROMS RESOLUTION                                     
REMARK   1  REF    J.MOL.BIOL.                   V. 183   113 1985              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.BOLOGNESI,E.CANNILLO,P.ASCENZI,G.M.GIACOMETTI,A.MERLI,     
REMARK   1  AUTH 2 M.BRUNORI                                                    
REMARK   1  TITL   REACTIVITY OF FERRIC APLYSIA AND SPERM WHALE MYOGLOBINS      
REMARK   1  TITL 2 TOWARDS IMIDAZOLE. X-RAY AND BINDING STUDY                   
REMARK   1  REF    J.MOL.BIOL.                   V. 158   305 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.BOLOGNESI,E.CANNILLO,R.OBERTI,G.ROSSI,L.UNGARETTI          
REMARK   1  TITL   THE STRUCTURE OF APLYSIA LIMACINA MYOGLOBIN AT 3.6 ANGSTROMS 
REMARK   1  TITL 2 RESOLUTION                                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  34    62 1978              
REMARK   1  REF  2 (SUPPLEMENT)                                                 
REMARK   1  REFN                   ISSN 0567-7394                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   L.UNGARETTI,M.BOLOGNESI,E.CANNILLO,R.OBERTI,G.ROSSI          
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF MET-MYOGLOBIN FROM APLYSIA LIMACINA 
REMARK   1  TITL 2 AT 5 ANGSTROMS RESOLUTION                                    
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.B      V.  34  3658 1978              
REMARK   1  REFN                   ISSN 0108-7681                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   T.L.BLUNDELL,M.BRUNORI,B.CURTI,M.BOLOGNESI,A.CODA,           
REMARK   1  AUTH 2 M.FUMAGALLI,L.UNGARETTI                                      
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES ON 
REMARK   1  TITL 2 MET-MYOGLOBIN FROM APLYSIA LIMACINA                          
REMARK   1  REF    J.MOL.BIOL.                   V.  97   665 1975              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   L.TENTORI,G.VIVALDI,S.CARTA,M.MARINUCCI,A.MASSA,E.ANTONINI,  
REMARK   1  AUTH 2 M.BRUNORI                                                    
REMARK   1  TITL   THE AMINO ACID SEQUENCE OF MYOGLOBIN FROM THE MOLLUSC        
REMARK   1  TITL 2 APLYSIA LIMACINA                                             
REMARK   1  REF    INT.J.PEPT.PROTEIN RES.       V.   5   187 1973              
REMARK   1  REFN                   ISSN 0367-8377                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.139                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1086                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.015 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.350 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179737.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       26.49000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       16.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       16.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.49000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   12   CD   CE   NZ                                        
REMARK 480     LYS A   21   NZ                                                  
REMARK 480     ASP A   27   CG   OD1  OD2                                       
REMARK 480     LYS A   35   CD   CE   NZ                                        
REMARK 480     LYS A   47   CG   CD   CE   NZ                                   
REMARK 480     LYS A   49   CE   NZ                                             
REMARK 480     LYS A   55   NZ                                                  
REMARK 480     LYS A   83   NZ                                                  
REMARK 480     GLY A  145   C                                                   
REMARK 480     ALA A  146   OXT                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   185     O    HOH A   271     4433     1.07            
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    ASP A   8   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    PHE A  33   CB  -  CG  -  CD1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 AZIDE ION IS BOUND TO THE HEME IRON AT THE DISTAL SITE AND           
REMARK 600 TRIGGERS A LARGE CONFORMATIONAL CHANGE IN THE SIDE CHAIN OF          
REMARK 600 RESIDUE ARG 66.  A HYDROGEN BOND OCCURS BETWEEN AZIDE ATOM           
REMARK 600 N1 AND NE1 ARG 66.  THIS CONFORMATIONAL CHANGE AT RESIDUE            
REMARK 600 ARG 66 BECAME EVIDENT ONLY IN THE LATER STAGES OF                    
REMARK 600 REFINEMENT.  THE SIDE CHAIN OF ARG 66 IS NOT FULLY OCCUPIED          
REMARK 600 BEYOND THE CB ATOM.                                                  
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 148  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  95   NE2                                                    
REMARK 620 2 HEM A 148   NA   87.9                                              
REMARK 620 3 HEM A 148   NB   96.0  95.8                                        
REMARK 620 4 HEM A 148   NC   93.3 177.4  86.4                                  
REMARK 620 5 HEM A 148   ND   91.3  84.6 172.7  93.0                            
REMARK 620 6 AZI A 149   N2  149.7  65.7 100.9 112.6  72.7                      
REMARK 620 7 AZI A 149   N3  169.1  85.3  93.2  93.2  79.6  20.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 149                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 148                 
DBREF  5MBA A    1   145  UNP    P02210   GLB_APLLI        1    145             
SEQADV 5MBA ASN A   22  UNP  P02210    ASP    22 CONFLICT                       
SEQADV 5MBA LEU A   26  UNP  P02210    ASP    26 CONFLICT                       
SEQADV 5MBA ASP A   27  UNP  P02210    ALA    27 CONFLICT                       
SEQADV 5MBA ASN A   80  UNP  P02210    ASP    80 CONFLICT                       
SEQRES   1 A  147  ACE SER LEU SER ALA ALA GLU ALA ASP LEU ALA GLY LYS          
SEQRES   2 A  147  SER TRP ALA PRO VAL PHE ALA ASN LYS ASN ALA ASN GLY          
SEQRES   3 A  147  LEU ASP PHE LEU VAL ALA LEU PHE GLU LYS PHE PRO ASP          
SEQRES   4 A  147  SER ALA ASN PHE PHE ALA ASP PHE LYS GLY LYS SER VAL          
SEQRES   5 A  147  ALA ASP ILE LYS ALA SER PRO LYS LEU ARG ASP VAL SER          
SEQRES   6 A  147  SER ARG ILE PHE THR ARG LEU ASN GLU PHE VAL ASN ASN          
SEQRES   7 A  147  ALA ALA ASN ALA GLY LYS MET SER ALA MET LEU SER GLN          
SEQRES   8 A  147  PHE ALA LYS GLU HIS VAL GLY PHE GLY VAL GLY SER ALA          
SEQRES   9 A  147  GLN PHE GLU ASN VAL ARG SER MET PHE PRO GLY PHE VAL          
SEQRES  10 A  147  ALA SER VAL ALA ALA PRO PRO ALA GLY ALA ASP ALA ALA          
SEQRES  11 A  147  TRP THR LYS LEU PHE GLY LEU ILE ILE ASP ALA LEU LYS          
SEQRES  12 A  147  ALA ALA GLY ALA                                              
HET    ACE  A   0       3                                                       
HET    AZI  A 149       3                                                       
HET    HEM  A 148      43                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     AZI AZIDE ION                                                        
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2  AZI    N3 1-                                                        
FORMUL   3  HEM    C34 H32 FE N4 O4                                             
FORMUL   4  HOH   *126(H2 O)                                                    
HELIX    1   A ALA A    4  ALA A   19  1BENT ALPHA-HELIX, RESIDUE 16      16    
HELIX    2   B LYS A   21  LYS A   35  1                                  15    
HELIX    3   C PRO A   37  PHE A   42  5                                   6    
HELIX    4   D VAL A   51  LYS A   55  1                                   5    
HELIX    5   E LYS A   59  ASN A   76  1                                  18    
HELIX    6   F ALA A   81  GLY A   97  1                                  17    
HELIX    7   G SER A  102  SER A  118  1BENT ALPHA-HELIX, RESIDUE 113     17    
HELIX    8   H ALA A  126  ALA A  143  1                                  18    
LINK         C   ACE A   0                 N   SER A   1     1555   1555  1.31  
LINK         NE2 HIS A  95                FE   HEM A 148     1555   1555  2.04  
LINK        FE   HEM A 148                 N2  AZI A 149     1555   1555  2.92  
LINK        FE   HEM A 148                 N3  AZI A 149     1555   1555  2.08  
SITE     1 AC1  4 PHE A  43  ARG A  66  ILE A  67  HEM A 148                    
SITE     1 AC2 16 PHE A  28  SER A  39  PHE A  42  PHE A  43                    
SITE     2 AC2 16 ARG A  66  ILE A  67  ARG A  70  PHE A  91                    
SITE     3 AC2 16 HIS A  95  PHE A  98  VAL A 100  GLN A 104                    
SITE     4 AC2 16 PHE A 105  AZI A 149  HOH A 239  HOH A 253                    
CRYST1   52.980   70.700   32.500  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018875  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014144  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030769        0.00000                         
HETATM    1  C   ACE A   0     -71.115 -51.040 -24.606  0.92 29.04           C  
HETATM    2  O   ACE A   0     -70.863 -49.833 -24.414  0.95 30.51           O  
HETATM    3  CH3 ACE A   0     -72.102 -51.582 -25.632  1.00 28.59           C  
ATOM      4  N   SER A   1     -70.545 -52.006 -23.925  1.00 30.30           N  
ATOM      5  CA  SER A   1     -69.565 -51.726 -22.905  1.00 25.52           C  
ATOM      6  C   SER A   1     -68.740 -52.946 -22.563  1.00 20.07           C  
ATOM      7  O   SER A   1     -68.888 -54.074 -23.084  1.00 26.51           O  
ATOM      8  CB  SER A   1     -70.249 -51.257 -21.622  1.00 41.70           C  
ATOM      9  OG  SER A   1     -71.174 -52.229 -21.157  1.00 34.41           O  
ATOM     10  N   LEU A   2     -67.863 -52.697 -21.598  1.00 19.22           N  
ATOM     11  CA  LEU A   2     -67.038 -53.742 -21.022  1.00 17.86           C  
ATOM     12  C   LEU A   2     -67.714 -54.140 -19.685  1.00  8.01           C  
ATOM     13  O   LEU A   2     -68.545 -53.401 -19.110  1.00 16.50           O  
ATOM     14  CB  LEU A   2     -65.652 -53.181 -20.627  1.00 20.68           C  
ATOM     15  CG  LEU A   2     -64.666 -53.245 -21.758  1.00 19.59           C  
ATOM     16  CD1 LEU A   2     -65.182 -52.376 -22.881  1.00 21.81           C  
ATOM     17  CD2 LEU A   2     -63.375 -52.641 -21.230  1.00 12.28           C  
ATOM     18  N   SER A   3     -67.336 -55.315 -19.178  1.00 21.40           N  
ATOM     19  CA  SER A   3     -67.884 -55.697 -17.886  1.00 21.81           C  
ATOM     20  C   SER A   3     -67.028 -54.954 -16.866  1.00 16.13           C  
ATOM     21  O   SER A   3     -65.984 -54.374 -17.195  1.00 10.80           O  
ATOM     22  CB  SER A   3     -67.735 -57.184 -17.613  1.00 10.05           C  
ATOM     23  OG  SER A   3     -66.369 -57.523 -17.749  1.00 20.59           O  
ATOM     24  N   ALA A   4     -67.448 -55.008 -15.610  1.00 11.08           N  
ATOM     25  CA  ALA A   4     -66.706 -54.359 -14.560  1.00 19.07           C  
ATOM     26  C   ALA A   4     -65.375 -55.034 -14.423  1.00 17.16           C  
ATOM     27  O   ALA A   4     -64.388 -54.412 -14.136  1.00 17.22           O  
ATOM     28  CB  ALA A   4     -67.422 -54.529 -13.247  1.00 14.85           C  
ATOM     29  N   ALA A   5     -65.372 -56.341 -14.584  1.00  9.53           N  
ATOM     30  CA  ALA A   5     -64.118 -57.025 -14.484  1.00  8.97           C  
ATOM     31  C   ALA A   5     -63.131 -56.558 -15.562  1.00 15.09           C  
ATOM     32  O   ALA A   5     -61.940 -56.247 -15.339  1.00 17.41           O  
ATOM     33  CB  ALA A   5     -64.467 -58.497 -14.621  1.00 12.33           C  
ATOM     34  N   GLU A   6     -63.622 -56.558 -16.778  1.00 10.23           N  
ATOM     35  CA  GLU A   6     -62.804 -56.146 -17.922  1.00 18.85           C  
ATOM     36  C   GLU A   6     -62.382 -54.691 -17.733  1.00 22.54           C  
ATOM     37  O   GLU A   6     -61.231 -54.298 -17.935  1.00 15.89           O  
ATOM     38  CB  GLU A   6     -63.588 -56.278 -19.260  1.00 14.97           C  
ATOM     39  CG  GLU A   6     -64.020 -57.709 -19.625  1.00 12.46           C  
ATOM     40  CD  GLU A   6     -64.944 -57.819 -20.829  1.00 18.88           C  
ATOM     41  OE1 GLU A   6     -65.942 -56.968 -20.846  1.00 19.77           O  
ATOM     42  OE2 GLU A   6     -64.791 -58.680 -21.664  1.00 40.50           O  
ATOM     43  N   ALA A   7     -63.332 -53.854 -17.376  1.00  8.69           N  
ATOM     44  CA  ALA A   7     -62.954 -52.467 -17.206  1.00 12.04           C  
ATOM     45  C   ALA A   7     -61.831 -52.288 -16.171  1.00 14.85           C  
ATOM     46  O   ALA A   7     -60.902 -51.445 -16.250  1.00 12.72           O  
ATOM     47  CB  ALA A   7     -64.202 -51.691 -16.831  1.00 25.45           C  
ATOM     48  N   ASP A   8     -61.880 -53.126 -15.163  1.00 13.05           N  
ATOM     49  CA  ASP A   8     -60.858 -53.016 -14.144  1.00 20.33           C  
ATOM     50  C   ASP A   8     -59.507 -53.369 -14.707  1.00 22.19           C  
ATOM     51  O   ASP A   8     -58.489 -52.758 -14.371  1.00 17.69           O  
ATOM     52  CB  ASP A   8     -61.180 -53.824 -12.850  1.00 36.80           C  
ATOM     53  CG  ASP A   8     -62.350 -53.306 -12.011  1.00 64.84           C  
ATOM     54  OD1 ASP A   8     -62.458 -51.996 -11.972  1.00 38.00           O  
ATOM     55  OD2 ASP A   8     -63.149 -54.021 -11.428  1.00 61.93           O  
ATOM     56  N   LEU A   9     -59.490 -54.389 -15.560  1.00 13.36           N  
ATOM     57  CA  LEU A   9     -58.224 -54.826 -16.142  1.00  5.55           C  
ATOM     58  C   LEU A   9     -57.640 -53.755 -17.019  1.00 12.22           C  
ATOM     59  O   LEU A   9     -56.422 -53.523 -17.009  1.00 14.64           O  
ATOM     60  CB  LEU A   9     -58.292 -56.153 -16.886  1.00 15.34           C  
ATOM     61  CG  LEU A   9     -58.763 -57.292 -16.021  1.00 16.35           C  
ATOM     62  CD1 LEU A   9     -59.033 -58.528 -16.872  1.00 20.06           C  
ATOM     63  CD2 LEU A   9     -57.606 -57.604 -15.123  1.00 12.36           C  
ATOM     64  N   ALA A  10     -58.531 -53.084 -17.747  1.00  8.78           N  
ATOM     65  CA  ALA A  10     -58.068 -52.006 -18.592  1.00 10.65           C  
ATOM     66  C   ALA A  10     -57.536 -50.857 -17.720  1.00  5.54           C  
