CNRS Nantes University UFIP UFIP
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***  HYDROLASE 07-SEP-92 1POB  ***

elNémo ID: 221003212828139764

Job options:

ID        	=	 221003212828139764
JOBID     	=	 HYDROLASE 07-SEP-92 1POB
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    HYDROLASE                               07-SEP-92   1POB              
TITLE     CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A 
TITLE    2 TRANSITION-STATE ANALOGUE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOLIPASE A2;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.4;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NAJA ATRA;                                      
SOURCE   3 ORGANISM_COMMON: CHINESE COBRA;                                      
SOURCE   4 ORGANISM_TAXID: 8656                                                 
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.P.WHITE,D.L.SCOTT,Z.OTWINOWSKI,P.B.SIGLER                           
REVDAT   4   14-AUG-19 1POB    1       REMARK                                   
REVDAT   3   17-JUL-19 1POB    1       REMARK LINK                              
REVDAT   2   24-FEB-09 1POB    1       VERSN                                    
REVDAT   1   31-OCT-93 1POB    0                                                
JRNL        AUTH   S.P.WHITE,D.L.SCOTT,Z.OTWINOWSKI,M.H.GELB,P.B.SIGLER         
JRNL        TITL   CRYSTAL STRUCTURE OF COBRA-VENOM PHOSPHOLIPASE A2 IN A       
JRNL        TITL 2 COMPLEX WITH A TRANSITION-STATE ANALOGUE.                    
JRNL        REF    SCIENCE                       V. 250  1560 1990              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   2274787                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.L.SCOTT,S.P.WHITE,Z.OTWINOWSKI,W.YUAN,M.H.GELB,P.B.SIGLER  
REMARK   1  TITL   INTERFACIAL CATALYSIS: THE MECHANISM OF PHOSPHOLIPASE A2     
REMARK   1  REF    SCIENCE                       V. 250  1541 1990              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
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  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
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  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
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            : 1828                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1POB 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_1000175762.                                   
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.93                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.80000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.80000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       17.30000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       36.75000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       17.30000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       36.75000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.80000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       17.30000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       36.75000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.80000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       17.30000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       36.75000            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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                              CA A 801  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  48   OD2                                                    
REMARK 620 2 GEL A 930   O4P  89.1                                              
REMARK 620 3 GEL A 930   O2P 131.4 101.3                                        
REMARK 620 4 TYR A  27   O   102.5 160.2  83.1                                  
REMARK 620 5 GLY A  31   O    77.3  82.1 150.7  84.9                            
REMARK 620 6 GLY A  29   O   150.6  72.3  75.9  90.4  77.6                      
REMARK 620 7 ASP A  48   OD1  56.0  81.0  78.7 118.8 130.2 138.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 803  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  24   O                                                      
REMARK 620 2 CYS A  28   O    62.7                                              
REMARK 620 3 GLY A  25   O    63.4 125.5                                        
REMARK 620 4 HOH A 429   O   136.9  93.4 121.7                                  
REMARK 620 5 HOH A 709   O   121.5  83.7 132.6  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 802  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B  29   O                                                      
REMARK 620 2 ASP B  48   OD1 144.4                                              
REMARK 620 3 GEL B 935   O2P  80.5  79.1                                        
REMARK 620 4 GEL B 935   O4P  76.1  80.5 103.1                                  
REMARK 620 5 TYR B  27   O    93.5 112.7  83.4 166.4                            
REMARK 620 6 ASP B  48   OD2 145.7  55.7 132.3  85.2  99.3                      
REMARK 620 7 GLY B  31   O    78.3 125.4 155.5  83.7  85.5  71.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 804  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR B  24   O                                                      
REMARK 620 2 GLY B  25   O    62.6                                              
REMARK 620 3 HOH B 481   O   146.3 119.4                                        
REMARK 620 4 CYS B  28   O    67.1 127.9  95.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CA1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA3                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CA4                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 801                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 803                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 804                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GEL A 930                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GEL B 935                 
DBREF  1POB A    1   118  UNP    P00598   PA21_NAJAT      28    145             
DBREF  1POB B    1   118  UNP    P00598   PA21_NAJAT      28    145             
SEQADV 1POB ASP A  107  UNP  P00598    ASN   134 CONFLICT                       
SEQADV 1POB ASP A  109  UNP  P00598    ASN   136 CONFLICT                       
SEQADV 1POB ASN A  113  UNP  P00598    ASP   140 CONFLICT                       
SEQADV 1POB ASP B  107  UNP  P00598    ASN   134 CONFLICT                       
SEQADV 1POB ASP B  109  UNP  P00598    ASN   136 CONFLICT                       
SEQADV 1POB ASN B  113  UNP  P00598    ASP   140 CONFLICT                       
SEQRES   1 A  118  ASN LEU TYR GLN PHE LYS ASN MET ILE GLN CYS THR VAL          
SEQRES   2 A  118  PRO SER ARG SER TRP TRP ASP PHE ALA ASP TYR GLY CYS          
SEQRES   3 A  118  TYR CYS GLY ARG GLY GLY SER GLY THR PRO VAL ASP ASP          
SEQRES   4 A  118  LEU ASP ARG CYS CYS GLN VAL HIS ASP ASN CYS TYR ASN          
SEQRES   5 A  118  GLU ALA GLU LYS ILE SER GLY CYS TRP PRO TYR PHE LYS          
SEQRES   6 A  118  THR TYR SER TYR GLU CYS SER GLN GLY THR LEU THR CYS          
SEQRES   7 A  118  LYS GLY GLY ASN ASN ALA CYS ALA ALA ALA VAL CYS ASP          
SEQRES   8 A  118  CYS ASP ARG LEU ALA ALA ILE CYS PHE ALA GLY ALA PRO          
SEQRES   9 A  118  TYR ASN ASP ASN ASP TYR ASN ILE ASN LEU LYS ALA ARG          
SEQRES  10 A  118  CYS                                                          
SEQRES   1 B  118  ASN LEU TYR GLN PHE LYS ASN MET ILE GLN CYS THR VAL          
SEQRES   2 B  118  PRO SER ARG SER TRP TRP ASP PHE ALA ASP TYR GLY CYS          
SEQRES   3 B  118  TYR CYS GLY ARG GLY GLY SER GLY THR PRO VAL ASP ASP          
SEQRES   4 B  118  LEU ASP ARG CYS CYS GLN VAL HIS ASP ASN CYS TYR ASN          
SEQRES   5 B  118  GLU ALA GLU LYS ILE SER GLY CYS TRP PRO TYR PHE LYS          
SEQRES   6 B  118  THR TYR SER TYR GLU CYS SER GLN GLY THR LEU THR CYS          
SEQRES   7 B  118  LYS GLY GLY ASN ASN ALA CYS ALA ALA ALA VAL CYS ASP          
SEQRES   8 B  118  CYS ASP ARG LEU ALA ALA ILE CYS PHE ALA GLY ALA PRO          
SEQRES   9 B  118  TYR ASN ASP ASN ASP TYR ASN ILE ASN LEU LYS ALA ARG          
SEQRES  10 B  118  CYS                                                          
HET     CA  A 801       1                                                       
HET     CA  A 803       1                                                       
HET    GEL  A 930      31                                                       
HET     CA  B 802       1                                                       
HET     CA  B 804       1                                                       
HET    GEL  B 935      31                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GEL 1-O-OCTYL-2-HEPTYLPHOSPHONYL-SN-GLYCERO-3-                       
HETNAM   2 GEL  PHOSPHOETHANOLAMINE                                             
FORMUL   3   CA    4(CA 2+)                                                     
FORMUL   5  GEL    2(C20 H45 N O8 P2)                                           
FORMUL   9  HOH   *242(H2 O)                                                    
HELIX    1  H1 ASN A    1  PRO A   14  1                                  14    
HELIX    2  H2 ASP A   38  ILE A   57  1                                  20    
HELIX    3  H3 ASN A   83  ALA A  103  1                                  21    
HELIX    4  H4 ASN A  113  CYS A  118  1                                   6    
HELIX    5  H5 ASN B    1  PRO B   14  1                                  14    
HELIX    6  H6 ASP B   38  ILE B   57  1                                  20    
HELIX    7  H7 ASN B   83  ALA B  103  1                                  21    
HELIX    8  H8 ASN B  113  CYS B  118  1                                   6    
SHEET    1   A 2 TYR A  69  SER A  72  0                                        
SHEET    2   A 2 THR A  75  CYS A  78 -1  O  THR A  75   N  SER A  72           
SHEET    1   B 2 TYR B  69  SER B  72  0                                        
SHEET    2   B 2 THR B  75  CYS B  78 -1  O  THR B  75   N  SER B  72           
SSBOND   1 CYS A   11    CYS A   71                          1555   1555  2.16  
SSBOND   2 CYS A   26    CYS A  118                          1555   1555  2.00  
SSBOND   3 CYS A   28    CYS A   44                          1555   1555  1.84  
SSBOND   4 CYS A   43    CYS A   99                          1555   1555  1.91  
SSBOND   5 CYS A   50    CYS A   92                          1555   1555  2.00  
SSBOND   6 CYS A   60    CYS A   85                          1555   1555  2.07  
SSBOND   7 CYS A   78    CYS A   90                          1555   1555  2.04  
SSBOND   8 CYS B   11    CYS B   71                          1555   1555  1.99  
SSBOND   9 CYS B   26    CYS B  118                          1555   1555  2.04  
SSBOND  10 CYS B   28    CYS B   44                          1555   1555  1.59  
SSBOND  11 CYS B   43    CYS B   99                          1555   1555  2.32  
SSBOND  12 CYS B   50    CYS B   92                          1555   1555  2.27  
SSBOND  13 CYS B   60    CYS B   85                          1555   1555  1.59  
LINK         ND2 ASN A  52                 N3  GEL A 930     1555   1555  1.59  
LINK        CA    CA A 801                 OD2 ASP A  48     1555   1555  2.28  
LINK        CA    CA A 801                 O4P GEL A 930     1555   1555  2.52  
LINK        CA    CA A 801                 O2P GEL A 930     1555   1555  2.39  
LINK        CA    CA A 801                 O   TYR A  27     1555   1555  2.22  
LINK        CA    CA A 801                 O   GLY A  31     1555   1555  2.52  
LINK        CA    CA A 801                 O   GLY A  29     1555   1555  2.60  
LINK        CA    CA A 801                 OD1 ASP A  48     1555   1555  2.46  
LINK        CA    CA A 803                 O   TYR A  24     1555   1555  3.35  
LINK        CA    CA A 803                 O   CYS A  28     1555   1555  2.82  
LINK        CA    CA A 803                 O   GLY A  25     1555   1555  2.90  
LINK        CA    CA A 803                 O   HOH A 429     1555   1555  2.47  
LINK        CA    CA A 803                 O   HOH A 709     1555   1555  3.08  
LINK        CA    CA B 802                 O   GLY B  29     1555   1555  2.38  
LINK        CA    CA B 802                 OD1 ASP B  48     1555   1555  2.41  
LINK        CA    CA B 802                 O2P GEL B 935     1555   1555  2.38  