ATOM     67  O   ALA A  10     -56.450 -50.271 -17.910  1.00 13.33           O  
ATOM     68  CB  ALA A  10     -59.222 -51.488 -19.404  1.00 13.08           C  
ATOM     69  N   GLY A  11     -58.270 -50.558 -16.686  1.00 21.51           N  
ATOM     70  CA  GLY A  11     -57.789 -49.485 -15.853  1.00  8.22           C  
ATOM     71  C   GLY A  11     -56.465 -49.811 -15.221  1.00 11.17           C  
ATOM     72  O   GLY A  11     -55.620 -48.946 -15.065  1.00 12.37           O  
ATOM     73  N   LYS A  12     -56.320 -51.043 -14.831  1.00  9.30           N  
ATOM     74  CA  LYS A  12     -55.096 -51.449 -14.206  1.00  8.37           C  
ATOM     75  C   LYS A  12     -53.904 -51.314 -15.136  1.00 25.83           C  
ATOM     76  O   LYS A  12     -52.856 -50.935 -14.675  1.00 12.92           O  
ATOM     77  CB  LYS A  12     -55.204 -52.904 -13.684  1.00 14.95           C  
ATOM     78  CG  LYS A  12     -54.907 -53.016 -12.214  1.00 39.46           C  
ATOM     79  CD  LYS A  12     -55.602 -54.169 -11.519  0.00 33.14           C  
ATOM     80  CE  LYS A  12     -55.598 -55.451 -12.329  0.00 19.54           C  
ATOM     81  NZ  LYS A  12     -56.672 -56.364 -11.918  0.00 15.53           N  
ATOM     82  N   SER A  13     -54.027 -51.671 -16.424  1.00 16.34           N  
ATOM     83  CA  SER A  13     -52.892 -51.588 -17.326  1.00 13.17           C  
ATOM     84  C   SER A  13     -52.625 -50.177 -17.724  1.00 11.07           C  
ATOM     85  O   SER A  13     -51.507 -49.854 -18.117  1.00 23.50           O  
ATOM     86  CB  SER A  13     -53.045 -52.389 -18.617  1.00 13.14           C  
ATOM     87  OG  SER A  13     -54.233 -52.006 -19.250  1.00 18.26           O  
ATOM     88  N   TRP A  14     -53.665 -49.348 -17.628  1.00 13.44           N  
ATOM     89  CA  TRP A  14     -53.591 -47.919 -18.046  1.00  8.73           C  
ATOM     90  C   TRP A  14     -52.874 -47.013 -17.085  1.00 11.68           C  
ATOM     91  O   TRP A  14     -52.177 -46.096 -17.484  1.00  9.20           O  
ATOM     92  CB  TRP A  14     -55.028 -47.406 -18.327  1.00  5.58           C  
ATOM     93  CG  TRP A  14     -55.173 -45.944 -18.687  1.00  9.84           C  
ATOM     94  CD1 TRP A  14     -55.862 -45.000 -17.998  1.00 11.23           C  
ATOM     95  CD2 TRP A  14     -54.695 -45.282 -19.861  1.00 14.20           C  
ATOM     96  NE1 TRP A  14     -55.840 -43.767 -18.617  1.00  8.30           N  
ATOM     97  CE2 TRP A  14     -55.125 -43.916 -19.778  1.00 14.98           C  
ATOM     98  CE3 TRP A  14     -53.941 -45.710 -20.949  1.00 18.96           C  
ATOM     99  CZ2 TRP A  14     -54.812 -42.990 -20.769  1.00 10.19           C  
ATOM    100  CZ3 TRP A  14     -53.641 -44.787 -21.922  1.00 15.52           C  
ATOM    101  CH2 TRP A  14     -54.100 -43.454 -21.852  1.00 10.74           C  
ATOM    102  N   ALA A  15     -53.076 -47.284 -15.815  1.00 22.55           N  
ATOM    103  CA  ALA A  15     -52.509 -46.513 -14.725  1.00 22.34           C  
ATOM    104  C   ALA A  15     -51.028 -46.199 -14.892  1.00  5.46           C  
ATOM    105  O   ALA A  15     -50.658 -45.036 -14.863  1.00 15.93           O  
ATOM    106  CB  ALA A  15     -52.856 -47.108 -13.351  1.00 20.17           C  
ATOM    107  N   PRO A  16     -50.183 -47.205 -15.036  1.00  6.06           N  
ATOM    108  CA  PRO A  16     -48.772 -46.874 -15.197  1.00  5.87           C  
ATOM    109  C   PRO A  16     -48.557 -45.952 -16.418  1.00 18.24           C  
ATOM    110  O   PRO A  16     -47.660 -45.102 -16.463  1.00 21.02           O  
ATOM    111  CB  PRO A  16     -48.099 -48.226 -15.472  1.00  6.27           C  
ATOM    112  CG  PRO A  16     -49.090 -49.334 -15.123  1.00 17.21           C  
ATOM    113  CD  PRO A  16     -50.449 -48.665 -15.041  1.00  4.00           C  
ATOM    114  N   VAL A  17     -49.358 -46.125 -17.467  1.00 21.21           N  
ATOM    115  CA  VAL A  17     -49.202 -45.311 -18.680  1.00 10.61           C  
ATOM    116  C   VAL A  17     -49.585 -43.900 -18.371  1.00  6.84           C  
ATOM    117  O   VAL A  17     -48.819 -42.969 -18.634  1.00 12.74           O  
ATOM    118  CB  VAL A  17     -50.076 -45.804 -19.852  1.00 12.39           C  
ATOM    119  CG1 VAL A  17     -49.947 -44.896 -21.065  1.00 10.88           C  
ATOM    120  CG2 VAL A  17     -49.690 -47.218 -20.254  1.00  7.25           C  
ATOM    121  N   PHE A  18     -50.807 -43.747 -17.845  1.00  6.64           N  
ATOM    122  CA  PHE A  18     -51.313 -42.413 -17.482  1.00 10.43           C  
ATOM    123  C   PHE A  18     -50.417 -41.695 -16.428  1.00  7.49           C  
ATOM    124  O   PHE A  18     -50.398 -40.452 -16.397  1.00 12.97           O  
ATOM    125  CB  PHE A  18     -52.788 -42.566 -17.005  1.00  6.29           C  
ATOM    126  CG  PHE A  18     -53.582 -41.299 -17.180  1.00 10.47           C  
ATOM    127  CD1 PHE A  18     -53.756 -40.667 -18.414  1.00  6.85           C  
ATOM    128  CD2 PHE A  18     -54.162 -40.729 -16.055  1.00 10.43           C  
ATOM    129  CE1 PHE A  18     -54.507 -39.502 -18.531  1.00 14.77           C  
ATOM    130  CE2 PHE A  18     -54.899 -39.545 -16.147  1.00 16.87           C  
ATOM    131  CZ  PHE A  18     -55.069 -38.928 -17.388  1.00 21.76           C  
ATOM    132  N   ALA A  19     -49.690 -42.467 -15.572  1.00 21.25           N  
ATOM    133  CA  ALA A  19     -48.842 -41.885 -14.529  1.00 16.44           C  
ATOM    134  C   ALA A  19     -47.889 -40.842 -15.039  1.00 23.91           C  
ATOM    135  O   ALA A  19     -47.525 -39.917 -14.342  1.00 19.49           O  
ATOM    136  CB  ALA A  19     -48.106 -42.893 -13.678  1.00 18.75           C  
ATOM    137  N   ASN A  20     -47.460 -41.012 -16.264  1.00  9.35           N  
ATOM    138  CA  ASN A  20     -46.550 -40.071 -16.893  1.00  8.00           C  
ATOM    139  C   ASN A  20     -47.275 -39.730 -18.185  1.00 10.39           C  
ATOM    140  O   ASN A  20     -46.914 -40.182 -19.230  1.00 11.81           O  
ATOM    141  CB  ASN A  20     -45.245 -40.810 -17.225  1.00  7.74           C  
ATOM    142  CG  ASN A  20     -44.389 -41.047 -15.976  1.00 10.70           C  
ATOM    143  OD1 ASN A  20     -43.946 -42.169 -15.700  1.00 29.62           O  
ATOM    144  ND2 ASN A  20     -44.169 -39.988 -15.212  1.00 19.58           N  
ATOM    145  N   LYS A  21     -48.330 -38.963 -18.062  1.00  6.27           N  
ATOM    146  CA  LYS A  21     -49.167 -38.574 -19.161  1.00 13.36           C  
ATOM    147  C   LYS A  21     -48.469 -37.748 -20.259  1.00 14.55           C  
ATOM    148  O   LYS A  21     -48.639 -38.034 -21.420  1.00 15.39           O  
ATOM    149  CB  LYS A  21     -50.366 -37.867 -18.536  1.00 16.77           C  
ATOM    150  CG  LYS A  21     -51.327 -37.313 -19.546  1.00 24.95           C  
ATOM    151  CD  LYS A  21     -52.231 -36.219 -19.034  1.00 40.42           C  
ATOM    152  CE  LYS A  21     -53.128 -35.732 -20.167  1.00 68.16           C  
ATOM    153  NZ  LYS A  21     -53.782 -34.454 -19.873  0.00 47.17           N  
ATOM    154  N   ASN A  22     -47.645 -36.736 -19.910  1.00 15.78           N  
ATOM    155  CA  ASN A  22     -46.951 -35.935 -20.899  1.00 11.73           C  
ATOM    156  C   ASN A  22     -46.031 -36.800 -21.740  1.00 14.60           C  
ATOM    157  O   ASN A  22     -46.133 -36.860 -22.937  1.00 12.03           O  
ATOM    158  CB  ASN A  22     -46.098 -34.901 -20.180  1.00 10.58           C  
ATOM    159  CG  ASN A  22     -46.907 -33.781 -19.568  1.00 20.00           C  
ATOM    160  OD1 ASN A  22     -46.348 -32.991 -18.817  1.00 35.61           O  
ATOM    161  ND2 ASN A  22     -48.193 -33.673 -19.889  1.00 13.12           N  
ATOM    162  N   ALA A  23     -45.069 -37.454 -21.106  1.00 11.61           N  
ATOM    163  CA  ALA A  23     -44.123 -38.271 -21.860  1.00  6.69           C  
ATOM    164  C   ALA A  23     -44.723 -39.444 -22.585  1.00 12.83           C  
ATOM    165  O   ALA A  23     -44.240 -39.758 -23.670  1.00 13.25           O  
ATOM    166  CB  ALA A  23     -42.955 -38.810 -21.041  1.00  5.70           C  
ATOM    167  N   ASN A  24     -45.715 -40.107 -21.962  1.00  5.18           N  
ATOM    168  CA  ASN A  24     -46.342 -41.267 -22.576  1.00 11.99           C  
ATOM    169  C   ASN A  24     -47.319 -40.890 -23.658  1.00 13.70           C  
ATOM    170  O   ASN A  24     -47.403 -41.605 -24.666  1.00 10.31           O  
ATOM    171  CB  ASN A  24     -46.978 -42.207 -21.572  1.00  9.02           C  
ATOM    172  CG  ASN A  24     -45.931 -42.878 -20.744  1.00 24.41           C  
ATOM    173  OD1 ASN A  24     -46.140 -43.285 -19.584  1.00 19.37           O  
ATOM    174  ND2 ASN A  24     -44.813 -43.020 -21.348  1.00  6.51           N  
ATOM    175  N   GLY A  25     -48.045 -39.785 -23.444  1.00  9.70           N  
ATOM    176  CA  GLY A  25     -48.968 -39.353 -24.476  1.00 12.25           C  
ATOM    177  C   GLY A  25     -48.219 -38.983 -25.770  1.00 11.53           C  
ATOM    178  O   GLY A  25     -48.672 -39.313 -26.852  1.00  9.74           O  
ATOM    179  N   LEU A  26     -47.067 -38.276 -25.670  1.00 10.87           N  
ATOM    180  CA  LEU A  26     -46.260 -37.878 -26.818  1.00  5.19           C  
ATOM    181  C   LEU A  26     -45.781 -39.171 -27.489  1.00  8.22           C  
ATOM    182  O   LEU A  26     -45.875 -39.353 -28.704  1.00 13.93           O  
ATOM    183  CB  LEU A  26     -45.042 -37.064 -26.342  1.00  6.62           C  
ATOM    184  CG  LEU A  26     -45.266 -35.565 -26.407  1.00 12.92           C  
ATOM    185  CD1 LEU A  26     -46.598 -35.125 -25.911  1.00  4.00           C  
ATOM    186  CD2 LEU A  26     -44.299 -34.872 -25.523  1.00  4.80           C  
ATOM    187  N   ASP A  27     -45.290 -40.090 -26.678  1.00  4.60           N  
ATOM    188  CA  ASP A  27     -44.819 -41.386 -27.183  1.00 12.98           C  
ATOM    189  C   ASP A  27     -45.830 -42.201 -27.994  1.00 13.43           C  
ATOM    190  O   ASP A  27     -45.490 -42.835 -28.987  1.00  9.91           O  
ATOM    191  CB  ASP A  27     -44.244 -42.274 -26.048  1.00 12.90           C  
ATOM    192  CG  ASP A  27     -42.783 -42.015 -25.775  0.00 14.00           C  
ATOM    193  OD1 ASP A  27     -42.059 -41.927 -26.865  0.00 14.90           O  
ATOM    194  OD2 ASP A  27     -42.325 -41.890 -24.653  0.00 14.90           O  
ATOM    195  N   PHE A  28     -47.081 -42.235 -27.546  1.00  5.15           N  
ATOM    196  CA  PHE A  28     -48.118 -42.981 -28.225  1.00  4.00           C  
ATOM    197  C   PHE A  28     -48.321 -42.398 -29.617  1.00  9.17           C  
ATOM    198  O   PHE A  28     -48.444 -43.106 -30.603  1.00 11.47           O  
ATOM    199  CB  PHE A  28     -49.442 -42.888 -27.415  1.00 10.18           C  
ATOM    200  CG  PHE A  28     -50.675 -43.268 -28.209  1.00 28.89           C  
ATOM    201  CD1 PHE A  28     -50.861 -44.610 -28.555  1.00 23.75           C  
ATOM    202  CD2 PHE A  28     -51.629 -42.330 -28.624  1.00  7.91           C  
ATOM    203  CE1 PHE A  28     -51.956 -45.054 -29.307  1.00 13.31           C  
ATOM    204  CE2 PHE A  28     -52.726 -42.766 -29.378  1.00 18.62           C  
ATOM    205  CZ  PHE A  28     -52.906 -44.118 -29.700  1.00 14.60           C  
ATOM    206  N   LEU A  29     -48.367 -41.066 -29.700  1.00  6.85           N  
ATOM    207  CA  LEU A  29     -48.598 -40.335 -30.936  1.00  8.75           C  
ATOM    208  C   LEU A  29     -47.479 -40.603 -31.905  1.00 17.93           C  
ATOM    209  O   LEU A  29     -47.766 -40.957 -33.037  1.00 19.64           O  
ATOM    210  CB  LEU A  29     -49.005 -38.850 -30.709  1.00 11.76           C  
ATOM    211  CG  LEU A  29     -50.010 -38.371 -31.737  1.00 26.47           C  
ATOM    212  CD1 LEU A  29     -51.273 -39.194 -31.714  1.00 13.97           C  
ATOM    213  CD2 LEU A  29     -50.231 -36.872 -31.618  1.00 15.29           C  
ATOM    214  N   VAL A  30     -46.214 -40.520 -31.437  1.00  7.72           N  
ATOM    215  CA  VAL A  30     -45.039 -40.814 -32.216  1.00  4.00           C  
ATOM    216  C   VAL A  30     -45.042 -42.261 -32.734  1.00  8.46           C  
ATOM    217  O   VAL A  30     -44.828 -42.526 -33.897  1.00 14.19           O  
ATOM    218  CB  VAL A  30     -43.750 -40.460 -31.480  1.00 14.18           C  
ATOM    219  CG1 VAL A  30     -42.616 -41.060 -32.273  1.00 16.44           C  
ATOM    220  CG2 VAL A  30     -43.559 -38.962 -31.427  1.00 12.35           C  
ATOM    221  N   ALA A  31     -45.294 -43.235 -31.866  1.00 14.41           N  
ATOM    222  CA  ALA A  31     -45.371 -44.639 -32.238  1.00 13.60           C  
ATOM    223  C   ALA A  31     -46.455 -44.858 -33.358  1.00 27.00           C  
ATOM    224  O   ALA A  31     -46.282 -45.632 -34.324  1.00 14.39           O  
ATOM    225  CB  ALA A  31     -45.668 -45.434 -30.963  1.00 10.97           C  
ATOM    226  N   LEU A  32     -47.623 -44.173 -33.255  1.00 13.97           N  
ATOM    227  CA  LEU A  32     -48.716 -44.321 -34.202  1.00 14.05           C  
ATOM    228  C   LEU A  32     -48.198 -43.889 -35.543  1.00 21.57           C  
ATOM    229  O   LEU A  32     -48.282 -44.570 -36.579  1.00 14.38           O  
ATOM    230  CB  LEU A  32     -49.922 -43.451 -33.799  1.00 13.82           C  
ATOM    231  CG  LEU A  32     -51.129 -43.657 -34.707  1.00 10.41           C  
ATOM    232  CD1 LEU A  32     -51.711 -45.072 -34.546  1.00 13.90           C  
ATOM    233  CD2 LEU A  32     -52.178 -42.606 -34.434  1.00 11.37           C  
ATOM    234  N   PHE A  33     -47.628 -42.692 -35.523  1.00 20.26           N  
ATOM    235  CA  PHE A  33     -47.103 -42.115 -36.757  1.00 19.06           C  
ATOM    236  C   PHE A  33     -46.011 -42.930 -37.392  1.00 16.38           C  
ATOM    237  O   PHE A  33     -45.840 -43.012 -38.627  1.00 21.32           O  
ATOM    238  CB  PHE A  33     -46.668 -40.675 -36.561  1.00 18.91           C  
ATOM    239  CG  PHE A  33     -47.840 -39.770 -36.248  1.00 13.78           C  
ATOM    240  CD1 PHE A  33     -49.180 -40.065 -36.528  1.00 28.55           C  
ATOM    241  CD2 PHE A  33     -47.557 -38.550 -35.640  1.00 11.02           C  
ATOM    242  CE1 PHE A  33     -50.186 -39.150 -36.201  1.00 38.27           C  
ATOM    243  CE2 PHE A  33     -48.545 -37.622 -35.312  1.00 20.32           C  