LINK        CA    CA B 802                 O4P GEL B 935     1555   1555  2.43  
LINK        CA    CA B 802                 O   TYR B  27     1555   1555  2.26  
LINK        CA    CA B 802                 OD2 ASP B  48     1555   1555  2.36  
LINK        CA    CA B 802                 O   GLY B  31     1555   1555  2.43  
LINK        CA    CA B 804                 O   TYR B  24     1555   1555  3.24  
LINK        CA    CA B 804                 O   GLY B  25     1555   1555  2.85  
LINK        CA    CA B 804                 O   HOH B 481     1555   1555  2.96  
LINK        CA    CA B 804                 O   CYS B  28     1555   1555  2.70  
SITE     1 CA1  4 CYS A  28  ARG A  30  GLY A  32  ASN A  49                    
SITE     1 CA2  3 TYR A  24  GLY A  25  CYS A  28                               
SITE     1 CA3  4 CYS B  28  ARG B  30  GLY B  32  ASN B  49                    
SITE     1 CA4  3 TYR B  24  GLY B  25  CYS B  28                               
SITE     1 AC1  5 TYR A  27  GLY A  29  GLY A  31  ASP A  48                    
SITE     2 AC1  5 GEL A 930                                                     
SITE     1 AC2  5 TYR B  27  GLY B  29  GLY B  31  ASP B  48                    
SITE     2 AC2  5 GEL B 935                                                     
SITE     1 AC3  5 TYR A  24  GLY A  25  CYS A  28  HOH A 429                    
SITE     2 AC3  5 HOH A 709                                                     
SITE     1 AC4  4 TYR B  24  GLY B  25  CYS B  28  HOH B 481                    
SITE     1 AC5 15 LEU A   2  TRP A  18  PHE A  21  TYR A  27                    
SITE     2 AC5 15 GLY A  29  ARG A  30  GLY A  31  CYS A  44                    
SITE     3 AC5 15 HIS A  47  ASP A  48  ASN A  52  TYR A  63                    
SITE     4 AC5 15 HOH A 421  HOH A 711   CA A 801                               
SITE     1 AC6 15 LEU B   2  LYS B   6  ILE B   9  TRP B  18                    
SITE     2 AC6 15 TYR B  27  GLY B  29  GLY B  31  CYS B  44                    
SITE     3 AC6 15 HIS B  47  ASP B  48  TYR B  51  ASN B  52                    
SITE     4 AC6 15 TYR B  63  PHE B  64   CA B 802                               
CRYST1   34.600   73.500  181.600  90.00  90.00  90.00 C 2 2 21     16          
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      0.028902  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013605  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005507        0.00000                         
ATOM      1  N   ASN A   1       7.589   3.928  39.994  1.00 11.27           N  
ATOM      2  CA  ASN A   1       8.364   4.863  40.857  1.00 11.42           C  
ATOM      3  C   ASN A   1       9.691   5.267  40.201  1.00 11.16           C  
ATOM      4  O   ASN A   1      10.273   4.528  39.404  1.00 10.99           O  
ATOM      5  CB  ASN A   1       8.470   4.335  42.250  1.00 13.41           C  
ATOM      6  CG  ASN A   1       9.775   3.745  42.757  1.00 14.95           C  
ATOM      7  OD1 ASN A   1      10.850   4.249  42.466  1.00 15.86           O  
ATOM      8  ND2 ASN A   1       9.719   2.688  43.554  1.00 16.81           N  
ATOM      9  N   LEU A   2      10.090   6.468  40.587  1.00 11.30           N  
ATOM     10  CA  LEU A   2      11.236   7.194  40.018  1.00 11.35           C  
ATOM     11  C   LEU A   2      12.545   6.381  39.998  1.00 11.24           C  
ATOM     12  O   LEU A   2      13.407   6.595  39.136  1.00 11.40           O  
ATOM     13  CB  LEU A   2      11.193   8.611  40.768  1.00 13.27           C  
ATOM     14  CG  LEU A   2      11.214  10.029  40.172  1.00 14.97           C  
ATOM     15  CD1 LEU A   2       9.836  10.703  40.184  1.00 16.05           C  
ATOM     16  CD2 LEU A   2      12.158  10.984  40.908  1.00 14.74           C  
ATOM     17  N   TYR A   3      12.715   5.451  40.922  1.00 11.42           N  
ATOM     18  CA  TYR A   3      13.932   4.606  40.929  1.00 11.55           C  
ATOM     19  C   TYR A   3      13.876   3.636  39.746  1.00 11.82           C  
ATOM     20  O   TYR A   3      14.898   3.324  39.120  1.00 11.81           O  
ATOM     21  CB  TYR A   3      14.036   3.780  42.211  1.00 12.80           C  
ATOM     22  CG  TYR A   3      15.002   4.356  43.258  1.00 11.72           C  
ATOM     23  CD1 TYR A   3      16.390   4.338  43.046  1.00 11.52           C  
ATOM     24  CD2 TYR A   3      14.492   4.899  44.437  1.00 12.12           C  
ATOM     25  CE1 TYR A   3      17.257   4.829  44.029  1.00 12.69           C  
ATOM     26  CE2 TYR A   3      15.357   5.394  45.416  1.00 12.74           C  
ATOM     27  CZ  TYR A   3      16.739   5.351  45.218  1.00 12.81           C  
ATOM     28  OH  TYR A   3      17.578   5.810  46.184  1.00 13.42           O  
ATOM     29  N   GLN A   4      12.665   3.187  39.477  1.00 11.58           N  
ATOM     30  CA  GLN A   4      12.405   2.247  38.388  1.00 11.73           C  
ATOM     31  C   GLN A   4      12.530   2.961  37.044  1.00 11.64           C  
ATOM     32  O   GLN A   4      13.043   2.398  36.071  1.00 11.70           O  
ATOM     33  CB  GLN A   4      11.016   1.649  38.538  1.00 10.45           C  
ATOM     34  CG  GLN A   4      10.855   0.883  39.846  1.00  9.04           C  
ATOM     35  CD  GLN A   4       9.515   0.182  39.933  1.00  8.28           C  
ATOM     36  OE1 GLN A   4       8.493   0.853  40.055  1.00  9.03           O  
ATOM     37  NE2 GLN A   4       9.461  -1.134  39.863  1.00  7.77           N  
ATOM     38  N   PHE A   5      12.062   4.197  37.007  1.00 11.74           N  
ATOM     39  CA  PHE A   5      12.131   5.006  35.775  1.00 11.65           C  
ATOM     40  C   PHE A   5      13.596   5.230  35.388  1.00 11.87           C  
ATOM     41  O   PHE A   5      13.961   5.156  34.208  1.00 11.72           O  
ATOM     42  CB  PHE A   5      11.448   6.355  35.974  1.00 11.27           C  
ATOM     43  CG  PHE A   5      11.391   7.217  34.704  1.00  9.74           C  
ATOM     44  CD1 PHE A   5      11.225   6.624  33.442  1.00  8.79           C  
ATOM     45  CD2 PHE A   5      11.498   8.607  34.811  1.00  9.80           C  
ATOM     46  CE1 PHE A   5      11.153   7.428  32.294  1.00  8.48           C  
ATOM     47  CE2 PHE A   5      11.421   9.409  33.666  1.00  9.57           C  
ATOM     48  CZ  PHE A   5      11.246   8.820  32.408  1.00  9.55           C  
ATOM     49  N   LYS A   6      14.395   5.507  36.401  1.00 11.94           N  
ATOM     50  CA  LYS A   6      15.838   5.730  36.243  1.00 12.30           C  
ATOM     51  C   LYS A   6      16.476   4.508  35.575  1.00 12.42           C  
ATOM     52  O   LYS A   6      17.368   4.628  34.721  1.00 12.07           O  
ATOM     53  CB  LYS A   6      16.472   5.948  37.620  1.00 15.20           C  
ATOM     54  CG  LYS A   6      17.973   5.670  37.656  1.00 17.25           C  
ATOM     55  CD  LYS A   6      18.576   5.934  39.034  1.00 18.89           C  
ATOM     56  CE  LYS A   6      19.085   4.662  39.706  1.00 19.58           C  
ATOM     57  NZ  LYS A   6      20.012   4.936  40.811  1.00 20.83           N  
ATOM     58  N   ASN A   7      15.988   3.350  35.976  1.00 12.44           N  
ATOM     59  CA  ASN A   7      16.498   2.071  35.471  1.00 13.12           C  
ATOM     60  C   ASN A   7      15.985   1.813  34.051  1.00 13.05           C  
ATOM     61  O   ASN A   7      16.669   1.191  33.230  1.00 13.17           O  
ATOM     62  CB  ASN A   7      16.123   0.958  36.437  1.00 14.94           C  
ATOM     63  CG  ASN A   7      17.062   0.968  37.644  1.00 18.54           C  
ATOM     64  OD1 ASN A   7      16.705   0.477  38.712  1.00 20.69           O  
ATOM     65  ND2 ASN A   7      18.260   1.517  37.526  1.00 19.10           N  
ATOM     66  N   MET A   8      14.798   2.298  33.767  1.00 13.17           N  
ATOM     67  CA  MET A   8      14.226   2.176  32.421  1.00 13.30           C  
ATOM     68  C   MET A   8      15.081   2.949  31.407  1.00 13.71           C  
ATOM     69  O   MET A   8      15.299   2.492  30.276  1.00 13.40           O  
ATOM     70  CB  MET A   8      12.826   2.759  32.380  1.00 11.84           C  
ATOM     71  CG  MET A   8      11.774   1.721  32.697  1.00 12.54           C  
ATOM     72  SD  MET A   8      10.131   2.257  32.324  1.00 13.14           S  
ATOM     73  CE  MET A   8       8.989   1.101  33.037  1.00 11.97           C  
ATOM     74  N   ILE A   9      15.531   4.124  31.837  1.00 13.87           N  
ATOM     75  CA  ILE A   9      16.358   5.008  30.991  1.00 14.52           C  
ATOM     76  C   ILE A   9      17.717   4.368  30.753  1.00 14.90           C  
ATOM     77  O   ILE A   9      18.344   4.575  29.706  1.00 14.87           O  
ATOM     78  CB  ILE A   9      16.563   6.376  31.644  1.00 14.60           C  
ATOM     79  CG1 ILE A   9      15.274   7.210  31.663  1.00 14.48           C  
ATOM     80  CG2 ILE A   9      17.624   7.211  30.911  1.00 14.79           C  
ATOM     81  CD1 ILE A   9      15.320   8.392  32.636  1.00 15.19           C  
ATOM     82  N   GLN A  10      18.121   3.620  31.751  1.00 15.37           N  
ATOM     83  CA  GLN A  10      19.368   2.863  31.722  1.00 15.98           C  
ATOM     84  C   GLN A  10      19.254   1.777  30.656  1.00 16.06           C  
ATOM     85  O   GLN A  10      20.227   1.440  29.971  1.00 16.30           O  
ATOM     86  CB  GLN A  10      19.586   2.198  33.076  1.00 20.50           C  
ATOM     87  CG  GLN A  10      20.659   2.869  33.920  1.00 25.88           C  
ATOM     88  CD  GLN A  10      21.424   3.936  34.692  1.00 29.08           C  
ATOM     89  OE1 GLN A  10      22.224   3.602  35.569  1.00 30.26           O  
ATOM     90  NE2 GLN A  10      21.232   5.207  34.404  1.00 30.70           N  
ATOM     91  N   CYS A  11      18.049   1.260  30.567  1.00 16.27           N  
ATOM     92  CA  CYS A  11      17.705   0.201  29.626  1.00 16.33           C  
ATOM     93  C   CYS A  11      17.838   0.685  28.172  1.00 16.21           C  
ATOM     94  O   CYS A  11      18.471   0.029  27.335  1.00 16.33           O  
ATOM     95  CB  CYS A  11      16.257  -0.260  29.856  1.00 17.51           C  
ATOM     96  SG  CYS A  11      15.732  -1.613  28.690  1.00 18.37           S  
ATOM     97  N   THR A  12      17.249   1.843  27.886  1.00 16.36           N  
ATOM     98  CA  THR A  12      17.193   2.365  26.498  1.00 16.01           C  
ATOM     99  C   THR A  12      18.308   3.369  26.131  1.00 16.36           C  
ATOM    100  O   THR A  12      18.608   3.563  24.949  1.00 16.15           O  
ATOM    101  CB  THR A  12      15.854   3.049  26.225  1.00 14.25           C  
ATOM    102  OG1 THR A  12      15.716   4.193  27.055  1.00 12.64           O  
ATOM    103  CG2 THR A  12      14.658   2.122  26.474  1.00 13.80           C  
ATOM    104  N   VAL A  13      18.904   4.022  27.111  1.00 16.32           N  
ATOM    105  CA  VAL A  13      20.030   4.958  26.847  1.00 16.90           C  
ATOM    106  C   VAL A  13      21.116   4.715  27.889  1.00 17.37           C  
ATOM    107  O   VAL A  13      21.290   5.518  28.820  1.00 17.35           O  
ATOM    108  CB  VAL A  13      19.567   6.415  26.883  1.00 17.02           C  
ATOM    109  CG1 VAL A  13      20.627   7.387  26.342  1.00 17.96           C  
ATOM    110  CG2 VAL A  13      18.309   6.657  26.045  1.00 17.18           C  
ATOM    111  N   PRO A  14      21.851   3.605  27.734  1.00 17.55           N  
ATOM    112  CA  PRO A  14      22.889   3.198  28.671  1.00 17.82           C  
ATOM    113  C   PRO A  14      24.070   4.146  28.734  1.00 17.90           C  
ATOM    114  O   PRO A  14      24.730   4.231  29.812  1.00 18.15           O  
ATOM    115  CB  PRO A  14      23.408   1.895  28.111  1.00 17.81           C  
ATOM    116  CG  PRO A  14      22.666   1.616  26.819  1.00 17.73           C  
ATOM    117  CD  PRO A  14      21.651   2.689  26.604  1.00 17.70           C  
ATOM    118  N   SER A  15      24.311   4.816  27.623  1.00 17.91           N  
ATOM    119  CA  SER A  15      25.500   5.684  27.429  1.00 18.29           C  
ATOM    120  C   SER A  15      25.400   7.075  28.068  1.00 18.01           C  
ATOM    121  O   SER A  15      26.351   7.868  28.015  1.00 18.47           O  
ATOM    122  CB  SER A  15      25.724   5.918  25.934  1.00 19.15           C  
ATOM    123  OG  SER A  15      24.527   6.397  25.333  1.00 21.19           O  
ATOM    124  N   ARG A  16      24.279   7.359  28.662  1.00 17.92           N  
ATOM    125  CA  ARG A  16      24.025   8.678  29.250  1.00 17.41           C  
ATOM    126  C   ARG A  16      23.570   8.512  30.698  1.00 17.24           C  