ATOM    244  CZ  PHE A  33     -49.871 -37.929 -35.605  1.00 22.21           C  
ATOM    245  N   GLU A  34     -45.259 -43.576 -36.542  1.00 12.76           N  
ATOM    246  CA  GLU A  34     -44.205 -44.413 -37.088  1.00 15.29           C  
ATOM    247  C   GLU A  34     -44.729 -45.686 -37.719  1.00 35.13           C  
ATOM    248  O   GLU A  34     -44.258 -46.111 -38.764  1.00 23.65           O  
ATOM    249  CB  GLU A  34     -43.170 -44.815 -36.026  1.00 37.00           C  
ATOM    250  CG  GLU A  34     -42.465 -43.630 -35.365  1.00 31.08           C  
ATOM    251  CD  GLU A  34     -41.345 -44.091 -34.480  1.00 80.00           C  
ATOM    252  OE1 GLU A  34     -41.705 -45.029 -33.634  1.00 33.14           O  
ATOM    253  OE2 GLU A  34     -40.224 -43.642 -34.568  1.00 38.33           O  
ATOM    254  N   LYS A  35     -45.687 -46.305 -37.056  1.00 19.69           N  
ATOM    255  CA  LYS A  35     -46.246 -47.555 -37.541  1.00 13.48           C  
ATOM    256  C   LYS A  35     -47.308 -47.383 -38.634  1.00 31.12           C  
ATOM    257  O   LYS A  35     -47.561 -48.251 -39.482  1.00 12.65           O  
ATOM    258  CB  LYS A  35     -46.863 -48.310 -36.392  1.00 20.05           C  
ATOM    259  CG  LYS A  35     -45.889 -48.775 -35.326  1.00 32.96           C  
ATOM    260  CD  LYS A  35     -46.626 -49.313 -34.110  0.00 18.29           C  
ATOM    261  CE  LYS A  35     -45.822 -50.320 -33.305  0.00 20.67           C  
ATOM    262  NZ  LYS A  35     -46.346 -51.689 -33.410  0.00 37.40           N  
ATOM    263  N   PHE A  36     -47.959 -46.246 -38.615  1.00 13.43           N  
ATOM    264  CA  PHE A  36     -48.998 -46.010 -39.584  1.00 13.86           C  
ATOM    265  C   PHE A  36     -48.818 -44.594 -40.069  1.00 17.12           C  
ATOM    266  O   PHE A  36     -49.500 -43.705 -39.620  1.00 23.86           O  
ATOM    267  CB  PHE A  36     -50.393 -46.274 -38.940  1.00 17.71           C  
ATOM    268  CG  PHE A  36     -50.476 -47.699 -38.404  1.00 14.95           C  
ATOM    269  CD1 PHE A  36     -50.867 -48.752 -39.225  1.00 25.92           C  
ATOM    270  CD2 PHE A  36     -50.139 -48.006 -37.087  1.00 14.50           C  
ATOM    271  CE1 PHE A  36     -50.965 -50.068 -38.782  1.00 28.43           C  
ATOM    272  CE2 PHE A  36     -50.236 -49.316 -36.619  1.00 16.47           C  
ATOM    273  CZ  PHE A  36     -50.635 -50.345 -37.459  1.00 22.44           C  
ATOM    274  N   PRO A  37     -47.881 -44.401 -40.983  1.00 22.90           N  
ATOM    275  CA  PRO A  37     -47.513 -43.125 -41.573  1.00 26.09           C  
ATOM    276  C   PRO A  37     -48.634 -42.298 -42.134  1.00 10.83           C  
ATOM    277  O   PRO A  37     -48.594 -41.068 -42.029  1.00 24.17           O  
ATOM    278  CB  PRO A  37     -46.474 -43.408 -42.644  1.00 33.46           C  
ATOM    279  CG  PRO A  37     -46.189 -44.906 -42.589  1.00 42.00           C  
ATOM    280  CD  PRO A  37     -47.041 -45.506 -41.494  1.00 24.56           C  
ATOM    281  N   ASP A  38     -49.653 -42.945 -42.724  1.00 20.12           N  
ATOM    282  CA  ASP A  38     -50.789 -42.221 -43.278  1.00 23.93           C  
ATOM    283  C   ASP A  38     -51.566 -41.420 -42.229  1.00 31.39           C  
ATOM    284  O   ASP A  38     -52.278 -40.430 -42.481  1.00 23.66           O  
ATOM    285  CB  ASP A  38     -51.802 -43.194 -43.963  1.00 27.60           C  
ATOM    286  CG  ASP A  38     -52.349 -44.323 -43.081  1.00 12.07           C  
ATOM    287  OD1 ASP A  38     -51.636 -45.144 -42.515  1.00 28.32           O  
ATOM    288  OD2 ASP A  38     -53.657 -44.433 -43.086  1.00 37.87           O  
ATOM    289  N   SER A  39     -51.473 -41.869 -40.991  1.00 12.76           N  
ATOM    290  CA  SER A  39     -52.248 -41.186 -39.948  1.00 12.84           C  
ATOM    291  C   SER A  39     -51.972 -39.744 -39.734  1.00 10.74           C  
ATOM    292  O   SER A  39     -52.848 -38.977 -39.407  1.00 14.45           O  
ATOM    293  CB  SER A  39     -52.376 -41.909 -38.634  1.00 10.10           C  
ATOM    294  OG  SER A  39     -51.142 -42.482 -38.266  1.00 44.64           O  
ATOM    295  N   ALA A  40     -50.738 -39.354 -39.925  1.00 15.46           N  
ATOM    296  CA  ALA A  40     -50.399 -37.978 -39.701  1.00 14.88           C  
ATOM    297  C   ALA A  40     -51.022 -36.972 -40.625  1.00 26.61           C  
ATOM    298  O   ALA A  40     -51.148 -35.772 -40.314  1.00 22.67           O  
ATOM    299  CB  ALA A  40     -48.889 -37.845 -39.695  1.00 28.45           C  
ATOM    300  N   ASN A  41     -51.359 -37.501 -41.786  1.00 24.60           N  
ATOM    301  CA  ASN A  41     -51.953 -36.750 -42.869  1.00 18.99           C  
ATOM    302  C   ASN A  41     -53.325 -36.244 -42.543  1.00 18.40           C  
ATOM    303  O   ASN A  41     -53.795 -35.333 -43.238  1.00 28.07           O  
ATOM    304  CB  ASN A  41     -51.940 -37.547 -44.177  1.00 34.05           C  
ATOM    305  CG  ASN A  41     -50.546 -37.579 -44.784  1.00 76.29           C  
ATOM    306  OD1 ASN A  41     -49.609 -36.900 -44.314  1.00 52.23           O  
ATOM    307  ND2 ASN A  41     -50.417 -38.372 -45.844  1.00 80.00           N  
ATOM    308  N   PHE A  42     -53.962 -36.804 -41.471  1.00 12.65           N  
ATOM    309  CA  PHE A  42     -55.318 -36.363 -41.082  1.00  5.76           C  
ATOM    310  C   PHE A  42     -55.255 -35.140 -40.237  1.00 18.57           C  
ATOM    311  O   PHE A  42     -56.244 -34.419 -40.103  1.00 22.76           O  
ATOM    312  CB  PHE A  42     -55.992 -37.469 -40.283  1.00 19.78           C  
ATOM    313  CG  PHE A  42     -56.424 -38.646 -41.124  1.00 21.32           C  
ATOM    314  CD1 PHE A  42     -57.652 -38.650 -41.795  1.00 17.84           C  
ATOM    315  CD2 PHE A  42     -55.583 -39.750 -41.232  1.00 14.68           C  
ATOM    316  CE1 PHE A  42     -58.060 -39.749 -42.547  1.00 14.54           C  
ATOM    317  CE2 PHE A  42     -55.968 -40.852 -41.999  1.00 26.90           C  
ATOM    318  CZ  PHE A  42     -57.199 -40.844 -42.655  1.00 17.70           C  
ATOM    319  N   PHE A  43     -54.067 -34.941 -39.691  1.00 14.70           N  
ATOM    320  CA  PHE A  43     -53.800 -33.820 -38.842  1.00 22.86           C  
ATOM    321  C   PHE A  43     -53.316 -32.612 -39.619  1.00 17.02           C  
ATOM    322  O   PHE A  43     -52.332 -32.620 -40.338  1.00 24.32           O  
ATOM    323  CB  PHE A  43     -52.785 -34.143 -37.721  1.00 49.07           C  
ATOM    324  CG  PHE A  43     -53.276 -35.096 -36.665  1.00 11.75           C  
ATOM    325  CD1 PHE A  43     -53.193 -36.475 -36.854  1.00 17.04           C  
ATOM    326  CD2 PHE A  43     -53.859 -34.614 -35.499  1.00  9.05           C  
ATOM    327  CE1 PHE A  43     -53.628 -37.380 -35.901  1.00 29.37           C  
ATOM    328  CE2 PHE A  43     -54.332 -35.508 -34.545  1.00 17.14           C  
ATOM    329  CZ  PHE A  43     -54.211 -36.880 -34.731  1.00 27.97           C  
ATOM    330  N   ALA A  44     -54.045 -31.544 -39.428  1.00 21.92           N  
ATOM    331  CA  ALA A  44     -53.738 -30.305 -40.046  1.00 41.81           C  
ATOM    332  C   ALA A  44     -52.315 -29.923 -39.706  1.00 29.68           C  
ATOM    333  O   ALA A  44     -51.492 -29.621 -40.558  1.00 41.40           O  
ATOM    334  CB  ALA A  44     -54.696 -29.292 -39.436  1.00 31.10           C  
ATOM    335  N   ASP A  45     -52.016 -29.983 -38.426  1.00 15.05           N  
ATOM    336  CA  ASP A  45     -50.710 -29.594 -37.926  1.00 22.87           C  
ATOM    337  C   ASP A  45     -49.530 -30.442 -38.308  1.00 38.34           C  
ATOM    338  O   ASP A  45     -48.422 -29.952 -38.245  1.00 34.34           O  
ATOM    339  CB  ASP A  45     -50.712 -29.467 -36.383  1.00 27.80           C  
ATOM    340  CG  ASP A  45     -51.776 -28.598 -35.720  1.00 69.36           C  
ATOM    341  OD1 ASP A  45     -51.754 -27.329 -36.040  1.00 31.76           O  
ATOM    342  OD2 ASP A  45     -52.570 -29.028 -34.908  1.00 36.59           O  
ATOM    343  N   PHE A  46     -49.758 -31.704 -38.680  1.00 18.47           N  
ATOM    344  CA  PHE A  46     -48.689 -32.645 -38.999  1.00 16.55           C  
ATOM    345  C   PHE A  46     -48.618 -33.181 -40.421  1.00 20.69           C  
ATOM    346  O   PHE A  46     -47.663 -33.919 -40.714  1.00 20.33           O  
ATOM    347  CB  PHE A  46     -48.829 -33.880 -38.096  1.00 17.88           C  
ATOM    348  CG  PHE A  46     -48.951 -33.522 -36.624  1.00 29.66           C  
ATOM    349  CD1 PHE A  46     -48.182 -32.488 -36.085  1.00 14.87           C  
ATOM    350  CD2 PHE A  46     -49.818 -34.243 -35.802  1.00 25.03           C  
ATOM    351  CE1 PHE A  46     -48.270 -32.159 -34.728  1.00 15.44           C  
ATOM    352  CE2 PHE A  46     -49.911 -33.924 -34.449  1.00 15.73           C  
ATOM    353  CZ  PHE A  46     -49.160 -32.876 -33.929  1.00 18.77           C  
ATOM    354  N   LYS A  47     -49.601 -32.853 -41.269  1.00 30.59           N  
ATOM    355  CA  LYS A  47     -49.624 -33.334 -42.648  1.00 34.67           C  
ATOM    356  C   LYS A  47     -48.346 -32.990 -43.371  1.00 13.52           C  
ATOM    357  O   LYS A  47     -47.912 -31.824 -43.361  1.00 35.60           O  
ATOM    358  CB  LYS A  47     -50.814 -32.764 -43.397  1.00 18.34           C  
ATOM    359  CG  LYS A  47     -50.999 -33.347 -44.788  0.00 15.26           C  
ATOM    360  CD  LYS A  47     -52.203 -32.751 -45.500  0.00 15.05           C  
ATOM    361  CE  LYS A  47     -52.297 -33.125 -46.970  0.00 15.00           C  
ATOM    362  NZ  LYS A  47     -53.449 -32.504 -47.640  0.00 15.00           N  
ATOM    363  N   GLY A  48     -47.692 -33.961 -43.988  1.00 28.44           N  
ATOM    364  CA  GLY A  48     -46.454 -33.616 -44.690  1.00 27.05           C  
ATOM    365  C   GLY A  48     -45.134 -33.704 -43.909  1.00 40.69           C  
ATOM    366  O   GLY A  48     -44.025 -33.967 -44.402  1.00 35.25           O  
ATOM    367  N   LYS A  49     -45.229 -33.514 -42.636  1.00 19.02           N  
ATOM    368  CA  LYS A  49     -44.062 -33.559 -41.807  1.00 15.38           C  
ATOM    369  C   LYS A  49     -43.624 -34.949 -41.506  1.00 15.10           C  
ATOM    370  O   LYS A  49     -44.469 -35.849 -41.463  1.00 25.79           O  
ATOM    371  CB  LYS A  49     -44.480 -32.985 -40.479  1.00 18.16           C  
ATOM    372  CG  LYS A  49     -45.018 -31.583 -40.593  1.00 17.69           C  
ATOM    373  CD  LYS A  49     -45.462 -31.049 -39.264  1.00 38.74           C  
ATOM    374  CE  LYS A  49     -45.382 -29.546 -39.162  0.00 18.39           C  
ATOM    375  NZ  LYS A  49     -45.602 -29.085 -37.784  0.00 15.40           N  
ATOM    376  N   SER A  50     -42.302 -35.076 -41.219  1.00 13.41           N  
ATOM    377  CA  SER A  50     -41.680 -36.351 -40.904  1.00 19.35           C  
ATOM    378  C   SER A  50     -41.832 -36.609 -39.406  1.00 20.49           C  
ATOM    379  O   SER A  50     -42.192 -35.703 -38.644  1.00 15.85           O  
ATOM    380  CB  SER A  50     -40.188 -36.211 -41.195  1.00 24.35           C  
ATOM    381  OG  SER A  50     -39.678 -35.199 -40.356  1.00 18.70           O  
ATOM    382  N   VAL A  51     -41.506 -37.808 -38.930  1.00 19.55           N  
ATOM    383  CA  VAL A  51     -41.599 -38.044 -37.488  1.00 19.35           C  
ATOM    384  C   VAL A  51     -40.706 -37.102 -36.660  1.00 13.78           C  
ATOM    385  O   VAL A  51     -41.129 -36.598 -35.613  1.00 17.79           O  
ATOM    386  CB  VAL A  51     -41.459 -39.502 -37.079  1.00 18.69           C  
ATOM    387  CG1 VAL A  51     -41.307 -39.569 -35.568  1.00 42.28           C  
ATOM    388  CG2 VAL A  51     -42.745 -40.218 -37.486  1.00 15.34           C  
ATOM    389  N   ALA A  52     -39.474 -36.831 -37.114  1.00  9.11           N  
ATOM    390  CA  ALA A  52     -38.542 -35.900 -36.435  1.00 18.21           C  
ATOM    391  C   ALA A  52     -39.164 -34.514 -36.365  1.00 13.43           C  
ATOM    392  O   ALA A  52     -39.142 -33.867 -35.319  1.00 10.52           O  
ATOM    393  CB  ALA A  52     -37.174 -35.792 -37.098  1.00 15.69           C  
ATOM    394  N   ASP A  53     -39.788 -34.079 -37.464  1.00  6.98           N  
ATOM    395  CA  ASP A  53     -40.441 -32.790 -37.464  1.00  8.78           C  
ATOM    396  C   ASP A  53     -41.540 -32.755 -36.441  1.00 13.67           C  
ATOM    397  O   ASP A  53     -41.720 -31.738 -35.783  1.00 15.15           O  
ATOM    398  CB  ASP A  53     -41.131 -32.448 -38.804  1.00 13.28           C  
ATOM    399  CG  ASP A  53     -40.196 -32.151 -39.936  1.00 26.67           C  
ATOM    400  OD1 ASP A  53     -39.195 -31.336 -39.624  1.00 16.07           O  
ATOM    401  OD2 ASP A  53     -40.423 -32.635 -41.030  1.00 34.88           O  
ATOM    402  N   ILE A  54     -42.306 -33.841 -36.366  1.00 18.90           N  
ATOM    403  CA  ILE A  54     -43.443 -33.967 -35.421  1.00 15.32           C  
ATOM    404  C   ILE A  54     -42.879 -33.967 -34.003  1.00  8.14           C  
ATOM    405  O   ILE A  54     -43.381 -33.252 -33.121  1.00 15.91           O  
ATOM    406  CB  ILE A  54     -44.413 -35.149 -35.733  1.00  8.01           C  
ATOM    407  CG1 ILE A  54     -45.191 -34.906 -37.047  1.00 11.74           C  
ATOM    408  CG2 ILE A  54     -45.480 -35.385 -34.663  1.00  8.33           C  
ATOM    409  CD1 ILE A  54     -45.750 -36.229 -37.571  1.00 22.15           C  
ATOM    410  N   LYS A  55     -41.823 -34.751 -33.774  1.00 10.46           N  
ATOM    411  CA  LYS A  55     -41.286 -34.746 -32.438  1.00 13.33           C  
ATOM    412  C   LYS A  55     -40.854 -33.352 -31.991  1.00 15.28           C  
ATOM    413  O   LYS A  55     -41.008 -32.989 -30.828  1.00 28.37           O  
ATOM    414  CB  LYS A  55     -40.088 -35.677 -32.240  1.00  8.79           C  
ATOM    415  CG  LYS A  55     -40.316 -37.067 -32.695  1.00 19.03           C  
ATOM    416  CD  LYS A  55     -39.382 -38.011 -31.992  1.00 20.94           C  
ATOM    417  CE  LYS A  55     -38.296 -38.567 -32.876  1.00 57.94           C  
ATOM    418  NZ  LYS A  55     -37.395 -39.461 -32.135  0.00 17.43           N  
ATOM    419  N   ALA A  56     -40.294 -32.570 -32.917  1.00 18.41           N  
ATOM    420  CA  ALA A  56     -39.774 -31.254 -32.652  1.00 13.88           C  
ATOM    421  C   ALA A  56     -40.856 -30.195 -32.585  1.00 12.01           C  
ATOM    422  O   ALA A  56     -40.652 -29.070 -32.214  1.00 22.33           O  
ATOM    423  CB  ALA A  56     -38.744 -30.921 -33.730  1.00 25.97           C  
ATOM    424  N   SER A  57     -42.073 -30.565 -32.918  1.00 11.84           N  
ATOM    425  CA  SER A  57     -43.156 -29.590 -32.919  1.00 17.35           C  
ATOM    426  C   SER A  57     -43.700 -29.143 -31.560  1.00 22.88           C  
ATOM    427  O   SER A  57     -44.042 -29.956 -30.673  1.00 14.24           O  
ATOM    428  CB  SER A  57     -44.325 -30.195 -33.679  1.00  8.75           C  
ATOM    429  OG  SER A  57     -45.420 -29.277 -33.637  1.00 20.67           O  
ATOM    430  N   PRO A  58     -43.841 -27.829 -31.429  1.00 14.01           N  
ATOM    431  CA  PRO A  58     -44.381 -27.258 -30.222  1.00 13.90           C  
ATOM    432  C   PRO A  58     -45.877 -27.540 -30.133  1.00 20.81           C  
ATOM    433  O   PRO A  58     -46.528 -27.252 -29.135  1.00 28.90           O  
ATOM    434  CB  PRO A  58     -44.256 -25.744 -30.360  1.00 23.52           C  
ATOM    435  CG  PRO A  58     -43.709 -25.464 -31.743  1.00 23.60           C  
ATOM    436  CD  PRO A  58     -43.237 -26.792 -32.300  1.00 20.79           C  
ATOM    437  N   LYS A  59     -46.435 -28.118 -31.186  1.00 14.10           N  
ATOM    438  CA  LYS A  59     -47.858 -28.447 -31.178  1.00 10.53           C  
ATOM    439  C   LYS A  59     -48.165 -29.874 -30.690  1.00 13.54           C  
ATOM    440  O   LYS A  59     -49.292 -30.220 -30.425  1.00 23.72           O  
ATOM    441  CB  LYS A  59     -48.427 -28.420 -32.585  1.00 16.58           C  
ATOM    442  CG  LYS A  59     -48.191 -27.080 -33.273  1.00 20.33           C  
ATOM    443  CD  LYS A  59     -49.152 -26.890 -34.449  1.00 29.13           C  
ATOM    444  CE  LYS A  59     -48.967 -25.587 -35.230  1.00 43.62           C  
ATOM    445  NZ  LYS A  59     -49.946 -25.424 -36.314  1.00 43.68           N  
ATOM    446  N   LEU A  60     -47.162 -30.717 -30.580  1.00  6.26           N  
ATOM    447  CA  LEU A  60     -47.269 -32.121 -30.243  1.00  6.76           C  
ATOM    448  C   LEU A  60     -47.949 -32.402 -28.948  1.00  9.78           C  
ATOM    449  O   LEU A  60     -48.807 -33.266 -28.895  1.00 13.64           O  
ATOM    450  CB  LEU A  60     -45.904 -32.901 -30.355  1.00  6.34           C  
ATOM    451  CG  LEU A  60     -45.985 -34.394 -30.013  1.00  9.09           C  
ATOM    452  CD1 LEU A  60     -46.795 -35.268 -30.944  1.00 11.65           C  
ATOM    453  CD2 LEU A  60     -44.572 -34.943 -29.943  1.00 16.89           C  
ATOM    454  N   ARG A  61     -47.527 -31.643 -27.940  1.00 10.86           N  
ATOM    455  CA  ARG A  61     -48.069 -31.786 -26.593  1.00 10.55           C  
ATOM    456  C   ARG A  61     -49.551 -31.477 -26.453  1.00 20.06           C  
ATOM    457  O   ARG A  61     -50.236 -32.172 -25.698  1.00 22.14           O  
ATOM    458  CB  ARG A  61     -47.231 -31.110 -25.551  1.00  7.82           C  
ATOM    459  CG  ARG A  61     -47.863 -31.150 -24.168  1.00  8.47           C  
ATOM    460  CD  ARG A  61     -47.679 -32.530 -23.512  1.00 15.29           C  
ATOM    461  NE  ARG A  61     -46.334 -33.035 -23.772  1.00 14.35           N  
ATOM    462  CZ  ARG A  61     -45.247 -32.629 -23.107  1.00 22.23           C  
ATOM    463  NH1 ARG A  61     -45.309 -31.743 -22.122  1.00 10.11           N  
ATOM    464  NH2 ARG A  61     -44.093 -33.159 -23.450  1.00 11.74           N  
ATOM    465  N   ASP A  62     -50.005 -30.443 -27.151  1.00 13.91           N  
ATOM    466  CA  ASP A  62     -51.410 -30.103 -27.144  1.00 15.00           C  
ATOM    467  C   ASP A  62     -52.222 -31.309 -27.686  1.00 14.83           C  
ATOM    468  O   ASP A  62     -53.238 -31.722 -27.123  1.00 16.53           O  
ATOM    469  CB  ASP A  62     -51.711 -28.842 -28.004  1.00 22.41           C  
ATOM    470  CG  ASP A  62     -51.821 -27.589 -27.166  1.00 30.21           C  
ATOM    471  OD1 ASP A  62     -50.949 -27.541 -26.193  1.00 46.32           O  
ATOM    472  OD2 ASP A  62     -52.656 -26.734 -27.347  1.00 64.05           O  
ATOM    473  N   VAL A  63     -51.771 -31.882 -28.800  1.00  9.35           N  
ATOM    474  CA  VAL A  63     -52.449 -32.998 -29.425  1.00 10.39           C  
ATOM    475  C   VAL A  63     -52.467 -34.260 -28.577  1.00 13.80           C  
ATOM    476  O   VAL A  63     -53.497 -34.914 -28.293  1.00 10.01           O  
ATOM    477  CB  VAL A  63     -51.861 -33.253 -30.852  1.00  7.74           C  
ATOM    478  CG1 VAL A  63     -52.730 -34.255 -31.580  1.00 11.87           C  
ATOM    479  CG2 VAL A  63     -52.013 -31.944 -31.613  1.00  8.81           C  
ATOM    480  N   SER A  64     -51.287 -34.656 -28.188  1.00  6.77           N  
ATOM    481  CA  SER A  64     -51.202 -35.871 -27.410  1.00  7.13           C  
ATOM    482  C   SER A  64     -51.917 -35.788 -26.044  1.00  8.17           C  
ATOM    483  O   SER A  64     -52.420 -36.770 -25.469  1.00 10.36           O  
ATOM    484  CB  SER A  64     -49.740 -36.282 -27.233  1.00 18.27           C  
ATOM    485  OG  SER A  64     -49.195 -35.541 -26.149  1.00 12.66           O  
ATOM    486  N   SER A  65     -51.931 -34.605 -25.470  1.00 14.36           N  
ATOM    487  CA  SER A  65     -52.585 -34.458 -24.192  1.00  7.35           C  
ATOM    488  C   SER A  65     -54.108 -34.558 -24.304  1.00 11.16           C  
ATOM    489  O   SER A  65     -54.794 -35.167 -23.474  1.00 13.51           O  
ATOM    490  CB  SER A  65     -52.112 -33.244 -23.396  1.00 17.53           C  
ATOM    491  OG  SER A  65     -52.406 -32.052 -24.090  1.00 30.11           O  
ATOM    492  N   ARG A  66     -54.663 -33.957 -25.359  1.00 12.85           N  
ATOM    493  CA  ARG A  66     -56.119 -34.067 -25.468  1.00 15.48           C  
ATOM    494  C   ARG A  66     -56.538 -35.512 -25.717  1.00 22.71           C  
ATOM    495  O   ARG A  66     -57.605 -35.987 -25.309  1.00 17.59           O  
ATOM    496  CB  ARG A  66     -56.603 -33.167 -26.600  1.00 21.40           C  
ATOM    497  CG  ARG A  66     -56.564 -33.900 -27.947  0.80 50.57           C  
ATOM    498  CD  ARG A  66     -57.360 -33.170 -29.033  0.80 78.19           C  
ATOM    499  NE  ARG A  66     -56.919 -31.805 -29.180  0.80 44.04           N  
ATOM    500  CZ  ARG A  66     -56.443 -31.273 -30.316  0.80 80.00           C  
ATOM    501  NH1 ARG A  66     -56.396 -31.989 -31.449  0.80 54.56           N  
ATOM    502  NH2 ARG A  66     -56.030 -29.977 -30.334  0.80 44.63           N  
ATOM    503  N   ILE A  67     -55.712 -36.239 -26.432  1.00  9.55           N  
ATOM    504  CA  ILE A  67     -55.976 -37.617 -26.717  1.00  4.00           C  
ATOM    505  C   ILE A  67     -55.942 -38.414 -25.439  1.00 10.97           C  
ATOM    506  O   ILE A  67     -56.833 -39.184 -25.185  1.00  9.01           O  
ATOM    507  CB  ILE A  67     -54.946 -38.255 -27.635  1.00  5.61           C  
ATOM    508  CG1 ILE A  67     -55.191 -37.820 -29.092  1.00 12.54           C  
ATOM    509  CG2 ILE A  67     -54.971 -39.809 -27.546  1.00 19.72           C  
ATOM    510  CD1 ILE A  67     -53.998 -38.124 -30.010  1.00 13.11           C  
ATOM    511  N   PHE A  68     -54.902 -38.260 -24.607  1.00  7.66           N  
ATOM    512  CA  PHE A  68     -54.866 -39.086 -23.405  1.00  5.20           C  
ATOM    513  C   PHE A  68     -55.929 -38.704 -22.417  1.00  9.58           C  
ATOM    514  O   PHE A  68     -56.360 -39.535 -21.626  1.00 15.54           O  
ATOM    515  CB  PHE A  68     -53.481 -38.976 -22.658  1.00  7.92           C  
ATOM    516  CG  PHE A  68     -52.539 -40.109 -23.025  1.00  5.51           C  
ATOM    517  CD1 PHE A  68     -52.603 -40.723 -24.288  1.00  9.28           C  
ATOM    518  CD2 PHE A  68     -51.574 -40.538 -22.119  1.00 12.67           C  
ATOM    519  CE1 PHE A  68     -51.745 -41.756 -24.669  1.00 12.23           C  
ATOM    520  CE2 PHE A  68     -50.701 -41.571 -22.471  1.00 15.90           C  
ATOM    521  CZ  PHE A  68     -50.801 -42.175 -23.730  1.00 15.66           C  
ATOM    522  N   THR A  69     -56.286 -37.430 -22.398  1.00 13.29           N  
ATOM    523  CA  THR A  69     -57.296 -36.980 -21.437  1.00  7.57           C  
ATOM    524  C   THR A  69     -58.588 -37.650 -21.792  1.00 18.46           C  
ATOM    525  O   THR A  69     -59.318 -38.049 -20.894  1.00 13.34           O  
ATOM    526  CB  THR A  69     -57.448 -35.424 -21.490  1.00  8.44           C  
ATOM    527  OG1 THR A  69     -56.253 -34.787 -21.075  1.00  8.62           O  
ATOM    528  CG2 THR A  69     -58.670 -34.890 -20.713  1.00 13.98           C  
ATOM    529  N   ARG A  70     -58.889 -37.750 -23.108  1.00  6.73           N  
ATOM    530  CA  ARG A  70     -60.179 -38.375 -23.474  1.00  5.20           C  
ATOM    531  C   ARG A  70     -60.135 -39.923 -23.278  1.00 12.60           C  
ATOM    532  O   ARG A  70     -61.115 -40.573 -22.884  1.00 11.48           O  
ATOM    533  CB  ARG A  70     -60.591 -37.960 -24.886  1.00  7.92           C  
ATOM    534  CG  ARG A  70     -61.841 -38.658 -25.422  1.00 11.16           C  
ATOM    535  CD  ARG A  70     -63.123 -38.003 -24.889  1.00 11.77           C  
ATOM    536  NE  ARG A  70     -63.059 -36.579 -25.118  1.00 22.42           N  
ATOM    537  CZ  ARG A  70     -63.702 -36.062 -26.156  1.00 22.70           C  
ATOM    538  NH1 ARG A  70     -64.437 -36.828 -26.963  1.00 23.44           N  
ATOM    539  NH2 ARG A  70     -63.621 -34.747 -26.380  1.00 27.47           N  
ATOM    540  N   LEU A  71     -58.978 -40.547 -23.514  1.00  9.74           N  
ATOM    541  CA  LEU A  71     -58.840 -41.987 -23.353  1.00 15.33           C  
ATOM    542  C   LEU A  71     -59.020 -42.377 -21.892  1.00 15.87           C  
ATOM    543  O   LEU A  71     -59.533 -43.442 -21.549  1.00 11.75           O  
ATOM    544  CB  LEU A  71     -57.417 -42.448 -23.767  1.00 18.59           C  
ATOM    545  CG  LEU A  71     -57.345 -43.493 -24.869  1.00 20.29           C  
ATOM    546  CD1 LEU A  71     -56.002 -44.214 -24.813  1.00 74.17           C  
ATOM    547  CD2 LEU A  71     -58.508 -44.443 -24.787  1.00 29.49           C  
ATOM    548  N   ASN A  72     -58.520 -41.503 -21.044  1.00  6.82           N  
ATOM    549  CA  ASN A  72     -58.647 -41.744 -19.611  1.00  6.05           C  
ATOM    550  C   ASN A  72     -60.150 -41.771 -19.261  1.00  4.97           C  
ATOM    551  O   ASN A  72     -60.625 -42.613 -18.489  1.00 14.67           O  
ATOM    552  CB  ASN A  72     -57.952 -40.592 -18.877  1.00  4.72           C  
ATOM    553  CG  ASN A  72     -57.959 -40.832 -17.404  1.00 12.27           C  
ATOM    554  OD1 ASN A  72     -58.529 -40.026 -16.668  1.00 19.79           O  
ATOM    555  ND2 ASN A  72     -57.384 -41.969 -17.023  1.00  8.95           N  
ATOM    556  N   GLU A  73     -60.914 -40.848 -19.838  1.00  5.99           N  
ATOM    557  CA  GLU A  73     -62.360 -40.844 -19.597  1.00  8.58           C  
ATOM    558  C   GLU A  73     -63.043 -42.100 -20.171  1.00  9.65           C  
ATOM    559  O   GLU A  73     -63.999 -42.651 -19.630  1.00 10.89           O  
ATOM    560  CB  GLU A  73     -62.975 -39.531 -20.092  1.00  8.98           C  
ATOM    561  CG  GLU A  73     -62.471 -38.277 -19.346  1.00 17.50           C  
ATOM    562  CD  GLU A  73     -62.591 -38.377 -17.838  1.00 20.07           C  
ATOM    563  OE1 GLU A  73     -63.735 -38.860 -17.406  1.00 26.57           O  
ATOM    564  OE2 GLU A  73     -61.673 -38.082 -17.105  1.00 26.75           O  
ATOM    565  N   PHE A  74     -62.564 -42.630 -21.293  1.00  8.66           N  
ATOM    566  CA  PHE A  74     -63.170 -43.838 -21.832  1.00  9.50           C  
ATOM    567  C   PHE A  74     -62.862 -44.992 -20.912  1.00 11.69           C  
ATOM    568  O   PHE A  74     -63.744 -45.784 -20.668  1.00 14.90           O  
ATOM    569  CB  PHE A  74     -62.607 -44.211 -23.200  1.00  7.57           C  
ATOM    570  CG  PHE A  74     -63.333 -43.582 -24.365  1.00 18.76           C  
ATOM    571  CD1 PHE A  74     -64.663 -43.926 -24.602  1.00 23.55           C  
ATOM    572  CD2 PHE A  74     -62.681 -42.717 -25.245  1.00 27.57           C  
ATOM    573  CE1 PHE A  74     -65.377 -43.389 -25.672  1.00 19.59           C  
ATOM    574  CE2 PHE A  74     -63.379 -42.175 -26.322  1.00 24.01           C  
ATOM    575  CZ  PHE A  74     -64.719 -42.499 -26.520  1.00 52.19           C  
ATOM    576  N   VAL A  75     -61.618 -45.066 -20.383  1.00 12.19           N  
ATOM    577  CA  VAL A  75     -61.221 -46.133 -19.472  1.00  8.40           C  
ATOM    578  C   VAL A  75     -62.079 -46.068 -18.228  1.00 11.85           C  
ATOM    579  O   VAL A  75     -62.552 -47.092 -17.757  1.00 16.06           O  
ATOM    580  CB  VAL A  75     -59.761 -46.162 -19.054  1.00 14.76           C  
ATOM    581  CG1 VAL A  75     -59.587 -47.331 -18.111  1.00 30.14           C  
ATOM    582  CG2 VAL A  75     -58.820 -46.336 -20.235  1.00 11.98           C  
ATOM    583  N   ASN A  76     -62.262 -44.847 -17.730  1.00 11.14           N  
ATOM    584  CA  ASN A  76     -63.070 -44.618 -16.534  1.00 25.06           C  
ATOM    585  C   ASN A  76     -64.536 -44.986 -16.672  1.00 17.23           C  
ATOM    586  O   ASN A  76     -65.172 -45.400 -15.722  1.00 18.56           O  
ATOM    587  CB  ASN A  76     -63.106 -43.130 -16.117  1.00 14.71           C  
ATOM    588  CG  ASN A  76     -61.858 -42.698 -15.371  1.00 80.00           C  
ATOM    589  OD1 ASN A  76     -61.028 -43.530 -15.032  1.00 17.57           O  
ATOM    590  ND2 ASN A  76     -61.706 -41.400 -15.099  1.00 34.95           N  
ATOM    591  N   ASN A  77     -65.131 -44.828 -17.832  1.00 19.62           N  
ATOM    592  CA  ASN A  77     -66.563 -45.104 -17.951  1.00 13.85           C  
ATOM    593  C   ASN A  77     -66.938 -46.354 -18.696  1.00 10.03           C  
ATOM    594  O   ASN A  77     -68.089 -46.683 -18.943  1.00 21.02           O  
ATOM    595  CB  ASN A  77     -67.098 -43.937 -18.768  1.00 11.91           C  
ATOM    596  CG  ASN A  77     -67.045 -42.680 -17.925  1.00 25.09           C  
ATOM    597  OD1 ASN A  77     -67.412 -42.746 -16.745  1.00 25.44           O  
ATOM    598  ND2 ASN A  77     -66.507 -41.605 -18.508  1.00 29.40           N  
ATOM    599  N   ALA A  78     -65.919 -47.064 -19.041  1.00 10.21           N  