ATOM    127  O   ARG A  16      22.860   7.563  31.040  1.00 17.26           O  
ATOM    128  CB  ARG A  16      22.932   9.317  28.402  1.00 18.15           C  
ATOM    129  CG  ARG A  16      22.629  10.754  28.714  1.00 19.05           C  
ATOM    130  CD  ARG A  16      22.235  11.512  27.453  1.00 19.38           C  
ATOM    131  NE  ARG A  16      23.112  12.583  27.328  1.00 19.73           N  
ATOM    132  CZ  ARG A  16      23.977  12.938  26.409  1.00 20.25           C  
ATOM    133  NH1 ARG A  16      24.150  12.344  25.224  1.00 20.58           N  
ATOM    134  NH2 ARG A  16      24.796  13.921  26.673  1.00 20.23           N  
ATOM    135  N   SER A  17      23.991   9.429  31.548  1.00 16.90           N  
ATOM    136  CA  SER A  17      23.573   9.402  32.959  1.00 16.25           C  
ATOM    137  C   SER A  17      22.162   9.963  33.023  1.00 15.68           C  
ATOM    138  O   SER A  17      21.832  10.903  32.295  1.00 15.53           O  
ATOM    139  CB  SER A  17      24.509  10.266  33.811  1.00 17.87           C  
ATOM    140  OG  SER A  17      23.993  10.387  35.131  1.00 18.75           O  
ATOM    141  N   TRP A  18      21.336   9.387  33.880  1.00 15.36           N  
ATOM    142  CA  TRP A  18      19.951   9.865  34.022  1.00 14.69           C  
ATOM    143  C   TRP A  18      19.953  11.344  34.429  1.00 14.10           C  
ATOM    144  O   TRP A  18      19.020  12.088  34.110  1.00 13.87           O  
ATOM    145  CB  TRP A  18      19.166   9.053  35.071  1.00 16.01           C  
ATOM    146  CG  TRP A  18      19.752   9.126  36.481  1.00 17.04           C  
ATOM    147  CD1 TRP A  18      20.692   8.328  36.998  1.00 17.70           C  
ATOM    148  CD2 TRP A  18      19.378  10.065  37.481  1.00 17.08           C  
ATOM    149  NE1 TRP A  18      20.944   8.776  38.330  1.00 18.40           N  
ATOM    150  CE2 TRP A  18      20.175   9.808  38.590  1.00 18.35           C  
ATOM    151  CE3 TRP A  18      18.457  11.120  37.532  1.00 17.09           C  
ATOM    152  CZ2 TRP A  18      20.137  10.580  39.757  1.00 18.67           C  
ATOM    153  CZ3 TRP A  18      18.410  11.879  38.719  1.00 18.86           C  
ATOM    154  CH2 TRP A  18      19.216  11.624  39.777  1.00 19.47           C  
ATOM    155  N   TRP A  19      21.012  11.730  35.127  1.00 13.55           N  
ATOM    156  CA  TRP A  19      21.183  13.111  35.630  1.00 13.17           C  
ATOM    157  C   TRP A  19      21.048  14.148  34.512  1.00 12.61           C  
ATOM    158  O   TRP A  19      20.625  15.286  34.749  1.00 12.40           O  
ATOM    159  CB  TRP A  19      22.583  13.319  36.228  1.00 16.15           C  
ATOM    160  CG  TRP A  19      22.705  12.865  37.682  1.00 18.96           C  
ATOM    161  CD1 TRP A  19      23.408  11.820  38.132  1.00 19.60           C  
ATOM    162  CD2 TRP A  19      22.085  13.491  38.798  1.00 20.21           C  
ATOM    163  NE1 TRP A  19      23.223  11.764  39.546  1.00 20.72           N  
ATOM    164  CE2 TRP A  19      22.434  12.746  39.918  1.00 22.12           C  
ATOM    165  CE3 TRP A  19      21.258  14.612  38.956  1.00 21.87           C  
ATOM    166  CZ2 TRP A  19      21.978  13.042  41.209  1.00 23.42           C  
ATOM    167  CZ3 TRP A  19      20.821  14.916  40.263  1.00 23.55           C  
ATOM    168  CH2 TRP A  19      21.163  14.164  41.336  1.00 23.74           C  
ATOM    169  N   ASP A  20      21.416  13.729  33.320  1.00 12.00           N  
ATOM    170  CA  ASP A  20      21.429  14.608  32.139  1.00 11.36           C  
ATOM    171  C   ASP A  20      20.017  14.981  31.680  1.00 10.86           C  
ATOM    172  O   ASP A  20      19.823  15.965  30.948  1.00 10.52           O  
ATOM    173  CB  ASP A  20      22.149  13.914  30.987  1.00 12.71           C  
ATOM    174  CG  ASP A  20      23.668  13.946  31.142  1.00 13.07           C  
ATOM    175  OD1 ASP A  20      24.191  14.202  32.291  1.00 11.87           O  
ATOM    176  OD2 ASP A  20      24.422  13.712  30.127  1.00 14.68           O  
ATOM    177  N   PHE A  21      19.060  14.195  32.118  1.00 10.08           N  
ATOM    178  CA  PHE A  21      17.654  14.395  31.740  1.00 10.12           C  
ATOM    179  C   PHE A  21      16.860  15.069  32.855  1.00  9.85           C  
ATOM    180  O   PHE A  21      15.697  15.443  32.671  1.00  9.87           O  
ATOM    181  CB  PHE A  21      16.973  13.039  31.477  1.00 10.41           C  
ATOM    182  CG  PHE A  21      17.577  12.275  30.302  1.00 10.68           C  
ATOM    183  CD1 PHE A  21      17.311  12.690  28.996  1.00  9.78           C  
ATOM    184  CD2 PHE A  21      18.391  11.161  30.535  1.00 10.36           C  
ATOM    185  CE1 PHE A  21      17.884  12.012  27.918  1.00 10.32           C  
ATOM    186  CE2 PHE A  21      18.972  10.485  29.456  1.00 10.91           C  
ATOM    187  CZ  PHE A  21      18.722  10.916  28.148  1.00 10.59           C  
ATOM    188  N   ALA A  22      17.496  15.219  33.996  1.00 10.06           N  
ATOM    189  CA  ALA A  22      16.816  15.737  35.199  1.00 10.48           C  
ATOM    190  C   ALA A  22      16.653  17.276  35.206  1.00 10.66           C  
ATOM    191  O   ALA A  22      15.834  17.826  35.954  1.00 10.97           O  
ATOM    192  CB  ALA A  22      17.578  15.302  36.448  1.00 10.43           C  
ATOM    193  N   ASP A  23      17.416  17.969  34.382  1.00 10.87           N  
ATOM    194  CA  ASP A  23      17.340  19.452  34.289  1.00 11.07           C  
ATOM    195  C   ASP A  23      17.642  19.872  32.854  1.00 10.83           C  
ATOM    196  O   ASP A  23      18.724  20.396  32.559  1.00 11.05           O  
ATOM    197  CB  ASP A  23      18.360  20.082  35.241  1.00 12.77           C  
ATOM    198  CG  ASP A  23      18.171  21.587  35.440  1.00 15.49           C  
ATOM    199  OD1 ASP A  23      17.158  22.188  34.920  1.00 16.97           O  
ATOM    200  OD2 ASP A  23      19.032  22.256  36.125  1.00 15.73           O  
ATOM    201  N   TYR A  24      16.655  19.641  32.010  1.00 10.96           N  
ATOM    202  CA  TYR A  24      16.792  19.863  30.571  1.00 10.79           C  
ATOM    203  C   TYR A  24      15.531  20.477  29.957  1.00 10.83           C  
ATOM    204  O   TYR A  24      14.409  20.002  30.185  1.00 10.64           O  
ATOM    205  CB  TYR A  24      17.040  18.509  29.911  1.00 11.05           C  
ATOM    206  CG  TYR A  24      17.350  18.611  28.429  1.00 10.68           C  
ATOM    207  CD1 TYR A  24      16.311  18.762  27.504  1.00 10.49           C  
ATOM    208  CD2 TYR A  24      18.676  18.553  28.003  1.00 10.13           C  
ATOM    209  CE1 TYR A  24      16.606  18.842  26.138  1.00 11.35           C  
ATOM    210  CE2 TYR A  24      18.971  18.628  26.641  1.00 10.95           C  
ATOM    211  CZ  TYR A  24      17.938  18.772  25.710  1.00 10.63           C  
ATOM    212  OH  TYR A  24      18.242  18.843  24.387  1.00 13.10           O  
ATOM    213  N   GLY A  25      15.775  21.520  29.182  1.00 10.74           N  
ATOM    214  CA  GLY A  25      14.725  22.249  28.459  1.00 11.00           C  
ATOM    215  C   GLY A  25      13.769  22.901  29.445  1.00 11.07           C  
ATOM    216  O   GLY A  25      14.161  23.278  30.553  1.00 11.42           O  
ATOM    217  N   CYS A  26      12.530  23.003  29.015  1.00 11.20           N  
ATOM    218  CA  CYS A  26      11.473  23.620  29.816  1.00 11.66           C  
ATOM    219  C   CYS A  26      10.617  22.574  30.540  1.00 11.57           C  
ATOM    220  O   CYS A  26       9.796  22.917  31.404  1.00 11.45           O  
ATOM    221  CB  CYS A  26      10.528  24.432  28.918  1.00 14.26           C  
ATOM    222  SG  CYS A  26      11.355  25.892  28.122  1.00 15.59           S  
ATOM    223  N   TYR A  27      10.821  21.295  30.216  1.00 11.53           N  
ATOM    224  CA  TYR A  27       9.940  20.247  30.772  1.00 11.59           C  
ATOM    225  C   TYR A  27      10.617  19.065  31.485  1.00 11.68           C  
ATOM    226  O   TYR A  27       9.992  18.423  32.339  1.00 11.58           O  
ATOM    227  CB  TYR A  27       9.090  19.655  29.666  1.00 10.57           C  
ATOM    228  CG  TYR A  27       7.954  20.593  29.304  1.00 11.75           C  
ATOM    229  CD1 TYR A  27       6.769  20.557  30.040  1.00 11.00           C  
ATOM    230  CD2 TYR A  27       8.110  21.496  28.250  1.00 11.32           C  
ATOM    231  CE1 TYR A  27       5.728  21.427  29.718  1.00 12.78           C  
ATOM    232  CE2 TYR A  27       7.070  22.371  27.930  1.00 12.10           C  
ATOM    233  CZ  TYR A  27       5.878  22.334  28.662  1.00 13.31           C  
ATOM    234  OH  TYR A  27       4.861  23.173  28.340  1.00 16.17           O  
ATOM    235  N   CYS A  28      11.856  18.736  31.148  1.00 11.64           N  
ATOM    236  CA  CYS A  28      12.544  17.605  31.831  1.00 11.89           C  
ATOM    237  C   CYS A  28      13.090  18.126  33.180  1.00 12.30           C  
ATOM    238  O   CYS A  28      14.015  18.951  33.226  1.00 11.83           O  
ATOM    239  CB  CYS A  28      13.653  17.014  30.942  1.00  9.74           C  
ATOM    240  SG  CYS A  28      13.095  16.648  29.184  1.00  9.29           S  
ATOM    241  N   GLY A  29      12.472  17.614  34.233  1.00 12.82           N  
ATOM    242  CA  GLY A  29      12.728  18.004  35.638  1.00 13.45           C  
ATOM    243  C   GLY A  29      11.354  18.140  36.313  1.00 13.94           C  
ATOM    244  O   GLY A  29      10.319  17.853  35.704  1.00 13.96           O  
ATOM    245  N   ARG A  30      11.320  18.574  37.565  1.00 14.60           N  
ATOM    246  CA  ARG A  30      10.026  18.728  38.286  1.00 15.20           C  
ATOM    247  C   ARG A  30       9.246  19.879  37.645  1.00 15.33           C  
ATOM    248  O   ARG A  30       9.759  20.994  37.516  1.00 15.37           O  
ATOM    249  CB  ARG A  30      10.274  19.020  39.771  1.00 19.12           C  
ATOM    250  CG  ARG A  30       9.026  18.915  40.697  1.00 22.51           C  
ATOM    251  CD  ARG A  30       9.482  18.980  42.152  1.00 26.17           C  
ATOM    252  NE  ARG A  30      10.917  19.098  42.082  1.00 30.09           N  
ATOM    253  CZ  ARG A  30      11.760  19.729  42.873  1.00 33.31           C  
ATOM    254  NH1 ARG A  30      11.407  20.285  44.035  1.00 34.65           N  
ATOM    255  NH2 ARG A  30      13.012  19.939  42.493  1.00 33.99           N  
ATOM    256  N   GLY A  31       8.026  19.566  37.237  1.00 15.50           N  
ATOM    257  CA  GLY A  31       7.119  20.543  36.596  1.00 15.92           C  
ATOM    258  C   GLY A  31       7.538  20.801  35.140  1.00 16.17           C  
ATOM    259  O   GLY A  31       8.231  19.983  34.518  1.00 15.93           O  
ATOM    260  N   GLY A  32       7.081  21.939  34.632  1.00 16.52           N  
ATOM    261  CA  GLY A  32       7.397  22.383  33.263  1.00 17.26           C  
ATOM    262  C   GLY A  32       6.269  23.243  32.680  1.00 17.51           C  
ATOM    263  O   GLY A  32       5.096  23.103  33.049  1.00 17.93           O  
ATOM    264  N   SER A  33       6.671  24.116  31.776  1.00 17.64           N  
ATOM    265  CA  SER A  33       5.753  25.011  31.055  1.00 17.73           C  
ATOM    266  C   SER A  33       6.528  25.736  29.956  1.00 17.45           C  
ATOM    267  O   SER A  33       7.762  25.661  29.898  1.00 17.74           O  
ATOM    268  CB  SER A  33       5.133  26.022  32.016  1.00 19.47           C  
ATOM    269  OG  SER A  33       6.153  26.804  32.609  1.00 22.08           O  
ATOM    270  N   GLY A  34       5.777  26.417  29.112  1.00 17.45           N  
ATOM    271  CA  GLY A  34       6.335  27.159  27.973  1.00 16.98           C  
ATOM    272  C   GLY A  34       6.311  26.260  26.736  1.00 16.83           C  
ATOM    273  O   GLY A  34       5.559  25.281  26.674  1.00 16.84           O  
ATOM    274  N   THR A  35       7.136  26.616  25.780  1.00 16.69           N  
ATOM    275  CA  THR A  35       7.259  25.873  24.516  1.00 16.39           C  
ATOM    276  C   THR A  35       8.379  24.852  24.603  1.00 15.74           C  
ATOM    277  O   THR A  35       9.517  25.214  24.937  1.00 15.83           O  
ATOM    278  CB  THR A  35       7.650  26.837  23.386  1.00 19.86           C  
ATOM    279  OG1 THR A  35       6.926  28.049  23.519  1.00 23.20           O  
ATOM    280  CG2 THR A  35       7.390  26.277  21.982  1.00 20.54           C  
ATOM    281  N   PRO A  36       8.151  23.550  24.307  1.00 15.33           N  
ATOM    282  CA  PRO A  36       9.244  22.601  24.303  1.00 14.66           C  