ATOM    600  CA  ALA A  78     -66.053 -48.235 -19.842  1.00 16.37           C  
ATOM    601  C   ALA A  78     -67.119 -49.253 -19.541  1.00 11.29           C  
ATOM    602  O   ALA A  78     -67.609 -49.924 -20.459  1.00 23.38           O  
ATOM    603  CB  ALA A  78     -64.692 -48.909 -19.898  1.00 16.48           C  
ATOM    604  N   ALA A  79     -67.403 -49.424 -18.254  1.00 15.90           N  
ATOM    605  CA  ALA A  79     -68.339 -50.433 -17.802  1.00 20.61           C  
ATOM    606  C   ALA A  79     -69.739 -49.913 -17.651  1.00 32.75           C  
ATOM    607  O   ALA A  79     -70.621 -50.582 -17.142  1.00 25.21           O  
ATOM    608  CB  ALA A  79     -67.877 -50.987 -16.477  1.00  7.59           C  
ATOM    609  N   ASN A  80     -69.930 -48.712 -18.105  1.00 19.35           N  
ATOM    610  CA  ASN A  80     -71.227 -48.096 -18.006  1.00 14.12           C  
ATOM    611  C   ASN A  80     -71.712 -47.831 -19.410  1.00 39.76           C  
ATOM    612  O   ASN A  80     -71.317 -46.854 -20.034  1.00 26.57           O  
ATOM    613  CB  ASN A  80     -70.998 -46.768 -17.242  1.00 20.47           C  
ATOM    614  CG  ASN A  80     -72.270 -46.040 -16.917  1.00 21.07           C  
ATOM    615  OD1 ASN A  80     -73.254 -46.153 -17.648  1.00 36.90           O  
ATOM    616  ND2 ASN A  80     -72.218 -45.314 -15.814  1.00 17.68           N  
ATOM    617  N   ALA A  81     -72.547 -48.735 -19.895  1.00 22.46           N  
ATOM    618  CA  ALA A  81     -73.071 -48.659 -21.248  1.00 29.42           C  
ATOM    619  C   ALA A  81     -73.704 -47.345 -21.570  1.00 35.53           C  
ATOM    620  O   ALA A  81     -73.666 -46.873 -22.714  1.00 31.39           O  
ATOM    621  CB  ALA A  81     -73.968 -49.847 -21.635  1.00 20.65           C  
ATOM    622  N   GLY A  82     -74.285 -46.766 -20.551  1.00 21.26           N  
ATOM    623  CA  GLY A  82     -74.945 -45.503 -20.758  1.00 29.52           C  
ATOM    624  C   GLY A  82     -73.978 -44.399 -21.110  1.00 30.33           C  
ATOM    625  O   GLY A  82     -74.192 -43.716 -22.089  1.00 24.04           O  
ATOM    626  N   LYS A  83     -72.929 -44.237 -20.297  1.00 30.71           N  
ATOM    627  CA  LYS A  83     -71.955 -43.187 -20.531  1.00 22.44           C  
ATOM    628  C   LYS A  83     -71.213 -43.449 -21.822  1.00 32.39           C  
ATOM    629  O   LYS A  83     -70.867 -42.539 -22.583  1.00 16.90           O  
ATOM    630  CB  LYS A  83     -70.995 -42.990 -19.369  1.00 16.34           C  
ATOM    631  CG  LYS A  83     -71.593 -42.243 -18.187  1.00 20.30           C  
ATOM    632  CD  LYS A  83     -70.746 -42.429 -16.952  1.00 19.17           C  
ATOM    633  CE  LYS A  83     -71.442 -41.939 -15.702  1.00 30.48           C  
ATOM    634  NZ  LYS A  83     -72.905 -41.900 -15.847  0.00 18.92           N  
ATOM    635  N   MET A  84     -70.962 -44.735 -22.066  1.00 20.33           N  
ATOM    636  CA  MET A  84     -70.271 -45.139 -23.289  1.00 14.10           C  
ATOM    637  C   MET A  84     -71.059 -44.705 -24.491  1.00 27.32           C  
ATOM    638  O   MET A  84     -70.481 -44.209 -25.446  1.00 19.53           O  
ATOM    639  CB  MET A  84     -69.993 -46.654 -23.436  1.00 10.20           C  
ATOM    640  CG  MET A  84     -68.890 -47.086 -22.537  1.00 13.97           C  
ATOM    641  SD  MET A  84     -67.283 -46.306 -22.886  1.00 24.42           S  
ATOM    642  CE  MET A  84     -66.593 -47.588 -23.949  1.00 29.78           C  
ATOM    643  N   SER A  85     -72.363 -44.907 -24.434  1.00 27.22           N  
ATOM    644  CA  SER A  85     -73.230 -44.528 -25.536  1.00 16.55           C  
ATOM    645  C   SER A  85     -72.961 -43.132 -26.065  1.00 21.67           C  
ATOM    646  O   SER A  85     -72.624 -42.941 -27.229  1.00 28.59           O  
ATOM    647  CB  SER A  85     -74.696 -44.635 -25.161  1.00 40.68           C  
ATOM    648  OG  SER A  85     -75.201 -45.783 -25.801  1.00 62.00           O  
ATOM    649  N   ALA A  86     -73.158 -42.185 -25.161  1.00 14.11           N  
ATOM    650  CA  ALA A  86     -72.970 -40.787 -25.395  1.00 28.11           C  
ATOM    651  C   ALA A  86     -71.537 -40.534 -25.788  1.00 28.48           C  
ATOM    652  O   ALA A  86     -71.319 -39.833 -26.750  1.00 27.41           O  
ATOM    653  CB  ALA A  86     -73.347 -39.935 -24.174  1.00 27.65           C  
ATOM    654  N   MET A  87     -70.575 -41.100 -25.054  1.00 15.80           N  
ATOM    655  CA  MET A  87     -69.170 -40.871 -25.323  1.00 10.78           C  
ATOM    656  C   MET A  87     -68.791 -41.338 -26.704  1.00 12.11           C  
ATOM    657  O   MET A  87     -68.115 -40.627 -27.449  1.00 14.53           O  
ATOM    658  CB  MET A  87     -68.267 -41.485 -24.254  1.00 13.14           C  
ATOM    659  CG  MET A  87     -67.866 -40.475 -23.226  1.00 17.15           C  
ATOM    660  SD  MET A  87     -66.637 -41.211 -22.138  1.00 28.85           S  
ATOM    661  CE  MET A  87     -67.654 -42.531 -21.428  1.00 32.22           C  
ATOM    662  N   LEU A  88     -69.242 -42.520 -27.069  1.00  6.50           N  
ATOM    663  CA  LEU A  88     -68.945 -43.048 -28.376  1.00 18.24           C  
ATOM    664  C   LEU A  88     -69.550 -42.215 -29.503  1.00 23.50           C  
ATOM    665  O   LEU A  88     -68.869 -41.944 -30.492  1.00 14.98           O  
ATOM    666  CB  LEU A  88     -69.307 -44.550 -28.494  1.00 17.74           C  
ATOM    667  CG  LEU A  88     -68.430 -45.417 -27.596  1.00 24.74           C  
ATOM    668  CD1 LEU A  88     -69.008 -46.799 -27.388  1.00 20.14           C  
ATOM    669  CD2 LEU A  88     -67.013 -45.589 -28.096  1.00 16.73           C  
ATOM    670  N   SER A  89     -70.818 -41.817 -29.345  1.00 24.17           N  
ATOM    671  CA  SER A  89     -71.509 -41.033 -30.338  1.00 14.88           C  
ATOM    672  C   SER A  89     -70.734 -39.769 -30.618  1.00 12.94           C  
ATOM    673  O   SER A  89     -70.354 -39.501 -31.738  1.00 22.72           O  
ATOM    674  CB  SER A  89     -72.915 -40.684 -29.897  1.00 18.08           C  
ATOM    675  OG  SER A  89     -73.733 -41.747 -30.316  1.00 45.83           O  
ATOM    676  N   GLN A  90     -70.533 -39.027 -29.569  1.00 12.31           N  
ATOM    677  CA  GLN A  90     -69.845 -37.800 -29.657  1.00  7.66           C  
ATOM    678  C   GLN A  90     -68.438 -37.944 -30.213  1.00 11.57           C  
ATOM    679  O   GLN A  90     -68.031 -37.163 -31.041  1.00 16.28           O  
ATOM    680  CB  GLN A  90     -69.906 -37.087 -28.310  1.00  6.42           C  
ATOM    681  CG  GLN A  90     -68.928 -35.889 -28.218  1.00 15.48           C  
ATOM    682  CD  GLN A  90     -69.526 -34.645 -28.869  1.00 24.41           C  
ATOM    683  OE1 GLN A  90     -68.892 -33.580 -28.984  1.00 45.56           O  
ATOM    684  NE2 GLN A  90     -70.737 -34.855 -29.378  1.00 29.88           N  
ATOM    685  N   PHE A  91     -67.702 -38.933 -29.805  1.00 13.47           N  
ATOM    686  CA  PHE A  91     -66.344 -39.104 -30.318  1.00  8.31           C  
ATOM    687  C   PHE A  91     -66.372 -39.399 -31.818  1.00 14.49           C  
ATOM    688  O   PHE A  91     -65.610 -38.825 -32.598  1.00  8.27           O  
ATOM    689  CB  PHE A  91     -65.831 -40.376 -29.635  1.00 11.36           C  
ATOM    690  CG  PHE A  91     -64.397 -40.645 -29.910  1.00  5.32           C  
ATOM    691  CD1 PHE A  91     -63.429 -39.860 -29.290  1.00  9.92           C  
ATOM    692  CD2 PHE A  91     -64.016 -41.657 -30.790  1.00  7.21           C  
ATOM    693  CE1 PHE A  91     -62.074 -40.092 -29.543  1.00 12.13           C  
ATOM    694  CE2 PHE A  91     -62.668 -41.911 -31.066  1.00 13.12           C  
ATOM    695  CZ  PHE A  91     -61.709 -41.127 -30.408  1.00 13.93           C  
ATOM    696  N   ALA A  92     -67.224 -40.371 -32.224  1.00 21.42           N  
ATOM    697  CA  ALA A  92     -67.354 -40.731 -33.635  1.00 20.24           C  
ATOM    698  C   ALA A  92     -67.690 -39.478 -34.484  1.00 18.84           C  
ATOM    699  O   ALA A  92     -67.028 -39.150 -35.465  1.00 13.63           O  
ATOM    700  CB  ALA A  92     -68.320 -41.886 -33.833  1.00 11.31           C  
ATOM    701  N   LYS A  93     -68.748 -38.771 -34.068  1.00 15.02           N  
ATOM    702  CA  LYS A  93     -69.276 -37.559 -34.692  1.00 22.20           C  
ATOM    703  C   LYS A  93     -68.122 -36.603 -34.984  1.00 20.89           C  
ATOM    704  O   LYS A  93     -67.871 -36.113 -36.081  1.00 27.43           O  
ATOM    705  CB  LYS A  93     -70.435 -36.861 -33.928  1.00 15.45           C  
ATOM    706  CG  LYS A  93     -71.754 -37.592 -33.994  1.00 33.01           C  
ATOM    707  CD  LYS A  93     -72.913 -36.871 -33.284  1.00 41.41           C  
ATOM    708  CE  LYS A  93     -74.132 -37.768 -32.909  1.00 35.27           C  
ATOM    709  NZ  LYS A  93     -74.354 -39.021 -33.685  1.00 80.00           N  
ATOM    710  N   GLU A  94     -67.359 -36.346 -33.955  1.00 20.48           N  
ATOM    711  CA  GLU A  94     -66.213 -35.504 -34.051  1.00 15.23           C  
ATOM    712  C   GLU A  94     -65.184 -35.996 -35.041  1.00 16.57           C  
ATOM    713  O   GLU A  94     -64.719 -35.231 -35.880  1.00 21.38           O  
ATOM    714  CB  GLU A  94     -65.509 -35.425 -32.694  1.00 12.07           C  
ATOM    715  CG  GLU A  94     -66.216 -34.440 -31.785  1.00 49.41           C  
ATOM    716  CD  GLU A  94     -65.785 -34.485 -30.355  1.00 73.21           C  
ATOM    717  OE1 GLU A  94     -64.926 -35.230 -29.928  1.00 39.18           O  
ATOM    718  OE2 GLU A  94     -66.447 -33.636 -29.612  1.00 48.19           O  
ATOM    719  N   HIS A  95     -64.792 -37.236 -34.940  1.00 16.25           N  
ATOM    720  CA  HIS A  95     -63.753 -37.738 -35.841  1.00 15.56           C  
ATOM    721  C   HIS A  95     -64.106 -37.832 -37.309  1.00 21.40           C  
ATOM    722  O   HIS A  95     -63.258 -37.639 -38.169  1.00 10.43           O  
ATOM    723  CB  HIS A  95     -63.104 -39.055 -35.324  1.00 24.33           C  
ATOM    724  CG  HIS A  95     -62.135 -38.719 -34.218  1.00 18.05           C  
ATOM    725  ND1 HIS A  95     -62.584 -38.383 -32.956  1.00 15.37           N  
ATOM    726  CD2 HIS A  95     -60.771 -38.636 -34.232  1.00 14.37           C  
ATOM    727  CE1 HIS A  95     -61.491 -38.049 -32.256  1.00 10.40           C  
ATOM    728  NE2 HIS A  95     -60.369 -38.192 -32.959  1.00 11.93           N  
ATOM    729  N   VAL A  96     -65.339 -38.193 -37.573  1.00 13.77           N  
ATOM    730  CA  VAL A  96     -65.834 -38.365 -38.917  1.00 11.52           C  
ATOM    731  C   VAL A  96     -65.728 -37.058 -39.683  1.00 10.42           C  
ATOM    732  O   VAL A  96     -65.359 -37.018 -40.862  1.00 18.57           O  
ATOM    733  CB  VAL A  96     -67.237 -39.014 -38.860  1.00 13.74           C  
ATOM    734  CG1 VAL A  96     -68.045 -38.653 -40.082  1.00 38.11           C  
ATOM    735  CG2 VAL A  96     -67.011 -40.529 -38.854  1.00 14.59           C  
ATOM    736  N   GLY A  97     -66.070 -35.971 -38.999  1.00  8.54           N  
ATOM    737  CA  GLY A  97     -66.033 -34.621 -39.580  1.00 18.89           C  
ATOM    738  C   GLY A  97     -64.625 -34.218 -40.022  1.00 18.71           C  
ATOM    739  O   GLY A  97     -64.366 -33.342 -40.896  1.00 19.06           O  
ATOM    740  N   PHE A  98     -63.669 -34.876 -39.388  1.00 19.65           N  
ATOM    741  CA  PHE A  98     -62.325 -34.575 -39.766  1.00 13.69           C  
ATOM    742  C   PHE A  98     -61.889 -35.561 -40.837  1.00 14.12           C  
ATOM    743  O   PHE A  98     -60.782 -35.515 -41.331  1.00 33.19           O  
ATOM    744  CB  PHE A  98     -61.363 -34.609 -38.560  1.00 13.54           C  
ATOM    745  CG  PHE A  98     -61.748 -33.760 -37.348  1.00 17.25           C  
ATOM    746  CD1 PHE A  98     -62.158 -32.421 -37.495  1.00 33.41           C  
ATOM    747  CD2 PHE A  98     -61.603 -34.255 -36.039  1.00 80.00           C  
ATOM    748  CE1 PHE A  98     -62.466 -31.668 -36.388  1.00 30.31           C  
ATOM    749  CE2 PHE A  98     -61.984 -33.483 -34.904  1.00 24.42           C  
ATOM    750  CZ  PHE A  98     -62.382 -32.187 -35.095  1.00 40.37           C  
ATOM    751  N   GLY A  99     -62.699 -36.543 -41.188  1.00 12.92           N  
ATOM    752  CA  GLY A  99     -62.231 -37.470 -42.214  1.00 15.61           C  
ATOM    753  C   GLY A  99     -61.600 -38.762 -41.714  1.00 24.93           C  
ATOM    754  O   GLY A  99     -61.075 -39.587 -42.446  1.00 21.75           O  
ATOM    755  N   VAL A 100     -61.635 -38.950 -40.420  1.00 17.28           N  
ATOM    756  CA  VAL A 100     -61.073 -40.141 -39.827  1.00 10.27           C  
ATOM    757  C   VAL A 100     -62.182 -41.223 -39.755  1.00 12.64           C  
ATOM    758  O   VAL A 100     -63.352 -40.956 -39.431  1.00 31.97           O  
ATOM    759  CB  VAL A 100     -60.521 -39.812 -38.424  1.00  9.33           C  
ATOM    760  CG1 VAL A 100     -59.639 -40.991 -38.014  1.00 17.55           C  
ATOM    761  CG2 VAL A 100     -59.669 -38.545 -38.431  1.00 10.24           C  
ATOM    762  N   GLY A 101     -61.826 -42.463 -40.089  1.00 10.99           N  
ATOM    763  CA  GLY A 101     -62.825 -43.484 -40.048  1.00 17.96           C  
ATOM    764  C   GLY A 101     -62.277 -44.669 -39.308  1.00 17.40           C  
ATOM    765  O   GLY A 101     -61.180 -44.612 -38.813  1.00 13.69           O  
ATOM    766  N   SER A 102     -63.042 -45.729 -39.259  1.00 10.28           N  
ATOM    767  CA  SER A 102     -62.739 -46.940 -38.552  1.00 15.02           C  
ATOM    768  C   SER A 102     -61.440 -47.583 -38.900  1.00 14.84           C  
ATOM    769  O   SER A 102     -60.841 -48.250 -38.078  1.00 19.39           O  
ATOM    770  CB  SER A 102     -63.849 -47.944 -38.689  1.00 21.73           C  
ATOM    771  OG  SER A 102     -63.750 -48.420 -39.999  1.00 24.64           O  
ATOM    772  N   ALA A 103     -60.995 -47.438 -40.107  1.00 10.67           N  
ATOM    773  CA  ALA A 103     -59.735 -48.072 -40.458  1.00 16.03           C  
ATOM    774  C   ALA A 103     -58.574 -47.537 -39.610  1.00 25.27           C  
ATOM    775  O   ALA A 103     -57.645 -48.253 -39.250  1.00 16.90           O  
ATOM    776  CB  ALA A 103     -59.457 -47.874 -41.954  1.00 22.35           C  
ATOM    777  N   GLN A 104     -58.624 -46.242 -39.295  1.00 13.32           N  