ATOM    283  C   PRO A  36      10.319  23.157  23.412  1.00 14.28           C  
ATOM    284  O   PRO A  36       9.998  23.729  22.332  1.00 14.35           O  
ATOM    285  CB  PRO A  36       8.612  21.307  23.859  1.00 14.82           C  
ATOM    286  CG  PRO A  36       7.124  21.555  23.688  1.00 14.91           C  
ATOM    287  CD  PRO A  36       6.833  22.995  23.998  1.00 15.00           C  
ATOM    288  N   VAL A  37      11.520  22.971  23.870  1.00 13.71           N  
ATOM    289  CA  VAL A  37      12.725  23.546  23.276  1.00 13.07           C  
ATOM    290  C   VAL A  37      13.259  22.684  22.099  1.00 12.62           C  
ATOM    291  O   VAL A  37      13.922  23.179  21.170  1.00 12.67           O  
ATOM    292  CB  VAL A  37      13.663  23.723  24.470  1.00 12.15           C  
ATOM    293  CG1 VAL A  37      15.063  23.168  24.274  1.00 11.60           C  
ATOM    294  CG2 VAL A  37      13.805  25.192  24.875  1.00 12.91           C  
ATOM    295  N   ASP A  38      12.960  21.412  22.128  1.00 12.28           N  
ATOM    296  CA  ASP A  38      13.377  20.482  21.064  1.00 11.65           C  
ATOM    297  C   ASP A  38      12.615  19.169  21.271  1.00 11.47           C  
ATOM    298  O   ASP A  38      11.702  19.089  22.100  1.00 11.08           O  
ATOM    299  CB  ASP A  38      14.905  20.319  21.079  1.00 10.50           C  
ATOM    300  CG  ASP A  38      15.456  19.758  22.382  1.00 10.50           C  
ATOM    301  OD1 ASP A  38      14.652  19.330  23.285  1.00 11.48           O  
ATOM    302  OD2 ASP A  38      16.730  19.702  22.567  1.00 10.56           O  
ATOM    303  N   ASP A  39      12.981  18.148  20.526  1.00 11.11           N  
ATOM    304  CA  ASP A  39      12.255  16.863  20.586  1.00 11.14           C  
ATOM    305  C   ASP A  39      12.375  16.168  21.940  1.00 10.61           C  
ATOM    306  O   ASP A  39      11.408  15.572  22.426  1.00 10.79           O  
ATOM    307  CB  ASP A  39      12.740  15.925  19.506  1.00 11.94           C  
ATOM    308  CG  ASP A  39      12.322  16.441  18.147  1.00 13.22           C  
ATOM    309  OD1 ASP A  39      11.156  16.968  18.007  1.00 15.27           O  
ATOM    310  OD2 ASP A  39      13.137  16.374  17.166  1.00 16.20           O  
ATOM    311  N   LEU A  40      13.549  16.225  22.533  1.00 10.52           N  
ATOM    312  CA  LEU A  40      13.764  15.591  23.847  1.00 10.08           C  
ATOM    313  C   LEU A  40      12.841  16.244  24.892  1.00  9.56           C  
ATOM    314  O   LEU A  40      12.243  15.557  25.731  1.00  9.52           O  
ATOM    315  CB  LEU A  40      15.228  15.724  24.275  1.00 11.06           C  
ATOM    316  CG  LEU A  40      15.569  14.928  25.542  1.00 12.18           C  
ATOM    317  CD1 LEU A  40      15.372  13.418  25.379  1.00 12.83           C  
ATOM    318  CD2 LEU A  40      17.024  15.111  25.980  1.00 11.86           C  
ATOM    319  N   ASP A  41      12.747  17.567  24.820  1.00  9.19           N  
ATOM    320  CA  ASP A  41      11.893  18.349  25.738  1.00  9.13           C  
ATOM    321  C   ASP A  41      10.426  17.950  25.563  1.00  9.11           C  
ATOM    322  O   ASP A  41       9.651  17.934  26.531  1.00  8.86           O  
ATOM    323  CB  ASP A  41      12.017  19.851  25.462  1.00  7.80           C  
ATOM    324  CG  ASP A  41      11.786  20.716  26.708  1.00  7.19           C  
ATOM    325  OD1 ASP A  41      11.726  20.175  27.874  1.00  6.44           O  
ATOM    326  OD2 ASP A  41      11.668  21.991  26.594  1.00  7.78           O  
ATOM    327  N   ARG A  42      10.073  17.637  24.322  1.00  9.12           N  
ATOM    328  CA  ARG A  42       8.698  17.230  23.989  1.00  9.47           C  
ATOM    329  C   ARG A  42       8.430  15.835  24.576  1.00  8.88           C  
ATOM    330  O   ARG A  42       7.294  15.491  24.909  1.00  9.25           O  
ATOM    331  CB  ARG A  42       8.466  17.310  22.466  1.00 12.99           C  
ATOM    332  CG  ARG A  42       8.542  18.779  21.982  1.00 18.09           C  
ATOM    333  CD  ARG A  42       7.967  19.072  20.582  1.00 23.41           C  
ATOM    334  NE  ARG A  42       8.103  17.974  19.679  1.00 27.58           N  
ATOM    335  CZ  ARG A  42       8.161  17.975  18.345  1.00 30.32           C  
ATOM    336  NH1 ARG A  42       8.197  19.088  17.586  1.00 31.31           N  
ATOM    337  NH2 ARG A  42       8.108  16.840  17.677  1.00 32.03           N  
ATOM    338  N   CYS A  43       9.476  15.035  24.724  1.00  8.73           N  
ATOM    339  CA  CYS A  43       9.324  13.712  25.357  1.00  8.16           C  
ATOM    340  C   CYS A  43       8.848  13.904  26.806  1.00  7.77           C  
ATOM    341  O   CYS A  43       7.962  13.191  27.295  1.00  7.61           O  
ATOM    342  CB  CYS A  43      10.653  12.954  25.388  1.00  7.72           C  
ATOM    343  SG  CYS A  43      11.186  12.340  23.722  1.00  7.51           S  
ATOM    344  N   CYS A  44       9.461  14.878  27.455  1.00  7.34           N  
ATOM    345  CA  CYS A  44       9.170  15.216  28.859  1.00  7.22           C  
ATOM    346  C   CYS A  44       7.788  15.863  28.997  1.00  7.11           C  
ATOM    347  O   CYS A  44       7.032  15.569  29.937  1.00  6.77           O  
ATOM    348  CB  CYS A  44      10.245  16.157  29.388  1.00  8.76           C  
ATOM    349  SG  CYS A  44      11.889  15.304  29.516  1.00  9.80           S  
ATOM    350  N   GLN A  45       7.467  16.744  28.066  1.00  7.07           N  
ATOM    351  CA  GLN A  45       6.161  17.416  28.080  1.00  8.11           C  
ATOM    352  C   GLN A  45       5.045  16.369  28.014  1.00  8.15           C  
ATOM    353  O   GLN A  45       4.047  16.442  28.741  1.00  8.53           O  
ATOM    354  CB  GLN A  45       6.007  18.373  26.892  1.00  9.04           C  
ATOM    355  CG  GLN A  45       4.657  19.104  26.903  1.00 13.46           C  
ATOM    356  CD  GLN A  45       4.385  19.902  25.626  1.00 14.76           C  
ATOM    357  OE1 GLN A  45       4.831  19.517  24.547  1.00 17.71           O  
ATOM    358  NE2 GLN A  45       3.677  21.012  25.681  1.00 14.91           N  
ATOM    359  N   VAL A  46       5.235  15.399  27.139  1.00  8.49           N  
ATOM    360  CA  VAL A  46       4.248  14.324  26.942  1.00  8.57           C  
ATOM    361  C   VAL A  46       4.154  13.454  28.202  1.00  8.37           C  
ATOM    362  O   VAL A  46       3.054  13.057  28.618  1.00  8.43           O  
ATOM    363  CB  VAL A  46       4.649  13.458  25.747  1.00 11.28           C  
ATOM    364  CG1 VAL A  46       4.170  12.008  25.874  1.00 12.43           C  
ATOM    365  CG2 VAL A  46       4.083  13.981  24.422  1.00 12.02           C  
ATOM    366  N   HIS A  47       5.325  13.196  28.762  1.00  8.49           N  
ATOM    367  CA  HIS A  47       5.487  12.373  29.976  1.00  8.58           C  
ATOM    368  C   HIS A  47       4.779  13.042  31.158  1.00  9.10           C  
ATOM    369  O   HIS A  47       4.060  12.391  31.928  1.00  8.89           O  
ATOM    370  CB  HIS A  47       6.976  12.203  30.278  1.00  6.96           C  
ATOM    371  CG  HIS A  47       7.259  11.288  31.469  1.00  7.37           C  
ATOM    372  ND1 HIS A  47       8.131  11.665  32.480  1.00  8.20           N  
ATOM    373  CD2 HIS A  47       6.802  10.052  31.803  1.00  6.32           C  
ATOM    374  CE1 HIS A  47       8.194  10.682  33.358  1.00  8.35           C  
ATOM    375  NE2 HIS A  47       7.409   9.711  32.967  1.00  6.39           N  
ATOM    376  N   ASP A  48       4.992  14.339  31.276  1.00  9.46           N  
ATOM    377  CA  ASP A  48       4.350  15.136  32.330  1.00 10.02           C  
ATOM    378  C   ASP A  48       2.821  15.023  32.217  1.00 10.05           C  
ATOM    379  O   ASP A  48       2.104  14.868  33.211  1.00 10.01           O  
ATOM    380  CB  ASP A  48       4.745  16.610  32.206  1.00  9.84           C  
ATOM    381  CG  ASP A  48       6.145  16.892  32.741  1.00 11.16           C  
ATOM    382  OD1 ASP A  48       6.923  15.915  33.049  1.00 11.30           O  
ATOM    383  OD2 ASP A  48       6.546  18.106  32.886  1.00 12.03           O  
ATOM    384  N   ASN A  49       2.327  15.097  31.000  1.00 10.36           N  
ATOM    385  CA  ASN A  49       0.878  15.037  30.756  1.00 10.72           C  
ATOM    386  C   ASN A  49       0.335  13.632  31.061  1.00 10.35           C  
ATOM    387  O   ASN A  49      -0.811  13.473  31.508  1.00 10.35           O  
ATOM    388  CB  ASN A  49       0.586  15.446  29.318  1.00 16.79           C  
ATOM    389  CG  ASN A  49       0.746  16.955  29.121  1.00 22.50           C  
ATOM    390  OD1 ASN A  49      -0.103  17.731  29.570  1.00 25.92           O  
ATOM    391  ND2 ASN A  49       1.795  17.423  28.472  1.00 24.14           N  
ATOM    392  N   CYS A  50       1.170  12.639  30.821  1.00 10.18           N  
ATOM    393  CA  CYS A  50       0.815  11.230  31.064  1.00  9.97           C  
ATOM    394  C   CYS A  50       0.612  10.994  32.566  1.00  9.87           C  
ATOM    395  O   CYS A  50      -0.321  10.290  32.982  1.00  9.12           O  
ATOM    396  CB  CYS A  50       1.927  10.317  30.536  1.00 10.09           C  
ATOM    397  SG  CYS A  50       1.339   8.582  30.223  1.00  9.80           S  
ATOM    398  N   TYR A  51       1.498  11.597  33.341  1.00  9.85           N  
ATOM    399  CA  TYR A  51       1.469  11.501  34.811  1.00 10.35           C  
ATOM    400  C   TYR A  51       0.198  12.177  35.351  1.00 10.43           C  
ATOM    401  O   TYR A  51      -0.477  11.652  36.248  1.00 10.43           O  
ATOM    402  CB  TYR A  51       2.700  12.194  35.412  1.00  9.50           C  
ATOM    403  CG  TYR A  51       3.880  11.244  35.681  1.00  8.31           C  
ATOM    404  CD1 TYR A  51       3.936   9.986  35.062  1.00  7.81           C  
ATOM    405  CD2 TYR A  51       4.911  11.636  36.548  1.00  7.77           C  
ATOM    406  CE1 TYR A  51       5.019   9.126  35.312  1.00  7.83           C  
ATOM    407  CE2 TYR A  51       5.990  10.777  36.796  1.00  7.55           C  
ATOM    408  CZ  TYR A  51       6.045   9.522  36.179  1.00  7.35           C  
ATOM    409  OH  TYR A  51       7.093   8.689  36.424  1.00  6.80           O  
ATOM    410  N   ASN A  52      -0.092  13.335  34.778  1.00 10.71           N  
ATOM    411  CA  ASN A  52      -1.267  14.141  35.156  1.00 10.92           C  
ATOM    412  C   ASN A  52      -2.554  13.346  34.912  1.00 11.06           C  
ATOM    413  O   ASN A  52      -3.553  13.508  35.627  1.00 10.90           O  
ATOM    414  CB  ASN A  52      -1.308  15.432  34.336  1.00 14.88           C  
ATOM    415  CG  ASN A  52      -0.352  16.504  34.867  1.00 17.29           C  
ATOM    416  OD1 ASN A  52       0.001  17.429  34.138  1.00 19.27           O  
ATOM    417  ND2 ASN A  52       0.094  16.435  36.108  1.00 18.56           N  
ATOM    418  N   GLU A  53      -2.497  12.499  33.900  1.00 11.09           N  
ATOM    419  CA  GLU A  53      -3.630  11.638  33.530  1.00 11.50           C  
ATOM    420  C   GLU A  53      -3.758  10.490  34.535  1.00 11.38           C  
ATOM    421  O   GLU A  53      -4.866  10.097  34.923  1.00 11.55           O  
ATOM    422  CB  GLU A  53      -3.421  11.036  32.136  1.00 13.13           C  
ATOM    423  CG  GLU A  53      -3.754  12.004  30.995  1.00 15.03           C  
ATOM    424  CD  GLU A  53      -5.146  12.631  31.112  1.00 16.85           C  
ATOM    425  OE1 GLU A  53      -6.187  11.880  31.247  1.00 16.81           O  
ATOM    426  OE2 GLU A  53      -5.280  13.913  31.073  1.00 20.42           O  
ATOM    427  N   ALA A  54      -2.603   9.986  34.931  1.00 11.34           N  
ATOM    428  CA  ALA A  54      -2.505   8.862  35.875  1.00 11.42           C  
ATOM    429  C   ALA A  54      -2.947   9.288  37.282  1.00 11.65           C  
ATOM    430  O   ALA A  54      -3.410   8.463  38.082  1.00 11.68           O  
ATOM    431  CB  ALA A  54      -1.061   8.358  35.944  1.00  9.20           C  
ATOM    432  N   GLU A  55      -2.799  10.574  37.550  1.00 11.82           N  
ATOM    433  CA  GLU A  55      -3.144  11.155  38.861  1.00 12.07           C  
ATOM    434  C   GLU A  55      -4.662  11.217  39.063  1.00 12.11           C  
ATOM    435  O   GLU A  55      -5.148  11.396  40.188  1.00 12.18           O  
ATOM    436  CB  GLU A  55      -2.582  12.572  38.983  1.00 14.67           C  
ATOM    437  CG  GLU A  55      -1.055  12.611  38.922  1.00 17.62           C  
ATOM    438  CD  GLU A  55      -0.465  13.927  39.432  1.00 20.42           C  
ATOM    439  OE1 GLU A  55      -1.159  15.012  39.372  1.00 21.98           O  
ATOM    440  OE2 GLU A  55       0.729  13.951  39.920  1.00 22.96           O  
ATOM    441  N   LYS A  56      -5.393  11.068  37.971  1.00 11.96           N  
ATOM    442  CA  LYS A  56      -6.865  11.095  38.022  1.00 12.25           C  
ATOM    443  C   LYS A  56      -7.398   9.761  38.559  1.00 12.45           C  
ATOM    444  O   LYS A  56      -8.571   9.647  38.936  1.00 13.02           O  
ATOM    445  CB  LYS A  56      -7.459  11.360  36.646  1.00 12.16           C  
ATOM    446  CG  LYS A  56      -7.306  12.811  36.188  1.00 11.03           C  
ATOM    447  CD  LYS A  56      -7.430  12.940  34.673  1.00 12.28           C  
ATOM    448  CE  LYS A  56      -7.436  14.381  34.176  1.00 12.38           C  
ATOM    449  NZ  LYS A  56      -7.646  14.470  32.723  1.00 12.85           N  
ATOM    450  N   ILE A  57      -6.525   8.765  38.573  1.00 12.58           N  
ATOM    451  CA  ILE A  57      -6.852   7.458  39.162  1.00 12.59           C  
ATOM    452  C   ILE A  57      -6.721   7.653  40.673  1.00 12.85           C  
ATOM    453  O   ILE A  57      -5.653   8.016  41.184  1.00 12.70           O  
ATOM    454  CB  ILE A  57      -5.913   6.380  38.596  1.00 12.41           C  
ATOM    455  CG1 ILE A  57      -6.177   6.110  37.107  1.00 12.65           C  
ATOM    456  CG2 ILE A  57      -6.052   5.025  39.302  1.00 12.33           C  
ATOM    457  CD1 ILE A  57      -4.930   5.687  36.327  1.00 13.44           C  
ATOM    458  N   SER A  58      -7.815   7.442  41.374  1.00 12.96           N  
ATOM    459  CA  SER A  58      -7.850   7.700  42.819  1.00 13.38           C  
ATOM    460  C   SER A  58      -6.775   6.867  43.529  1.00 12.94           C  
ATOM    461  O   SER A  58      -6.649   5.653  43.307  1.00 13.28           O  
ATOM    462  CB  SER A  58      -9.261   7.448  43.375  1.00 17.51           C  
ATOM    463  OG  SER A  58      -9.477   6.072  43.616  1.00 19.69           O  
ATOM    464  N   GLY A  59      -6.023   7.592  44.343  1.00 12.69           N  
ATOM    465  CA  GLY A  59      -4.933   7.045  45.166  1.00 12.28           C  
ATOM    466  C   GLY A  59      -3.673   6.776  44.332  1.00 12.20           C  
ATOM    467  O   GLY A  59      -2.754   6.071  44.774  1.00 12.09           O  
ATOM    468  N   CYS A  60      -3.639   7.341  43.137  1.00 11.81           N  
ATOM    469  CA  CYS A  60      -2.500   7.145  42.221  1.00 11.85           C  
ATOM    470  C   CYS A  60      -1.535   8.338  42.249  1.00 11.71           C  
ATOM    471  O   CYS A  60      -1.897   9.465  41.880  1.00 11.71           O  
ATOM    472  CB  CYS A  60      -2.984   6.965  40.780  1.00 11.02           C  
ATOM    473  SG  CYS A  60      -1.648   6.318  39.659  1.00 10.75           S  
ATOM    474  N   TRP A  61      -0.324   8.029  42.691  1.00 11.87           N  
ATOM    475  CA  TRP A  61       0.793   8.991  42.752  1.00 12.04           C  
ATOM    476  C   TRP A  61       1.946   8.417  41.926  1.00 11.65           C  
ATOM    477  O   TRP A  61       2.708   7.560  42.404  1.00 12.06           O  
ATOM    478  CB  TRP A  61       1.195   9.252  44.205  1.00 17.79           C  
ATOM    479  CG  TRP A  61      -0.020   9.537  45.087  1.00 22.43           C  
ATOM    480  CD1 TRP A  61      -0.605   8.670  45.904  1.00 24.29           C  
ATOM    481  CD2 TRP A  61      -0.732  10.780  45.178  1.00 24.79           C  
ATOM    482  NE1 TRP A  61      -1.721   9.328  46.494  1.00 26.58           N  
ATOM    483  CE2 TRP A  61      -1.792  10.556  46.047  1.00 26.05           C  
ATOM    484  CE3 TRP A  61      -0.602  12.053  44.592  1.00 27.71           C  
ATOM    485  CZ2 TRP A  61      -2.765  11.515  46.352  1.00 28.55           C  
ATOM    486  CZ3 TRP A  61      -1.582  13.023  44.915  1.00 28.35           C  
ATOM    487  CH2 TRP A  61      -2.614  12.762  45.751  1.00 28.93           C  
ATOM    488  N   PRO A  62       2.090   8.887  40.680  1.00 11.36           N  
ATOM    489  CA  PRO A  62       3.078   8.363  39.741  1.00 11.31           C  
ATOM    490  C   PRO A  62       4.503   8.323  40.268  1.00 11.36           C  
ATOM    491  O   PRO A  62       5.217   7.299  40.046  1.00 11.36           O  
ATOM    492  CB  PRO A  62       2.912   9.232  38.515  1.00 11.20           C  
ATOM    493  CG  PRO A  62       1.764  10.193  38.775  1.00 11.14           C  
ATOM    494  CD  PRO A  62       1.242   9.962  40.155  1.00 11.15           C  
ATOM    495  N   TYR A  63       4.934   9.364  40.935  1.00 11.24           N  
ATOM    496  CA  TYR A  63       6.319   9.442  41.448  1.00 11.48           C  
ATOM    497  C   TYR A  63       6.704   8.255  42.358  1.00 11.52           C  
ATOM    498  O   TYR A  63       7.863   7.805  42.373  1.00 11.42           O  
ATOM    499  CB  TYR A  63       6.499  10.664  42.351  1.00 12.46           C  
ATOM    500  CG  TYR A  63       6.813  11.980  41.636  1.00 13.82           C  
ATOM    501  CD1 TYR A  63       6.255  12.269  40.381  1.00 13.63           C  
ATOM    502  CD2 TYR A  63       7.664  12.901  42.255  1.00 16.00           C  
ATOM    503  CE1 TYR A  63       6.517  13.507  39.771  1.00 15.38           C  
ATOM    504  CE2 TYR A  63       7.915  14.138  41.653  1.00 17.15           C  
ATOM    505  CZ  TYR A  63       7.335  14.446  40.418  1.00 17.06           C  
ATOM    506  OH  TYR A  63       7.548  15.670  39.863  1.00 18.27           O  
ATOM    507  N   PHE A  64       5.720   7.764  43.095  1.00 11.73           N  
ATOM    508  CA  PHE A  64       5.960   6.780  44.168  1.00 11.73           C  
ATOM    509  C   PHE A  64       5.463   5.344  43.890  1.00 11.72           C  
ATOM    510  O   PHE A  64       5.942   4.377  44.503  1.00 11.95           O  
ATOM    511  CB  PHE A  64       5.272   7.290  45.437  1.00 11.57           C  
ATOM    512  CG  PHE A  64       5.724   8.712  45.799  1.00 11.90           C  
ATOM    513  CD1 PHE A  64       7.012   8.921  46.297  1.00 12.31           C  
ATOM    514  CD2 PHE A  64       4.858   9.804  45.630  1.00 12.37           C  
ATOM    515  CE1 PHE A  64       7.442  10.213  46.618  1.00 13.56           C  
ATOM    516  CE2 PHE A  64       5.289  11.098  45.948  1.00 12.80           C  
ATOM    517  CZ  PHE A  64       6.582  11.302  46.441  1.00 12.43           C  
ATOM    518  N   LYS A  65       4.518   5.179  42.984  1.00 11.66           N  
ATOM    519  CA  LYS A  65       3.946   3.836  42.713  1.00 12.00           C  
ATOM    520  C   LYS A  65       4.944   2.936  41.973  1.00 11.77           C  
ATOM    521  O   LYS A  65       5.453   3.280  40.897  1.00 11.79           O  
ATOM    522  CB  LYS A  65       2.670   3.940  41.871  1.00 12.62           C  
ATOM    523  CG  LYS A  65       1.857   2.634  41.845  1.00 13.38           C  
ATOM    524  CD  LYS A  65       1.457   2.150  43.242  1.00 15.71           C  
ATOM    525  CE  LYS A  65       0.790   0.772  43.246  1.00 16.77           C  
ATOM    526  NZ  LYS A  65      -0.046   0.552  44.438  1.00 17.99           N  
ATOM    527  N   THR A  66       5.197   1.793  42.589  1.00 11.80           N  
ATOM    528  CA  THR A  66       6.090   0.773  42.028  1.00 11.79           C  
ATOM    529  C   THR A  66       5.257  -0.136  41.126  1.00 11.64           C  
ATOM    530  O   THR A  66       4.107  -0.467  41.447  1.00 11.46           O  
ATOM    531  CB  THR A  66       6.745  -0.041  43.153  1.00 13.73           C  
ATOM    532  OG1 THR A  66       5.777  -0.871  43.778  1.00 14.47           O  
ATOM    533  CG2 THR A  66       7.383   0.837  44.236  1.00 12.44           C  
ATOM    534  N   TYR A  67       5.856  -0.500  40.012  1.00 11.77           N  
ATOM    535  CA  TYR A  67       5.204  -1.349  39.007  1.00 12.22           C  
ATOM    536  C   TYR A  67       6.160  -2.471  38.582  1.00 12.64           C  
ATOM    537  O   TYR A  67       7.341  -2.479  38.956  1.00 12.76           O  
ATOM    538  CB  TYR A  67       4.803  -0.486  37.789  1.00  9.88           C  
ATOM    539  CG  TYR A  67       5.906   0.476  37.297  1.00  9.37           C  
ATOM    540  CD1 TYR A  67       7.076  -0.032  36.717  1.00  9.48           C  
ATOM    541  CD2 TYR A  67       5.748   1.868  37.419  1.00  7.41           C  
ATOM    542  CE1 TYR A  67       8.074   0.841  36.255  1.00  9.41           C  
ATOM    543  CE2 TYR A  67       6.745   2.739  36.955  1.00  8.06           C  
ATOM    544  CZ  TYR A  67       7.906   2.226  36.370  1.00  9.06           C  
ATOM    545  OH  TYR A  67       8.869   3.071  35.909  1.00  7.60           O  
ATOM    546  N   SER A  68       5.628  -3.418  37.821  1.00 13.09           N  
ATOM    547  CA  SER A  68       6.441  -4.520  37.272  1.00 13.53           C  
ATOM    548  C   SER A  68       6.672  -4.291  35.789  1.00 13.68           C  
ATOM    549  O   SER A  68       5.743  -3.959  35.042  1.00 13.43           O  
ATOM    550  CB  SER A  68       5.762  -5.888  37.400  1.00 16.18           C  
ATOM    551  OG  SER A  68       4.711  -5.842  38.340  1.00 18.96           O  
ATOM    552  N   TYR A  69       7.903  -4.485  35.416  1.00 14.08           N  
ATOM    553  CA  TYR A  69       8.350  -4.335  34.038  1.00 15.10           C  
ATOM    554  C   TYR A  69       9.660  -5.084  33.885  1.00 15.72           C  
ATOM    555  O   TYR A  69      10.298  -5.461  34.875  1.00 15.85           O  
ATOM    556  CB  TYR A  69       8.593  -2.857  33.738  1.00 14.50           C  
ATOM    557  CG  TYR A  69       9.928  -2.397  34.308  1.00 12.94           C  
ATOM    558  CD1 TYR A  69      10.041  -2.134  35.676  1.00 14.19           C  
ATOM    559  CD2 TYR A  69      11.034  -2.253  33.466  1.00 13.86           C  
ATOM    560  CE1 TYR A  69      11.275  -1.751  36.209  1.00 14.30           C  
ATOM    561  CE2 TYR A  69      12.267  -1.866  33.998  1.00 13.97           C  
ATOM    562  CZ  TYR A  69      12.389  -1.622  35.372  1.00 15.03           C  
ATOM    563  OH  TYR A  69      13.592  -1.272  35.897  1.00 17.25           O  
ATOM    564  N   GLU A  70      10.041  -5.296  32.656  1.00 16.31           N  
ATOM    565  CA  GLU A  70      11.307  -5.954  32.361  1.00 17.44           C  
ATOM    566  C   GLU A  70      11.977  -5.254  31.196  1.00 17.73           C  
ATOM    567  O   GLU A  70      11.312  -4.777  30.267  1.00 17.70           O  
ATOM    568  CB  GLU A  70      11.083  -7.429  32.015  1.00 21.33           C  
ATOM    569  CG  GLU A  70      11.701  -7.844  30.678  1.00 26.20           C  
ATOM    570  CD  GLU A  70      11.022  -9.074  30.080  1.00 29.42           C  
ATOM    571  OE1 GLU A  70      10.823 -10.117  30.812  1.00 31.16           O  
ATOM    572  OE2 GLU A  70      10.647  -9.061  28.849  1.00 30.28           O  
ATOM    573  N   CYS A  71      13.277  -5.194  31.297  1.00 18.42           N  
ATOM    574  CA  CYS A  71      14.116  -4.641  30.243  1.00 19.44           C  
ATOM    575  C   CYS A  71      14.805  -5.812  29.558  1.00 20.12           C  
ATOM    576  O   CYS A  71      15.451  -6.638  30.211  1.00 20.09           O  
ATOM    577  CB  CYS A  71      15.158  -3.689  30.833  1.00 18.04           C  
ATOM    578  SG  CYS A  71      16.563  -3.353  29.666  1.00 18.36           S  
ATOM    579  N   SER A  72      14.644  -5.881  28.256  1.00 21.08           N  
ATOM    580  CA  SER A  72      15.260  -6.954  27.458  1.00 22.28           C  
ATOM    581  C   SER A  72      15.871  -6.344  26.202  1.00 22.63           C  
ATOM    582  O   SER A  72      15.161  -5.801  25.340  1.00 22.90           O  
ATOM    583  CB  SER A  72      14.215  -8.012  27.121  1.00 25.13           C  
ATOM    584  OG  SER A  72      14.168  -8.222  25.723  1.00 28.60           O  
ATOM    585  N   GLN A  73      17.180  -6.471  26.147  1.00 23.29           N  
ATOM    586  CA  GLN A  73      17.989  -5.855  25.100  1.00 23.91           C  
ATOM    587  C   GLN A  73      17.936  -4.346  25.375  1.00 23.78           C  
ATOM    588  O   GLN A  73      18.579  -3.853  26.314  1.00 24.39           O  
ATOM    589  CB  GLN A  73      17.447  -6.228  23.713  1.00 27.80           C  
ATOM    590  CG  GLN A  73      16.835  -7.639  23.645  1.00 31.11           C  
ATOM    591  CD  GLN A  73      17.738  -8.754  24.197  1.00 32.61           C  
ATOM    592  OE1 GLN A  73      17.963  -8.831  25.405  1.00 33.64           O  
ATOM    593  NE2 GLN A  73      18.265  -9.647  23.376  1.00 33.32           N  
ATOM    594  N   GLY A  74      17.153  -3.654  24.572  1.00 23.51           N  
ATOM    595  CA  GLY A  74      16.940  -2.204  24.721  1.00 22.46           C  