ATOM    778  CA  GLN A 104     -57.567 -45.651 -38.503  1.00  5.60           C  
ATOM    779  C   GLN A 104     -57.586 -46.170 -37.097  1.00 18.13           C  
ATOM    780  O   GLN A 104     -56.548 -46.221 -36.454  1.00 16.37           O  
ATOM    781  CB  GLN A 104     -57.703 -44.093 -38.429  1.00 14.55           C  
ATOM    782  CG  GLN A 104     -57.258 -43.353 -39.721  1.00 25.45           C  
ATOM    783  CD  GLN A 104     -58.046 -43.737 -40.947  1.00 14.10           C  
ATOM    784  OE1 GLN A 104     -57.466 -44.291 -41.877  1.00 34.82           O  
ATOM    785  NE2 GLN A 104     -59.350 -43.460 -40.961  1.00 20.55           N  
ATOM    786  N   PHE A 105     -58.784 -46.526 -36.637  1.00 14.68           N  
ATOM    787  CA  PHE A 105     -58.993 -47.049 -35.313  1.00 16.37           C  
ATOM    788  C   PHE A 105     -58.600 -48.509 -35.268  1.00 27.04           C  
ATOM    789  O   PHE A 105     -58.156 -48.996 -34.238  1.00 11.02           O  
ATOM    790  CB  PHE A 105     -60.357 -46.683 -34.722  1.00 16.30           C  
ATOM    791  CG  PHE A 105     -60.241 -45.271 -34.183  1.00 26.57           C  
ATOM    792  CD1 PHE A 105     -59.698 -45.035 -32.913  1.00  9.84           C  
ATOM    793  CD2 PHE A 105     -60.614 -44.183 -34.975  1.00 15.50           C  
ATOM    794  CE1 PHE A 105     -59.612 -43.719 -32.443  1.00 18.30           C  
ATOM    795  CE2 PHE A 105     -60.486 -42.864 -34.531  1.00 22.58           C  
ATOM    796  CZ  PHE A 105     -59.996 -42.639 -33.243  1.00 14.20           C  
ATOM    797  N   GLU A 106     -58.698 -49.188 -36.418  1.00  9.14           N  
ATOM    798  CA  GLU A 106     -58.258 -50.579 -36.508  1.00  6.52           C  
ATOM    799  C   GLU A 106     -56.730 -50.552 -36.298  1.00 10.73           C  
ATOM    800  O   GLU A 106     -56.073 -51.399 -35.648  1.00 12.40           O  
ATOM    801  CB  GLU A 106     -58.688 -51.268 -37.827  1.00  8.05           C  
ATOM    802  CG  GLU A 106     -60.202 -51.601 -37.897  1.00 37.98           C  
ATOM    803  CD  GLU A 106     -60.805 -51.775 -39.290  1.00 80.00           C  
ATOM    804  OE1 GLU A 106     -60.294 -50.952 -40.178  1.00 80.00           O  
ATOM    805  OE2 GLU A 106     -61.682 -52.597 -39.557  1.00 51.47           O  
ATOM    806  N   ASN A 107     -56.100 -49.502 -36.812  1.00 12.21           N  
ATOM    807  CA  ASN A 107     -54.647 -49.381 -36.620  1.00 14.57           C  
ATOM    808  C   ASN A 107     -54.280 -49.101 -35.161  1.00 17.84           C  
ATOM    809  O   ASN A 107     -53.402 -49.746 -34.609  1.00 16.84           O  
ATOM    810  CB  ASN A 107     -54.042 -48.311 -37.498  1.00 19.25           C  
ATOM    811  CG  ASN A 107     -54.234 -48.611 -38.950  1.00 15.19           C  
ATOM    812  OD1 ASN A 107     -54.241 -47.620 -39.719  1.00 25.75           O  
ATOM    813  ND2 ASN A 107     -54.361 -49.911 -39.267  1.00 13.62           N  
ATOM    814  N   VAL A 108     -54.943 -48.148 -34.526  1.00 10.44           N  
ATOM    815  CA  VAL A 108     -54.689 -47.885 -33.133  1.00 10.51           C  
ATOM    816  C   VAL A 108     -54.818 -49.195 -32.375  1.00  9.55           C  
ATOM    817  O   VAL A 108     -53.884 -49.610 -31.672  1.00 12.59           O  
ATOM    818  CB  VAL A 108     -55.640 -46.880 -32.547  1.00 18.11           C  
ATOM    819  CG1 VAL A 108     -55.347 -46.877 -31.034  1.00 15.42           C  
ATOM    820  CG2 VAL A 108     -55.418 -45.526 -33.213  1.00 14.06           C  
ATOM    821  N   ARG A 109     -55.928 -49.890 -32.526  1.00 11.21           N  
ATOM    822  CA  ARG A 109     -56.149 -51.179 -31.879  1.00 15.70           C  
ATOM    823  C   ARG A 109     -55.002 -52.153 -32.098  1.00 38.57           C  
ATOM    824  O   ARG A 109     -54.600 -52.902 -31.241  1.00 11.99           O  
ATOM    825  CB  ARG A 109     -57.511 -51.834 -32.233  1.00 14.39           C  
ATOM    826  CG  ARG A 109     -57.786 -53.169 -31.549  1.00 17.79           C  
ATOM    827  CD  ARG A 109     -59.178 -53.734 -31.850  1.00 12.13           C  
ATOM    828  NE  ARG A 109     -59.304 -54.072 -33.251  1.00 27.44           N  
ATOM    829  CZ  ARG A 109     -60.465 -54.315 -33.822  1.00 41.64           C  
ATOM    830  NH1 ARG A 109     -61.593 -54.230 -33.105  1.00 56.80           N  
ATOM    831  NH2 ARG A 109     -60.461 -54.604 -35.124  1.00 49.50           N  
ATOM    832  N   SER A 110     -54.422 -52.178 -33.268  1.00 15.04           N  
ATOM    833  CA  SER A 110     -53.385 -53.148 -33.511  1.00 14.63           C  
ATOM    834  C   SER A 110     -52.146 -52.887 -32.726  1.00 34.45           C  
ATOM    835  O   SER A 110     -51.398 -53.767 -32.351  1.00 26.22           O  
ATOM    836  CB  SER A 110     -52.993 -53.141 -35.009  1.00 11.70           C  
ATOM    837  OG  SER A 110     -54.173 -53.251 -35.780  1.00 49.51           O  
ATOM    838  N   MET A 111     -51.893 -51.619 -32.534  1.00 13.30           N  
ATOM    839  CA  MET A 111     -50.645 -51.248 -31.910  1.00 12.35           C  
ATOM    840  C   MET A 111     -50.705 -50.902 -30.414  1.00  9.27           C  
ATOM    841  O   MET A 111     -49.683 -50.805 -29.732  1.00 16.91           O  
ATOM    842  CB  MET A 111     -50.103 -50.134 -32.828  1.00 15.13           C  
ATOM    843  CG  MET A 111     -49.411 -49.007 -32.144  1.00 41.70           C  
ATOM    844  SD  MET A 111     -50.517 -47.683 -31.749  1.00 37.17           S  
ATOM    845  CE  MET A 111     -49.205 -46.553 -31.260  1.00 33.17           C  
ATOM    846  N   PHE A 112     -51.926 -50.774 -29.931  1.00 12.79           N  
ATOM    847  CA  PHE A 112     -52.157 -50.429 -28.548  1.00 17.16           C  
ATOM    848  C   PHE A 112     -51.555 -51.318 -27.458  1.00 19.96           C  
ATOM    849  O   PHE A 112     -50.742 -50.877 -26.645  1.00 16.05           O  
ATOM    850  CB  PHE A 112     -53.586 -49.991 -28.299  1.00 19.60           C  
ATOM    851  CG  PHE A 112     -53.643 -49.029 -27.135  1.00 13.04           C  
ATOM    852  CD1 PHE A 112     -53.368 -47.680 -27.320  1.00 17.00           C  
ATOM    853  CD2 PHE A 112     -54.008 -49.463 -25.863  1.00 14.41           C  
ATOM    854  CE1 PHE A 112     -53.423 -46.804 -26.241  1.00 41.74           C  
ATOM    855  CE2 PHE A 112     -54.119 -48.602 -24.780  1.00 12.08           C  
ATOM    856  CZ  PHE A 112     -53.819 -47.263 -24.979  1.00 16.87           C  
ATOM    857  N   PRO A 113     -51.929 -52.577 -27.435  1.00 33.14           N  
ATOM    858  CA  PRO A 113     -51.402 -53.495 -26.436  1.00 15.25           C  
ATOM    859  C   PRO A 113     -49.898 -53.463 -26.382  1.00 12.97           C  
ATOM    860  O   PRO A 113     -49.342 -53.523 -25.318  1.00 20.31           O  
ATOM    861  CB  PRO A 113     -51.877 -54.885 -26.881  1.00 25.37           C  
ATOM    862  CG  PRO A 113     -52.997 -54.653 -27.908  1.00 30.02           C  
ATOM    863  CD  PRO A 113     -52.716 -53.273 -28.489  1.00 18.79           C  
ATOM    864  N   GLY A 114     -49.226 -53.364 -27.505  1.00 14.44           N  
ATOM    865  CA  GLY A 114     -47.793 -53.355 -27.536  1.00  6.96           C  
ATOM    866  C   GLY A 114     -47.232 -52.071 -26.973  1.00 14.05           C  
ATOM    867  O   GLY A 114     -46.130 -52.035 -26.433  1.00 21.91           O  
ATOM    868  N   PHE A 115     -47.973 -50.993 -27.127  1.00 13.93           N  
ATOM    869  CA  PHE A 115     -47.540 -49.712 -26.598  1.00  6.90           C  
ATOM    870  C   PHE A 115     -47.625 -49.707 -25.027  1.00 11.40           C  
ATOM    871  O   PHE A 115     -46.702 -49.313 -24.306  1.00  9.28           O  
ATOM    872  CB  PHE A 115     -48.472 -48.646 -27.227  1.00 10.80           C  
ATOM    873  CG  PHE A 115     -48.224 -47.330 -26.541  1.00 11.90           C  
ATOM    874  CD1 PHE A 115     -47.026 -46.646 -26.734  1.00  9.37           C  
ATOM    875  CD2 PHE A 115     -49.134 -46.860 -25.595  1.00 27.22           C  
ATOM    876  CE1 PHE A 115     -46.817 -45.454 -26.042  1.00 15.24           C  
ATOM    877  CE2 PHE A 115     -48.921 -45.685 -24.887  1.00 19.65           C  
ATOM    878  CZ  PHE A 115     -47.742 -44.977 -25.116  1.00 23.63           C  
ATOM    879  N   VAL A 116     -48.764 -50.194 -24.497  1.00 11.77           N  
ATOM    880  CA  VAL A 116     -48.965 -50.299 -23.056  1.00 14.23           C  
ATOM    881  C   VAL A 116     -47.831 -51.178 -22.468  1.00 17.57           C  
ATOM    882  O   VAL A 116     -47.124 -50.808 -21.534  1.00 15.93           O  
ATOM    883  CB  VAL A 116     -50.370 -50.892 -22.817  1.00 15.77           C  
ATOM    884  CG1 VAL A 116     -50.579 -51.243 -21.366  1.00 26.54           C  
ATOM    885  CG2 VAL A 116     -51.437 -49.889 -23.166  1.00 16.98           C  
ATOM    886  N   ALA A 117     -47.620 -52.364 -23.038  1.00 13.55           N  
ATOM    887  CA  ALA A 117     -46.593 -53.288 -22.597  1.00 14.38           C  
ATOM    888  C   ALA A 117     -45.216 -52.657 -22.623  1.00 22.89           C  
ATOM    889  O   ALA A 117     -44.317 -52.980 -21.877  1.00 14.36           O  
ATOM    890  CB  ALA A 117     -46.711 -54.534 -23.440  1.00 15.34           C  
ATOM    891  N   SER A 118     -45.003 -51.662 -23.443  1.00 14.22           N  
ATOM    892  CA  SER A 118     -43.695 -51.042 -23.418  1.00  7.94           C  
ATOM    893  C   SER A 118     -43.531 -50.196 -22.188  1.00 15.57           C  
ATOM    894  O   SER A 118     -42.425 -49.768 -21.918  1.00 14.59           O  
ATOM    895  CB  SER A 118     -43.487 -50.109 -24.614  1.00 24.43           C  
ATOM    896  OG  SER A 118     -44.228 -48.922 -24.396  1.00 27.47           O  
ATOM    897  N   VAL A 119     -44.618 -49.912 -21.484  1.00 14.67           N  
ATOM    898  CA  VAL A 119     -44.545 -49.132 -20.259  1.00 34.96           C  
ATOM    899  C   VAL A 119     -44.442 -50.082 -19.075  1.00 22.04           C  
ATOM    900  O   VAL A 119     -43.598 -49.885 -18.207  1.00 14.21           O  
ATOM    901  CB  VAL A 119     -45.693 -48.127 -20.057  1.00 23.77           C  
ATOM    902  CG1 VAL A 119     -45.667 -47.492 -18.661  1.00 16.89           C  
ATOM    903  CG2 VAL A 119     -45.655 -47.037 -21.127  1.00 18.30           C  
ATOM    904  N   ALA A 120     -45.301 -51.092 -19.048  1.00 19.58           N  
ATOM    905  CA  ALA A 120     -45.299 -52.052 -17.972  1.00 20.03           C  
ATOM    906  C   ALA A 120     -46.128 -53.226 -18.392  1.00  9.65           C  
ATOM    907  O   ALA A 120     -47.123 -53.017 -19.100  1.00 18.98           O  
ATOM    908  CB  ALA A 120     -45.898 -51.402 -16.751  1.00 30.99           C  
ATOM    909  N   ALA A 121     -45.717 -54.447 -17.991  1.00 18.97           N  
ATOM    910  CA  ALA A 121     -46.493 -55.609 -18.393  1.00 31.59           C  
ATOM    911  C   ALA A 121     -47.928 -55.537 -17.892  1.00 19.67           C  
ATOM    912  O   ALA A 121     -48.264 -55.404 -16.711  1.00 24.89           O  
ATOM    913  CB  ALA A 121     -45.830 -56.939 -18.057  1.00 22.69           C  
ATOM    914  N   PRO A 122     -48.837 -55.639 -18.798  1.00 21.96           N  
ATOM    915  CA  PRO A 122     -50.215 -55.573 -18.347  1.00 23.89           C  
ATOM    916  C   PRO A 122     -50.680 -56.866 -17.680  1.00 23.66           C  
ATOM    917  O   PRO A 122     -50.159 -57.948 -17.910  1.00 15.34           O  
ATOM    918  CB  PRO A 122     -50.985 -55.422 -19.653  1.00 30.28           C  
ATOM    919  CG  PRO A 122     -50.088 -55.995 -20.743  1.00 19.03           C  
ATOM    920  CD  PRO A 122     -48.672 -56.102 -20.194  1.00 21.50           C  
ATOM    921  N   PRO A 123     -51.695 -56.787 -16.866  1.00 18.99           N  
ATOM    922  CA  PRO A 123     -52.243 -57.983 -16.240  1.00 23.37           C  
ATOM    923  C   PRO A 123     -52.895 -58.877 -17.303  1.00 23.25           C  
ATOM    924  O   PRO A 123     -53.319 -58.406 -18.357  1.00 17.68           O  
ATOM    925  CB  PRO A 123     -53.369 -57.491 -15.324  1.00 23.84           C  
ATOM    926  CG  PRO A 123     -53.531 -56.009 -15.614  1.00 29.48           C  
ATOM    927  CD  PRO A 123     -52.317 -55.532 -16.393  1.00 30.98           C  
ATOM    928  N   ALA A 124     -52.984 -60.177 -17.020  1.00 16.40           N  
ATOM    929  CA  ALA A 124     -53.612 -61.092 -17.949  1.00 15.48           C  
ATOM    930  C   ALA A 124     -55.053 -60.615 -18.199  1.00 11.76           C  
ATOM    931  O   ALA A 124     -55.702 -60.080 -17.307  1.00 17.28           O  
ATOM    932  CB  ALA A 124     -53.544 -62.528 -17.408  1.00 16.89           C  
ATOM    933  N   GLY A 125     -55.550 -60.774 -19.413  1.00 17.78           N  
ATOM    934  CA  GLY A 125     -56.892 -60.319 -19.689  1.00 18.62           C  
ATOM    935  C   GLY A 125     -56.923 -58.841 -20.064  1.00 22.98           C  
ATOM    936  O   GLY A 125     -57.878 -58.443 -20.680  1.00 21.55           O  
ATOM    937  N   ALA A 126     -55.907 -58.005 -19.756  1.00 23.10           N  
ATOM    938  CA  ALA A 126     -55.962 -56.563 -20.126  1.00 17.37           C  
ATOM    939  C   ALA A 126     -55.944 -56.323 -21.636  1.00 25.67           C  
ATOM    940  O   ALA A 126     -56.697 -55.501 -22.166  1.00 21.95           O  
ATOM    941  CB  ALA A 126     -54.824 -55.754 -19.481  1.00 16.34           C  
ATOM    942  N   ASP A 127     -55.085 -57.048 -22.348  1.00 16.04           N  
ATOM    943  CA  ASP A 127     -55.022 -56.874 -23.773  1.00 21.10           C  
ATOM    944  C   ASP A 127     -56.363 -57.095 -24.425  1.00 27.87           C  
ATOM    945  O   ASP A 127     -56.715 -56.278 -25.239  1.00 17.93           O  
ATOM    946  CB  ASP A 127     -53.942 -57.725 -24.409  1.00 16.76           C  
ATOM    947  CG  ASP A 127     -52.513 -57.262 -24.176  1.00 24.83           C  
ATOM    948  OD1 ASP A 127     -52.357 -56.076 -23.598  1.00 30.37           O  
ATOM    949  OD2 ASP A 127     -51.556 -57.952 -24.495  1.00 39.84           O  
ATOM    950  N   ALA A 128     -57.098 -58.145 -24.035  1.00 19.73           N  
ATOM    951  CA  ALA A 128     -58.425 -58.429 -24.553  1.00 13.59           C  
ATOM    952  C   ALA A 128     -59.414 -57.304 -24.187  1.00 14.48           C  
ATOM    953  O   ALA A 128     -60.298 -56.898 -24.940  1.00 13.89           O  
ATOM    954  CB  ALA A 128     -58.841 -59.864 -24.208  1.00  7.23           C  