ATOM    596  C   GLY A  74      15.444  -1.900  24.604  1.00 21.93           C  
ATOM    597  O   GLY A  74      15.033  -0.755  24.362  1.00 22.18           O  
ATOM    598  N   THR A  75      14.665  -2.953  24.768  1.00 21.34           N  
ATOM    599  CA  THR A  75      13.201  -2.866  24.704  1.00 20.36           C  
ATOM    600  C   THR A  75      12.639  -3.050  26.120  1.00 19.80           C  
ATOM    601  O   THR A  75      13.219  -3.769  26.947  1.00 19.98           O  
ATOM    602  CB  THR A  75      12.652  -3.906  23.720  1.00 19.98           C  
ATOM    603  OG1 THR A  75      12.317  -5.101  24.407  1.00 18.96           O  
ATOM    604  CG2 THR A  75      13.647  -4.265  22.610  1.00 20.70           C  
ATOM    605  N   LEU A  76      11.526  -2.381  26.330  1.00 19.22           N  
ATOM    606  CA  LEU A  76      10.830  -2.295  27.629  1.00 18.46           C  
ATOM    607  C   LEU A  76       9.396  -2.851  27.537  1.00 18.03           C  
ATOM    608  O   LEU A  76       8.679  -2.593  26.563  1.00 18.49           O  
ATOM    609  CB  LEU A  76      10.649  -0.803  27.956  1.00 17.34           C  
ATOM    610  CG  LEU A  76      11.716  -0.206  28.715  1.00 17.09           C  
ATOM    611  CD1 LEU A  76      12.115   1.271  28.600  1.00 14.71           C  
ATOM    612  CD2 LEU A  76      12.600  -0.800  29.810  1.00 13.35           C  
ATOM    613  N   THR A  77       8.990  -3.597  28.561  1.00 17.45           N  
ATOM    614  CA  THR A  77       7.595  -4.098  28.666  1.00 16.71           C  
ATOM    615  C   THR A  77       7.141  -4.176  30.124  1.00 15.87           C  
ATOM    616  O   THR A  77       7.877  -4.665  30.994  1.00 16.17           O  
ATOM    617  CB  THR A  77       7.401  -5.512  28.098  1.00 18.07           C  
ATOM    618  OG1 THR A  77       8.427  -5.833  27.177  1.00 20.55           O  
ATOM    619  CG2 THR A  77       6.055  -5.669  27.373  1.00 18.84           C  
ATOM    620  N   CYS A  78       5.929  -3.686  30.331  1.00 15.37           N  
ATOM    621  CA  CYS A  78       5.258  -3.722  31.642  1.00 14.65           C  
ATOM    622  C   CYS A  78       4.662  -5.122  31.813  1.00 14.61           C  
ATOM    623  O   CYS A  78       4.067  -5.680  30.879  1.00 14.22           O  
ATOM    624  CB  CYS A  78       4.173  -2.647  31.691  1.00 12.27           C  
ATOM    625  SG  CYS A  78       4.856  -0.932  31.460  1.00 11.63           S  
ATOM    626  N   LYS A  79       4.823  -5.668  33.004  1.00 14.52           N  
ATOM    627  CA  LYS A  79       4.416  -7.056  33.275  1.00 14.56           C  
ATOM    628  C   LYS A  79       3.276  -7.164  34.294  1.00 14.60           C  
ATOM    629  O   LYS A  79       2.751  -6.159  34.793  1.00 14.37           O  
ATOM    630  CB  LYS A  79       5.625  -7.836  33.776  1.00 15.14           C  
ATOM    631  CG  LYS A  79       6.774  -7.830  32.765  1.00 17.03           C  
ATOM    632  CD  LYS A  79       6.980  -9.187  32.094  1.00 20.15           C  
ATOM    633  CE  LYS A  79       6.035  -9.423  30.915  1.00 21.58           C  
ATOM    634  NZ  LYS A  79       5.736 -10.846  30.703  1.00 22.84           N  
ATOM    635  N   GLY A  80       2.932  -8.414  34.550  1.00 14.68           N  
ATOM    636  CA  GLY A  80       1.836  -8.783  35.453  1.00 14.70           C  
ATOM    637  C   GLY A  80       2.107  -8.283  36.869  1.00 14.77           C  
ATOM    638  O   GLY A  80       3.263  -8.048  37.253  1.00 14.82           O  
ATOM    639  N   GLY A  81       1.011  -8.123  37.593  1.00 14.71           N  
ATOM    640  CA  GLY A  81       1.042  -7.719  39.006  1.00 14.90           C  
ATOM    641  C   GLY A  81       0.624  -6.257  39.219  1.00 14.78           C  
ATOM    642  O   GLY A  81       0.376  -5.824  40.351  1.00 15.14           O  
ATOM    643  N   ASN A  82       0.547  -5.508  38.143  1.00 14.50           N  
ATOM    644  CA  ASN A  82       0.194  -4.081  38.220  1.00 14.23           C  
ATOM    645  C   ASN A  82      -1.314  -3.877  38.363  1.00 14.20           C  
ATOM    646  O   ASN A  82      -2.114  -4.527  37.675  1.00 14.51           O  
ATOM    647  CB  ASN A  82       0.629  -3.359  36.942  1.00 12.99           C  
ATOM    648  CG  ASN A  82       2.145  -3.257  36.812  1.00 11.30           C  
ATOM    649  OD1 ASN A  82       2.840  -3.194  37.823  1.00 11.09           O  
ATOM    650  ND2 ASN A  82       2.705  -3.241  35.617  1.00 11.02           N  
ATOM    651  N   ASN A  83      -1.665  -2.973  39.270  1.00 13.88           N  
ATOM    652  CA  ASN A  83      -3.061  -2.554  39.435  1.00 13.39           C  
ATOM    653  C   ASN A  83      -3.258  -1.395  38.451  1.00 12.90           C  
ATOM    654  O   ASN A  83      -2.356  -1.075  37.662  1.00 12.78           O  
ATOM    655  CB  ASN A  83      -3.372  -2.201  40.901  1.00 13.72           C  
ATOM    656  CG  ASN A  83      -2.684  -0.940  41.417  1.00 15.49           C  
ATOM    657  OD1 ASN A  83      -1.946  -0.294  40.678  1.00 14.37           O  
ATOM    658  ND2 ASN A  83      -2.885  -0.553  42.665  1.00 16.44           N  
ATOM    659  N   ALA A  84      -4.416  -0.780  38.489  1.00 12.67           N  
ATOM    660  CA  ALA A  84      -4.751   0.281  37.522  1.00 12.20           C  
ATOM    661  C   ALA A  84      -3.709   1.404  37.533  1.00 11.82           C  
ATOM    662  O   ALA A  84      -3.289   1.890  36.473  1.00 11.53           O  
ATOM    663  CB  ALA A  84      -6.127   0.869  37.818  1.00 14.03           C  
ATOM    664  N   CYS A  85      -3.304   1.797  38.725  1.00 11.32           N  
ATOM    665  CA  CYS A  85      -2.332   2.886  38.887  1.00 11.16           C  
ATOM    666  C   CYS A  85      -0.942   2.493  38.348  1.00 10.81           C  
ATOM    667  O   CYS A  85      -0.331   3.224  37.559  1.00 11.28           O  
ATOM    668  CB  CYS A  85      -2.180   3.286  40.355  1.00 10.83           C  
ATOM    669  SG  CYS A  85      -0.899   4.611  40.559  1.00 10.38           S  
ATOM    670  N   ALA A  86      -0.455   1.341  38.777  1.00 10.39           N  
ATOM    671  CA  ALA A  86       0.888   0.858  38.384  1.00  9.88           C  
ATOM    672  C   ALA A  86       1.006   0.702  36.861  1.00  9.44           C  
ATOM    673  O   ALA A  86       2.017   1.083  36.252  1.00  9.43           O  
ATOM    674  CB  ALA A  86       1.178  -0.499  39.027  1.00 10.09           C  
ATOM    675  N   ALA A  87      -0.032   0.135  36.282  1.00  9.15           N  
ATOM    676  CA  ALA A  87      -0.092  -0.116  34.834  1.00  9.01           C  
ATOM    677  C   ALA A  87       0.008   1.208  34.057  1.00  8.62           C  
ATOM    678  O   ALA A  87       0.796   1.337  33.111  1.00  8.95           O  
ATOM    679  CB  ALA A  87      -1.399  -0.830  34.484  1.00  7.93           C  
ATOM    680  N   ALA A  88      -0.791   2.169  34.482  1.00  8.63           N  
ATOM    681  CA  ALA A  88      -0.842   3.504  33.854  1.00  8.13           C  
ATOM    682  C   ALA A  88       0.517   4.225  33.947  1.00  8.13           C  
ATOM    683  O   ALA A  88       0.987   4.841  32.978  1.00  8.12           O  
ATOM    684  CB  ALA A  88      -1.893   4.372  34.547  1.00  7.28           C  
ATOM    685  N   VAL A  89       1.127   4.144  35.119  1.00  8.12           N  
ATOM    686  CA  VAL A  89       2.421   4.804  35.379  1.00  7.91           C  
ATOM    687  C   VAL A  89       3.558   4.099  34.639  1.00  8.16           C  
ATOM    688  O   VAL A  89       4.442   4.746  34.060  1.00  7.69           O  
ATOM    689  CB  VAL A  89       2.742   4.813  36.871  1.00  7.38           C  
ATOM    690  CG1 VAL A  89       4.129   5.390  37.170  1.00  8.00           C  
ATOM    691  CG2 VAL A  89       1.751   5.653  37.679  1.00  6.48           C  
ATOM    692  N   CYS A  90       3.528   2.783  34.677  1.00  8.47           N  
ATOM    693  CA  CYS A  90       4.540   1.980  33.988  1.00  8.55           C  
ATOM    694  C   CYS A  90       4.555   2.348  32.503  1.00  8.49           C  
ATOM    695  O   CYS A  90       5.619   2.537  31.900  1.00  8.66           O  
ATOM    696  CB  CYS A  90       4.242   0.486  34.127  1.00  9.91           C  
ATOM    697  SG  CYS A  90       5.553  -0.583  33.350  1.00 12.16           S  
ATOM    698  N   ASP A  91       3.360   2.453  31.935  1.00  8.48           N  
ATOM    699  CA  ASP A  91       3.209   2.770  30.504  1.00  8.72           C  
ATOM    700  C   ASP A  91       3.768   4.164  30.200  1.00  8.43           C  
ATOM    701  O   ASP A  91       4.480   4.355  29.207  1.00  8.95           O  
ATOM    702  CB  ASP A  91       1.745   2.711  30.068  1.00 10.52           C  
ATOM    703  CG  ASP A  91       1.604   2.659  28.543  1.00 12.11           C  
ATOM    704  OD1 ASP A  91       2.300   1.816  27.856  1.00 13.82           O  
ATOM    705  OD2 ASP A  91       0.800   3.463  27.940  1.00 11.61           O  
ATOM    706  N   CYS A  92       3.426   5.101  31.066  1.00  8.35           N  
ATOM    707  CA  CYS A  92       3.886   6.496  30.954  1.00  7.98           C  
ATOM    708  C   CYS A  92       5.424   6.549  30.902  1.00  7.88           C  
ATOM    709  O   CYS A  92       6.020   7.227  30.054  1.00  7.63           O  
ATOM    710  CB  CYS A  92       3.423   7.306  32.173  1.00  9.28           C  
ATOM    711  SG  CYS A  92       1.649   7.867  32.069  1.00 10.20           S  
ATOM    712  N   ASP A  93       6.045   5.821  31.823  1.00  7.85           N  
ATOM    713  CA  ASP A  93       7.523   5.778  31.956  1.00  7.92           C  
ATOM    714  C   ASP A  93       8.165   5.039  30.777  1.00  7.97           C  
ATOM    715  O   ASP A  93       9.216   5.442  30.261  1.00  7.85           O  
ATOM    716  CB  ASP A  93       7.920   5.056  33.249  1.00 10.23           C  
ATOM    717  CG  ASP A  93       7.779   5.940  34.489  1.00 10.67           C  
ATOM    718  OD1 ASP A  93       7.422   7.169  34.359  1.00 10.21           O  
ATOM    719  OD2 ASP A  93       8.017   5.457  35.661  1.00 10.74           O  
ATOM    720  N   ARG A  94       7.509   3.976  30.407  1.00  8.28           N  
ATOM    721  CA  ARG A  94       7.916   3.101  29.306  1.00  8.75           C  
ATOM    722  C   ARG A  94       8.129   3.929  28.025  1.00  8.76           C  
ATOM    723  O   ARG A  94       9.204   3.891  27.403  1.00  8.93           O  
ATOM    724  CB  ARG A  94       6.787   2.098  29.119  1.00  9.68           C  
ATOM    725  CG  ARG A  94       7.111   0.928  28.227  1.00 10.62           C  
ATOM    726  CD  ARG A  94       5.841   0.210  27.784  1.00 10.88           C  
ATOM    727  NE  ARG A  94       5.804   0.150  26.366  1.00 12.81           N  
ATOM    728  CZ  ARG A  94       4.935   0.681  25.520  1.00 11.59           C  
ATOM    729  NH1 ARG A  94       3.821   1.323  25.888  1.00 11.83           N  
ATOM    730  NH2 ARG A  94       5.166   0.656  24.227  1.00 12.64           N  
ATOM    731  N   LEU A  95       7.078   4.651  27.694  1.00  8.61           N  
ATOM    732  CA  LEU A  95       6.991   5.506  26.496  1.00  8.77           C  
ATOM    733  C   LEU A  95       8.046   6.632  26.526  1.00  8.23           C  
ATOM    734  O   LEU A  95       8.653   6.977  25.499  1.00  8.53           O  
ATOM    735  CB  LEU A  95       5.599   6.148  26.448  1.00 11.46           C  
ATOM    736  CG  LEU A  95       4.686   5.619  25.332  1.00 14.44           C  
ATOM    737  CD1 LEU A  95       5.208   4.350  24.655  1.00 15.53           C  
ATOM    738  CD2 LEU A  95       3.276   5.279  25.828  1.00 14.63           C  
ATOM    739  N   ALA A  96       8.244   7.185  27.709  1.00  7.78           N  
ATOM    740  CA  ALA A  96       9.184   8.302  27.920  1.00  7.14           C  
ATOM    741  C   ALA A  96      10.644   7.867  27.687  1.00  7.03           C  
ATOM    742  O   ALA A  96      11.430   8.583  27.051  1.00  6.42           O  
ATOM    743  CB  ALA A  96       9.046   8.845  29.344  1.00  7.26           C  
ATOM    744  N   ALA A  97      10.989   6.696  28.204  1.00  6.76           N  
ATOM    745  CA  ALA A  97      12.359   6.154  28.080  1.00  6.90           C  
ATOM    746  C   ALA A  97      12.654   5.757  26.627  1.00  7.24           C  
ATOM    747  O   ALA A  97      13.795   5.865  26.151  1.00  7.49           O  
ATOM    748  CB  ALA A  97      12.539   4.936  28.986  1.00  5.89           C  
ATOM    749  N   ILE A  98      11.616   5.297  25.948  1.00  7.17           N  
ATOM    750  CA  ILE A  98      11.719   4.916  24.534  1.00  7.69           C  
ATOM    751  C   ILE A  98      11.906   6.197  23.702  1.00  7.64           C  
ATOM    752  O   ILE A  98      12.681   6.231  22.740  1.00  7.49           O  
ATOM    753  CB  ILE A  98      10.468   4.121  24.109  1.00  9.21           C  
ATOM    754  CG1 ILE A  98      10.496   2.668  24.611  1.00  9.35           C  
ATOM    755  CG2 ILE A  98      10.289   4.028  22.587  1.00 11.42           C  
ATOM    756  CD1 ILE A  98       9.161   1.936  24.441  1.00 10.46           C  
ATOM    757  N   CYS A  99      11.208   7.246  24.110  1.00  7.92           N  
ATOM    758  CA  CYS A  99      11.265   8.549  23.420  1.00  8.22           C  
ATOM    759  C   CYS A  99      12.671   9.182  23.532  1.00  8.60           C  
ATOM    760  O   CYS A  99      13.239   9.672  22.542  1.00  8.03           O  
ATOM    761  CB  CYS A  99      10.239   9.517  24.015  1.00  7.78           C  
ATOM    762  SG  CYS A  99      10.025  11.029  22.962  1.00  8.32           S  
ATOM    763  N   PHE A 100      13.211   9.162  24.741  1.00  8.76           N  
ATOM    764  CA  PHE A 100      14.542   9.744  25.032  1.00  9.47           C  
ATOM    765  C   PHE A 100      15.639   9.137  24.152  1.00  9.87           C  
ATOM    766  O   PHE A 100      16.586   9.821  23.743  1.00  9.94           O  
ATOM    767  CB  PHE A 100      15.003   9.433  26.454  1.00 10.83           C  
ATOM    768  CG  PHE A 100      14.296  10.198  27.571  1.00 11.44           C  
ATOM    769  CD1 PHE A 100      13.219  11.054  27.297  1.00 12.00           C  
ATOM    770  CD2 PHE A 100      14.744  10.028  28.885  1.00 11.63           C  
ATOM    771  CE1 PHE A 100      12.580  11.727  28.351  1.00 13.43           C  
ATOM    772  CE2 PHE A 100      14.107  10.699  29.935  1.00 12.13           C  
ATOM    773  CZ  PHE A 100      13.024  11.546  29.670  1.00 12.86           C  
ATOM    774  N   ALA A 101      15.496   7.852  23.903  1.00  9.92           N  
ATOM    775  CA  ALA A 101      16.476   7.089  23.120  1.00 10.30           C  
ATOM    776  C   ALA A 101      16.435   7.465  21.631  1.00 10.62           C  
ATOM    777  O   ALA A 101      17.363   7.169  20.870  1.00 10.97           O  
ATOM    778  CB  ALA A 101      16.195   5.588  23.240  1.00 10.06           C  
ATOM    779  N   GLY A 102      15.371   8.128  21.220  1.00 10.68           N  
ATOM    780  CA  GLY A 102      15.190   8.478  19.798  1.00 10.91           C  
ATOM    781  C   GLY A 102      15.365   9.976  19.529  1.00 11.09           C  
ATOM    782  O   GLY A 102      15.210  10.441  18.390  1.00 11.00           O  
ATOM    783  N   ALA A 103      15.685  10.722  20.566  1.00 11.07           N  
ATOM    784  CA  ALA A 103      15.833  12.181  20.438  1.00 11.45           C  
ATOM    785  C   ALA A 103      17.276  12.625  20.666  1.00 11.71           C  
ATOM    786  O   ALA A 103      17.960  12.145  21.585  1.00 11.55           O  
ATOM    787  CB  ALA A 103      14.940  12.895  21.451  1.00 10.23           C  
ATOM    788  N   PRO A 104      17.792  13.534  19.831  1.00 12.13           N  
ATOM    789  CA  PRO A 104      19.131  14.051  20.007  1.00 12.57           C  
ATOM    790  C   PRO A 104      19.206  14.828  21.297  1.00 12.70           C  
ATOM    791  O   PRO A 104      18.220  15.543  21.647  1.00 13.39           O  
ATOM    792  CB  PRO A 104      19.321  14.977  18.824  1.00 12.36           C  
ATOM    793  CG  PRO A 104      18.031  14.975  18.019  1.00 12.36           C  
ATOM    794  CD  PRO A 104      17.043  14.084  18.701  1.00 12.13           C  
ATOM    795  N   TYR A 105      20.325  14.695  21.985  1.00 13.24           N  
ATOM    796  CA  TYR A 105      20.578  15.464  23.220  1.00 13.29           C  
ATOM    797  C   TYR A 105      21.442  16.668  22.854  1.00 13.67           C  
ATOM    798  O   TYR A 105      22.579  16.513  22.392  1.00 13.44           O  
ATOM    799  CB  TYR A 105      21.319  14.609  24.262  1.00 13.84           C  
ATOM    800  CG  TYR A 105      21.446  15.286  25.644  1.00 13.95           C  
ATOM    801  CD1 TYR A 105      22.489  16.193  25.901  1.00 12.23           C  
ATOM    802  CD2 TYR A 105      20.521  14.996  26.657  1.00 11.97           C  
ATOM    803  CE1 TYR A 105      22.606  16.794  27.166  1.00 12.31           C  
ATOM    804  CE2 TYR A 105      20.640  15.595  27.919  1.00 11.83           C  
ATOM    805  CZ  TYR A 105      21.682  16.491  28.174  1.00 11.84           C  
ATOM    806  OH  TYR A 105      21.798  17.063  29.404  1.00 11.50           O  
ATOM    807  N   ASN A 106      20.873  17.842  23.048  1.00 13.82           N  
ATOM    808  CA  ASN A 106      21.570  19.109  22.776  1.00 14.36           C  
ATOM    809  C   ASN A 106      22.022  19.692  24.114  1.00 14.73           C  
ATOM    810  O   ASN A 106      21.198  20.023  24.978  1.00 14.30           O  
ATOM    811  CB  ASN A 106      20.640  20.058  22.023  1.00 13.81           C  
ATOM    812  CG  ASN A 106      20.077  19.433  20.742  1.00 13.48           C  
ATOM    813  OD1 ASN A 106      20.839  18.944  19.907  1.00 16.24           O  
ATOM    814  ND2 ASN A 106      18.774  19.418  20.531  1.00 14.54           N  
ATOM    815  N   ASP A 107      23.327  19.790  24.235  1.00 14.92           N  
ATOM    816  CA  ASP A 107      23.990  20.224  25.471  1.00 15.93           C  
ATOM    817  C   ASP A 107      23.637  21.671  25.850  1.00 15.52           C  
ATOM    818  O   ASP A 107      23.631  22.034  27.036  1.00 15.77           O  
ATOM    819  CB  ASP A 107      25.498  20.060  25.318  1.00 21.15           C  
ATOM    820  CG  ASP A 107      25.999  18.829  26.069  1.00 24.40           C  
ATOM    821  OD1 ASP A 107      25.991  18.824  27.356  1.00 26.57           O  
ATOM    822  OD2 ASP A 107      26.411  17.796  25.417  1.00 25.34           O  
ATOM    823  N   ASN A 108      23.338  22.467  24.847  1.00 15.44           N  
ATOM    824  CA  ASN A 108      22.991  23.885  25.042  1.00 14.99           C  
ATOM    825  C   ASN A 108      21.642  24.044  25.759  1.00 14.52           C  
ATOM    826  O   ASN A 108      21.291  25.136  26.229  1.00 14.19           O  
ATOM    827  CB  ASN A 108      22.877  24.600  23.687  1.00 17.89           C  
ATOM    828  CG  ASN A 108      22.029  23.837  22.660  1.00 19.14           C  
ATOM    829  OD1 ASN A 108      21.026  24.362  22.173  1.00 20.16           O  
ATOM    830  ND2 ASN A 108      22.378  22.618  22.291  1.00 18.81           N  
ATOM    831  N   ASP A 109      20.904  22.951  25.843  1.00 14.34           N  
ATOM    832  CA  ASP A 109      19.550  22.980  26.424  1.00 14.05           C  
ATOM    833  C   ASP A 109      19.495  22.394  27.842  1.00 13.78           C  
ATOM    834  O   ASP A 109      18.409  22.242  28.422  1.00 13.40           O  
ATOM    835  CB  ASP A 109      18.585  22.203  25.530  1.00 16.84           C  
ATOM    836  CG  ASP A 109      18.239  22.961  24.247  1.00 19.01           C  
ATOM    837  OD1 ASP A 109      18.348  24.246  24.210  1.00 18.07           O  
ATOM    838  OD2 ASP A 109      17.840  22.317  23.204  1.00 20.49           O  
ATOM    839  N   TYR A 110      20.657  22.074  28.382  1.00 13.34           N  
ATOM    840  CA  TYR A 110      20.756  21.547  29.755  1.00 13.37           C  
ATOM    841  C   TYR A 110      20.939  22.704  30.745  1.00 13.32           C  
ATOM    842  O   TYR A 110      21.827  23.549  30.572  1.00 13.06           O  
ATOM    843  CB  TYR A 110      21.960  20.607  29.906  1.00 14.41           C  
ATOM    844  CG  TYR A 110      22.150  20.148  31.356  1.00 15.40           C  
ATOM    845  CD1 TYR A 110      21.275  19.206  31.908  1.00 16.58           C  
ATOM    846  CD2 TYR A 110      23.193  20.671  32.134  1.00 16.25           C  
ATOM    847  CE1 TYR A 110      21.423  18.805  33.240  1.00 17.48           C  
ATOM    848  CE2 TYR A 110      23.344  20.266  33.468  1.00 17.89           C  
ATOM    849  CZ  TYR A 110      22.452  19.339  34.022  1.00 18.71           C  
ATOM    850  OH  TYR A 110      22.577  18.963  35.323  1.00 20.46           O  
ATOM    851  N   ASN A 111      20.080  22.706  31.756  1.00 13.42           N  
ATOM    852  CA  ASN A 111      20.109  23.712  32.838  1.00 13.58           C  
ATOM    853  C   ASN A 111      19.987  25.126  32.260  1.00 13.98           C  
ATOM    854  O   ASN A 111      20.811  26.006  32.534  1.00 13.85           O  
ATOM    855  CB  ASN A 111      21.441  23.588  33.598  1.00 13.97           C  
ATOM    856  CG  ASN A 111      21.594  24.550  34.784  1.00 14.21           C  
ATOM    857  OD1 ASN A 111      22.700  25.030  35.047  1.00 16.04           O  
ATOM    858  ND2 ASN A 111      20.550  24.860  35.529  1.00 12.43           N  
ATOM    859  N   ILE A 112      18.959  25.336  31.453  1.00 14.10           N  
ATOM    860  CA  ILE A 112      18.736  26.653  30.836  1.00 14.58           C  
ATOM    861  C   ILE A 112      17.993  27.559  31.823  1.00 15.10           C  
ATOM    862  O   ILE A 112      17.403  27.087  32.807  1.00 14.92           O  
ATOM    863  CB  ILE A 112      17.951  26.516  29.516  1.00 14.29           C  
ATOM    864  CG1 ILE A 112      16.560  25.890  29.684  1.00 14.18           C  
ATOM    865  CG2 ILE A 112      18.685  25.653  28.483  1.00 13.71           C  
ATOM    866  CD1 ILE A 112      15.711  25.942  28.404  1.00 14.55           C  
ATOM    867  N   ASN A 113      18.069  28.848  31.537  1.00 15.60           N  
ATOM    868  CA  ASN A 113      17.397  29.883  32.337  1.00 16.22           C  
ATOM    869  C   ASN A 113      15.907  29.861  31.988  1.00 16.86           C  
ATOM    870  O   ASN A 113      15.473  30.475  31.003  1.00 16.77           O  
ATOM    871  CB  ASN A 113      18.000  31.255  32.030  1.00 16.06           C  
ATOM    872  CG  ASN A 113      17.494  32.338  32.978  1.00 16.97           C  
ATOM    873  OD1 ASN A 113      18.230  33.269  33.298  1.00 18.13           O  
ATOM    874  ND2 ASN A 113      16.267  32.264  33.455  1.00 17.07           N  
ATOM    875  N   LEU A 114      15.184  29.146  32.825  1.00 17.22           N  
ATOM    876  CA  LEU A 114      13.744  28.887  32.656  1.00 18.28           C  
ATOM    877  C   LEU A 114      12.901  30.177  32.578  1.00 18.91           C  
ATOM    878  O   LEU A 114      11.866  30.223  31.894  1.00 18.93           O  
ATOM    879  CB  LEU A 114      13.234  28.042  33.824  1.00 19.26           C  
ATOM    880  CG  LEU A 114      13.214  26.534  33.530  1.00 19.35           C  
ATOM    881  CD1 LEU A 114      14.145  26.121  32.385  1.00 18.17           C  
ATOM    882  CD2 LEU A 114      13.638  25.692  34.736  1.00 20.54           C  
ATOM    883  N   LYS A 115      13.331  31.215  33.280  1.00 19.39           N  
ATOM    884  CA  LYS A 115      12.594  32.501  33.294  1.00 20.31           C  
ATOM    885  C   LYS A 115      12.794  33.263  31.979  1.00 20.50           C  
ATOM    886  O   LYS A 115      11.923  34.034  31.553  1.00 20.65           O  
ATOM    887  CB  LYS A 115      13.074  33.415  34.428  1.00 22.36           C  
ATOM    888  CG  LYS A 115      12.624  32.959  35.819  1.00 23.67           C  
ATOM    889  CD  LYS A 115      11.128  33.152  36.082  1.00 25.96           C  
ATOM    890  CE  LYS A 115      10.626  32.288  37.244  1.00 27.50           C  
ATOM    891  NZ  LYS A 115       9.593  32.948  38.054  1.00 29.39           N  
ATOM    892  N   ALA A 116      13.944  33.031  31.368  1.00 20.79           N  
ATOM    893  CA  ALA A 116      14.318  33.685  30.099  1.00 21.39           C  
ATOM    894  C   ALA A 116      13.723  32.932  28.908  1.00 21.87           C  
ATOM    895  O   ALA A 116      13.376  33.553  27.881  1.00 21.68           O  
ATOM    896  CB  ALA A 116      15.840  33.718  29.951  1.00 21.38           C  
ATOM    897  N   ARG A 117      13.805  31.587  29.010  1.00 22.05           N  
ATOM    898  CA  ARG A 117      13.573  30.762  27.811  1.00 22.37           C  
ATOM    899  C   ARG A 117      12.194  30.128  27.771  1.00 22.20           C  
ATOM    900  O   ARG A 117      11.799  29.624  26.702  1.00 22.29           O  
ATOM    901  CB  ARG A 117      14.649  29.744  27.526  1.00 25.04           C  
ATOM    902  CG  ARG A 117      16.093  30.151  27.387  1.00 27.34           C  
ATOM    903  CD  ARG A 117      16.590  30.043  25.990  1.00 29.98           C  
ATOM    904  NE  ARG A 117      16.065  28.885  25.269  1.00 32.66           N  
ATOM    905  CZ  ARG A 117      16.836  27.822  24.972  1.00 34.25           C  
ATOM    906  NH1 ARG A 117      18.142  27.839  25.271  1.00 35.08           N  
ATOM    907  NH2 ARG A 117      16.326  26.704  24.455  1.00 35.03           N  
ATOM    908  N   CYS A 118      11.518  30.032  28.894  1.00 22.38           N  