ATOM    955  N   ALA A 129     -59.266 -56.712 -23.018  1.00 10.11           N  
ATOM    956  CA  ALA A 129     -60.165 -55.632 -22.634  1.00 11.36           C  
ATOM    957  C   ALA A 129     -59.975 -54.425 -23.569  1.00  8.31           C  
ATOM    958  O   ALA A 129     -60.948 -53.806 -23.998  1.00  9.87           O  
ATOM    959  CB  ALA A 129     -60.048 -55.258 -21.159  1.00 14.99           C  
ATOM    960  N   TRP A 130     -58.718 -54.100 -23.927  1.00 10.41           N  
ATOM    961  CA  TRP A 130     -58.423 -52.980 -24.822  1.00 15.69           C  
ATOM    962  C   TRP A 130     -58.927 -53.194 -26.216  1.00 14.21           C  
ATOM    963  O   TRP A 130     -59.419 -52.264 -26.864  1.00 13.06           O  
ATOM    964  CB  TRP A 130     -56.926 -52.724 -24.979  1.00 14.59           C  
ATOM    965  CG  TRP A 130     -56.405 -52.074 -23.753  1.00 17.86           C  
ATOM    966  CD1 TRP A 130     -55.579 -52.624 -22.823  1.00 12.63           C  
ATOM    967  CD2 TRP A 130     -56.718 -50.760 -23.324  1.00 24.41           C  
ATOM    968  NE1 TRP A 130     -55.324 -51.714 -21.840  1.00 25.94           N  
ATOM    969  CE2 TRP A 130     -56.032 -50.579 -22.119  1.00 25.31           C  
ATOM    970  CE3 TRP A 130     -57.466 -49.721 -23.877  1.00 20.10           C  
ATOM    971  CZ2 TRP A 130     -56.084 -49.376 -21.482  1.00 16.89           C  
ATOM    972  CZ3 TRP A 130     -57.543 -48.515 -23.225  1.00 22.82           C  
ATOM    973  CH2 TRP A 130     -56.832 -48.357 -22.040  1.00 16.31           C  
ATOM    974  N   THR A 131     -58.761 -54.428 -26.672  1.00 11.22           N  
ATOM    975  CA  THR A 131     -59.235 -54.707 -27.996  1.00 11.93           C  
ATOM    976  C   THR A 131     -60.749 -54.614 -28.034  1.00 13.59           C  
ATOM    977  O   THR A 131     -61.294 -54.242 -29.084  1.00 16.37           O  
ATOM    978  CB  THR A 131     -58.744 -56.021 -28.593  1.00 15.62           C  
ATOM    979  OG1 THR A 131     -59.573 -57.083 -28.187  1.00 62.61           O  
ATOM    980  CG2 THR A 131     -57.279 -56.254 -28.284  1.00 10.62           C  
ATOM    981  N   LYS A 132     -61.432 -54.946 -26.910  1.00  8.65           N  
ATOM    982  CA  LYS A 132     -62.896 -54.861 -26.867  1.00 13.81           C  
ATOM    983  C   LYS A 132     -63.302 -53.391 -26.837  1.00 18.72           C  
ATOM    984  O   LYS A 132     -64.239 -52.952 -27.518  1.00 17.17           O  
ATOM    985  CB  LYS A 132     -63.448 -55.642 -25.686  1.00 24.48           C  
ATOM    986  CG  LYS A 132     -64.902 -56.037 -25.815  1.00 23.16           C  
ATOM    987  CD  LYS A 132     -65.608 -55.856 -24.496  1.00 39.03           C  
ATOM    988  CE  LYS A 132     -66.787 -56.778 -24.301  1.00 39.38           C  
ATOM    989  NZ  LYS A 132     -66.359 -58.119 -23.865  1.00 52.03           N  
ATOM    990  N   LEU A 133     -62.545 -52.621 -26.054  1.00 11.48           N  
ATOM    991  CA  LEU A 133     -62.808 -51.173 -25.959  1.00 15.25           C  
ATOM    992  C   LEU A 133     -62.637 -50.498 -27.316  1.00 13.76           C  
ATOM    993  O   LEU A 133     -63.439 -49.688 -27.798  1.00  8.73           O  
ATOM    994  CB  LEU A 133     -61.920 -50.442 -24.926  1.00 16.12           C  
ATOM    995  CG  LEU A 133     -62.257 -48.956 -24.635  1.00 22.65           C  
ATOM    996  CD1 LEU A 133     -63.730 -48.678 -24.287  1.00 14.88           C  
ATOM    997  CD2 LEU A 133     -61.385 -48.476 -23.473  1.00 20.47           C  
ATOM    998  N   PHE A 134     -61.536 -50.816 -27.961  1.00  9.57           N  
ATOM    999  CA  PHE A 134     -61.311 -50.208 -29.265  1.00 30.93           C  
ATOM   1000  C   PHE A 134     -62.334 -50.704 -30.264  1.00 20.30           C  
ATOM   1001  O   PHE A 134     -62.647 -49.985 -31.188  1.00 16.41           O  
ATOM   1002  CB  PHE A 134     -59.885 -50.449 -29.772  1.00 17.89           C  
ATOM   1003  CG  PHE A 134     -58.970 -49.425 -29.163  1.00 18.83           C  
ATOM   1004  CD1 PHE A 134     -59.164 -48.069 -29.410  1.00 18.41           C  
ATOM   1005  CD2 PHE A 134     -57.934 -49.810 -28.317  1.00 12.21           C  
ATOM   1006  CE1 PHE A 134     -58.337 -47.101 -28.839  1.00 22.28           C  
ATOM   1007  CE2 PHE A 134     -57.088 -48.863 -27.748  1.00 34.66           C  
ATOM   1008  CZ  PHE A 134     -57.305 -47.509 -28.003  1.00 17.05           C  
ATOM   1009  N   GLY A 135     -62.850 -51.917 -30.030  1.00 15.41           N  
ATOM   1010  CA  GLY A 135     -63.867 -52.524 -30.839  1.00  7.35           C  
ATOM   1011  C   GLY A 135     -65.099 -51.667 -30.777  1.00 16.47           C  
ATOM   1012  O   GLY A 135     -65.761 -51.464 -31.784  1.00 18.47           O  
ATOM   1013  N   LEU A 136     -65.415 -51.159 -29.591  1.00  8.11           N  
ATOM   1014  CA  LEU A 136     -66.611 -50.336 -29.454  1.00 12.47           C  
ATOM   1015  C   LEU A 136     -66.473 -49.012 -30.196  1.00 15.83           C  
ATOM   1016  O   LEU A 136     -67.402 -48.399 -30.674  1.00 11.84           O  
ATOM   1017  CB  LEU A 136     -66.920 -50.066 -27.963  1.00 10.63           C  
ATOM   1018  CG  LEU A 136     -67.395 -51.345 -27.261  1.00 18.23           C  
ATOM   1019  CD1 LEU A 136     -67.330 -51.087 -25.755  1.00 14.42           C  
ATOM   1020  CD2 LEU A 136     -68.845 -51.652 -27.658  1.00 13.18           C  
ATOM   1021  N   ILE A 137     -65.264 -48.525 -30.258  1.00 10.74           N  
ATOM   1022  CA  ILE A 137     -64.975 -47.261 -30.915  1.00  8.15           C  
ATOM   1023  C   ILE A 137     -65.075 -47.427 -32.450  1.00 13.15           C  
ATOM   1024  O   ILE A 137     -65.610 -46.588 -33.157  1.00 10.89           O  
ATOM   1025  CB  ILE A 137     -63.591 -46.812 -30.483  1.00 14.92           C  
ATOM   1026  CG1 ILE A 137     -63.699 -46.301 -29.037  1.00 17.99           C  
ATOM   1027  CG2 ILE A 137     -63.096 -45.721 -31.431  1.00 12.50           C  
ATOM   1028  CD1 ILE A 137     -62.440 -45.660 -28.437  1.00 13.41           C  
ATOM   1029  N   ILE A 138     -64.573 -48.542 -32.941  1.00  8.76           N  
ATOM   1030  CA  ILE A 138     -64.601 -48.897 -34.336  1.00 13.12           C  
ATOM   1031  C   ILE A 138     -66.044 -48.973 -34.811  1.00 22.26           C  
ATOM   1032  O   ILE A 138     -66.354 -48.465 -35.906  1.00 27.85           O  
ATOM   1033  CB  ILE A 138     -63.813 -50.172 -34.579  1.00 14.93           C  
ATOM   1034  CG1 ILE A 138     -62.329 -49.837 -34.340  1.00 14.83           C  
ATOM   1035  CG2 ILE A 138     -64.050 -50.623 -36.027  1.00 18.12           C  
ATOM   1036  CD1 ILE A 138     -61.395 -51.054 -34.194  1.00  7.63           C  
ATOM   1037  N   ASP A 139     -66.898 -49.614 -33.989  1.00 18.78           N  
ATOM   1038  CA  ASP A 139     -68.326 -49.751 -34.318  1.00 10.55           C  
ATOM   1039  C   ASP A 139     -68.970 -48.404 -34.405  1.00 15.22           C  
ATOM   1040  O   ASP A 139     -69.739 -48.187 -35.300  1.00 23.75           O  
ATOM   1041  CB  ASP A 139     -69.144 -50.623 -33.362  1.00 23.55           C  
ATOM   1042  CG  ASP A 139     -68.724 -52.034 -33.516  1.00 23.32           C  
ATOM   1043  OD1 ASP A 139     -68.132 -52.409 -34.502  1.00 25.97           O  
ATOM   1044  OD2 ASP A 139     -68.968 -52.783 -32.483  1.00 34.81           O  
ATOM   1045  N   ALA A 140     -68.640 -47.529 -33.480  1.00 13.12           N  
ATOM   1046  CA  ALA A 140     -69.205 -46.202 -33.456  1.00  9.36           C  
ATOM   1047  C   ALA A 140     -68.897 -45.428 -34.749  1.00 17.64           C  
ATOM   1048  O   ALA A 140     -69.729 -44.769 -35.372  1.00 20.67           O  
ATOM   1049  CB  ALA A 140     -68.868 -45.445 -32.175  1.00 12.65           C  
ATOM   1050  N   LEU A 141     -67.649 -45.510 -35.189  1.00 21.34           N  
ATOM   1051  CA  LEU A 141     -67.179 -44.860 -36.402  1.00 25.96           C  
ATOM   1052  C   LEU A 141     -67.951 -45.345 -37.616  1.00 35.71           C  
ATOM   1053  O   LEU A 141     -68.338 -44.560 -38.471  1.00 28.77           O  
ATOM   1054  CB  LEU A 141     -65.642 -44.839 -36.636  1.00 14.13           C  
ATOM   1055  CG  LEU A 141     -64.955 -43.912 -35.663  1.00 18.92           C  
ATOM   1056  CD1 LEU A 141     -63.561 -44.420 -35.383  1.00 23.68           C  
ATOM   1057  CD2 LEU A 141     -64.905 -42.504 -36.210  1.00 20.37           C  
ATOM   1058  N   LYS A 142     -68.175 -46.632 -37.674  1.00 13.83           N  
ATOM   1059  CA  LYS A 142     -68.935 -47.202 -38.736  1.00 24.57           C  
ATOM   1060  C   LYS A 142     -70.350 -46.658 -38.714  1.00 18.72           C  
ATOM   1061  O   LYS A 142     -70.859 -46.292 -39.750  1.00 35.41           O  
ATOM   1062  CB  LYS A 142     -68.975 -48.691 -38.568  1.00 23.20           C  
ATOM   1063  CG  LYS A 142     -67.634 -49.302 -38.870  1.00 41.30           C  
ATOM   1064  CD  LYS A 142     -67.691 -50.746 -39.339  1.00 43.49           C  
ATOM   1065  CE  LYS A 142     -66.319 -51.431 -39.303  1.00 29.19           C  
ATOM   1066  NZ  LYS A 142     -66.321 -52.891 -39.061  1.00 69.96           N  
ATOM   1067  N   ALA A 143     -70.999 -46.608 -37.549  1.00 30.94           N  
ATOM   1068  CA  ALA A 143     -72.349 -46.087 -37.537  1.00 14.87           C  
ATOM   1069  C   ALA A 143     -72.394 -44.615 -37.888  1.00 49.43           C  
ATOM   1070  O   ALA A 143     -73.386 -44.097 -38.405  1.00 35.59           O  
ATOM   1071  CB  ALA A 143     -73.006 -46.282 -36.185  1.00 24.14           C  
ATOM   1072  N   ALA A 144     -71.280 -43.974 -37.566  1.00 22.84           N  
ATOM   1073  CA  ALA A 144     -71.101 -42.556 -37.821  1.00 25.18           C  
ATOM   1074  C   ALA A 144     -70.930 -42.221 -39.301  1.00 31.27           C  
ATOM   1075  O   ALA A 144     -70.915 -41.055 -39.723  1.00 25.15           O  
ATOM   1076  CB  ALA A 144     -70.177 -41.867 -36.848  1.00 40.81           C  
ATOM   1077  N   GLY A 145     -70.768 -43.300 -40.072  1.00 28.56           N  
ATOM   1078  CA  GLY A 145     -70.677 -43.238 -41.518  1.00 42.47           C  
ATOM   1079  C   GLY A 145     -69.333 -43.407 -42.153  0.00 26.25           C  
ATOM   1080  O   GLY A 145     -69.173 -43.074 -43.320  1.00 80.00           O  
ATOM   1081  N   ALA A 146     -68.387 -43.943 -41.403  1.00 51.11           N  
ATOM   1082  CA  ALA A 146     -67.046 -44.158 -41.898  1.00 18.41           C  
ATOM   1083  C   ALA A 146     -66.334 -45.360 -41.259  1.00 35.81           C  
ATOM   1084  O   ALA A 146     -66.491 -46.485 -41.767  1.00 30.65           O  
ATOM   1085  CB  ALA A 146     -66.256 -42.898 -41.598  1.00 30.80           C  
ATOM   1086  OXT ALA A 146     -65.660 -45.183 -40.222  0.00 18.00           O  
TER    1087      ALA A 146                                                      
HETATM 1088  N1  AZI A 149     -56.362 -34.748 -31.001  1.00 21.47           N  
HETATM 1089  N2  AZI A 149     -56.483 -35.811 -31.481  1.00 18.31           N  
HETATM 1090  N3  AZI A 149     -56.597 -36.915 -31.978  1.00 15.92           N  
HETATM 1091  CHA HEM A 148     -59.420 -34.385 -32.577  1.00 20.16           C  
HETATM 1092  CHB HEM A 148     -59.198 -37.868 -29.208  1.00  8.22           C  
HETATM 1093  CHC HEM A 148     -57.326 -40.996 -32.299  1.00 10.17           C  
HETATM 1094  CHD HEM A 148     -57.570 -37.521 -35.630  1.00 22.76           C  
HETATM 1095  C1A HEM A 148     -59.581 -35.124 -31.430  1.00 12.07           C  
HETATM 1096  C2A HEM A 148     -60.162 -34.570 -30.223  1.00 26.52           C  
HETATM 1097  C3A HEM A 148     -60.028 -35.503 -29.247  1.00 10.45           C  
HETATM 1098  C4A HEM A 148     -59.493 -36.700 -29.920  1.00  6.72           C  
HETATM 1099  CMA HEM A 148     -60.471 -35.468 -27.749  1.00 13.44           C  
HETATM 1100  CAA HEM A 148     -60.497 -33.064 -30.093  1.00 24.36           C  
HETATM 1101  CBA HEM A 148     -61.982 -32.907 -30.421  1.00 31.18           C  
HETATM 1102  CGA HEM A 148     -62.402 -31.469 -30.472  1.00 80.00           C  
HETATM 1103  O1A HEM A 148     -61.660 -30.677 -29.870  1.00 80.00           O  
HETATM 1104  O2A HEM A 148     -63.462 -31.170 -31.088  1.00 42.56           O  
HETATM 1105  C1B HEM A 148     -58.645 -39.049 -29.701  1.00  7.50           C  
HETATM 1106  C2B HEM A 148     -58.478 -40.280 -28.986  1.00  8.80           C  
HETATM 1107  C3B HEM A 148     -57.929 -41.160 -29.841  1.00  4.95           C  
HETATM 1108  C4B HEM A 148     -57.982 -40.528 -31.164  1.00  9.73           C  
HETATM 1109  CMB HEM A 148     -58.806 -40.557 -27.511  1.00 11.20           C  
HETATM 1110  CAB HEM A 148     -57.614 -42.674 -29.601  1.00 12.80           C  
HETATM 1111  CBB HEM A 148     -56.408 -43.208 -29.634  1.00 16.62           C  
HETATM 1112  C1C HEM A 148     -57.289 -40.309 -33.502  1.00 16.11           C  
HETATM 1113  C2C HEM A 148     -56.747 -40.861 -34.747  1.00 10.25           C  
HETATM 1114  C3C HEM A 148     -56.715 -39.817 -35.620  1.00  9.78           C  
HETATM 1115  C4C HEM A 148     -57.360 -38.693 -34.954  1.00 30.14           C  
HETATM 1116  CMC HEM A 148     -56.250 -42.317 -34.887  1.00  8.81           C  
HETATM 1117  CAC HEM A 148     -56.234 -39.800 -37.085  1.00 18.03           C  
HETATM 1118  CBC HEM A 148     -55.727 -40.922 -37.565  1.00 28.52           C  
HETATM 1119  C1D HEM A 148     -58.060 -36.355 -35.122  1.00 10.06           C  
HETATM 1120  C2D HEM A 148     -58.143 -35.076 -35.850  1.00  6.18           C  
HETATM 1121  C3D HEM A 148     -58.648 -34.183 -34.973  1.00 17.93           C  
HETATM 1122  C4D HEM A 148     -58.973 -34.948 -33.761  1.00  9.78           C  
HETATM 1123  CMD HEM A 148     -57.741 -34.934 -37.339  1.00 15.67           C  
HETATM 1124  CAD HEM A 148     -58.935 -32.675 -35.208  1.00 16.12           C  
HETATM 1125  CBD HEM A 148     -58.131 -31.787 -34.271  1.00 45.64           C  
HETATM 1126  CGD HEM A 148     -57.103 -31.007 -35.011  1.00 43.87           C  
HETATM 1127  O1D HEM A 148     -56.160 -31.639 -35.539  1.00 65.67           O  
HETATM 1128  O2D HEM A 148     -57.281 -29.780 -35.038  1.00 62.09           O  
HETATM 1129  NA  HEM A 148     -59.155 -36.426 -31.265  1.00  8.07           N  
HETATM 1130  NB  HEM A 148     -58.277 -39.201 -31.021  1.00 17.39           N  
HETATM 1131  NC  HEM A 148     -57.719 -38.991 -33.638  1.00 19.49           N  
HETATM 1132  ND  HEM A 148     -58.383 -36.219 -33.804  1.00 11.40           N  