ATOM    909  CA  CYS A 118      10.277  29.222  28.957  1.00 22.12           C  
ATOM    910  C   CYS A 118       9.050  30.077  29.139  1.00 22.72           C  
ATOM    911  O   CYS A 118       8.313  29.852  30.126  1.00 22.83           O  
ATOM    912  CB  CYS A 118      10.401  28.106  29.976  1.00 17.23           C  
ATOM    913  SG  CYS A 118      11.821  27.032  29.698  1.00 14.69           S  
ATOM    914  OXT CYS A 118       8.730  30.748  28.130  1.00 27.38           O  
TER     915      CYS A 118                                                      
HETATM 1831 CA    CA A 801       8.560  17.585  33.810  1.00 14.63          CA  
HETATM 1832 CA    CA A 803      13.601  21.725  32.941  1.00 28.26          CA  
HETATM 1833  C1  GEL A 930       9.580  13.438  37.067  1.00 17.64           C  
HETATM 1834  O1  GEL A 930      10.984  13.654  37.316  1.00 18.76           O  
HETATM 1835  C11 GEL A 930      11.284  14.633  38.321  1.00 19.03           C  
HETATM 1836  C12 GEL A 930      12.796  14.838  38.232  1.00 19.69           C  
HETATM 1837  C13 GEL A 930      13.545  14.765  39.549  1.00 20.23           C  
HETATM 1838  C14 GEL A 930      14.552  13.649  39.672  1.00 20.72           C  
HETATM 1839  C15 GEL A 930      14.780  12.934  40.985  1.00 21.15           C  
HETATM 1840  C16 GEL A 930      15.581  11.650  40.949  1.00 21.27           C  
HETATM 1841  C17 GEL A 930      15.132  10.487  41.804  1.00 21.41           C  
HETATM 1842  C18 GEL A 930      15.815   9.150  41.562  1.00 21.40           C  
HETATM 1843  C2  GEL A 930       9.124  14.123  35.811  1.00 17.03           C  
HETATM 1844  O2  GEL A 930       9.554  13.387  34.600  1.00 16.57           O  
HETATM 1845  P2  GEL A 930      10.338  14.229  33.463  1.00 15.81           P  
HETATM 1846  O1P GEL A 930       9.677  13.759  32.198  1.00 16.11           O  
HETATM 1847  O2P GEL A 930       9.935  15.640  33.608  1.00 15.82           O  
HETATM 1848  C22 GEL A 930      12.162  14.024  33.347  1.00 16.36           C  
HETATM 1849  C23 GEL A 930      12.824  13.397  34.523  1.00 16.71           C  
HETATM 1850  C24 GEL A 930      14.239  12.912  34.298  1.00 17.18           C  
HETATM 1851  C25 GEL A 930      14.844  12.366  35.583  1.00 17.49           C  
HETATM 1852  C26 GEL A 930      14.447  10.908  35.809  1.00 18.00           C  
HETATM 1853  C27 GEL A 930      14.240  10.628  37.288  1.00 18.10           C  
HETATM 1854  C28 GEL A 930      14.613   9.230  37.703  1.00 18.26           C  
HETATM 1855  C3  GEL A 930       7.608  14.197  35.563  1.00 16.83           C  
HETATM 1856  O3  GEL A 930       6.966  14.755  36.714  1.00 16.61           O  
HETATM 1857  P3  GEL A 930       6.491  16.289  36.761  1.00 16.43           P  
HETATM 1858  O3P GEL A 930       6.276  16.642  38.190  1.00 16.54           O  
HETATM 1859  O4P GEL A 930       7.397  17.144  36.003  1.00 16.40           O  
HETATM 1860  O5P GEL A 930       5.109  15.991  36.094  1.00 16.79           O  
HETATM 1861  C31 GEL A 930       3.878  15.751  36.751  1.00 17.19           C  
HETATM 1862  C32 GEL A 930       2.999  16.953  36.564  1.00 17.36           C  
HETATM 1863  N3  GEL A 930       1.586  16.479  36.668  1.00 17.70           N  
CONECT   96  578                                                                
CONECT  204 1832                                                                
CONECT  216 1832                                                                
CONECT  222  913                                                                
CONECT  226 1831                                                                
CONECT  238 1832                                                                
CONECT  240  349                                                                
CONECT  244 1831                                                                
CONECT  259 1831                                                                
CONECT  343  762                                                                
CONECT  349  240                                                                
CONECT  382 1831                                                                
CONECT  383 1831                                                                
CONECT  397  711                                                                
CONECT  417 1863                                                                
CONECT  473  669                                                                
CONECT  578   96                                                                
CONECT  625  697                                                                
CONECT  669  473                                                                
CONECT  697  625                                                                
CONECT  711  397                                                                
CONECT  762  343                                                                
CONECT  913  222                                                                
CONECT 1011 1493                                                                
CONECT 1119 1865                                                                
CONECT 1131 1865                                                                
CONECT 1137 1828                                                                
CONECT 1141 1864                                                                
CONECT 1153 1865                                                                
CONECT 1155 1264                                                                
CONECT 1159 1864                                                                
CONECT 1174 1864                                                                
CONECT 1258 1677                                                                
CONECT 1264 1155                                                                
CONECT 1297 1864                                                                
CONECT 1298 1864                                                                
CONECT 1312 1626                                                                
CONECT 1388 1584                                                                
CONECT 1493 1011                                                                
CONECT 1584 1388                                                                
CONECT 1626 1312                                                                
CONECT 1677 1258                                                                
CONECT 1828 1137                                                                
CONECT 1831  226  244  259  382                                                 
CONECT 1831  383 1847 1859                                                      
CONECT 1832  204  216  238 1922                                                 
CONECT 1832 2032                                                                
CONECT 1833 1834 1843                                                           
CONECT 1834 1833 1835                                                           
CONECT 1835 1834 1836                                                           
CONECT 1836 1835 1837                                                           
CONECT 1837 1836 1838                                                           
CONECT 1838 1837 1839                                                           
CONECT 1839 1838 1840                                                           
CONECT 1840 1839 1841                                                           
CONECT 1841 1840 1842                                                           
CONECT 1842 1841                                                                
CONECT 1843 1833 1844 1855                                                      
CONECT 1844 1843 1845                                                           
CONECT 1845 1844 1846 1847 1848                                                 
CONECT 1846 1845                                                                
CONECT 1847 1831 1845                                                           
CONECT 1848 1845 1849                                                           
CONECT 1849 1848 1850                                                           
CONECT 1850 1849 1851                                                           
CONECT 1851 1850 1852                                                           
CONECT 1852 1851 1853                                                           
CONECT 1853 1852 1854                                                           
CONECT 1854 1853                                                                
CONECT 1855 1843 1856                                                           
CONECT 1856 1855 1857                                                           
CONECT 1857 1856 1858 1859 1860                                                 
CONECT 1858 1857                                                                
CONECT 1859 1831 1857                                                           
CONECT 1860 1857 1861                                                           
CONECT 1861 1860 1862                                                           
CONECT 1862 1861 1863                                                           
CONECT 1863  417 1862                                                           
CONECT 1864 1141 1159 1174 1297                                                 
CONECT 1864 1298 1880 1892                                                      
CONECT 1865 1119 1131 1153 2047                                                 
CONECT 1866 1867 1876                                                           
CONECT 1867 1866 1868                                                           
CONECT 1868 1867 1869                                                           
CONECT 1869 1868 1870                                                           
CONECT 1870 1869 1871                                                           
CONECT 1871 1870 1872                                                           
CONECT 1872 1871 1873                                                           
CONECT 1873 1872 1874                                                           
CONECT 1874 1873 1875                                                           
CONECT 1875 1874                                                                
CONECT 1876 1866 1877 1888                                                      
CONECT 1877 1876 1878                                                           
CONECT 1878 1877 1879 1880 1881                                                 
CONECT 1879 1878                                                                
CONECT 1880 1864 1878                                                           
CONECT 1881 1878 1882                                                           
CONECT 1882 1881 1883                                                           
CONECT 1883 1882 1884                                                           
CONECT 1884 1883 1885                                                           
CONECT 1885 1884 1886                                                           
CONECT 1886 1885 1887                                                           
CONECT 1887 1886                                                                
CONECT 1888 1876 1889                                                           
CONECT 1889 1888 1890                                                           
CONECT 1890 1889 1891 1892 1893                                                 
CONECT 1891 1890                                                                
CONECT 1892 1864 1890                                                           
CONECT 1893 1890 1894                                                           
CONECT 1894 1893 1895                                                           
CONECT 1895 1894 1896                                                           
CONECT 1896 1895                                                                
CONECT 1922 1832                                                                
CONECT 2032 1832                                                                
CONECT 2047 1865                                                                
MASTER      303    0    6    8    4    0   19    6 2136    2  115   20          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.