HETATM 1133 FE   HEM A 148     -58.453 -37.746 -32.434  1.00 12.92          FE  
HETATM 1134  O   HOH A 150     -41.209 -29.647 -28.300  0.70 67.28           O  
HETATM 1135  O   HOH A 151     -44.819 -37.385 -18.134  0.88 21.59           O  
HETATM 1136  O   HOH A 152     -56.740 -54.264 -35.183  1.00 41.35           O  
HETATM 1137  O   HOH A 153     -72.718 -36.262 -29.146  1.00 43.18           O  
HETATM 1138  O   HOH A 154     -56.521 -46.359 -14.568  0.88 29.45           O  
HETATM 1139  O   HOH A 155     -38.618 -42.331 -30.026  0.94 40.55           O  
HETATM 1140  O   HOH A 156     -45.729 -31.089 -47.291  0.91 79.87           O  
HETATM 1141  O   HOH A 157     -50.960 -39.346 -27.002  0.81 49.50           O  
HETATM 1142  O   HOH A 158     -52.973 -56.980 -35.555  0.89 45.58           O  
HETATM 1143  O   HOH A 159     -47.639 -30.046 -20.923  0.98 33.98           O  
HETATM 1144  O   HOH A 160     -49.846 -54.562 -30.113  0.95 25.13           O  
HETATM 1145  O   HOH A 161     -66.166 -32.169 -42.438  1.00 13.14           O  
HETATM 1146  O   HOH A 162     -73.236 -55.216 -25.539  0.91 44.50           O  
HETATM 1147  O   HOH A 163     -53.230 -58.832 -20.944  1.00 13.43           O  
HETATM 1148  O   HOH A 164     -42.896 -43.402 -29.107  0.86 23.34           O  
HETATM 1149  O   HOH A 165     -36.027 -38.220 -42.950  0.96 26.45           O  
HETATM 1150  O   HOH A 166     -37.123 -39.981 -36.849  1.00 23.95           O  
HETATM 1151  O   HOH A 167     -62.568 -59.098 -23.302  1.00 37.93           O  
HETATM 1152  O   HOH A 168     -70.576 -54.737 -25.495  0.97 41.21           O  
HETATM 1153  O   HOH A 169     -73.825 -53.609 -27.912  0.82 37.14           O  
HETATM 1154  O   HOH A 170     -56.387 -58.647 -11.408  0.76 80.00           O  
HETATM 1155  O   HOH A 171     -67.757 -58.114 -14.275  1.00 18.92           O  
HETATM 1156  O   HOH A 172     -65.898 -60.160 -17.670  0.86 40.67           O  
HETATM 1157  O   HOH A 173     -68.966 -61.073 -15.073  0.97 47.48           O  
HETATM 1158  O   HOH A 174     -43.905 -53.663 -26.282  1.00 29.03           O  
HETATM 1159  O   HOH A 175     -48.533 -57.092 -26.506  0.77 62.94           O  
HETATM 1160  O   HOH A 176     -44.973 -55.927 -28.789  0.67 50.32           O  
HETATM 1161  O   HOH A 177     -66.753 -64.793 -10.441  1.00 34.66           O  
HETATM 1162  O   HOH A 178     -40.102 -33.380 -44.063  0.98 47.95           O  
HETATM 1163  O   HOH A 179     -37.581 -31.766 -44.223  1.00 22.87           O  
HETATM 1164  O   HOH A 180     -46.990 -35.976 -49.377  1.00 21.76           O  
HETATM 1165  O   HOH A 181     -53.939 -44.757 -39.955  0.92 51.12           O  
HETATM 1166  O   HOH A 182     -55.215 -32.147 -44.003  1.00 65.98           O  
HETATM 1167  O   HOH A 183     -68.206 -55.582 -27.520  0.87 54.65           O  
HETATM 1168  O   HOH A 184     -68.294 -57.432 -29.692  0.66 58.21           O  
HETATM 1169  O   HOH A 185     -68.647 -62.067 -24.959  1.00 73.72           O  
HETATM 1170  O   HOH A 186     -42.884 -48.370 -43.170  1.00 49.70           O  
HETATM 1171  O   HOH A 187     -53.500 -51.488 -41.973  0.89 40.04           O  
HETATM 1172  O   HOH A 188     -56.885 -50.328 -41.209  0.89 35.04           O  
HETATM 1173  O   HOH A 189     -55.979 -49.254 -43.849  0.92 36.37           O  
HETATM 1174  O   HOH A 190     -58.923 -50.069 -44.798  0.94 31.37           O  
HETATM 1175  O   HOH A 191     -49.666 -46.104 -43.233  1.00 47.86           O  
HETATM 1176  O   HOH A 192     -55.340 -44.008 -13.250  0.92 48.65           O  
HETATM 1177  O   HOH A 193     -44.751 -48.767 -28.700  1.00 45.38           O  
HETATM 1178  O   HOH A 194     -47.276 -51.619 -30.304  0.90 37.06           O  
HETATM 1179  O   HOH A 195     -63.607 -42.815 -44.002  1.00 54.64           O  
HETATM 1180  O   HOH A 196     -61.666 -45.983 -43.309  0.99 61.79           O  
HETATM 1181  O   HOH A 197     -66.873 -47.829 -48.295  0.96 36.01           O  
HETATM 1182  O   HOH A 198     -67.704 -53.398 -37.361  0.94 56.52           O  
HETATM 1183  O   HOH A 199     -60.681 -61.071 -35.340  0.99 50.41           O  
HETATM 1184  O   HOH A 200     -59.384 -34.030 -24.512  0.96 34.13           O  
HETATM 1185  O   HOH A 201     -62.462 -48.714 -15.417  1.00 33.77           O  
HETATM 1186  O   HOH A 202     -56.599 -35.981 -16.970  1.00 36.63           O  
HETATM 1187  O   HOH A 203     -44.067 -26.742 -35.867  1.00 61.73           O  
HETATM 1188  O   HOH A 204     -76.131 -53.042 -17.101  1.00 32.17           O  
HETATM 1189  O   HOH A 205     -77.161 -51.511 -19.833  0.94 65.88           O  
HETATM 1190  O   HOH A 206     -76.438 -53.840 -14.596  1.00 22.84           O  
HETATM 1191  O   HOH A 207     -73.299 -50.938 -17.856  0.87 38.14           O  
HETATM 1192  O   HOH A 208     -79.555 -51.807 -33.285  0.82 80.00           O  
HETATM 1193  O   HOH A 209     -59.390 -46.290 -46.578  0.94 35.37           O  
HETATM 1194  O   HOH A 210     -69.861 -50.834 -45.297  1.00 41.84           O  
HETATM 1195  O   HOH A 211     -54.122 -52.195 -38.737  0.98 32.25           O  
HETATM 1196  O   HOH A 212     -54.551 -56.096 -40.312  0.83 60.75           O  
HETATM 1197  O   HOH A 213     -56.107 -60.574 -23.269  0.96 25.91           O  
HETATM 1198  O   HOH A 214     -63.768 -56.605 -30.781  0.90 57.00           O  
HETATM 1199  O   HOH A 215     -61.621 -58.952 -26.447  1.00 41.23           O  
HETATM 1200  O   HOH A 216     -60.564 -62.841 -23.025  1.00 46.27           O  
HETATM 1201  O   HOH A 217     -64.459 -66.890 -25.790  1.00 35.85           O  
HETATM 1202  O   HOH A 218     -70.370 -48.758 -30.277  0.93 28.70           O  
HETATM 1203  O   HOH A 219     -44.746 -30.220 -27.795  0.93 21.53           O  
HETATM 1204  O   HOH A 220     -42.439 -36.227 -17.630  0.93 26.32           O  
HETATM 1205  O   HOH A 221     -41.742 -38.353 -44.339  0.14 15.00           O  
HETATM 1206  O   HOH A 222     -59.330 -37.504 -50.537  1.00 16.89           O  
HETATM 1207  O   HOH A 223     -60.558 -42.673 -43.782  1.00 38.19           O  
HETATM 1208  O   HOH A 224     -65.122 -39.585 -15.306  1.00 42.50           O  
HETATM 1209  O   HOH A 225     -58.087 -62.888 -26.228  0.84 49.18           O  
HETATM 1210  O   HOH A 226     -49.351 -49.418 -42.584  1.00 64.69           O  
HETATM 1211  O   HOH A 227     -41.938 -28.980 -36.374  1.00 24.15           O  
HETATM 1212  O   HOH A 228     -70.663 -58.592 -17.601  1.00 73.38           O  
HETATM 1213  O   HOH A 229     -43.660 -46.174 -24.276  0.79 41.33           O  
HETATM 1214  O   HOH A 230     -61.012 -57.908 -13.149  0.93 32.23           O  
HETATM 1215  O   HOH A 231     -44.027 -44.033 -45.770  0.91 70.41           O  
HETATM 1216  O   HOH A 232     -51.562 -50.708 -44.329  0.96 37.88           O  
HETATM 1217  O   HOH A 233     -42.398 -42.683 -19.755  0.88 36.21           O  
HETATM 1218  O   HOH A 234     -50.333 -34.373 -21.251  0.96 34.67           O  
HETATM 1219  O   HOH A 235     -49.391 -35.700 -23.339  1.00 18.83           O  
HETATM 1220  O   HOH A 236     -42.001 -36.302 -25.399  1.00 33.20           O  
HETATM 1221  O   HOH A 237     -42.189 -39.095 -25.194  0.96 12.04           O  
HETATM 1222  O   HOH A 238     -54.049 -25.651 -34.580  0.95 32.68           O  
HETATM 1223  O   HOH A 239     -53.972 -30.771 -36.537  1.00 21.39           O  
HETATM 1224  O   HOH A 240     -38.331 -36.453 -44.330  0.88 45.50           O  
HETATM 1225  O   HOH A 241     -48.581 -27.661 -25.024  0.95 36.18           O  
HETATM 1226  O   HOH A 242     -46.603 -47.350 -44.467  0.85 46.68           O  
HETATM 1227  O   HOH A 243     -52.218 -48.218 -42.458  0.98 80.00           O  
HETATM 1228  O   HOH A 244     -71.685 -43.344 -33.782  0.96 21.50           O  
HETATM 1229  O   HOH A 245     -71.998 -48.334 -33.106  0.84 42.72           O  
HETATM 1230  O   HOH A 246     -49.852 -56.050 -23.970  1.00 35.32           O  
HETATM 1231  O   HOH A 247     -66.031 -54.466 -29.062  1.00 25.24           O  
HETATM 1232  O   HOH A 248     -66.957 -66.670 -24.022  1.00 39.64           O  
HETATM 1233  O   HOH A 249     -40.117 -26.517 -34.875  0.73 50.60           O  
HETATM 1234  O   HOH A 250     -48.872 -58.056 -14.874  1.00 46.36           O  
HETATM 1235  O   HOH A 251     -54.546 -39.729 -45.100  0.96 50.46           O  
HETATM 1236  O   HOH A 252     -56.982 -37.878 -45.533  0.96 80.00           O  
HETATM 1237  O   HOH A 253     -54.928 -29.457 -33.439  0.87 40.29           O  
HETATM 1238  O   HOH A 254     -53.641 -26.754 -37.742  1.00 72.54           O  
HETATM 1239  O   HOH A 255     -67.009 -50.569 -45.102  0.98 53.31           O  
HETATM 1240  O   HOH A 256     -54.512 -56.305 -31.590  0.91 40.82           O  
HETATM 1241  O   HOH A 257     -55.825 -31.837 -21.748  0.94 35.33           O  
HETATM 1242  O   HOH A 258     -68.425 -52.381  -9.468  1.00 54.44           O  
HETATM 1243  O   HOH A 259     -72.628 -48.405 -25.685  0.96 38.09           O  
HETATM 1244  O   HOH A 260     -42.348 -37.467 -14.946  0.92 60.83           O  
HETATM 1245  O   HOH A 261     -51.816 -56.077 -37.968  0.92 37.34           O  
HETATM 1246  O   HOH A 262     -43.632 -33.718 -17.721  0.83 47.76           O  
HETATM 1247  O   HOH A 263     -52.403 -28.491 -23.667  0.95 63.13           O  
HETATM 1248  O   HOH A 264     -56.583 -53.445 -28.179  1.00 77.08           O  
HETATM 1249  O   HOH A 265     -61.041 -48.577 -45.754  1.00 56.88           O  
HETATM 1250  O   HOH A 266     -60.114 -60.441 -21.375  0.95 50.00           O  
HETATM 1251  O   HOH A 267     -72.703 -45.264 -31.301  0.90 59.81           O  
HETATM 1252  O   HOH A 268     -45.599 -37.030 -15.070  0.94 62.44           O  
HETATM 1253  O   HOH A 269     -48.747 -33.979 -47.654  0.90 69.40           O  
HETATM 1254  O   HOH A 270     -56.720 -31.911 -38.652  0.88 63.10           O  
HETATM 1255  O   HOH A 271     -41.467 -44.305 -39.293  1.00 79.34           O  
HETATM 1256  O   HOH A 272     -51.219 -22.657 -36.838  0.75 80.00           O  
HETATM 1257  O   HOH A 273     -44.577 -48.751 -14.398  0.96 53.88           O  
HETATM 1258  O   HOH A 274     -59.983 -60.439  -9.160  1.00 63.88           O  
HETATM 1259  O   HOH A 275     -62.177 -57.850 -10.967  0.88 52.66           O  
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1                                                                
CONECT  728 1133                                                                
CONECT 1088 1089                                                                
CONECT 1089 1088 1090 1133                                                      
CONECT 1090 1089 1133                                                           
CONECT 1091 1095 1122                                                           
CONECT 1092 1098 1105                                                           
CONECT 1093 1108 1112                                                           
CONECT 1094 1115 1119                                                           
CONECT 1095 1091 1096 1129                                                      
CONECT 1096 1095 1097 1100                                                      
CONECT 1097 1096 1098 1099                                                      
CONECT 1098 1092 1097 1129                                                      
CONECT 1099 1097                                                                
CONECT 1100 1096 1101                                                           
CONECT 1101 1100 1102                                                           
CONECT 1102 1101 1103 1104                                                      
CONECT 1103 1102                                                                
CONECT 1104 1102                                                                
CONECT 1105 1092 1106 1130                                                      
CONECT 1106 1105 1107 1109                                                      
CONECT 1107 1106 1108 1110                                                      
CONECT 1108 1093 1107 1130                                                      
CONECT 1109 1106                                                                
CONECT 1110 1107 1111                                                           
CONECT 1111 1110                                                                
CONECT 1112 1093 1113 1131                                                      
CONECT 1113 1112 1114 1116                                                      
CONECT 1114 1113 1115 1117                                                      
CONECT 1115 1094 1114 1131                                                      
CONECT 1116 1113                                                                
CONECT 1117 1114 1118                                                           
CONECT 1118 1117                                                                
CONECT 1119 1094 1120 1132                                                      
CONECT 1120 1119 1121 1123                                                      
CONECT 1121 1120 1122 1124                                                      
CONECT 1122 1091 1121 1132                                                      
CONECT 1123 1120                                                                
CONECT 1124 1121 1125                                                           
CONECT 1125 1124 1126                                                           
CONECT 1126 1125 1127 1128                                                      
CONECT 1127 1126                                                                
CONECT 1128 1126                                                                
CONECT 1129 1095 1098 1133                                                      
CONECT 1130 1105 1108 1133                                                      
CONECT 1131 1112 1115 1133                                                      
CONECT 1132 1119 1122 1133                                                      
CONECT 1133  728 1089 1090 1129                                                 
CONECT 1133 1130 1131 1132                                                      
MASTER      319    0    3    8    0    0    5    6 1258    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: April 25th, 2023.